{"text_format":"3","workbook":"xlsx","n_sheets":13,"sheets":["instruction","start","gene features","protein features","MaGe-Curated annotations","SwissProt","UniFIRE ","PRIAM EC number","COG","EGGNOG","FIGfam","InterProScan","PSortB"],"not_rendered":{"defined_names":1},"read":"whole","date_system":"1900"}

{"sheet":"instruction","index":0,"n_rows":14,"n_cols":2,"rows_kept":14,"merged":[[0,0,0,1]]}
["Additional file 5. Functional annotations of strain BL-3"]
["Worksheet name","Description"]
["start","information of the gene coding sequence"]
["gene features","measures of the predicted CDS"]
["protein features","measures of the predicted proteins"]
["MaGe-Curated annotations","results of functional gene annotations using the MaGe curated annotations"]
["SwissProt","results of functional gene annotations using SwissProt"]
["UniFIRE","results of functional gene annotations using UniFIRE"]
["PRIAM EC number","the PRIAM method used to predict enzymatic function at the level of the EC number"]
["COG","results of functional gene annotations using COG"]
["EGGNOG","results of functional gene annotations using EGGNOG"]
["FIGfam","results of functional gene annotations using FIGfam"]
["InterProScan","results of functional gene annotations using InterPro"]
["PSortB","results of bacterial protein subcellular localization prediction"]

{"sheet":"start","index":1,"n_rows":70,"n_cols":13,"rows_kept":70}
["CDS","Strand","length","Begin","End","AMIGene Start","AMIGene Lpcod","AMIGene Apcod","Matrix","Prodigal Begin","Prodigal End","Glimmer Begin","Glimmer End"]
["CLOSTRIBL3_v1_11086","R",1272,1049413,1050684,1050684,0.915606,0.915606,1,1049413,1050684,1049413,1050684]
["CLOSTRIBL3_v1_11116","R",1275,1079732,1081015,1081015,0.93988,0.93988,2,1079732,1081006,1079732,1081006]
["CLOSTRIBL3_v1_11117","R",1527,1081059,1082585,1082585,0.791231,0.791231,1,1081059,1082585,1081059,1082585]
["CLOSTRIBL3_v1_30024","R",1275,3731567,3732895,3732895,0.902583,0.902583,2,3731567,3732841,3731567,3732841]
["CLOSTRIBL3_v1_10010","R",1245,8920,10164,10164,0.676956,0.676956,1,8920,10164,8920,10164]
["CLOSTRIBL3_v1_10012","D",963,15277,16254,15277,0.948408,0.948408,1,15292,16254,15292,16254]
["CLOSTRIBL3_v1_12309","R",1071,2277379,2278449,2278449,0.908608,0.908608,2,2277379,2278449,2277379,2278398]
["CLOSTRIBL3_v1_12417","R",3522,2396261,2399794,2399794,0.930214,0.930214,2,2396261,2399782,2396261,2399782]
["CLOSTRIBL3_v1_12774","R",930,2742760,2743689,2743689,0.935049,0.935049,1,2742760,2743689,2742760,2743689]
["CLOSTRIBL3_v1_12775","R",1176,2743701,2744885,2744885,0.908512,0.908512,1,2743701,2744876,2743701,2744876]
["CLOSTRIBL3_v1_12776","R",297,2744896,2745192,2745192,0.73426,0.73426,1,2744896,2745192,2744896,2745192]
["CLOSTRIBL3_v1_12777","R",582,2745189,2745773,2745773,0.898693,0.898693,1,2745189,2745770,2745189,2745770]
["CLOSTRIBL3_v1_10343","D",3507,368365,371871,368365,0.959552,0.959552,2,368365,371871,368365,371871]
["CLOSTRIBL3_v1_20129","D",3513,3253230,3256742,3253230,0.923933,0.923933,1,3253230,3256742,3253230,3256742]
["CLOSTRIBL3_v1_12838","R",1179,2805278,2806456,2806456,0.953409,0.953409,1,2805278,2806456,2805278,2806456]
["CLOSTRIBL3_v1_13111","R",1176,3079379,3080554,3080554,0.921186,0.921186,1,3079379,3080554,3079379,3080554]
["CLOSTRIBL3_v1_11283","R",1200,1257719,1258918,1258918,0.94218,0.94218,1,1257719,1258852,1257719,1258918]
["CLOSTRIBL3_v1_11276","R",936,1250005,1250994,1250994,0.894324,0.894324,1,1250005,1250940,1250005,1250940]
["CLOSTRIBL3_v1_13113","R",867,3081380,3082258,3082258,0.879715,0.879715,2,3081380,3082246,3081380,3082246]
["CLOSTRIBL3_v1_20313","D",849,3449072,3449920,3449072,0.869807,0.869807,1,3449072,3449920,3449072,3449920]
["CLOSTRIBL3_v1_13112","R",768,3080571,3081338,3081338,0.910393,0.910393,1,3080571,3081338,3080571,3081338]
["CLOSTRIBL3_v1_11087","R",765,1050822,1051604,1051604,0.921833,0.921833,1,1050822,1051586,1050822,1051586]
["CLOSTRIBL3_v1_20109","D",417,3230179,3230595,3230179,0.848492,0.848492,1,3230179,3230595,3230179,3230595]
["CLOSTRIBL3_v1_20308","D",780,3445184,3445978,3445184,0.92335,0.92335,2,3445199,3445978,3445199,3445978]
["CLOSTRIBL3_v1_12502","R",1908,2479307,2481214,2481214,0.951329,0.951329,1,2479307,2481214,2479307,2481214]
["CLOSTRIBL3_v1_11587","R",1140,1572579,1573727,1573727,0.90979,0.90979,1,1572579,1573718,1572579,1573718]
["CLOSTRIBL3_v1_12012","R",1143,1976247,1977407,1977407,0.898554,0.898554,1,1976247,1977389,1976247,1977389]
["CLOSTRIBL3_v1_12013","R",1167,1977636,1978802,1978802,0.947212,0.947212,1,1977636,1978802,1977636,1978802]
["CLOSTRIBL3_v1_20310","D",1140,3446064,3447203,3446064,0.930544,0.930544,1,3446064,3447203,3446064,3447203]
["CLOSTRIBL3_v1_20311","D",780,3447218,3447997,3447218,0.926671,0.926671,2,3447218,3447997,3447218,3447997]
["CLOSTRIBL3_v1_20312","D",1002,3448014,3449015,3448014,0.945791,0.945791,2,3448014,3449015,3448014,3449015]
["CLOSTRIBL3_v1_11710","R",1077,1694499,1695575,1695575,0.950055,0.950055,1,1694499,1695560,1694499,1695575]
["CLOSTRIBL3_v1_11711","R",906,1695681,1696613,1696613,0.867263,0.867263,1,1695681,1696586,1695681,1696586]
["CLOSTRIBL3_v1_12016","R",903,1980848,1981822,1981822,0.910851,0.910851,1,1980848,1981750,1980848,1981750]
["CLOSTRIBL3_v1_12308","R",897,2276377,2277309,2277309,0.937002,0.937002,1,2276377,2277273,2276377,2277273]
["CLOSTRIBL3_v1_20086","D",1086,3210297,3211382,3210297,0.946124,0.946124,1,3210297,3211382,3210297,3211382]
["CLOSTRIBL3_v1_20087","D",1077,3211416,3212507,3211416,0.919321,0.919321,1,3211431,3212507,3211431,3212507]
["CLOSTRIBL3_v1_13110","R",1359,3077994,3079352,3079352,0.922183,0.922183,1,3077994,3079352,3077994,3079352]
["CLOSTRIBL3_v1_11114","R",1215,1077660,1078874,1078874,0.965545,0.965545,1,1077660,1078874,1077660,1078874]
["CLOSTRIBL3_v1_11115","R",789,1078895,1079683,1079683,0.920352,0.920352,2,1078895,1079683,1078895,1079683]
["CLOSTRIBL3_v1_11486","R",1416,1461251,1462666,1462666,0.940022,0.940022,2,1461251,1462666,1461251,1462636]
["CLOSTRIBL3_v1_11487","R",987,1462663,1463691,1463691,0.922502,0.922502,2,1462663,1463649,1462663,1463649]
["CLOSTRIBL3_v1_11488","R",798,1463654,1464451,1464451,0.922838,0.922838,1,1463654,1464451,1463654,1464451]
["CLOSTRIBL3_v1_12010","R",1011,1974420,1975430,1975430,0.949262,0.949262,1,1974420,1975430,1974420,1975430]
["CLOSTRIBL3_v1_12011","R",789,1975446,1976234,1976234,0.944921,0.944921,1,1975446,1976234,1975446,1976234]
["CLOSTRIBL3_v1_20124","D",798,3247471,3248268,3247471,0.896738,0.896738,1,3247471,3248268,3247471,3248268]
["CLOSTRIBL3_v1_20125","D",1002,3248348,3249349,3248348,0.930581,0.930581,1,3248348,3249349,3248348,3249349]
["CLOSTRIBL3_v1_10629","D",1374,605744,607117,605744,0.937597,0.937597,1,605744,607117,605744,607117]
["CLOSTRIBL3_v1_10630","D",996,607136,608131,607301,0.792306,0.866241,2,607136,608131,607136,608131]
["CLOSTRIBL3_v1_10631","D",558,608138,608695,608138,0.893275,0.893275,2,608138,608695,608138,608695]
["CLOSTRIBL3_v1_10632","D",639,608698,609336,608698,0.87447,0.87447,2,608698,609336,608698,609336]
["CLOSTRIBL3_v1_10633","D",582,609336,609917,609336,0.76087,0.76087,2,609336,609917,609336,609917]
["CLOSTRIBL3_v1_10634","D",864,609935,610798,609935,0.926156,0.926156,2,609935,610798,609935,610798]
["CLOSTRIBL3_v1_10096","D",567,107355,107972,107355,0.881283,0.881283,2,107406,107972,107406,107972]
["CLOSTRIBL3_v1_10095","D",1389,106004,107401,106004,0.884633,0.884633,1,106013,107401,106013,107401]
["CLOSTRIBL3_v1_10094","D",558,105413,105970,105413,0.87436,0.87436,1,105413,105970,105413,105970]
["CLOSTRIBL3_v1_10091","D",492,102236,102739,102236,0.848486,0.848486,2,102260,102739,102248,102739]
["CLOSTRIBL3_v1_10092","D",1800,102739,104538,102739,0.947588,0.947588,2,102739,104538,102739,104538]
["CLOSTRIBL3_v1_10093","D",756,104516,105307,104516,0.920454,0.920454,2,104552,105307,104552,105307]
["CLOSTRIBL3_v1_13020","D",1350,2986066,2987415,2986066,0.843849,0.843849,2,2986066,2987415,2986066,2987415]
["CLOSTRIBL3_v1_20317","D",1491,3454064,3455575,3454064,0.943626,0.943626,1,3454085,3455575,3454085,3455575]
["CLOSTRIBL3_v1_12009","R",1683,1972688,1974370,1974370,0.906179,0.906179,1,1972688,1974370,1972688,1974370]
["CLOSTRIBL3_v1_10745","D",996,713005,714075,713005,0.951824,0.951824,2,713080,714075,713080,714075]
["CLOSTRIBL3_v1_10746","D",1200,714154,715353,714154,0.938887,0.938887,1,714154,715353,714154,715353]
["CLOSTRIBL3_v1_11881","R",1164,1859405,1860589,1860589,0.917036,0.917036,1,1859405,1860568,1859405,1860568]
["CLOSTRIBL3_v1_20137","D",1149,3266060,3267232,3266060,0.942994,0.942994,1,3266084,3267232,3266084,3267232]
["CLOSTRIBL3_v1_12484","R",1593,2462826,2464433,2464433,0.825115,0.825115,1,2462826,2464418,2462826,2464418]
["CLOSTRIBL3_v1_12496","R",1491,2474179,2475669,2475669,0.882888,0.882888,2,2474179,2475669,2474179,2475669]
["CLOSTRIBL3_v1_12732","R",873,2707975,2708847,2708847,0.948695,0.948695,1,2707975,2708847,2707975,2708847]

{"sheet":"gene features","index":2,"n_rows":70,"n_cols":8,"rows_kept":70}
["CDS","GC Content","GC1 Content","GC2 Content","GC3 Content","CAI","GCskew","R/Y ratio"]
["CLOSTRIBL3_v1_11086",33.18,43.4,32.78,23.35,0.66,-0.218,1.396]
["CLOSTRIBL3_v1_11116",36.71,47.76,35.29,27.06,0.67,-0.141,1.392]
["CLOSTRIBL3_v1_11117",39.75,47.94,42.44,28.88,0.66,-0.094,1.052]
["CLOSTRIBL3_v1_30024",39.61,48.94,35.76,34.12,0.62,-0.156,1.339]
["CLOSTRIBL3_v1_10010",35.66,39.76,34.7,32.53,0.61,-0.058,1.173]
["CLOSTRIBL3_v1_10012",39.15,47.04,38.94,31.46,0.64,-0.188,1.287]
["CLOSTRIBL3_v1_12309",37.82,50.7,37.82,24.93,0.7,-0.279,1.462]
["CLOSTRIBL3_v1_12417",39.24,47.62,37.9,32.2,0.67,-0.22,1.337]
["CLOSTRIBL3_v1_12774",36.99,46.77,40.32,23.87,0.76,-0.168,1.331]
["CLOSTRIBL3_v1_12775",38.86,53.06,37.5,26.02,0.68,-0.234,1.445]
["CLOSTRIBL3_v1_12776",35.69,36.36,41.41,29.29,0.7,-0.264,1.434]
["CLOSTRIBL3_v1_12777",35.22,43.81,35.05,26.8,0.7,-0.2,1.435]
["CLOSTRIBL3_v1_10343",39.78,52.01,39.61,27.72,0.71,-0.146,1.343]
["CLOSTRIBL3_v1_20129",37.94,47.99,39.03,26.81,0.71,-0.22,1.347]
["CLOSTRIBL3_v1_12838",39.69,52.42,41.48,25.19,0.73,-0.299,1.503]
["CLOSTRIBL3_v1_13111",40.14,51.53,43.88,25,0.66,-0.229,1.435]
["CLOSTRIBL3_v1_11283",43.58,59.75,41,30,0.67,-0.312,1.419]
["CLOSTRIBL3_v1_11276",34.72,43.91,36.22,24.04,0.71,-0.225,1.317]
["CLOSTRIBL3_v1_13113",37.95,48.44,32.18,33.22,0.62,-0.24,1.337]
["CLOSTRIBL3_v1_20313",37.22,49.47,37.81,24.38,0.76,-0.298,1.447]
["CLOSTRIBL3_v1_13112",36.59,46.88,34.38,28.52,0.69,-0.366,1.667]
["CLOSTRIBL3_v1_11087",31.5,45.1,34.9,14.51,0.76,-0.286,1.368]
["CLOSTRIBL3_v1_20109",32.61,42.45,33.09,22.3,0.74,-0.235,1.317]
["CLOSTRIBL3_v1_20308",36.28,49.62,38.46,20.77,0.75,-0.336,1.566]
["CLOSTRIBL3_v1_12502",40.15,54.25,38.99,27.2,0.65,-0.219,1.318]
["CLOSTRIBL3_v1_11587",35.96,47.37,38.68,21.84,0.73,-0.303,1.533]
["CLOSTRIBL3_v1_12012",36.66,47.77,36.48,25.72,0.69,-0.231,1.254]
["CLOSTRIBL3_v1_12013",38.22,48.84,36.76,29.05,0.68,-0.287,1.382]
["CLOSTRIBL3_v1_20310",38.86,52.89,38.95,24.74,0.74,-0.282,1.462]
["CLOSTRIBL3_v1_20311",37.82,55.38,36.15,21.92,0.76,-0.22,1.5]
["CLOSTRIBL3_v1_20312",39.52,55.99,37.13,25.45,0.71,-0.293,1.53]
["CLOSTRIBL3_v1_11710",36.58,49.58,34.54,25.63,0.7,-0.32,1.552]
["CLOSTRIBL3_v1_11711",35.54,47.35,31.46,27.81,0.67,-0.23,1.416]
["CLOSTRIBL3_v1_12016",33.22,48.17,31.23,20.27,0.74,-0.26,1.72]
["CLOSTRIBL3_v1_12308",35.67,52.51,33.11,21.4,0.76,-0.287,1.506]
["CLOSTRIBL3_v1_20086",37.48,50.83,35.64,25.97,0.68,-0.263,1.457]
["CLOSTRIBL3_v1_20087",34.82,45.13,34.82,24.51,0.72,-0.387,1.516]
["CLOSTRIBL3_v1_13110",35.76,47.68,34,25.61,0.69,-0.206,1.323]
["CLOSTRIBL3_v1_11114",36.46,51.11,33.33,24.94,0.72,-0.251,1.505]
["CLOSTRIBL3_v1_11115",38.78,52.09,33.84,30.42,0.71,-0.209,1.545]
["CLOSTRIBL3_v1_11486",41.03,51.27,34.75,37.08,0.62,-0.246,1.454]
["CLOSTRIBL3_v1_11487",38.7,53.8,31.91,30.4,0.66,-0.267,1.551]
["CLOSTRIBL3_v1_11488",39.22,49.62,36.47,31.58,0.64,-0.336,1.642]
["CLOSTRIBL3_v1_12010",38.67,51.93,39.76,24.33,0.69,-0.325,1.43]
["CLOSTRIBL3_v1_12011",38.02,48.29,37.26,28.52,0.63,-0.253,1.362]
["CLOSTRIBL3_v1_20124",35.96,51.5,36.47,19.92,0.74,-0.303,1.486]
["CLOSTRIBL3_v1_20125",35.03,47.01,36.53,21.56,0.73,-0.202,1.369]
["CLOSTRIBL3_v1_10629",38.28,51.97,39.08,23.8,0.7,-0.247,1.419]
["CLOSTRIBL3_v1_10630",39.96,48.49,43.98,27.41,0.67,-0.176,1.028]
["CLOSTRIBL3_v1_10631",36.02,46.24,37.63,24.19,0.72,-0.234,1.447]
["CLOSTRIBL3_v1_10632",38.18,53.99,34.74,25.82,0.7,-0.147,1.022]
["CLOSTRIBL3_v1_10633",34.71,45.88,35.05,23.2,0.74,-0.168,0.902]
["CLOSTRIBL3_v1_10634",42.82,53.82,45.49,29.17,0.68,-0.286,1.316]
["CLOSTRIBL3_v1_10096",38.45,45.5,38.62,31.22,0.67,-0.349,1.554]
["CLOSTRIBL3_v1_10095",39.6,50.54,37.36,30.89,0.69,-0.291,1.407]
["CLOSTRIBL3_v1_10094",42.11,52.69,44.09,29.57,0.65,-0.37,1.571]
["CLOSTRIBL3_v1_10091",37.2,46.95,35.98,28.66,0.64,-0.202,1.388]
["CLOSTRIBL3_v1_10092",40.17,49.17,39.5,31.83,0.65,-0.35,1.539]
["CLOSTRIBL3_v1_10093",38.62,44.44,40.48,30.95,0.67,-0.253,1.454]
["CLOSTRIBL3_v1_13020",33.41,41.11,33.11,26,0.67,-0.135,1.324]
["CLOSTRIBL3_v1_20317",35.41,43.46,39.84,22.94,0.77,-0.318,1.444]
["CLOSTRIBL3_v1_12009",35.41,45.81,32.98,27.45,0.65,-0.346,1.367]
["CLOSTRIBL3_v1_10745",38.25,52.71,37.95,24.1,0.72,-0.254,1.534]
["CLOSTRIBL3_v1_10746",37.42,50,35.75,26.5,0.71,-0.274,1.391]
["CLOSTRIBL3_v1_11881",36.17,46.65,35.05,26.8,0.66,-0.173,1.323]
["CLOSTRIBL3_v1_20137",34.64,44.65,33.68,25.59,0.72,-0.166,1.298]
["CLOSTRIBL3_v1_12484",38.42,47.46,42.94,24.86,0.67,-0.173,1.213]
["CLOSTRIBL3_v1_12496",40.44,49.9,38.43,33,0.62,-0.201,1.28]
["CLOSTRIBL3_v1_12732",38.72,52.23,37.11,26.8,0.67,-0.219,1.445]

{"sheet":"protein features","index":3,"n_rows":70,"n_cols":14,"rows_kept":70}
["CDS","Mw (Da)","Hydrophobicity","Tiny","Small","Aliphatic","Aromatic","Non Polar","Polar","Charged","Basic","Acidic","pI","Oxyphobic Index"]
["CLOSTRIBL3_v1_11086",46934.21,-0.1,26,48.94,27.19,10.4,54.37,45.63,26.95,14.89,12.06,8.72,8.68]
["CLOSTRIBL3_v1_11116",46236.72,-0.07,28.77,48.58,25.47,7.78,54.01,45.99,27.59,15.09,12.5,7.15,8.64]
["CLOSTRIBL3_v1_11117",53204.88,1.1,36.22,53.94,33.27,10.24,72.83,27.17,9.65,6.5,3.15,9.57,8.02]
["CLOSTRIBL3_v1_30024",46907.52,-0.14,26.18,49.53,25.24,8.02,53.54,46.46,28.77,16.27,12.5,8.85,8.97]
["CLOSTRIBL3_v1_10010",47619.64,-0.37,25.36,45.41,21.74,15.46,53.38,46.62,25.36,14.49,10.87,8.75,9.07]
["CLOSTRIBL3_v1_10012",34973.78,-0.11,30.94,53.44,24.06,8.75,54.06,45.94,26.56,13.75,12.81,6.03,9.08]
["CLOSTRIBL3_v1_12309",37918.43,0.12,30.62,54.21,26.97,6.74,60.39,39.61,23.31,12.36,10.96,7.7,9.01]
["CLOSTRIBL3_v1_12417",130662.11,-0.3,28.82,50.3,20.12,11.42,54.65,45.35,26.09,13.56,12.53,6.34,9.41]
["CLOSTRIBL3_v1_12774",34419.19,-0.34,31.39,50.81,19.09,12.3,55.66,44.34,25.24,15.21,10.03,9,9.32]
["CLOSTRIBL3_v1_12775",43193.49,-0.13,28.9,51.15,22.76,11,56.78,43.22,25.58,12.28,13.3,5.3,9.62]
["CLOSTRIBL3_v1_12776",11147.26,-0.42,33.67,52.04,14.29,12.24,53.06,46.94,27.55,12.24,15.31,4.86,10.02]
["CLOSTRIBL3_v1_12777",21452.81,-0.36,25.91,49.22,21.76,9.84,52.85,47.15,27.46,16.06,11.4,9.34,9.01]
["CLOSTRIBL3_v1_10343",127869.54,-0.25,31.42,52.14,19.69,11.04,56.16,43.84,25.34,13.1,12.24,6.15,9.26]
["CLOSTRIBL3_v1_20129",129569.5,-0.31,30.43,50.68,19.4,11.54,54.87,45.13,25.64,13.5,12.14,6.55,9.32]
["CLOSTRIBL3_v1_12838",41639.36,0.01,33.67,54.59,22.96,6.38,58.93,41.07,25.26,13.52,11.73,8.72,9.13]
["CLOSTRIBL3_v1_13111",41754.36,-0.03,34.78,53.96,23.53,6.39,57.8,42.2,23.27,12.53,10.74,8.11,9.39]
["CLOSTRIBL3_v1_11283",42114.34,0.07,34.09,56.64,23.06,8.02,60.65,39.35,24.06,11.03,13.03,5,9.82]
["CLOSTRIBL3_v1_11276",34636.08,-0.04,26.37,46.62,27.01,8.68,56.91,43.09,24.44,13.83,10.61,8.78,8.99]
["CLOSTRIBL3_v1_13113",32129.9,-0.13,26.39,49.65,23.26,11.46,54.51,45.49,28.82,15.62,13.19,7.76,9.04]
["CLOSTRIBL3_v1_20313",30382.26,0.03,30.5,50.35,25.53,6.38,57.8,42.2,28.01,15.25,12.77,8.71,8.67]
["CLOSTRIBL3_v1_13112",28343.86,-0.15,25.1,44.71,23.53,7.06,57.25,42.75,28.24,14.12,14.12,6.7,9.42]
["CLOSTRIBL3_v1_11087",28507.66,-0.09,27.17,50.79,22.83,11.42,58.27,41.73,24.8,12.99,11.81,7.72,10.1]
["CLOSTRIBL3_v1_20109",15445.2,-0.17,26.81,47.83,23.19,13.04,55.8,44.2,27.54,14.49,13.04,6.34,8.97]
["CLOSTRIBL3_v1_20308",27880.07,-0.05,32.05,50.58,22.78,5.79,56.37,43.63,27.03,13.51,13.51,6.68,9.21]
["CLOSTRIBL3_v1_12502",68688.89,-0.19,31.34,50.55,21.1,9.76,58.43,41.57,25.67,13.39,12.28,6.35,9.41]
["CLOSTRIBL3_v1_11587",41823.19,-0.29,30.34,47.49,19.79,9.5,57.26,42.74,24.8,12.14,12.66,5.74,9.97]
["CLOSTRIBL3_v1_12012",41855.54,-0.09,30.26,48.42,21.32,9.74,56.05,43.95,24.74,12.11,12.63,5.54,9.36]
["CLOSTRIBL3_v1_12013",43850.78,-0.31,26.29,46.65,19.59,11.86,56.19,43.81,28.35,15.21,13.14,6.83,10.02]
["CLOSTRIBL3_v1_20310",41192.65,-0.12,32.45,49.08,20.84,9.23,57.26,42.74,25.33,11.87,13.46,5.2,9.35]
["CLOSTRIBL3_v1_20311",28288.41,-0.19,27.41,51.35,25.1,6.56,55.21,44.79,29.34,14.29,15.06,5.45,9.21]
["CLOSTRIBL3_v1_20312",35928.97,-0.04,29.73,51.95,25.53,6.61,58.26,41.74,28.83,14.11,14.71,5.48,9]
["CLOSTRIBL3_v1_11710",39871.34,-0.29,25.98,48.04,23.74,8.38,54.19,45.81,31.56,16.48,15.08,6.47,9.61]
["CLOSTRIBL3_v1_11711",32767.73,-0.07,25.91,51.16,25.91,6.31,55.15,44.85,26.58,14.95,11.63,9.04,8.92]
["CLOSTRIBL3_v1_12016",32905.25,0,25.33,45.33,29,4.67,54.33,45.67,29.33,16,13.33,8.92,8.37]
["CLOSTRIBL3_v1_12308",31689.96,0.29,29.19,52.35,30.87,4.7,58.72,41.28,24.83,14.09,10.74,8.96,8.5]
["CLOSTRIBL3_v1_20086",39421.96,-0.02,27.42,50.14,27.15,6.93,56.23,43.77,25.76,14.13,11.63,8.7,9.22]
["CLOSTRIBL3_v1_20087",39558.24,-0.03,27.1,48.32,26.54,8.94,57.54,42.46,27.1,14.8,12.29,8.58,9.25]
["CLOSTRIBL3_v1_13110",50204.36,-0.26,26.11,50.66,23.89,10.62,53.98,46.02,24.78,13.5,11.28,8.36,8.87]
["CLOSTRIBL3_v1_11114",44484.1,-0.07,25.74,49.26,26.24,7.92,56.68,43.32,28.96,15.84,13.12,8.55,8.96]
["CLOSTRIBL3_v1_11115",29024.38,-0.26,24.81,49.24,24.43,6.11,52.67,47.33,29.77,14.12,15.65,5.22,9.14]
["CLOSTRIBL3_v1_11486",51381.78,-0.18,27.18,50.11,25.48,7.64,55.2,44.8,26.54,12.31,14.23,5.08,9.15]
["CLOSTRIBL3_v1_11487",35988.86,-0.11,25.3,47.26,26.52,8.23,56.1,43.9,28.05,12.8,15.24,5.01,8.78]
["CLOSTRIBL3_v1_11488",28917.19,-0.23,27.92,50.57,25.28,4.91,51.32,48.68,30.57,15.09,15.47,5.78,8.67]
["CLOSTRIBL3_v1_12010",36420.18,-0.12,31.55,52.98,23.21,8.04,56.85,43.15,25,12.5,12.5,5.94,9.27]
["CLOSTRIBL3_v1_12011",28596.96,-0.17,29.01,51.53,27.1,5.34,51.14,48.86,29.01,15.65,13.36,8.59,8.63]
["CLOSTRIBL3_v1_20124",28797.11,-0.08,27.92,53.58,26.04,5.28,54.72,45.28,28.68,13.58,15.09,5.25,8.79]
["CLOSTRIBL3_v1_20125",36417.5,-0.14,28.83,48.65,24.32,7.51,54.05,45.95,26.43,13.51,12.91,6.06,8.82]
["CLOSTRIBL3_v1_10629",49231.93,-0.15,29.32,55.36,23.85,6.35,57.33,42.67,26.26,14.44,11.82,8.64,9.36]
["CLOSTRIBL3_v1_10630",35200.37,0.67,35.35,53.17,27.49,12.08,69.18,30.82,13.9,9.06,4.83,9.44,8.48]
["CLOSTRIBL3_v1_10631",19724.7,-0.18,34.05,60,21.08,7.57,52.43,47.57,22.7,14.05,8.65,9.54,8.64]
["CLOSTRIBL3_v1_10632",22826.74,1.05,27.83,51.89,36.32,9.91,73.11,26.89,11.79,7.55,4.25,9,8.83]
["CLOSTRIBL3_v1_10633",20895.38,1.23,29.53,50.26,36.79,11.92,72.54,27.46,8.29,5.18,3.11,9.04,8.26]
["CLOSTRIBL3_v1_10634",29876.86,0.28,37.98,62.37,23.69,5.23,65.16,34.84,20.56,12.54,8.01,8.63,10.06]
["CLOSTRIBL3_v1_10096",20722.1,-0.22,29.79,56.91,21.28,5.32,53.72,46.28,27.13,14.36,12.77,7.85,10.48]
["CLOSTRIBL3_v1_10095",51922.84,-0.32,26.84,48.05,21,10.17,54.98,45.02,30.09,15.37,14.72,5.97,9.94]
["CLOSTRIBL3_v1_10094",19776.26,-0.08,31.89,60,23.78,2.7,58.38,41.62,27.57,15.68,11.89,8.46,10.45]
["CLOSTRIBL3_v1_10091",18192.55,-0.18,28.22,46.01,23.93,7.98,56.44,43.56,25.77,14.11,11.66,8.52,9.56]
["CLOSTRIBL3_v1_10092",65492.73,-0.24,31.05,52.92,22.04,7.18,55.43,44.57,29.05,14.86,14.19,6.65,9.77]
["CLOSTRIBL3_v1_10093",28128.04,-0.13,29.08,50.2,22.71,7.17,56.18,43.82,30.28,17.93,12.35,8.93,9.95]
["CLOSTRIBL3_v1_13020",49899.15,-0.16,27.62,48.33,21.83,9.35,53.67,46.33,29.18,16.04,13.14,8.51,8.65]
["CLOSTRIBL3_v1_20317",54812.66,-0.23,30.85,52.22,19.56,7.26,54.44,45.56,28.63,16.33,12.3,8.83,9.85]
["CLOSTRIBL3_v1_12009",63525.88,-0.25,23.57,46.79,25.36,10.36,54.11,45.89,28.93,15.18,13.75,7.18,9.49]
["CLOSTRIBL3_v1_10745",35388.38,-0.01,30.82,54.38,25.08,5.14,56.8,43.2,25.68,12.69,12.99,5.68,8.95]
["CLOSTRIBL3_v1_10746",43392.56,-0.01,28.57,52.38,25.31,8.77,57.89,42.11,26.32,14.79,11.53,8.07,9.14]
["CLOSTRIBL3_v1_11881",41885.07,0.05,28.17,50.65,28.42,6.2,55.81,44.19,24.03,12.92,11.11,7.86,8.49]
["CLOSTRIBL3_v1_20137",42163.36,-0.22,27.49,51.57,23.3,9.42,50.79,49.21,27.49,14.14,13.35,5.91,8.87]
["CLOSTRIBL3_v1_12484",56436.02,-0.14,36.6,57.92,20.19,7.55,54.34,45.66,21.89,11.89,10,7.19,9.29]
["CLOSTRIBL3_v1_12496",54446.7,-0.14,30.04,50.2,23.19,8.47,55.04,44.96,25.81,14.11,11.69,7.63,9.35]
["CLOSTRIBL3_v1_12732",31156.14,0.04,28.28,52.76,27.24,5.52,59.31,40.69,23.45,13.45,10,9.13,9.15]

{"sheet":"MaGe-Curated annotations","index":4,"n_rows":1178,"n_cols":26,"rows_kept":1178}
["CLOSTRIBL3_v1_11086","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"SBF1_v1_1830014","_","Desulfosporosinus sp. SbF1","larA_2","putative nickel-dependent lactate racemase LarA","LACTATE-RACEMASE-RXN ; RHEA:10960 ;",0.99766,1.00709,40.85,{"v":3e-117,"d":"3.00E-117"},1,1,"_","5.1.2.1","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,423,423,1,425,427]
[]
["CLOSTRIBL3_v1_11116","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_30024","_","Clostridiaceae BL-3","larA","Lactate racemase","RHEA:10963 ;",0.99764,0.99764,77.54,0,1,1,"_","5.1.2.1","2 : Cytoplasmic","_","e : enzyme",24710389,"1c : Function from experimental evidences in the studied genus",1,423,424,1,423,424]
[null,"CD630_11700",null,"Clostridium difficile 630","_","Conserved hypothetical protein","_",0.99764,0.99764,65.72,0,1,1,"_","_","1 : Unknown","_","u : unknown","_","4 : Unknown function but conserved in other organisms",1,423,424,1,423,424]
[null,"SBF1_v1_1280023","_","Desulfosporosinus sp. SbF1","larA","putative nickel-dependent lactate racemase LarA","LACTATE-RACEMASE-RXN ; RHEA:10960 ;",0.99292,1.00238,35.63,{"v":5e-76,"d":"5.00E-76"},1,1,"_","5.1.2.1","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",4,422,424,3,415,420]
[]
["CLOSTRIBL3_v1_11117","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"ECED1_5018","_","Escherichia coli ED1a","_","L-lactate permease","_",0.97297,0.99213,47.82,{"v":5e-156,"d":"5.00E-156"},1,1,"_","_","1 : Unknown","7 : Transport and binding proteins ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,496,508,4,507,518]
[null,"HELPY_0142",null,"Helicobacter pylori B38","_","Putative L-lactate permease, LctP family; putative membrane protein","_",0.95264,1.02953,38.05,{"v":5E-110,"d":"5.00E-110"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ; 4.2.A.14 : The Lactate Permease (LctP) Family ; 6.1 : Membrane ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","7.3 : Carbohydrates, organic alcohols, and acids ;","t : transporter","11785976, 8407843","3 : Putative function from multiple computational evidences",2,497,508,12,532,549]
[null,"NLA0588","_","Neisseria lactamica ST640","lldP","L-lactate permease","_",0.95795,1.0315,36.45,{"v":2E-107,"d":"2.00E-107"},1,1,"_","_","5 : Inner membrane protein","_","t : transporter","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,497,508,14,530,547]
[null,"HELPY_0143",null,"Helicobacter pylori B38","_","Putative L-lactate permease, LctP family; putative membrane protein","_",0.95644,1.0374,36.24,{"v":1e-103,"d":"1.00E-103"},2,1,"1.1.1 : Carbohydrates/Carbon compounds ; 4.2.A.14 : The Lactate Permease (LctP) Family ; 6.1 : Membrane ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","7.3 : Carbohydrates, organic alcohols, and acids ;","t : transporter","11785976, 8407843","3 : Putative function from multiple computational evidences",2,497,508,13,535,551]
[null,"PP_4735",null,"Pseudomonas putida KT2440","lldP","L-lactate permease","_",0.94065,1.02953,36.9,{"v":3E-103,"d":"3.00E-103"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ; 6.1 : Membrane ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","7.3 : Carbohydrates, organic alcohols, and acids ; 16.1 : Circulate ;","t : transporter","19196979, 22408166, 614007, 11785976","1b : Function from experimental evidences in the studied species",10,497,508,21,541,556]
[null,"EFER_3597","_","Escherichia fergusonii ATCC 35469T","lldP","L-lactate permease","_",0.96007,1.04134,35.16,{"v":7e-103,"d":"7.00E-103"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ; 4.2.A.14 : The Lactate Permease (LctP) Family ; 6.1 : Membrane ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","6 : Energy metabolism ;  7 : Transport and binding proteins ;","t : transporter","11283302, 11785976, 15849754, 16850406, 8407843","1b : Function from experimental evidences in the studied species",2,497,508,13,538,551]
[null,"ECS88_3349","_","Escherichia coli S88","yghK","glycolate transporter","_",0.94464,1.04134,36.86,{"v":2e-102,"d":"2.00E-102"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ; 4.2.A.14 : The Lactate Permease (LctP) Family ; 6.1 : Membrane ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","6 : Energy metabolism ;  7 : Transport and binding proteins ;","t : transporter","11283302, 11785976, 15849754, 16850406, 21178909","1b : Function from experimental evidences in the studied species",9,497,508,20,546,560]
[null,"ECUMN_3450","_","Escherichia coli UMN026","yghK","glycolate transporter","_",0.94464,1.04134,36.86,{"v":2e-102,"d":"2.00E-102"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ; 4.2.A.14 : The Lactate Permease (LctP) Family ; 6.1 : Membrane ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","6 : Energy metabolism ;  7 : Transport and binding proteins ;","t : transporter","11283302, 11785976, 15849754, 16850406, 21178909","1b : Function from experimental evidences in the studied species",9,497,508,20,546,560]
[null,"PSEEN0768",null,"Pseudomonas entomophila L48","lldP","L-lactate permease","_",0.94065,1.02953,36.71,{"v":4e-102,"d":"4.00E-102"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ; 4.2.A.14 : The Lactate Permease (LctP) Family ;","_","Inner membrane protein","7 : Transport and binding proteins ;","t : transporter","_","2a : Function from experimental evidences in other organisms",10,497,508,21,541,556]
[null,"BN874v1_1160014",null,"Candidatus Contendobacter odensis Run_B_J11","_","putative lactate permease","_",0.95722,1.05709,35.01,{"v":5e-102,"d":"5.00E-102"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ; 4.2.A.14 : The Lactate Permease (LctP) Family ; 6.1 : Membrane ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","6 : Energy metabolism ; 7 : Transport and binding proteins ;","t : transporter",11785976,"3 : Putative function from multiple computational evidences",2,499,508,14,543,561]
[null,"BN873v1_890142",null,"Candidatus Competibacter denitrificans Run_A_D11","_","putative lactate permease","_",0.95365,1.05315,35.14,{"v":7e-101,"d":"7.00E-101"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ; 4.2.A.14 : The Lactate Permease (LctP) Family ; 6.1 : Membrane ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","6 : Energy metabolism ; 7 : Transport and binding proteins ;","t : transporter",11785976,"3 : Putative function from multiple computational evidences",2,499,508,14,543,561]
[null,"Rmet_5896","_","Cupriavidus metallidurans CH34","_","glycolate transporter","_",0.9576,1.06693,35.79,{"v":7e-101,"d":"7.00E-101"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ; 4.2.A.14 : The Lactate Permease (LctP) Family ; 6.1 : Membrane ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","_","t : transporter","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,497,508,13,552,566]
[null,"SBF1_v1_320002",null,"Desulfosporosinus sp. SbF1","lutP","D-lactate, L-lactate, and/or glycolate permease","_",0.93309,1.01575,36.63,{"v":2e-98,"d":"2.00E-98"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ; 4.2.A.14 : The Lactate Permease (LctP) Family ; 6.1 : Membrane ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","6 : Energy metabolism ; 7 : Transport and binding proteins ;","t : transporter","11283302, 11785976, 21178909","2a : Function from experimental evidences in other organisms",12,499,508,23,535,553]
[null,"BSU34190",null,"Bacillus subtilis 168","lutP","L-lactate permease","_",0.9627,1.06693,35.42,{"v":2e-97,"d":"2.00E-97"},1,1,"1.2 : Transport/binding proteins and lipoproteins ;","_","5 : Inner membrane protein","16.1 : Circulate ;","t : transporter",25031425,"1b : Function from experimental evidences in the studied species",2,499,508,13,552,563]
[]
["CLOSTRIBL3_v1_30024","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_11116","_","Clostridiaceae BL-3","larA","Lactate racemase","LACTATE-RACEMASE-RXN ; RHEA:10960 ;",0.99764,0.99764,77.54,0,1,1,"4.S.107 : L-lactate ;","5.1.2.1","2 : Cytoplasmic","_","e : enzyme",24710389,"1c : Function from experimental evidences in the studied genus",1,423,424,1,423,424]
[]
["CLOSTRIBL3_v1_10012","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"BSU03050","_","Bacillus subtilis 168","lctE","L-lactate dehydrogenase","L-LACTATE-DEHYDROGENASE-RXN ; RHEA:23444 ;",0.96262,0.96562,35.92,{"v":4e-68,"d":"4.00E-68"},1,1,"_","1.1.1.27","2 : Cytoplasmic","16.10 : Respire ;","e : enzyme","10809684, 16207915, 19383131","1a : Function from experimental evidences in the studied strain",6,311,320,7,312,321]
[]
["CLOSTRIBL3_v1_12309","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_12630","_","Clostridium difficile 630","_","Putative FMN-dependent dehydrogenase","_",0.94663,0.99704,68.55,{"v":1E-173,"d":"1.00E-173"},1,1,"1.4.1 : Electron donor ;","_","1 : Unknown","6.5 : Electron transport ;","e : enzyme",18367206,"3 : Putative function from multiple computational evidences",18,354,356,1,337,338]
[null,"LEPBIa1341","_","Leptospira biflexa serovar Patoc Patoc 1","_","Putative oxidase or carboxylase","_",0.42667,0.89888,41.88,{"v":2E-78,"d":"2.00E-78"},1,1,"_","1.1.3.15, 4.1.1.21","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",35,353,356,425,744,750]
[]
["CLOSTRIBL3_v1_12417","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"SBF1_v1_1620011",null,"Desulfosporosinus sp. SbF1","pfoA_2","pyruvate synthase","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.9983,0.99915,67.83,0,1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,1172,1173,1,1172,1174]
[null,"BN874v1_1210009","_","Candidatus Contendobacter odensis Run_B_J11","_","putative pyruvate-flavodoxin oxidoreductase (nifJ)","_",0.99246,1.01023,47.43,0,1,1,"_","1.2.7.-","1 : Unknown","5 : Central intermediary metabolism ; 5.6 : Nitrogen fixation ;","e : enzyme","11167002, 21317262, 8415612","3 : Putative function from multiple computational evidences",3,1170,1173,4,1181,1194]
[null,"Ent638_2136","_","Enterobacter sp. 638","ydbK","Putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; 4Fe-4S cluster binding protein","_",1.01618,1.01705,47.44,0,1,1,"1.7.1 : Unassigned reversible reactions ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,1170,1173,1,1165,1174]
[null,"Spro_2604","_","Serratia proteamaculans 568","_","Putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; 4Fe-4S cluster binding protein (NifJ)","_",1.00425,1.00767,46.79,0,1,1,"1.7.1 : Unassigned reversible reactions ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 5 : Central intermediary metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,1170,1173,1,1168,1177]
[null,"ECK1374","_","Escherichia coli K12","ydbK","putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; 4Fe-4S cluster binding protein","PYRUFLAVREDUCT-RXN ;",1.01022,1.01108,47.13,0,1,1,"1.7.1 : Unassigned reversible reactions ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 5 : Central intermediary metabolism ;","e : enzyme",9025293,"3 : Putative function from multiple computational evidences",5,1170,1173,1,1165,1174]
[null,"BN11v3_340013","_","Tetrasphaera australiensis Ben110","_","putative pyruvate-flavodoxin oxidoreductase","_",0.9891,1.00597,46.36,0,1,1,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",8352652,"3 : Putative function from multiple computational evidences",7,1170,1173,8,1178,1193]
[null,"BN873v1_150048","_","Candidatus Competibacter denitrificans Run_A_D11","_","putative pyruvate-flavodoxin oxidoreductase (nifJ)","_",0.99413,1.01108,46.12,0,1,1,"_","1.2.7.-","1 : Unknown","5 : Central intermediary metabolism ; 5.6 : Nitrogen fixation ;","e : enzyme","11167002, 21317262, 8415612","3 : Putative function from multiple computational evidences",3,1170,1173,4,1181,1193]
[null,"FRAAL3253","_","Frankia alni ACN14a","_","Pyruvate-flavodoxin oxidoreductase","_",1.00085,1.00256,45.58,0,1,1,"1.7.1 : Unassigned reversible reactions ;","1.2.7.-","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,1167,1173,4,1160,1175]
[null,"SBF1_v1_1030024",null,"Desulfosporosinus sp. SbF1","pfoA_3a","fragment of pyruvate synthase (part 1/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.58483,0.97305,68.08,0,3,1,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",5,685,1173,4,689,705]
[null,"VCA0530","_","Vibrio cholerae N16961","_","putative Pyruvate-flavodoxin oxidoreductase","_",0.948,1.03058,38.94,0,1,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",9,1102,1173,6,1072,1079]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.39045,0.97447,67.69,0,2,2,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"2a : Function from experimental evidences in other organisms",1,458,1173,1,458,470]
[null,"SBF1_v1_1030023",null,"Desulfosporosinus sp. SbF1","pfoA_3b","fragment of pyruvate synthase (part 2/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.39386,0.98929,61.04,0,4,2,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",709,1170,1173,1,461,467]
[]
["CLOSTRIBL3_v1_12774","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"NBG4_v1_970001",null,"Candidatus Sulfobium mesophilum","porB","Pyruvate synthase subunit PorB","PYRUFLAVREDUCT-RXN ; RHEA:12765 ;",0.93851,0.98976,62.76,{"v":3e-135,"d":"3.00E-135"},1,1,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","11265457, 8620891","2a : Function from experimental evidences in other organisms",3,292,309,5,292,293]
[null,"HELPY_1081",null,"Helicobacter pylori B38","porB","Pyruvate synthase subunit porB (Pyruvate oxidoreductase beta chain) (POR) (Pyruvic-ferredoxin oxidoreductase subunit beta)","_",0.96815,0.98382,43.42,{"v":4e-98,"d":"4.00E-98"},1,1,"_","1.2.7.1","2 : Cytoplasmic","6.11 : TCA cycle ;","e : enzyme","7608066, 9495749","1a : Function from experimental evidences in the studied strain",5,306,309,8,309,314]
[null,"MGMSRv2_1069",null,"Magnetospirillum gryphiswaldense MSR-1 v2","porB","Pyruvate synthase subunit porB","_",0.81651,0.86408,49.06,{"v":7e-82,"d":"7.00E-82"},1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme",8688087,"2a : Function from experimental evidences in other organisms",15,281,309,18,276,327]
[null,"NIDE3873",null,"Candidatus Nitrospira defluvii","vorB","2-ketoisovalerate ferredoxin reductase, beta subunit","_",0.95833,0.96764,41.14,{"v":7e-63,"d":"7.00E-63"},1,1,"1.1.3.12 : Leucine degradation ; 1.1.3.14 : Valine degradation ;","1.2.7.7","1 : Unknown","6.2 : Amino acids and amines ;","e : enzyme","16472741, 8305426, 8380721, 8550425, 8620891","2b : Function from indirect experimental evidences (e.g. phenotypes)",13,306,309,17,310,312]
[null,"SCFA_v1_3810002",null,"Ca. Propionivorax syntrophicum F70","porB","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit","_",0.93569,0.94175,37.11,{"v":1E-59,"d":"1.00E-59"},1,2,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",17,306,309,17,293,311]
[]
["CLOSTRIBL3_v1_12775","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"NBG4_v1_970002",null,"Candidatus Sulfobium mesophilum","porA","Pyruvate synthase subunit PorA","PYRUFLAVREDUCT-RXN ; RHEA:12768 ;",1.00255,1.00512,55.22,{"v":1E-146,"d":"1.00E-146"},1,1,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","11265457, 8305426, 8620891","2a : Function from experimental evidences in other organisms",1,391,391,1,392,392]
[null,"HELPY_1079",null,"Helicobacter pylori B38","porA","Pyruvate synthase subunit porA (Pyruvate oxidoreductase alpha chain) (POR) (Pyruvic-ferredoxin oxidoreductase subunit alpha)","_",0.95086,0.98977,45.74,{"v":6e-111,"d":"6.00E-111"},1,1,"1.7.28 : Pyruvate catabolism ;","1.2.7.1","1 : Unknown","6.11 : TCA cycle ;","e : enzyme","7608066, 9495749","1a : Function from experimental evidences in the studied strain",9,390,391,15,400,407]
[null,"MGMSRv2_1070",null,"Magnetospirillum gryphiswaldense MSR-1 v2","porA","Pyruvate synthase subunit porA","_",0.91816,0.92765,39,{"v":5E-80,"d":"5.00E-80"},1,1,"_","1.2.7.1","1 : Unknown","_","e : enzyme","16980466, 8620891","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,363,391,4,358,387]
[null,"NIDE3874",null,"Candidatus Nitrospira defluvii","vorA","2-ketoisovalerate ferredoxin reductase, alpha subunit","_",0.9199,0.96931,37.99,{"v":3E-79,"d":"3.00E-79"},1,1,"1.1.3.12 : Leucine degradation ; 1.1.3.14 : Valine degradation ;","1.2.7.7","1 : Unknown","6.2 : Amino acids and amines ;","e : enzyme","10048931, 11752578, 16472741, 8305426, 8380721, 8550425, 8620891","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,380,391,6,381,412]
[null,"SCFA_v1_3810001",null,"Ca. Propionivorax syntrophicum F70","porA","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit","PYRUFLAVREDUCT-RXN ; RHEA:12765 ; RHEA:32135 ;",0.98721,1,37.31,{"v":7e-70,"d":"7.00E-70"},1,1,"_","1.2.7.1","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,383,391,2,380,386]
[]
["CLOSTRIBL3_v1_12776","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"NBG4_v1_970003",null,"Candidatus Sulfobium mesophilum","porD","Pyruvate synthase subunit PorD","PYRUFLAVREDUCT-RXN ; RHEA:12768 ;",0.91837,0.92784,43.33,{"v":5e-29,"d":"5.00E-29"},1,1,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","11265457, 8620891","2a : Function from experimental evidences in other organisms",13,98,98,6,95,97]
[]
["CLOSTRIBL3_v1_12777","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"NBG4_v1_970004",null,"Candidatus Sulfobium mesophilum","porC","Pyruvate synthase subunit PorC","PYRUFLAVREDUCT-RXN ; RHEA:12765 ;",0.97927,0.98953,43.92,{"v":1E-53,"d":"1.00E-53"},1,1,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","11265457, 8620891","2a : Function from experimental evidences in other organisms",5,192,193,4,190,191]
[null,"HELPY_1077",null,"Helicobacter pylori B38","porG","Pyruvate synthase subunit porC (Pyruvate oxidoreductase gamma chain) (POR) (Pyruvic-ferredoxin oxidoreductase subunit gamma)","_",0.98446,1.02151,38.42,{"v":4e-37,"d":"4.00E-37"},1,1,"_","1.2.7.1","1 : Unknown","6.11 : TCA cycle ;","e : enzyme","7608066, 9495749","1a : Function from experimental evidences in the studied strain",5,191,193,1,186,186]
[]
["CLOSTRIBL3_v1_10343","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_20129","_","Clostridiaceae BL-3","pfo","Pyruvate-flavodoxin oxidoreductase","PYRUFLAVREDUCT-RXN ; RHEA:12765 ;",0.99658,0.99829,67.58,0,1,1,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","8620891, 7608066, 9495749","1c : Function from experimental evidences in the studied genus",3,1165,1168,7,1169,1170]
[null,"CD630_26820","_","Clostridium difficile 630","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.99661,1.00599,67.06,0,1,1,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"1c : Function from experimental evidences in the studied genus",4,1165,1168,5,1178,1179]
[null,"CLOAM0324",null,"Candidatus Cloacamonas acidaminovorans Evry","_","putative pyruvate-ferredoxin oxidoreductase (por-like) or pyruvate-flavodoxin oxidoreductase (ydbK-like), 4Fe-4S domain","_",0.99915,1.00342,55.38,0,1,1,"1.7.1 : Unassigned reversible reactions ; 1.1.2.3 : Propionate degradation ; 1.3.5 : Fermentation ;","1.2.7.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",6,1165,1168,8,1171,1173]
[null,"AZOLI_p30297","_","Azospirillum lipoferum 4B","_","putative pyruvate-ferredoxin/flavodoxin oxidoreductase","_",1.00768,1.01113,47.76,0,1,1,"1.7.1 : Unassigned reversible reactions ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 5 : Central intermediary metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",7,1163,1168,1,1172,1172]
[null,"SBF1_v1_1030024",null,"Desulfosporosinus sp. SbF1","pfoA_3a","fragment of pyruvate synthase (part 1/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.59418,0.9844,67.44,0,3,2,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",1,689,1168,1,694,705]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.3887,0.96596,72.47,0,2,1,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"2a : Function from experimental evidences in other organisms",4,457,1168,5,458,470]
[null,"SBF1_v1_1030023",null,"Desulfosporosinus sp. SbF1","pfoA_3b","fragment of pyruvate synthase (part 2/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.39384,0.98501,63.04,0,4,1,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",710,1166,1168,3,462,467]
[null,"NBG4_v1_230036","_","Candidatus Sulfobium mesophilum","nifJ","Pyruvate:ferredoxin oxidoreductase","PYRUFLAVREDUCT-RXN ;",0.22945,0.98529,58.21,{"v":3e-100,"d":"3.00E-100"},1,1,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","1 : Unknown","6 : Energy metabolism ;","e : enzyme",11167002,"2a : Function from experimental evidences in other organisms",3,270,1168,4,271,272]
[]
["CLOSTRIBL3_v1_20129","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_10343","_","Clostridiaceae BL-3","pfo","Pyruvate-flavodoxin oxidoreductase","PYFLAVOXRE-RXN ; RHEA:12765 ;",0.99658,0.99829,67.58,0,1,1,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","8620891, 7608066, 9495749","1c : Function from experimental evidences in the studied genus",7,1169,1170,3,1165,1168]
[null,"SBF1_v1_1030024",null,"Desulfosporosinus sp. SbF1","pfoA_3a","fragment of pyruvate synthase (part 1/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.58718,0.97447,63.17,0,3,3,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",7,688,1170,3,689,705]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.38718,0.96383,67.11,0,2,3,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"2a : Function from experimental evidences in other organisms",9,461,1170,6,458,470]
[null,"SBF1_v1_1030023",null,"Desulfosporosinus sp. SbF1","pfoA_3b","fragment of pyruvate synthase (part 2/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.39487,0.98929,59.96,0,4,3,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",712,1169,1170,1,461,467]
[]
["CLOSTRIBL3_v1_12838","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_10590","_","Clostridium difficile 630","thlA1","Acetoacetyl-CoA thiolase 1","_",1,1.00256,69.9,0,1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","11075929, 2191949","1c : Function from experimental evidences in the studied genus",1,392,392,1,391,391]
[null,"PSEEN4635","_","Pseudomonas entomophila L48","phbA","acetyl-CoA acetyltransferase","_",0.96314,1,63.27,{"v":7E-176,"d":"7.00E-176"},1,1,"5.6.2 : Detoxification (xenobiotic metabolism) ;","2.3.1.9","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,392,392,15,406,407]
[null,"AZOLI_2388","_","Azospirillum lipoferum 4B","phbA3","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",1,1.00256,65.31,{"v":1E-174,"d":"1.00E-174"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.9","2 : Cytoplasmic","3.1 : Biosynthesis ;","e : enzyme","7582015, 12788722, 12039753","1c : Function from experimental evidences in the studied genus",1,392,392,1,390,391]
[null,"RALTA_A1351","_","Cupriavidus taiwanensis LMG19424","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.99746,1,64.03,{"v":2E-174,"d":"2.00E-174"},1,1,"1.6 : Macromolecules (cellular constituent) biosynthesis ;","2.3.1.9","1 : Unknown","_","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",1,392,392,1,392,393]
[null,"CMR15v5_2547","_","Ralstonia solanacearum CMR15","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.99746,1,64.03,{"v":2e-172,"d":"2.00E-172"},1,1,"1.6 : Macromolecules (cellular constituent) biosynthesis ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",1,392,392,1,392,393]
[null,"BN874v1_850028","_","Candidatus Contendobacter odensis Run_B_J11","phaA","Acetyl-CoA acetyltransferase","_",0.99746,1,62.24,{"v":2E-171,"d":"2.00E-171"},1,1,"1.3 : Energy metabolism (carbon) ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ; 6 : Energy metabolism ; 16.14 : Store ;","e : enzyme","1685080, 1755959, 7867955, 9904","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,392,1,392,393]
[null,"Rmet_1357",null,"Cupriavidus metallidurans CH34","phaA","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.99746,1,62.5,{"v":2E-171,"d":"2.00E-171"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,392,1,392,393]
[null,"BN873v1_100077","_","Candidatus Competibacter denitrificans Run_A_D11","phaA","Acetyl-CoA acetyltransferase","_",0.99746,1,61.48,{"v":5e-170,"d":"5.00E-170"},1,1,"_","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ; 6 : Energy metabolism ; 16.14 : Store ;","e : enzyme","1685080, 1755959, 7867955, 9904","2a : Function from experimental evidences in other organisms",1,392,392,1,392,393]
[null,"THI_1641","_","Thiomonas sp. 3As","phbA1","acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",1,1,62.24,{"v":2E-169,"d":"2.00E-169"},1,1,"1.3 : Energy metabolism (carbon) ;","2.3.1.9","2 : Cytoplasmic","15 : Cellular processes ; 6 : Energy metabolism ;","e : enzyme","2670935, 2670936","2a : Function from experimental evidences in other organisms",1,392,392,1,392,392]
[null,"BRADO0562","_","Bradyrhizobium sp. ORS278","phbA","acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98985,0.9949,62.31,{"v":2E-167,"d":"2.00E-167"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.9","1 : Unknown","16.2 : Construct biomass (Anabolism) ;","e : enzyme",7582015,"2b : Function from indirect experimental evidences (e.g. phenotypes)",3,392,392,6,393,394]
[null,"PP_4636","_","Pseudomonas putida KT2440","yqeF","acetyl-CoA acetyltransferase","METHYLACETOACETYLCOATHIOL-RXN ; RXN-12561 ; ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",1,1,60.71,{"v":6e-167,"d":"6.00E-167"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","4150713, 773366, 236278, 9904, 2883931","2a : Function from experimental evidences in other organisms",1,392,392,1,392,392]
[null,"METDI4272","_","Methylobacterium extorquens DM4","phaA","beta-ketothiolase","_",0.98985,0.9949,62.05,{"v":4e-166,"d":"4.00E-166"},1,1,"1.1 : Carbon compound utilization ; 1.7.37 : C1 assimilation, serine pathway ;","2.3.1.16","2 : Cytoplasmic","_","e : enzyme",11208803,"1b : Function from experimental evidences in the studied species",3,392,392,6,393,394]
[null,"MARHY3102","_","Marinobacter hydrocarbonoclasticus ATCC 49840","phbA","acetyl-CoA acetyltransferase with thiolase domain, PHB biosynthesis","_",1,1,59.44,{"v":1E-165,"d":"1.00E-165"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",1396692,"2a : Function from experimental evidences in other organisms",1,392,392,1,392,392]
[null,"HEAR0577","_","Herminiimonas arsenicoxydans","phbA","acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.98246,1,56.89,{"v":2e-164,"d":"2.00E-164"},1,1,"1.3 : Energy metabolism (carbon) ; 7.1 : Cytoplasm ;","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","1396692, 2670935","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,392,9,399,399]
[null,"NT26v4_3604","_","Rhizobium sp. NT-26","phbA","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98728,0.9898,60.05,{"v":2E-160,"d":"2.00E-160"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 1.3 : Energy metabolism (carbon) ; 7.1 : Cytoplasm ;","2.3.1.9","1 : Unknown","16.2 : Construct biomass (Anabolism) ; 6 : Energy metabolism ;","e : enzyme",7582015,"2b : Function from indirect experimental evidences (e.g. phenotypes)",4,391,392,6,391,393]
[null,"RM41v1_110012","_","Sinorhizobium sp. Rm41","phbA","acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98982,0.99235,59.38,{"v":7E-159,"d":"7.00E-159"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 1.7 : Central intermediary metabolism ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ; 16.2 : Construct biomass (Anabolism) ;","e : enzyme",7582015,"1b : Function from experimental evidences in the studied species",4,392,392,6,392,393]
[null,"MGMSRv2_1838","_","Magnetospirillum gryphiswaldense MSR-1 v2","phbA","acetyl-CoA acetyltransferase containing thiolase domain (Acetoacetyl-CoA thiolase)","_",1,1.00513,58.93,{"v":2e-157,"d":"2.00E-157"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 1.7 : Central intermediary metabolism ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,392,1,390,390]
[null,"Spro_0592","_","Serratia proteamaculans 568","atoB","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.98005,1.00255,56.23,{"v":3E-153,"d":"3.00E-153"},1,1,"1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,392,9,400,401]
[null,"HELPY_0683","_","Helicobacter pylori B38","atoB","Acetyl coenzyme A acetyltransferase","_",1,1.00256,54.34,{"v":4e-146,"d":"4.00E-146"},1,1,"1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.1 : General ;","e : enzyme",3025185,"2a : Function from experimental evidences in other organisms",1,392,392,1,390,391]
[null,"NBG4_v1_200004","_","Candidatus Sulfobium mesophilum","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.98734,0.9949,53.08,{"v":2e-145,"d":"2.00E-145"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.9","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",23468890,"2a : Function from experimental evidences in other organisms",3,392,392,10,395,395]
[null,"VIBNIv4_B1306","_","Vibrio nigripulchritudo SFn1","phbA","acetyl-CoA acetyltransferase","_",1,1.02296,52.62,{"v":4e-144,"d":"4.00E-144"},1,1,"1.1.2.7 : Acetoacetate degradation ; 7.1 : Cytoplasm ; 1.3 : Energy metabolism (carbon) ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ; 6 : Energy metabolism ;","e : enzyme","2670935, 16964242, 2670936","2a : Function from experimental evidences in other organisms",1,392,392,1,400,401]
[null,"Rmet_1362",null,"Cupriavidus metallidurans CH34","bktB","acetyl-CoA acetyltransferase","_",0.99746,1.00255,54.2,{"v":3e-142,"d":"3.00E-142"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,392,392,3,393,394]
[null,"BTCD_v1_1714","_","Brochothrix thermosphacta CD337","mevB","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",1,1.01031,56.12,{"v":3e-141,"d":"3.00E-141"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme",7763384,"2a : Function from experimental evidences in other organisms",1,392,392,1,387,388]
[null,"RPSI07_1730",null,"Ralstonia solanacearum PSI07","phaA","acetyl-CoA acetyltransferase, thiolase-like","_",0.99746,1.00255,52.93,{"v":2E-140,"d":"2.00E-140"},2,1,"1.7 : Central intermediary metabolism ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,392,392,3,393,394]
[null,"BN424_3179","_","Carnobacterium maltaromaticum LMA28 v1","thlA","Acetoacetyl-CoA thiolase","METHYLACETOACETYLCOATHIOL-RXN ; RXN-12561 ; ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",1,1.00771,52.3,{"v":2e-138,"d":"2.00E-138"},1,1,"_","2.3.1.9","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,392,1,388,389]
[null,"AZOLI_p10676","_","Azospirillum lipoferum 4B","phbA2","Acetyl-CoA acetyltransferase with thiolase domain (Beta-ketothiolase)","_",0.99491,0.99745,51.92,{"v":7e-137,"d":"7.00E-137"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.9","1 : Unknown","3.1 : Biosynthesis ; 3 : Fatty acid and phospholipid metabolism ;","e : enzyme","12534463, 9851987","2a : Function from experimental evidences in other organisms",3,392,392,4,392,393]
[null,"VS_II0585","_","Vibrio tasmaniensis LGP32","_","Acetyl-CoA C acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99256,1.02041,49.5,{"v":4e-133,"d":"4.00E-133"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ; 6.7 : Fermentation ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,391,392,1,399,403]
[null,"BSU24170","_","Bacillus subtilis 168","mmgA","degradative acetoacetyl-CoA thiolase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99491,0.99745,50.64,{"v":2e-129,"d":"2.00E-129"},1,1,"2.4 : Metabolism of lipids ;","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","16352833, 18246303, 19016856, 28956599","1a : Function from experimental evidences in the studied strain",1,391,392,1,391,393]
[null,"NIDE3116","_","Candidatus Nitrospira defluvii","atoB","Acetyl-CoA acetyltransferase","_",0.98477,0.9898,50,{"v":6e-128,"d":"6.00E-128"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.7 : Acetoacetate degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","15229654, 1685080, 1755959, 7867955, 9904","2a : Function from experimental evidences in other organisms",5,392,392,8,394,394]
[null,"METUNv2_520573","_","Methyloversatilis universalis FAM5","phbA","Acetyl-CoA acetyltransferase","_",0.99241,1,50.26,{"v":6e-128,"d":"6.00E-128"},1,1,"1 : Metabolism ; 1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.9","2 : Cytoplasmic","15.11 : Biosynthesis of natural products ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,392,392,5,394,395]
[null,"VIBNIv4_A1234","_","Vibrio nigripulchritudo SFn1","phbA","Acetyl-CoA acetyltransferase","_",0.98731,0.99235,49.1,{"v":7E-128,"d":"7.00E-128"},1,1,"1.7 : Central intermediary metabolism ; 7.1 : Cytoplasm ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",1396692,"2a : Function from experimental evidences in other organisms",3,391,392,5,391,394]
[null,"CLOSTRIBL3_v1_13111","_","Clostridiaceae BL-3","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",1,1.00256,49.23,{"v":9e-128,"d":"9.00E-128"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","7867955, 11075929, 11466286, 1685080","1c : Function from experimental evidences in the studied genus",1,391,392,1,390,391]
[null,"PSHAa1586","_","Pseudoalteromonas haloplanktis TAC125","atoB","acetyl-CoA acetyltransferase with thiolase domain, Acetoacetyl-CoA thiolase","_",0.9511,0.99235,50.9,{"v":1E-127,"d":"1.00E-127"},1,1,"_","2.3.1.9","cytoplasm (undefined)","_","e : enzyme",7867955,"2a : Function from experimental evidences in other organisms",4,391,392,21,407,409]
[null,"LEPBIa0355","_","Leptospira biflexa serovar Patoc Patoc 1","thiL1","Putative acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.99746,1,51.02,{"v":1e-126,"d":"1.00E-126"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme",15733928,"2a : Function from experimental evidences in other organisms",1,391,392,1,389,393]
[null,"LFAv2_0052","_","Legionella-Like Amoebal Pathogens 10","thlA","Acetyl-CoA acetyltransferase","_",0.98731,0.99235,48.33,{"v":8e-125,"d":"8.00E-125"},1,1,"_","2.3.1.9","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,391,392,5,392,394]
[null,"BN381v2_150043","_","Candidatus Microthrix parvicella RN1","phaA","acetyl-CoA acetyltransferase","_",0.99491,0.99745,51.66,{"v":1e-122,"d":"1.00E-122"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","18246303, 10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",1,390,392,1,390,393]
[null,"BN12v2_3170003","_","Tetrasphaera japonica T1-X7","phaA","acetyl-CoA acetyltransferase (fadA) (Acetoacetyl-CoA thiolase) (beta-ketothiolase)","_",0.97487,0.9898,50,{"v":4e-119,"d":"4.00E-119"},1,1,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",5,390,392,7,393,398]
[null,"pRALTA_0081","_","Cupriavidus taiwanensis LMG19424","_","acetyl-CoA acetyltransferase","_",0.98,1,46.94,{"v":2e-115,"d":"2.00E-115"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,391,392,9,398,400]
[null,"ACIAD0694","_","Acinetobacter baylyi ADP1","fadA","3-ketoacyl-CoA thiolase, Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RXN-11246 ; RXN-12561 ; RXN0-6512 ; RXN-12565 ; KETOACYLCOATHIOL-RXN ; RHEA:21039 ; RHEA:21567 ;",0.99745,1,45.27,{"v":7e-115,"d":"7.00E-115"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.16, 2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","11075929, 18246303, 21209787","2a : Function from experimental evidences in other organisms",1,391,392,1,389,391]
[null,"BN13v1_460011","_","Tetrasphaera jenkinsii Ben74","_","putative Acetyl-CoA acetyltransferase (beta-ketothiolase) (phaA)","_",0.97487,0.9898,50.26,{"v":1e-113,"d":"1.00E-113"},1,1,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","3 : Putative function from multiple computational evidences",5,390,392,7,393,398]
[null,"BN45v3_30404","_","Mycobacterium canettii STB-J","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98469,0.99229,47.41,{"v":3e-111,"d":"3.00E-111"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,390,392,1,386,389]
[null,"BN11v3_1860009","_","Tetrasphaera australiensis Ben110","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.97243,0.9898,49.48,{"v":9e-111,"d":"9.00E-111"},1,1,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",5,390,392,8,394,399]
[null,"BN42v3_21228","_","Mycobacterium canettii STB-K","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98469,0.99229,47.15,{"v":2e-110,"d":"2.00E-110"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,390,392,1,386,389]
[null,"BN44v3_11488","_","Mycobacterium canettii STB-D","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98469,0.99229,47.15,{"v":3e-110,"d":"3.00E-110"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,390,392,1,386,389]
[null,"BN43v3_30420","_","Mycobacterium canettii STB-L","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98469,0.99229,47.15,{"v":4e-110,"d":"4.00E-110"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,390,392,1,386,389]
[null,"FRAAL5910","_","Frankia alni ACN14a","atoB","acetyl-CoA acetyltransferase with thiolase domain","_",0.97975,0.98724,48.06,{"v":2E-109,"d":"2.00E-109"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,390,392,5,390,395]
[null,"Atu3475","_","Agrobacterium tumefaciens C58","fadAx","acetyl-CoA C-acetyltransferase","_",0.9466,0.9949,47.18,{"v":3e-109,"d":"3.00E-109"},1,1,"1 : Metabolism ;","_","2 : Cytoplasmic","_","e : enzyme",11251808,"2b : Function from indirect experimental evidences (e.g. phenotypes)",4,392,392,32,411,412]
[null,"AZOLI_p40026","_","Azospirillum lipoferum 4B","pcaF","Beta-ketoadipyl CoA thiolase","_",0.98522,1.02041,46.25,{"v":3e-109,"d":"3.00E-109"},1,1,"1.1 : Carbon compound utilization ;","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",9582432,"2a : Function from experimental evidences in other organisms",1,392,392,8,405,406]
[null,"Pars_0309","_","Pyrobaculum arsenaticum DSM 13514","thlA","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.96806,1.0051,46.7,{"v":5e-106,"d":"5.00E-106"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11075929, 11466286, 1685080, 7867955","2a : Function from experimental evidences in other organisms",3,391,392,15,405,407]
[null,"Rmet_3669","_","Cupriavidus metallidurans CH34","pcaF","acetyl-CoA acetyltransferase","_",1.0025,1.02296,42.89,{"v":4e-101,"d":"4.00E-101"},1,1,"1.1.2.7 : Acetoacetate degradation ;","_","1 : Unknown","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,392,392,1,399,400]
[null,"RALTA_B0208","_","Cupriavidus taiwanensis LMG19424","pcaF","Beta-ketoadipyl CoA thiolase","_",1.0025,1.02296,42.39,{"v":2E-100,"d":"2.00E-100"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.16","1 : Unknown","6 : Energy metabolism ;","e : enzyme",7961399,"2a : Function from experimental evidences in other organisms",1,392,392,1,399,400]
[null,"XPG1v4_0713","_","Xenorhabdus poinarii G6","pcaF","Beta-ketoadipyl-CoA thiolase","_",1,1.02041,42,{"v":4e-96,"d":"4.00E-96"},1,1,"_","2.3.1.174","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,392,1,399,400]
[null,"XDD1v4_3927","_","Xenorhabdus doucetiae FRM16","paaJ","protein PaaJ; Beta-ketoadipyl-CoA thiolase","_",0.99505,1.02551,42.79,{"v":2e-94,"d":"2.00E-94"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.174","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,392,392,1,402,404]
[null,"BN11v3_1350015",null,"Tetrasphaera australiensis Ben110","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",1.00739,1.04337,42.54,{"v":2E-92,"d":"2.00E-92"},2,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",1,392,392,1,404,406]
[null,"AZOLI_p30161","_","Azospirillum lipoferum 4B","phbA4","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",1.02041,1.02828,42.25,{"v":8e-92,"d":"8.00E-92"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.9","2 : Cytoplasmic","3.1 : Biosynthesis ;","e : enzyme","7582015, 1396692","2a : Function from experimental evidences in other organisms",5,391,392,6,387,389]
[null,"BN11v3_1360003",null,"Tetrasphaera australiensis Ben110","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase)","_",0.99745,1.01034,40.41,{"v":2e-86,"d":"2.00E-86"},3,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",17189250,"3 : Putative function from multiple computational evidences",2,391,392,4,385,387]
[]
["CLOSTRIBL3_v1_13111","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_12838","_","Clostridiaceae BL-3","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",1,1.00256,49.23,{"v":9e-128,"d":"9.00E-128"},1,1,"_","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","7867955, 11075929, 11466286, 1685080","2a : Function from experimental evidences in other organisms",1,390,391,1,391,392]
[null,"CD630_10590",null,"Clostridium difficile 630","thlA1","Acetoacetyl-CoA thiolase 1","_",1,1,46.29,{"v":1e-120,"d":"1.00E-120"},2,2,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","11075929, 2191949","1c : Function from experimental evidences in the studied genus",1,390,391,1,390,391]
[null,"Rmet_1357",null,"Cupriavidus metallidurans CH34","phaA","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.99746,1.00256,45.41,{"v":6e-115,"d":"6.00E-115"},1,2,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,390,391,1,391,393]
[null,"Rmet_1362",null,"Cupriavidus metallidurans CH34","bktB","acetyl-CoA acetyltransferase","_",0.98985,0.99744,45.38,{"v":9e-115,"d":"9.00E-115"},2,2,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,390,391,3,392,394]
[null,"NIDE3104",null,"Candidatus Nitrospira defluvii","fadA","3-ketoacyl-CoA thiolase","_",0.99747,1.01023,45.57,{"v":2E-113,"d":"2.00E-113"},1,2,"1.1.2.4 : Anaerobic fatty acid oxidation pathway ; 7.1 : Cytoplasm ;","2.3.1.16","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","12535077, 1354266, 15229654, 2191949, 6350283","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,390,391,1,394,396]
[null,"RPSI07_1730",null,"Ralstonia solanacearum PSI07","phaA","acetyl-CoA acetyltransferase, thiolase-like","_",0.98985,0.99744,43.33,{"v":5e-112,"d":"5.00E-112"},2,2,"1.7 : Central intermediary metabolism ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,390,391,3,392,394]
[null,"SCFA_v1_120020",null,"Ca. Phosphitivorax anaerolimi F81","yqeF","Acetyl-CoA acetyltransferase","_",1.0102,1.01279,42.93,{"v":3e-99,"d":"3.00E-99"},4,2,"1.7 : Central intermediary metabolism ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",7763384,"2a : Function from experimental evidences in other organisms",1,390,391,1,390,392]
[null,"ABAYE2367",null,"Acinetobacter baumannii AYE","paaJ","beta-ketoadipyl CoA thiolase with thiolase-like domain, phenylacetic acid degradation","_",1.01493,1.04348,41.91,{"v":2e-97,"d":"2.00E-97"},3,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","1 : Unknown","_","e : enzyme",9748275,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,390,391,1,399,402]
[null,"BN10v3_920035","_","Tetrasphaera elongata Lp2","_","Putative 3-ketoacyl-CoA thiolase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",0.99509,1.03581,42.96,{"v":3e-97,"d":"3.00E-97"},1,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,390,391,5,404,407]
[null,"NBG4_v1_200004",null,"Candidatus Sulfobium mesophilum","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99241,1.00256,39.54,{"v":3e-96,"d":"3.00E-96"},1,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.9","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",23468890,"2a : Function from experimental evidences in other organisms",4,390,391,11,394,395]
[null,"SCFA_v1_3830001",null,"Ca. Phosphitivorax butyraticus R76","atoB","fragment of acetyl-CoA acetyltransferase (part 2)","ACETYL-COA-ACETYLTRANSFER-RXN ;",0.94145,1.02813,42.04,{"v":3e-95,"d":"3.00E-95"},4,2,"1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,375,391,27,427,427]
[null,"MGMSRv2_3177",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaE","beta-ketoadipyl CoA thiolase","_",0.99501,1.02046,41.35,{"v":3e-95,"d":"3.00E-95"},2,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","10766858, 12846838, 17259607, 9748275","2a : Function from experimental evidences in other organisms",1,390,391,1,399,401]
[null,"PP_3280",null,"Pseudomonas putida KT2440","paaJ","3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase","RXN0-6512 ; RXN-3641 ; RHEA:34441 ; RHEA:19483 ;",0.98522,1.02302,42,{"v":3e-94,"d":"3.00E-94"},3,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-, 2.3.1.174","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","20660314, 17259607","2a : Function from experimental evidences in other organisms",3,390,391,8,404,406]
[null,"ECK1394",null,"Escherichia coli K12","paaE","beta-ketoadipyl CoA thiolase","RXN-3641 ; RXN0-6512 ;",1.01247,1.03836,40.39,{"v":6e-94,"d":"6.00E-94"},3,2,"1.1.5.1 : Phenylacetic acid degradation ;","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 17259607, 9748275","1a : Function from experimental evidences in the studied strain",1,390,391,1,399,401]
[null,"PSEEN2795",null,"Pseudomonas entomophila L48","pcaF-2","beta-ketoadipyl CoA thiolase","_",0.99015,1.02813,41.04,{"v":5e-93,"d":"5.00E-93"},4,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.9","Cytoplasmic","6 : Energy metabolism ;","e : enzyme","12534466, 15474299, 9600981","2a : Function from experimental evidences in other organisms",1,390,391,6,404,406]
[null,"XDD1v4_3927",null,"Xenorhabdus doucetiae FRM16","paaJ","protein PaaJ; Beta-ketoadipyl-CoA thiolase","_",1.01238,1.04604,40.1,{"v":1E-91,"d":"1.00E-91"},2,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.174","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,390,391,1,401,404]
[null,"ACIAD1689",null,"Acinetobacter baylyi ADP1","dcaF","beta-ketoadipyl CoA thiolase","2.3.1.155-RXN ; KETOACYLCOATHIOL-RXN ; RXN-3641 ;",1.00998,1.03581,41.23,{"v":2E-91,"d":"2.00E-91"},4,2,"_","2.3.1.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921, 11571189","1a : Function from experimental evidences in the studied strain",3,390,391,3,398,401]
[null,"BN45v3_30114",null,"Mycobacterium canettii STB-J","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",0.98049,1.02813,39.3,{"v":7e-88,"d":"7.00E-88"},1,2,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,390,391,10,407,410]
[null,"BN44v3_11190",null,"Mycobacterium canettii STB-D","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",0.98049,1.02813,39.3,{"v":1E-87,"d":"1.00E-87"},1,2,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,390,391,10,407,410]
[null,"BN43v3_30127",null,"Mycobacterium canettii STB-L","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",0.98049,1.02813,39.3,{"v":1E-87,"d":"1.00E-87"},1,2,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,390,391,10,407,410]
[null,"BN42v3_20922",null,"Mycobacterium canettii STB-K","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",0.99259,1.02813,39.3,{"v":1E-87,"d":"1.00E-87"},1,2,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,390,391,5,402,405]
[null,"BN13v1_250034","_","Tetrasphaera jenkinsii Ben74","_","Putative 3-ketoacyl-CoA thiolase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",0.99257,1.02558,39.65,{"v":1E-87,"d":"1.00E-87"},1,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","3 : Putative function from multiple computational evidences",5,390,391,5,401,404]
[null,"BN11v3_1350015",null,"Tetrasphaera australiensis Ben110","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.99261,1.03069,38.96,{"v":2E-87,"d":"2.00E-87"},1,2,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",5,390,391,5,403,406]
[null,"ABAYE2307",null,"Acinetobacter baumannii AYE","dcaF","beta-ketoadipyl CoA thiolase","_",1.00998,1.03581,39.01,{"v":5e-87,"d":"5.00E-87"},6,2,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",3,390,391,3,398,401]
[null,"Pars_1071","_","Pyrobaculum arsenaticum DSM 13514","_","putative acetyl-CoA acetyltransferase","_",0.99751,1.02558,38.15,{"v":8e-87,"d":"8.00E-87"},1,1,"1.3 : Energy metabolism (carbon) ;","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ; 15 : Cellular processes ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,390,391,8,400,402]
[null,"BN11v3_1360003",null,"Tetrasphaera australiensis Ben110","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase)","_",1.01023,1.02067,38.48,{"v":3e-83,"d":"3.00E-83"},3,2,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",17189250,"3 : Putative function from multiple computational evidences",2,391,391,4,386,387]
[null,"AZCBGv1_p150132","_","Azospirillum brasilense CBG497","phaA","Beta-ketothiolase (acetyl-CoA acetyltransferase with thiolase domain)(Acetyl-CoA C-acyltransferase)","_",0.99744,1.00775,38.72,{"v":1e-82,"d":"1.00E-82"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.16","2 : Cytoplasmic","3.1 : Biosynthesis ;","e : enzyme","12039753, 7582015","1b : Function from experimental evidences in the studied species",3,390,391,11,385,387]
[null,"PSEEN3547",null,"Pseudomonas entomophila L48","fadAx","acetyl-CoA acetyltransferase with thiolase domain FadAx","_",0.97985,0.99488,37.02,{"v":1e-80,"d":"1.00E-80"},5,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",11251808,"2b : Function from indirect experimental evidences (e.g. phenotypes)",4,390,391,8,394,397]
[null,"RALTA_A1469",null,"Cupriavidus taiwanensis LMG19424","_","putative 3-ketoacyl-CoA thiolase / acetyl-CoA acetyltransferase","_",1.02551,1.02813,37.81,{"v":2e-80,"d":"2.00E-80"},5,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16, 2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,391,391,1,391,392]
[null,"Rmet_1853",null,"Cupriavidus metallidurans CH34","atoB","acetyl-CoA acetyltransferase / thiolase","_",1.02551,1.02813,37.31,{"v":3E-79,"d":"3.00E-79"},5,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","_","c : carrier","_","3 : Putative function from multiple computational evidences",1,391,391,1,391,392]
[null,"PP_2215",null,"Pseudomonas putida KT2440","_","acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",0.97985,0.99488,36.25,{"v":7e-79,"d":"7.00E-79"},6,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","4150713, 773366, 236278, 9904, 2883931","2a : Function from experimental evidences in other organisms",4,390,391,8,394,397]
[null,"ACIAD1612",null,"Acinetobacter baylyi ADP1","_","putative acetyl-CoA C-acetyltransferase with thiolase domain","_",0.99237,0.99744,36.41,{"v":1E-78,"d":"1.00E-78"},7,2,"1.1.1 : carbon compounds ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",4,391,391,5,392,393]
[null,"RALSYv5_mp0378","_","Ralstonia syzygii R24","_","putative 3-ketoacyl-CoA thiolase / acetyl-CoA acetyltransferase (fragment)","_",0.4399,0.93989,41.28,{"v":4e-37,"d":"4.00E-37"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16, 2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",220,391,391,12,182,183]
[]
["CLOSTRIBL3_v1_11283","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"IBTHAUMv1_11360028","_","Ianthella basta symbiont thaum","_","Propanoyl-CoA C-acyltransferase t(hiolase)","_",0.97494,1.01302,36.76,{"v":8e-77,"d":"8.00E-77"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,386,399,1,372,384]
[null,"PSEEN2543","_","Pseudomonas entomophila L48","_","putative 3-ketoacyl-CoA thiolase","_",0.93888,0.96241,35.94,{"v":1E-59,"d":"1.00E-59"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,384,399,23,394,409]
[null,"BRADO3110","_","Bradyrhizobium sp. ORS278","_","putative 3-ketoacyl-CoA thiolase","_",0.9675,0.96992,36.18,{"v":6e-59,"d":"6.00E-59"},1,1,"1.1 : Carbon compound utilization ; 1.1.3 : Amino acids ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.9","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,384,399,16,386,400]
[]
["CLOSTRIBL3_v1_11276","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_20313",null,"Clostridiaceae BL-3","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.9164,1.01064,36.14,{"v":2E-51,"d":"2.00E-51"},1,2,"_","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286, 8001771","1c : Function from experimental evidences in the studied genus",5,288,311,1,280,282]
[]
["CLOSTRIBL3_v1_13113","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_10580",null,"Clostridium difficile 630","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.98264,1.00712,41.34,{"v":7e-64,"d":"7.00E-64"},1,2,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","6 : Energy metabolism ;","e : enzyme","15991056, 18060402, 7576770","1c : Function from experimental evidences in the studied genus",5,287,288,2,279,281]
[null,"CLOSTRIBL3_v1_20313",null,"Clostridiaceae BL-3","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.99306,1.01418,40.56,{"v":2e-62,"d":"2.00E-62"},1,1,"_","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286, 8001771","1c : Function from experimental evidences in the studied genus",3,288,288,1,281,282]
[null,"SCFA_v1_100019",null,"Ca. Phosphitivorax anaerolimi F81","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.75726,0.99653,37.98,{"v":1e-55,"d":"1.00E-55"},2,2,"_","1.1.1.157","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,287,288,1,281,379]
[null,"NBG4_v1_200002",null,"Candidatus Sulfobium mesophilum","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:22432 ;",1.00347,1.02482,35.99,{"v":5E-53,"d":"5.00E-53"},1,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",23468890,"2a : Function from experimental evidences in other organisms",1,287,288,1,281,282]
[null,"BN873v1_210050",null,"Candidatus Competibacter denitrificans Run_A_D11","_","putative hydroxyacyl/hydroxybutyrl -CoA dehydrogenase","_",0.96309,0.99653,35.54,{"v":3e-50,"d":"3.00E-50"},1,2,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,287,288,1,282,298]
[null,"NIDE3103",null,"Candidatus Nitrospira defluvii","_","putative 3-hydroxyacyl-CoA dehydrogenase","_",0.70762,1,37.85,{"v":1e-49,"d":"1.00E-49"},1,2,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.4 : Anaerobic fatty acid oxidation pathway ; 1.1.2.6 : Aerobic fatty acid oxidation pathway ;","1.1.1.35","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","12535077, 15229654","3 : Putative function from multiple computational evidences",1,287,288,1,280,407]
[null,"ABAYE2368",null,"Acinetobacter baumannii AYE","paaH","3-hydroxybutyryl-CoA dehydrogenase, phenylacetic acid degradation","_",0.55859,0.99306,37.06,{"v":5e-49,"d":"5.00E-49"},1,2,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","_","e : enzyme",9748275,"2a : Function from experimental evidences in other organisms",5,287,288,10,288,512]
[null,"Rmet_1855",null,"Cupriavidus metallidurans CH34","fadB","fused 3-hydroxybutyryl-CoA epimerase and delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase and enoyl-CoA hydratase ; 3-hydroxyacyl-CoA dehydrogenase","_",0.41414,0.99653,35.19,{"v":1e-43,"d":"1.00E-43"},2,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","5.3.3.8, 4.2.1.17, 5.1.2.3, 1.1.1.35","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,288,288,292,568,693]
[null,"RALTA_A1467",null,"Cupriavidus taiwanensis LMG19424","fadB","multifunctional: 3-hydroxybutyryl-CoA epimerase, delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase, enoyl-CoA hydratase (N-terminal); 3-hydroxyacyl-CoA dehydrogenase (C-terminal)","_",0.41414,0.99653,35.54,{"v":2e-43,"d":"2.00E-43"},2,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","4.2.1.17, 5.3.3.8, 1.1.1.35, 5.1.2.3","1 : Unknown","3.2 : Degradation ;","e : enzyme",8549802,"2a : Function from experimental evidences in other organisms",3,288,288,292,568,693]
[null,"SCFA_v1_130011",null,"Ca. Phosphitivorax anaerolimi F81","paaF","Enoyl-CoA hydratase/isomerase family (3-hydroxybutyryl-CoA dehydratase (Crotonase))","RXN-11667 ;",0.44529,1.01736,35.49,{"v":7e-42,"d":"7.00E-42"},6,4,"_","4.2.1.17, 5.1.2.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,287,288,2,283,658]
[]
["CLOSTRIBL3_v1_20313","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_10580",null,"Clostridium difficile 630","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.99291,0.99644,59.64,{"v":6e-116,"d":"6.00E-116"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","6 : Energy metabolism ;","e : enzyme","15991056, 18060402, 7576770","1c : Function from experimental evidences in the studied genus",3,282,282,2,281,281]
[null,"MGMSRv2_3942",null,"Magnetospirillum gryphiswaldense MSR-1 v2","mmgB","3-hydroxybutyryl-CoA dehydrogenase (Beta- hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.9589,0.99291,54.64,{"v":5E-108,"d":"5.00E-108"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",8759838,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,280,282,4,283,292]
[null,"AZCBGv1_p190002",null,"Azospirillum brasilense CBG497","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.96575,1,53.55,{"v":5e-107,"d":"5.00E-107"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.1.1.157","2 : Cytoplasmic","3.1 : Biosynthesis ;","e : enzyme","11466286, 12597275, 8655474, 8759838, 8969508","2a : Function from experimental evidences in other organisms",1,282,282,4,285,292]
[null,"MGMSRv2_1554",null,"Magnetospirillum gryphiswaldense MSR-1 v2","mmgB","3-hydroxybutyryl-CoA dehydrogenase,containing NAD(P)-binding domain","_",0.92409,0.99291,54.64,{"v":9e-106,"d":"9.00E-106"},2,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",8759838,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,280,282,15,294,303]
[null,"AZOLI_p50301",null,"Azospirillum lipoferum 4B","hbdA1","3-hydroxybutyryl-CoA dehydrogenase","_",0.96575,1,52.48,{"v":1e-105,"d":"1.00E-105"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.1.1.157","2 : Cytoplasmic","3.1 : Biosynthesis ;","e : enzyme","11466286, 12597275, 8655474, 8759838, 8969508","2a : Function from experimental evidences in other organisms",1,282,282,4,285,292]
[null,"BSU24160",null,"Bacillus subtilis 168","mmgB","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.98258,1,53.55,{"v":5e-105,"d":"5.00E-105"},1,1,"2.4 : Metabolism of lipids ;","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8759838, 18461320, 28956599","1a : Function from experimental evidences in the studied strain",1,282,282,3,284,287]
[null,"Rmet_0212","_","Cupriavidus metallidurans CH34","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.99296,1,51.06,{"v":3E-98,"d":"3.00E-98"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.5 : Building block biosynthesis ; 1.5.4 : Fatty acid and phosphatidic acid ;","1.1.1.157","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,282,282,3,284,284]
[null,"NBG4_v1_200002",null,"Candidatus Sulfobium mesophilum","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:22432 ;",0.99291,0.99291,52.14,{"v":5e-98,"d":"5.00E-98"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",23468890,"2a : Function from experimental evidences in other organisms",1,280,282,3,281,282]
[null,"BRADO3444","_","Bradyrhizobium sp. ORS278","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.99647,1,51.42,{"v":1E-97,"d":"1.00E-97"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","2 : Cytoplasmic","16.7 : Manage energy ;","e : enzyme",1444364,"2a : Function from experimental evidences in other organisms",1,282,282,2,283,283]
[null,"RM41v1_680007",null,"Sinorhizobium sp. Rm41","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta- hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.96897,0.99645,49.47,{"v":1e-96,"d":"1.00E-96"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 7.1 : Cytoplasm ;","1.1.1.157","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",8655474,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,281,282,2,282,290]
[null,"ADVE02_v2_10866",null,"Methylosinus trichosporium OB3b","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.95904,0.99645,49.11,{"v":3e-96,"d":"3.00E-96"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,281,282,5,285,293]
[null,"RALTA_A0220","_","Cupriavidus taiwanensis LMG19424","_","3-HYDROXYBUTYRYL-COA DEHYDROGENASE","_",0.99296,1,50.35,{"v":6e-96,"d":"6.00E-96"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","1 : Unknown","3.2 : Degradation ;  6 : Energy metabolism ;","e : enzyme",8655474,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,282,282,3,284,284]
[null,"BN381v2_100132","_","Candidatus Microthrix parvicella RN1","_","putative dehydrogenase","_",0.92409,0.99291,49.64,{"v":2E-95,"d":"2.00E-95"},1,1,"_","_","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","12846838, 8001771, 1699931","3 : Putative function from multiple computational evidences",3,282,282,24,303,303]
[null,"BBta_4257","_","Bradyrhizobium sp. BTAi1","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.96099,1,52.03,{"v":2e-94,"d":"2.00E-94"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","2 : Cytoplasmic","16.7 : Manage energy ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",12,282,282,1,271,271]
[null,"BRADO6490",null,"Bradyrhizobium sp. ORS278","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta- hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.89776,0.99645,48.4,{"v":5e-94,"d":"5.00E-94"},2,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.1.1.157","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme",8655474,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,281,282,25,305,313]
[null,"BBta_1142",null,"Bradyrhizobium sp. BTAi1","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.96233,0.99645,48.4,{"v":9e-94,"d":"9.00E-94"},2,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.1.1.157","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,281,282,4,284,292]
[null,"CMR15v5_0701","_","Ralstonia solanacearum CMR15","_","3-HYDROXYBUTYRYL-COA DEHYDROGENASE","_",0.99296,1,48.58,{"v":1e-92,"d":"1.00E-92"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","1 : Unknown","3.2 : Degradation ; 6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,282,282,3,284,284]
[null,"BDBv6_40067","_","Blood disease bacterium R229","_","3-HYDROXYBUTYRYL-COA DEHYDROGENASE","_",1.00352,1.01064,49.12,{"v":3e-92,"d":"3.00E-92"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","1 : Unknown","3.2 : Degradation ; 6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,282,282,3,284,284]
[null,"Mchl_1824",null,"Methylobacterium extorquens CM4","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.95904,0.99645,48.4,{"v":4E-92,"d":"4.00E-92"},1,1,"_","1.1.1.157","1 : Unknown","_","e : enzyme","2687255, 8655474","2a : Function from experimental evidences in other organisms",1,281,282,5,285,293]
[null,"METDI2209",null,"Methylobacterium extorquens DM4","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.92739,0.99645,48.4,{"v":6e-92,"d":"6.00E-92"},1,1,"_","1.1.1.157","1 : Unknown","_","e : enzyme","2687255, 8655474","2a : Function from experimental evidences in other organisms",1,281,282,15,295,303]
[null,"PSEEN3198","_","Pseudomonas entomophila L48","paaH","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.97518,1,45.82,{"v":4e-89,"d":"4.00E-89"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,280,282,1,275,275]
[null,"PSHAa0399","_","Pseudoalteromonas haloplanktis TAC125","bhbD","3-hydroxybutyryl-CoA dehydrogenase (Beta- hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",1,1.00356,48.23,{"v":3e-86,"d":"3.00E-86"},1,1,"_","1.1.1.157","unknown","_","e : enzyme",8001771,"2a : Function from experimental evidences in other organisms",3,280,282,2,281,281]
[null,"NIDE3117","_","Candidatus Nitrospira defluvii","paaH","3-hydroxybutyryl-CoA dehydrogenase","_",0.95238,0.99291,45.36,{"v":3e-83,"d":"3.00E-83"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","1 : Unknown","6 : Energy metabolism ; 3.2 : Degradation ;","e : enzyme","10766858, 12846838, 2204034, 8001771, 9748275","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,280,282,6,285,294]
[null,"BN11v3_1490005","_","Tetrasphaera australiensis Ben110","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD)","_",0.46959,0.98582,45.32,{"v":4e-82,"d":"4.00E-82"},1,1,"_","1.1.1.157","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",1444364,"3 : Putative function from multiple computational evidences",3,280,282,7,284,592]
[null,"BN10v3_1170022","_","Tetrasphaera elongata Lp2","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD))","_",0.47039,0.98582,44.96,{"v":6e-81,"d":"6.00E-81"},1,1,"_","1.1.1.157","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,280,282,7,284,591]
[null,"BN13v1_460001","_","Tetrasphaera jenkinsii Ben74","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD))","_",0.46959,0.98582,45.32,{"v":7e-80,"d":"7.00E-80"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,280,282,7,284,592]
[null,"BN874v1_720038",null,"Candidatus Contendobacter odensis Run_B_J11","_","putative hydroxyacyl/hydroxybutyrl -CoA dehydrogenase","RXN0-2044 ;",0.9396,0.99291,42.86,{"v":1e-77,"d":"1.00E-77"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,280,282,3,282,298]
[null,"BN12v2_1150036","_","Tetrasphaera japonica T1-X7","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD))","_",0.47128,0.98936,44.09,{"v":3e-77,"d":"3.00E-77"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,280,282,7,284,592]
[null,"BN42v3_20192","_","Mycobacterium canettii STB-K","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98601,1,40.78,{"v":5e-75,"d":"5.00E-75"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",1,280,282,5,286,286]
[null,"Npun_R3442",null,"Nostoc punctiforme ATCC 29133; PCC 73102","_","3-hydroxybutyryl-CoA dehydrogenase","_",0.97569,0.99645,41.99,{"v":9e-75,"d":"9.00E-75"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,280,282,4,284,288]
[null,"BN44v3_10518","_","Mycobacterium canettii STB-D","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98601,1,40.43,{"v":2e-74,"d":"2.00E-74"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",1,280,282,5,286,286]
[null,"BN43v3_10507","_","Mycobacterium canettii STB-L","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98601,1,40.43,{"v":2e-74,"d":"2.00E-74"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",1,280,282,5,286,286]
[null,"BN45v3_10517","_","Mycobacterium canettii STB-J","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98601,1,40.78,{"v":4e-74,"d":"4.00E-74"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",1,280,282,5,286,286]
[null,"BN873v1_210050",null,"Candidatus Competibacter denitrificans Run_A_D11","_","putative hydroxyacyl/hydroxybutyrl -CoA dehydrogenase","_",0.9396,0.99291,40.71,{"v":2e-71,"d":"2.00E-71"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,280,282,3,282,298]
[null,"NIDE3103",null,"Candidatus Nitrospira defluvii","_","putative 3-hydroxyacyl-CoA dehydrogenase","_",0.68796,0.99291,42.14,{"v":2e-69,"d":"2.00E-69"},2,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.4 : Anaerobic fatty acid oxidation pathway ; 1.1.2.6 : Aerobic fatty acid oxidation pathway ;","1.1.1.35","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","12535077, 15229654","3 : Putative function from multiple computational evidences",1,280,282,3,280,407]
[null,"MGMSRv2_3175",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaH","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.54653,0.97872,43.48,{"v":3e-69,"d":"3.00E-69"},3,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",6,280,282,12,287,505]
[null,"SCFA_v1_130011",null,"Ca. Phosphitivorax anaerolimi F81","paaF","Enoyl-CoA hydratase/isomerase family (3-hydroxybutyryl-CoA dehydratase (Crotonase))","RXN-11667 ;",0.42857,1,42.55,{"v":2e-67,"d":"2.00E-67"},3,1,"_","4.2.1.17, 5.1.2.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,280,282,4,283,658]
[null,"SCFA_v1_100019",null,"Ca. Phosphitivorax anaerolimi F81","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.74406,1,44.33,{"v":5e-67,"d":"5.00E-67"},4,1,"_","1.1.1.157","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,280,282,3,281,379]
[null,"NVIE_010920","_","Nitrososphaera viennensis EN76","_","hydroxyacyl-CoA dehydrogenase","_",0.7526,1.02482,39.45,{"v":8e-67,"d":"8.00E-67"},1,1,"_","1.1.1.35","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,281,282,7,288,384]
[null,"ABAYE2368",null,"Acinetobacter baumannii AYE","paaH","3-hydroxybutyryl-CoA dehydrogenase, phenylacetic acid degradation","_",0.54883,0.99645,39.5,{"v":6e-66,"d":"6.00E-66"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","_","e : enzyme",9748275,"2a : Function from experimental evidences in other organisms",3,282,282,10,290,512]
[null,"AZOLI_p40260",null,"Azospirillum lipoferum 4B","paaH","3-hydroxybutyryl-CoA dehydrogenase","_",0.50181,0.98582,40.65,{"v":3E-65,"d":"3.00E-65"},1,1,"1.1.1 : carbon compounds ; 1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.-","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9748275,"2a : Function from experimental evidences in other organisms",4,280,282,10,287,554]
[null,"PP_3282",null,"Pseudomonas putida KT2440","paaH","3-hydroxyadipyl-CoA dehydrogenase","RXN0-2044 ; RHEA:16199 ;",0.55842,1,41.13,{"v":1e-64,"d":"1.00E-64"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.35","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","12846838, 15137080, 20660314, 10766858, 22961985, 22398448, 21247899, 9748275","2a : Function from experimental evidences in other organisms",3,280,282,9,287,505]
[null,"PSEEN2793",null,"Pseudomonas entomophila L48","paaC","3-hydroxyacyl-CoA dehydrogenase phaC","_",0.54921,0.98936,39.78,{"v":2e-64,"d":"2.00E-64"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.-","Cytoplasmic","6 : Energy metabolism ;","e : enzyme","12534466, 15474299, 9600981","2a : Function from experimental evidences in other organisms",3,280,282,12,290,508]
[null,"SCFA_v1_3390003",null,"Ca. Phosphitivorax butyraticus R76","hbd","3-hydroxybutyryl-CoA dehydrogenase (modular protein)","_",0.42857,1,40.43,{"v":4e-64,"d":"4.00E-64"},3,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,280,282,4,283,658]
[null,"XNC1_1710",null,"Xenorhabdus nematophila ATCC19061","xcnB","3-hydroxyacyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",0.97895,0.98936,37.63,{"v":1e-63,"d":"1.00E-63"},2,1,"_","1.1.1.157","1 : Unknown","15.11 : Biosynthesis of natural products ;","e : enzyme","16349198, 1955881","1a : Function from experimental evidences in the studied strain",3,280,282,2,280,285]
[null,"ACIAD1690",null,"Acinetobacter baylyi ADP1","dcaH","dehydrogenase","1.1.1.259-RXN ; METHELENE-THMPT-OXI-RXN ; RXN0-2044 ;",0.55842,1,39.36,{"v":4e-63,"d":"4.00E-63"},1,1,"_","1.1.1.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921, 11571189","1a : Function from experimental evidences in the studied strain",1,281,282,5,286,505]
[null,"XDD1v4_1792",null,"Xenorhabdus doucetiae FRM16","xcnB","3-hydroxyacyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",0.97895,0.98936,37.99,{"v":4e-63,"d":"4.00E-63"},1,1,"_","1.1.1.157","1 : Unknown","15.11 : Biosynthesis of natural products ;","e : enzyme","16349198, 1955881","2a : Function from experimental evidences in other organisms",3,280,282,2,280,285]
[null,"IBTHAUMv1_1140010","_","Ianthella basta symbiont thaum","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.84397,0.92969,43.28,{"v":4e-63,"d":"4.00E-63"},1,1,"1.3 : Energy metabolism (carbon) ;","1.1.1.157","2 : Cytoplasmic","_","e : enzyme",11772643,"2b : Function from indirect experimental evidences (e.g. phenotypes)",2,237,282,4,241,256]
[null,"THI_3559","_","Thiomonas sp. 3As","_","putative 3-hydroxybutyryl-CoA dehydrogenase PaaH","_",0.55118,0.99291,41.07,{"v":2e-62,"d":"2.00E-62"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,281,282,10,289,508]
[null,"CLOSTRIBL3_v1_13113",null,"Clostridiaceae BL-3","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.99306,1.01418,40.56,{"v":2e-62,"d":"2.00E-62"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 25112316","1c : Function from experimental evidences in the studied genus",1,281,282,3,288,288]
[null,"ABAYE2306",null,"Acinetobacter baumannii AYE","dcaH","dehydrogenase","_",0.55621,1,37.59,{"v":7e-61,"d":"7.00E-61"},2,1,"1.1.1 : carbon compounds ;","1.1.1.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",1,281,282,5,286,507]
[null,"XDD1v4_3925",null,"Xenorhabdus doucetiae FRM16","paaH","protein PaaH; 3-hydroxybutyryl-CoA dehydrogenase","_",0.50823,0.98582,40.29,{"v":4e-60,"d":"4.00E-60"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",4,280,282,10,287,547]
[null,"MARHY2087",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","fadB","bifunctional enzyme (PBE) (PBFE) [Includes: Enoyl-CoA hydratase ; 3,2-trans-enoyl-CoA isomerase ; 3-hydroxyacyl-CoA dehydrogenase ]","_",0.40773,1.01064,40,{"v":2e-58,"d":"2.00E-58"},1,1,"_","5.3.3.8, 4.2.1.17, 1.1.1.35","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","4019459, 8549802","2a : Function from experimental evidences in other organisms",1,280,282,291,567,699]
[null,"AZOLI_p30575",null,"Azospirillum lipoferum 4B","pimF","Enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase","_",0.39745,0.99645,39.15,{"v":2e-58,"d":"2.00E-58"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17, 1.1.1.35","2 : Cytoplasmic","3.2 : Degradation ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",15758219,"2a : Function from experimental evidences in other organisms",1,281,282,305,582,707]
[null,"Rmet_5110","_","Cupriavidus metallidurans CH34","fadB1","short chain enoyl-CoA hydratase / 3-hydroxyacyl-CoA dehydrogenase","_",0.39301,0.99645,39.5,{"v":2e-57,"d":"2.00E-57"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","5.1.2.3, 1.1.1.35, 4.2.1.17","2 : Cytoplasmic","3.2 : Degradation ; 6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,281,282,311,588,715]
[null,"Spro_1832",null,"Serratia proteamaculans 568","paaH","3-hydroxyacyl-CoA dehydrogenase, NAD-binding","_",0.54813,0.98936,37.63,{"v":8e-54,"d":"8.00E-54"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,278,282,8,286,509]
[null,"VS_0041","_","Vibrio tasmaniensis LGP32","_","3-hydroxybutyryl-CoA epimerase, Fatty acid oxidation complex subunit alpha","_",0.39557,1.01418,37.41,{"v":1E-52,"d":"1.00E-52"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.6 : Aerobic fatty acid oxidation pathway ;","5.1.2.3","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ; 3.2 : Degradation ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,280,282,315,593,723]
[null,"CLOSTRIBL3_v1_11276",null,"Clostridiaceae BL-3","_","putative 3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16200 ;",0.9164,1.01064,36.14,{"v":2E-51,"d":"2.00E-51"},2,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,280,282,5,288,311]
[null,"VIBNIv4_A0032","_","Vibrio nigripulchritudo SFn1","fadB","Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase ; 3-hydroxyacyl-CoA dehydrogenase]","_",0.38866,0.99645,35.94,{"v":7e-50,"d":"7.00E-50"},1,1,"1.1.2.6 : Aerobic fatty acid oxidation pathway ; 7.1 : Cytoplasm ;","5.3.3.8, 4.2.1.17, 5.1.2.3, 1.1.1.35","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","1699931, 1712230, 2204034","2a : Function from experimental evidences in other organisms",3,280,282,316,593,723]
[null,"LMIv2_1447","_","Legionella micdadei","_","3-hydroxybutyryl-CoA epimerase","_",0.41308,0.98582,35.61,{"v":1e-49,"d":"1.00E-49"},1,1,"_","5.1.2.3","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,281,282,310,578,673]
[]
["CLOSTRIBL3_v1_13112","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"SCFA_v1_1190005","_","Ca. Phosphitivorax anaerolimi F81","crt","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",1,1.00791,50.2,{"v":9e-80,"d":"9.00E-80"},1,1,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,255,255,1,253,253]
[null,"CLOSTRIBL3_v1_20308",null,"Clostridiaceae BL-3","crt","Short-chain-enoyl-CoA hydratase","ENOYL-COA-HYDRAT-RXN ; RHEA:16105 ;",0.99228,1.00784,47.86,{"v":3e-74,"d":"3.00E-74"},1,1,"_","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 5057466","1c : Function from experimental evidences in the studied genus",2,255,255,4,259,259]
[null,"CD630_10570",null,"Clostridium difficile 630","crt2","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.94717,0.98431,47.41,{"v":4e-69,"d":"4.00E-69"},1,2,"_","4.2.1.55","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,249,255,10,259,265]
[null,"BN10v3_570010","_","Tetrasphaera elongata Lp2","_","putative enoyl-CoA hydratase echA8","_",0.96899,0.98039,46.4,{"v":1E-61,"d":"1.00E-61"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",12,255,255,13,258,258]
[null,"BN873v1_210051",null,"Candidatus Competibacter denitrificans Run_A_D11","_","putative enoyl-CoA hydratase-isomerase","_",0.97287,0.98431,40.64,{"v":1E-56,"d":"1.00E-56"},1,2,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","_","e : enzyme","8655474, 10727085, 2204034, 1743516","3 : Putative function from multiple computational evidences",2,250,255,4,253,258]
[null,"PSEEN3545",null,"Pseudomonas entomophila L48","fadB1x","enoyl-CoA hydratase, FadB1x","_",0.96863,0.988,40.49,{"v":2e-56,"d":"2.00E-56"},1,2,"1.5.4 : Fatty acid and phosphatidic acid ;","4.2.1.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",11251808,"2a : Function from experimental evidences in other organisms",10,255,255,5,250,250]
[null,"BN44v3_11186",null,"Mycobacterium canettii STB-D","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",0.93774,0.9451,41.49,{"v":1E-54,"d":"1.00E-54"},1,2,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",11,250,255,13,252,257]
[null,"BN43v3_30123",null,"Mycobacterium canettii STB-L","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",0.93774,0.9451,41.49,{"v":1E-54,"d":"1.00E-54"},1,2,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",11,250,255,13,252,257]
[null,"ABAYE2304",null,"Acinetobacter baumannii AYE","dcaE","enoyl-CoA hydratase","_",0.91513,0.97255,40.32,{"v":2e-54,"d":"2.00E-54"},2,2,"1.1.1 : carbon compounds ;","4.2.1.17","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",9,255,255,25,271,271]
[null,"BN45v3_30109",null,"Mycobacterium canettii STB-J","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",0.93774,0.9451,41.08,{"v":5e-54,"d":"5.00E-54"},1,2,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",11,250,255,13,252,257]
[null,"BN42v3_20918",null,"Mycobacterium canettii STB-K","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",0.93774,0.9451,41.08,{"v":8e-54,"d":"8.00E-54"},1,2,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",11,250,255,13,252,257]
[null,"ABAYE2370",null,"Acinetobacter baumannii AYE","paaF","enoyl-CoA hydratase, phenylacetic acid degradation","_",0.94553,0.95294,39.51,{"v":2e-53,"d":"2.00E-53"},3,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","_","e : enzyme",9748275,"2b : Function from indirect experimental evidences (e.g. phenotypes)",14,255,255,16,257,257]
[null,"XDD1v4_3923",null,"Xenorhabdus doucetiae FRM16","paaF","protein PaaF; enoyl-CoA hydratase-isomerase","_",0.95331,0.96078,38.78,{"v":4e-53,"d":"4.00E-53"},1,2,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",11,254,255,13,256,257]
[null,"ACIAD1608",null,"Acinetobacter baylyi ADP1","FadB","Enoyl-CoA hydratase (valine degradation) (valine degradation)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; ENOYL-COA-HYDRAT-RXN ; METHYLACYLYLCOA-HYDROXY-RXN ; RXN-902 ; TIGLYLCOA-HYDROXY-RXN ; RHEA:31178 ;",0.92607,0.93333,39.08,{"v":5E-52,"d":"5.00E-52"},1,2,"1.1.3.14 : Valine degradation ; 1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","7122152, 8938168, 21104317","2a : Function from experimental evidences in other organisms",12,248,255,14,250,257]
[null,"ACIAD1692",null,"Acinetobacter baylyi ADP1","dcaE","Enoyl-CoA hydratase (branched-chain amino acid degradation)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; ENOYL-COA-HYDRAT-RXN ; METHYLACYLYLCOA-HYDROXY-RXN ; RXN-2425 ; RXN-902 ; TIGLYLCOA-HYDROXY-RXN ; RXN0-6513 ; RXN-7838 ; RHEA:16107 ; RHEA:17850 ; RHEA:31178 ; RHEA:31122 ;",0.95019,0.97255,38.31,{"v":2E-51,"d":"2.00E-51"},2,2,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921, 11571189","1a : Function from experimental evidences in the studied strain",9,255,255,15,261,261]
[null,"NIDE3102",null,"Candidatus Nitrospira defluvii","paaF","putative Enoyl-CoA hydratase","_",0.9771,1.00392,39.45,{"v":1e-49,"d":"1.00E-49"},1,2,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.1 : Carbohydrates/Carbon compounds ; 1.1.3 : Amino acids ;","4.2.1.17","1 : Unknown","3.2 : Degradation ; 6.2 : Amino acids and amines ; 6.11 : Sugars ;","e : enzyme","10766858, 11263873, 12445775, 12846838, 9748275","3 : Putative function from multiple computational evidences",4,255,255,9,262,262]
[null,"PP_3284",null,"Pseudomonas putida KT2440","paaF","enoyl-CoA hydratase-isomerase","RXN0-6513 ; RHEA:34866 ;",0.95331,0.96078,40,{"v":2e-49,"d":"2.00E-49"},2,2,"_","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","12846838, 15137080, 18437357","2a : Function from experimental evidences in other organisms",12,255,255,14,257,257]
[null,"SCFA_v1_100018",null,"Ca. Phosphitivorax anaerolimi F81","_","Enoyl-CoA hydratase","_",1.00781,1.01176,37.98,{"v":6e-48,"d":"6.00E-48"},2,2,"_","4.2.1.17","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,255,255,4,256,256]
[null,"PSEEN2791",null,"Pseudomonas entomophila L48","phaA","enoyl-CoA hydratase/isomerase PhaA","_",0.94942,0.95686,36.89,{"v":3e-44,"d":"3.00E-44"},2,2,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","Cytoplasmic","6 : Energy metabolism ;","e : enzyme","12534466, 15474299, 9600981","2a : Function from experimental evidences in other organisms",12,254,255,14,256,257]
[null,"MGMSRv2_3173",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaF","enoyl-CoA hydratase-isomerase","_",0.9305,0.9451,37.76,{"v":5e-43,"d":"5.00E-43"},3,2,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",15,254,255,19,258,259]
[null,"SCFA_v1_130011",null,"Ca. Phosphitivorax anaerolimi F81","paaF","Enoyl-CoA hydratase/isomerase family (3-hydroxybutyryl-CoA dehydratase (Crotonase))","RXN-11667 ;",0.38146,0.98431,35.06,{"v":2e-42,"d":"2.00E-42"},3,3,"_","4.2.1.17, 5.1.2.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",12,255,255,413,658,658]
[null,"NBG4_v1_200001",null,"Candidatus Sulfobium mesophilum","echA","3-hydroxybutyryl-CoA dehydratase (fragment)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; RHEA:17849 ;",0.5098,0.92199,40,{"v":7e-26,"d":"7.00E-26"},1,2,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,130,255,11,140,141]
[]
["CLOSTRIBL3_v1_11087","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"ACIAD1820","_","Acinetobacter baylyi ADP1","scpB","Methylmalonyl-CoA decarboxylase","RXN0-310 ; METHYLMALONYL-COA-DECARBOXYLASE-RXN ; RHEA:21399 ; RHEA:27667 ;",0.98062,0.99606,36.36,{"v":7e-47,"d":"7.00E-47"},1,1,"1.1.5 : Others ; 4.S.34 : citrate/succinate ;","4.1.1.41","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","5646172, 10769118, 7070502","2a : Function from experimental evidences in other organisms",4,253,254,6,256,258]
[]
["CLOSTRIBL3_v1_20109","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"SCFA_v1_450041","_","Ca. Phosphitivorax anaerolimi F81","phaJ","crotonase","_",0.93197,0.99275,54.01,{"v":1e-44,"d":"1.00E-44"},1,1,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,136,138,1,137,147]
[null,"MGMSRv2_2229","_","Magnetospirillum gryphiswaldense MSR-1 v2","_","MaoC-like dehydratase, putative","_",0.96528,1.00725,47.48,{"v":2e-37,"d":"2.00E-37"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,138,138,6,143,144]
[null,"LEPBIa1114","_","Leptospira biflexa serovar Patoc Patoc 1","_","Putative MaoC family dehydratase","_",0.97143,0.98551,47.79,{"v":2e-37,"d":"2.00E-37"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,136,138,4,139,140]
[null,"ADVE02_v2_12431","_","Methylosinus trichosporium OB3b","croR","Crotonase","_",0.84177,0.96377,44.36,{"v":3e-31,"d":"3.00E-31"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,138,138,11,142,158]
[null,"AZOLI_0508","_","Azospirillum lipoferum 4B","_","Putative acyl dehydratase","_",0.92617,1,42.03,{"v":6e-31,"d":"6.00E-31"},1,1,"_","_","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,138,138,13,148,149]
[null,"METDI4248","_","Methylobacterium extorquens DM4","croR","crotonase","_",0.74866,1.01449,43.57,{"v":2e-30,"d":"2.00E-30"},1,1,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme",11872727,"1b : Function from experimental evidences in the studied species",1,138,138,35,172,187]
[null,"PSEEN3977",null,"Pseudomonas entomophila L48","phaJ1","enoyl-CoA hydratase, R-specific","_",0.85256,0.96377,39.85,{"v":8e-29,"d":"8.00E-29"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","_","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",12115060,"2a : Function from experimental evidences in other organisms",7,138,138,10,141,156]
[null,"MARHY1690",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","_","conserved hypothetical protein","_",0.86335,1.00725,38.85,{"v":1e-28,"d":"1.00E-28"},1,1,"_","_","1 : Unknown","18 : Unknown function ;","u : unknown","_","4 : Unknown function but conserved in other organisms",1,138,138,8,145,161]
[null,"Rmet_1672","_","Cupriavidus metallidurans CH34","_","MaoC-like dehydratase","_",0.94521,1,38.41,{"v":2e-26,"d":"2.00E-26"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,137,138,4,140,146]
[]
["CLOSTRIBL3_v1_20308","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_10570",null,"Clostridium difficile 630","crt2","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.95849,0.98069,61.42,{"v":1e-105,"d":"1.00E-105"},1,1,"_","4.2.1.55","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,256,259,9,262,265]
[null,"CD630_08000",null,"Clostridium difficile 630","crt1","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.98077,0.98456,54.9,{"v":4e-97,"d":"4.00E-97"},2,1,"1.6 : Macromolecules (cellular constituent) biosynthesis ;","4.2.1.55","1 : Unknown","6 : Energy metabolism ;","e : enzyme","8001771, 16346566, 11263873","2a : Function from experimental evidences in other organisms",5,259,259,6,260,260]
[null,"LEPBIa0927","_","Leptospira biflexa serovar Patoc Patoc 1","crt","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.93436,0.95276,51.24,{"v":1E-83,"d":"1.00E-83"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.55","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","12379132, 8490573","2a : Function from experimental evidences in other organisms",15,256,259,13,254,254]
[null,"NVIE_008340","_","Nitrososphaera viennensis EN76","_","3-hydroxybutyryl-CoA dehydratase","_",0.94314,1.0888,47.16,{"v":5e-78,"d":"5.00E-78"},1,1,"_","4.2.1.55","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,254,259,18,299,299]
[null,"RM41v1_60029","_","Sinorhizobium sp. Rm41","_","Putative enoyl-CoA hydratase","_",1,1.00778,47.49,{"v":6e-78,"d":"6.00E-78"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","1743516, 2204034, 2806264, 7815937","3 : Putative function from multiple computational evidences",1,259,259,1,257,257]
[null,"IBTHAUMv1_18460003","_","Ianthella basta symbiont thaum","crt","3-hydroxybutyryl-CoA dehydratase","_",0.96525,0.99206,50.4,{"v":3e-77,"d":"3.00E-77"},1,1,"1.1 : Carbon compound utilization ;","4.2.1.55","2 : Cytoplasmic","5.2 : One-carbon metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,254,259,3,252,252]
[null,"BN873v1_210051",null,"Candidatus Competibacter denitrificans Run_A_D11","_","putative enoyl-CoA hydratase-isomerase","_",1,1.00388,47.1,{"v":8e-76,"d":"8.00E-76"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","_","e : enzyme","8655474, 10727085, 2204034, 1743516","3 : Putative function from multiple computational evidences",1,259,259,1,258,258]
[null,"BN874v1_720037",null,"Candidatus Contendobacter odensis Run_B_J11","_","putative enoyl-CoA hydratase-isomerase","_",1.01158,1.0155,46.56,{"v":3e-75,"d":"3.00E-75"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.-","1 : Unknown","_","e : enzyme","8655474, 10727085, 2204034, 1743516","3 : Putative function from multiple computational evidences",1,259,259,1,258,258]
[null,"Rmet_3162","_","Cupriavidus metallidurans CH34","paaF","enoyl-CoA hydratase-isomerase","_",1,1.00388,45.56,{"v":3e-74,"d":"3.00E-74"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","_","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",1,259,259,1,258,258]
[null,"CLOSTRIBL3_v1_13112",null,"Clostridiaceae BL-3","crt","Short-chain-enoyl-CoA hydratase","RXN-11667 ; RHEA:52664 ;",0.99228,1.00784,47.86,{"v":3e-74,"d":"3.00E-74"},1,1,"_","4.2.1.150","2 : Cytoplasmic","_","e : enzyme","8655474, 5057466","1c : Function from experimental evidences in the studied genus",4,259,259,2,255,255]
[null,"AZOLI_3178","_","Azospirillum lipoferum 4B","paaF1","Enoyl-CoA hydratase-isomerase","_",1,1.00388,44.79,{"v":2E-73,"d":"2.00E-73"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",1,259,259,1,258,258]
[null,"BN44v3_11186","_","Mycobacterium canettii STB-D","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",1,1.00778,44.4,{"v":3e-73,"d":"3.00E-73"},1,1,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",1,259,259,1,257,257]
[null,"BN43v3_30123","_","Mycobacterium canettii STB-L","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",1,1.00778,44.4,{"v":3e-73,"d":"3.00E-73"},1,1,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",1,259,259,1,257,257]
[null,"PSEEN3545",null,"Pseudomonas entomophila L48","fadB1x","enoyl-CoA hydratase, FadB1x","_",0.97297,1.008,45.63,{"v":1e-72,"d":"1.00E-72"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","4.2.1.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",11251808,"2a : Function from experimental evidences in other organisms",8,259,259,1,250,250]
[null,"HEAR0207","_","Herminiimonas arsenicoxydans","ech","Enoyl-CoA hydratase","_",0.99614,1,46.9,{"v":4e-72,"d":"4.00E-72"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",8012501,"2a : Function from experimental evidences in other organisms",1,258,259,1,257,258]
[null,"ABAYE3764",null,"Acinetobacter baumannii AYE","_","putative Enoyl-CoA hydratase","_",1.00772,1.01556,44.83,{"v":4e-72,"d":"4.00E-72"},1,1,"_","4.2.1.17","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,259,259,1,257,257]
[null,"MGMSRv2_2895","_","Magnetospirillum gryphiswaldense MSR-1 v2","paaF","enoyl-CoA hydratase-isomerase","_",1,1.00388,44.02,{"v":1e-71,"d":"1.00E-71"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",1,259,259,1,258,258]
[null,"BN45v3_30109","_","Mycobacterium canettii STB-J","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",1,1.00778,43.63,{"v":2e-71,"d":"2.00E-71"},1,1,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",1,259,259,1,257,257]
[null,"BN42v3_20918","_","Mycobacterium canettii STB-K","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",1,1.00778,43.24,{"v":2e-71,"d":"2.00E-71"},1,1,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",1,259,259,1,257,257]
[null,"RALTA_A2759","_","Cupriavidus taiwanensis LMG19424","badK","cyclohex-1-ene-1-carboxyl-CoA hydratase","_",1,1.00388,44.79,{"v":2e-71,"d":"2.00E-71"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9177244,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,259,259,1,258,258]
[null,"NIDE3102",null,"Candidatus Nitrospira defluvii","paaF","putative Enoyl-CoA hydratase","_",0.9542,0.96525,45.6,{"v":7e-71,"d":"7.00E-71"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.1 : Carbohydrates/Carbon compounds ; 1.1.3 : Amino acids ;","4.2.1.17","1 : Unknown","3.2 : Degradation ; 6.2 : Amino acids and amines ; 6.11 : Sugars ;","e : enzyme","10766858, 11263873, 12445775, 12846838, 9748275","3 : Putative function from multiple computational evidences",11,259,259,14,262,262]
[null,"CMR15v5_1457","_","Ralstonia solanacearum CMR15","paaF","enoyl-CoA hydratase-isomerase","_",1,1.00388,45.56,{"v":4E-70,"d":"4.00E-70"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9748275,"2a : Function from experimental evidences in other organisms",1,259,259,1,258,258]
[null,"Rru_A3801","_","Rhodospirillum rubrum ATCC 11170","fadB","short chain enoyl-CoA hydratase","_",1,1.00388,42.08,{"v":5e-70,"d":"5.00E-70"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.5.4 : Fatty acid and phosphatidic acid ;","4.2.1.17","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,259,259,1,258,258]
[null,"BRADO2663","_","Bradyrhizobium sp. ORS278","_","Putative enoyl-CoA hydratase","_",0.97368,1,43.63,{"v":4e-69,"d":"4.00E-69"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","1743516, 2204034, 2806264, 7815937","3 : Putative function from multiple computational evidences",3,259,259,11,266,266]
[null,"BDBv6_60063","_","Blood disease bacterium R229","paaF","enoyl-CoA hydratase-isomerase","_",0.97683,0.98062,45.45,{"v":1e-68,"d":"1.00E-68"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9748275,"2a : Function from experimental evidences in other organisms",1,253,259,1,252,258]
[null,"ACIAD1608",null,"Acinetobacter baylyi ADP1","FadB","Enoyl-CoA hydratase (valine degradation) (valine degradation)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; ENOYL-COA-HYDRAT-RXN ; METHYLACYLYLCOA-HYDROXY-RXN ; RXN-902 ; TIGLYLCOA-HYDROXY-RXN ; RHEA:31178 ;",1.00772,1.01556,42.91,{"v":2e-68,"d":"2.00E-68"},1,1,"1.1.3.14 : Valine degradation ; 1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","7122152, 8938168, 21104317","2a : Function from experimental evidences in other organisms",1,259,259,1,257,257]
[null,"BSU18220",null,"Bacillus subtilis 168","ldeF","methylglutaconyl-CoA hydratase (leucine degradation)","METHYLGLUTACONYL-COA-HYDRATASE-RXN ; RHEA:21536 ;",0.96923,0.97297,46.03,{"v":2e-67,"d":"2.00E-67"},1,1,"_","4.2.1.18","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",19935659,"2b : Function from indirect experimental evidences (e.g. phenotypes)",10,257,259,10,258,260]
[null,"MGMSRv2_0209",null,"Magnetospirillum gryphiswaldense MSR-1 v2","_","probable enoyl-CoA hydratase","_",0.99228,0.99228,43.19,{"v":5e-67,"d":"5.00E-67"},2,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","1743516, 2204034, 2806264, 7815937, 7751302","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,259,259,4,259,259]
[null,"THI_0338","_","Thiomonas sp. 3As","fadB","enoyl-CoA hydratase-isomerase","_",0.97318,0.98069,43.7,{"v":2E-66,"d":"2.00E-66"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",6,259,259,9,261,261]
[null,"Rmet_2603",null,"Cupriavidus metallidurans CH34","paaG1","Enoyl-CoA hydratase/isomerase","_",1.0076,1.02317,42.64,{"v":1e-64,"d":"1.00E-64"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,256,259,1,260,263]
[null,"SCFA_v1_100018",null,"Ca. Phosphitivorax anaerolimi F81","_","Enoyl-CoA hydratase","_",1.01158,1.02344,41.98,{"v":3e-64,"d":"3.00E-64"},2,1,"_","4.2.1.17","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,259,259,1,256,256]
[null,"PP_3284",null,"Pseudomonas putida KT2440","paaF","enoyl-CoA hydratase-isomerase","RXN0-6513 ; RHEA:34866 ;",0.96139,0.96887,42.57,{"v":7e-63,"d":"7.00E-63"},2,1,"_","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","12846838, 15137080, 18437357","2a : Function from experimental evidences in other organisms",11,259,259,11,257,257]
[null,"PSEEN2791",null,"Pseudomonas entomophila L48","phaA","enoyl-CoA hydratase/isomerase PhaA","_",0.9305,0.93774,44.4,{"v":1E-62,"d":"1.00E-62"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","Cytoplasmic","6 : Energy metabolism ;","e : enzyme","12534466, 15474299, 9600981","2a : Function from experimental evidences in other organisms",16,256,259,16,254,257]
[null,"SCFA_v1_130011",null,"Ca. Phosphitivorax anaerolimi F81","paaF","Enoyl-CoA hydratase/isomerase family (3-hydroxybutyryl-CoA dehydratase (Crotonase))","RXN-11667 ;",0.37538,0.95367,43.32,{"v":5e-62,"d":"5.00E-62"},3,2,"_","4.2.1.17, 5.1.2.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",14,259,259,413,658,658]
[null,"VIBNIv4_A2943","_","Vibrio nigripulchritudo SFn1","Echs1","Enoyl-CoA hydratase","_",0.96139,0.98031,44.18,{"v":3e-61,"d":"3.00E-61"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 7.1 : Cytoplasm ;","4.2.1.17","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","2806264, 15489334, 7883013, 8895557, 9480773, 11851409, 12445775","2a : Function from experimental evidences in other organisms",12,257,259,9,252,254]
[null,"BN13v1_100067",null,"Tetrasphaera jenkinsii Ben74","_","putative enoyl-CoA hydratase echA8","_",0.94981,0.94981,42.28,{"v":2e-60,"d":"2.00E-60"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,251,259,5,249,259]
[null,"BN11v3_3200006",null,"Tetrasphaera australiensis Ben110","_","putative enoyl-CoA hydratase echA8","_",0.94981,0.94981,42.68,{"v":5e-60,"d":"5.00E-60"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,251,259,5,249,259]
[null,"MGMSRv2_3173",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaF","enoyl-CoA hydratase-isomerase","_",0.99228,0.99228,39.69,{"v":7e-60,"d":"7.00E-60"},3,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",2,257,259,3,257,259]
[null,"ABAYE2304",null,"Acinetobacter baumannii AYE","dcaE","enoyl-CoA hydratase","_",0.91144,0.95367,41.3,{"v":1E-59,"d":"1.00E-59"},2,1,"1.1.1 : carbon compounds ;","4.2.1.17","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",13,259,259,27,271,271]
[null,"SCFA_v1_3390003",null,"Ca. Phosphitivorax butyraticus R76","hbd","3-hydroxybutyryl-CoA dehydrogenase (modular protein)","_",0.37538,0.95367,41.3,{"v":8e-59,"d":"8.00E-59"},2,2,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",14,259,259,413,658,658]
[null,"XDD1v4_3923",null,"Xenorhabdus doucetiae FRM16","paaF","protein PaaF; enoyl-CoA hydratase-isomerase","_",0.99228,1,36.96,{"v":1e-57,"d":"1.00E-57"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,257,259,1,255,257]
[null,"BN12v2_350029",null,"Tetrasphaera japonica T1-X7","_","putative enoyl-CoA hydratase echA8","_",0.94656,0.95753,39.92,{"v":2e-57,"d":"2.00E-57"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,250,259,5,251,262]
[null,"BN10v3_570010",null,"Tetrasphaera elongata Lp2","_","putative enoyl-CoA hydratase echA8","_",0.98456,0.98837,40.78,{"v":3E-57,"d":"3.00E-57"},1,2,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,259,259,5,258,258]
[null,"BSU28540",null,"Bacillus subtilis 168","fadB","enoyl-CoA hydratase","OHBUTYRYL-COA-EPIM-RXN ; RXN-7838 ; ENOYL-COA-HYDRAT-RXN ; RHEA:20724 ; RHEA:34863 ;",0.96911,0.97287,42.63,{"v":1E-56,"d":"1.00E-56"},2,1,"2.4 : Metabolism of lipids ;","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","1a : Function from experimental evidences in the studied strain",14,259,259,12,258,258]
[null,"ACIAD1692",null,"Acinetobacter baylyi ADP1","dcaE","Enoyl-CoA hydratase (branched-chain amino acid degradation)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; ENOYL-COA-HYDRAT-RXN ; METHYLACYLYLCOA-HYDROXY-RXN ; RXN-2425 ; RXN-902 ; TIGLYLCOA-HYDROXY-RXN ; RXN0-6513 ; RXN-7838 ; RHEA:16107 ; RHEA:17850 ; RHEA:31178 ; RHEA:31122 ;",0.94636,0.95367,39.27,{"v":2e-56,"d":"2.00E-56"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921, 11571189","1a : Function from experimental evidences in the studied strain",13,259,259,17,261,261]
[null,"Rmet_5557","_","Cupriavidus metallidurans CH34","_","Enoyl-CoA hydratase/isomerase","_",0.99621,1.01544,37.26,{"v":7e-56,"d":"7.00E-56"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,259,259,3,264,264]
[null,"FRAAL5882",null,"Frankia alni ACN14a","echA","enoyl-CoA hydratase-isomerase","_",0.94208,0.94574,38.11,{"v":1E-53,"d":"1.00E-53"},3,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","4.2.1.17","1 : Unknown","16.2 : Construct biomass (Anabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,249,259,4,246,258]
[null,"VIBNIv3_pA0027","_","Vibrio nigripulchritudo SFn1","_","Putative enoyl-CoA hydratase/isomerase","_",0.97297,0.98054,36.9,{"v":2E-52,"d":"2.00E-52"},1,1,"_","_","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",2,253,259,6,257,257]
[null,"Rmet_5150",null,"Cupriavidus metallidurans CH34","_","enoyl-CoA hydratase","_",0.9697,0.98842,41.02,{"v":1E-51,"d":"1.00E-51"},2,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,257,259,8,263,264]
[null,"ECS88_4526","_","Escherichia coli S88","_","putative Enoyl-CoA hydratase/carnithine racemase","_",1.00386,1.00386,40,{"v":5E-51,"d":"5.00E-51"},1,1,"_","4.2.1.17","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,256,259,1,256,259]
[null,"AZCBGv1_p1100088","_","Azospirillum brasilense CBG497","_","enoyl-CoA hydratase-isomerase","_",0.96226,0.98456,37.65,{"v":9e-51,"d":"9.00E-51"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","e : enzyme","1743516, 2204034, 2806264, 7815937","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,259,259,14,265,265]
[null,"BN381v2_10064","_","Candidatus Microthrix parvicella RN1","_","putative enoyl-CoA hydratase-isomerase","_",0.9304,0.98069,40.16,{"v":9e-50,"d":"9.00E-50"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","8655474, 10727085, 2204034, 1743516","3 : Putative function from multiple computational evidences",6,248,259,8,260,273]
[null,"ABAYE2370",null,"Acinetobacter baumannii AYE","paaF","enoyl-CoA hydratase, phenylacetic acid degradation","_",0.94208,0.94942,37.3,{"v":2e-48,"d":"2.00E-48"},3,2,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","_","e : enzyme",9748275,"2b : Function from indirect experimental evidences (e.g. phenotypes)",16,259,259,16,257,257]
[null,"MARHY1100",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","paaF","enoyl-CoA hydratase-isomerase","_",0.98069,0.98069,37.8,{"v":2e-47,"d":"2.00E-47"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",8,259,259,7,259,259]
[null,"RALTA_A1578",null,"Cupriavidus taiwanensis LMG19424","_","putative Enoyl-CoA hydratase/isomerase","_",0.97358,0.99614,38.37,{"v":2e-47,"d":"2.00E-47"},3,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",6,256,259,5,262,265]
[null,"RALTA_B1107",null,"Cupriavidus taiwanensis LMG19424","_","putative ENOYL-COA HYDRATASE ISOMERASE; similar to paaF (E.coli)","_",0.96139,0.97266,38.96,{"v":6e-47,"d":"6.00E-47"},1,1,"1 : Metabolism ;","4.2.1.-","2 : Cytoplasmic","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",12,258,259,8,255,256]
[null,"CMR15v5_mp0937",null,"Ralstonia solanacearum CMR15","_","putative enoyl-CoA hydratase/isomerase (paaF)","_",0.91729,0.94208,40.16,{"v":1E-46,"d":"1.00E-46"},1,1,"1 : Metabolism ;","4.2.1.-","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",11,252,259,9,251,266]
[null,"AGR4A_v2_Lc60051","_","Agrobacterium genomosp. 4 B6","_","putative enoyl-CoA hydratase/isomerase","_",0.99228,0.99228,37.74,{"v":5e-46,"d":"5.00E-46"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",6,259,259,6,258,259]
[null,"METDI5699","_","Methylobacterium extorquens DM4","croA","3-hydroxybutyryl-CoA dehydratase","_",0.91071,0.98456,39.61,{"v":4e-44,"d":"4.00E-44"},1,1,"_","4.2.1.17","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",14,259,259,28,280,280]
[null,"Rmet_5154",null,"Cupriavidus metallidurans CH34","_","enoyl-CoA hydratase","_",1,1.01969,36.29,{"v":5e-44,"d":"5.00E-44"},3,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,259,259,5,254,254]
[null,"RALTA_A1582",null,"Cupriavidus taiwanensis LMG19424","caiD","crotonobetainyl-CoA hydratase","_",1,1.01969,35.91,{"v":5e-43,"d":"5.00E-43"},4,1,"1.1.4.2 : Carnitine degradation ; 1.7.22 : Carnitine metabolism ;","4.2.1.-","1 : Unknown","6.2 : Amino acids and amines ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",6,259,259,5,254,254]
[null,"NBG4_v1_200001",null,"Candidatus Sulfobium mesophilum","echA","3-hydroxybutyryl-CoA dehydratase (fragment)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; RHEA:17849 ;",0.49035,0.90071,48.03,{"v":9e-36,"d":"9.00E-36"},1,1,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,134,259,14,139,141]
[null,"Spro_1828",null,"Serratia proteamaculans 568","caiD","Crotonobetainyl CoA hydratase","_",0.81467,0.87917,35.55,{"v":4e-33,"d":"4.00E-33"},5,1,"1.1.4.2 : Carnitine degradation ; 1.7.22 : Carnitine metabolism ;","4.2.1.-","1 : Unknown","6.2 : Amino acids and amines ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,217,259,11,214,240]
[null,"AZOLI_p30575",null,"Azospirillum lipoferum 4B","pimF","Enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase","_",0.29986,0.81853,35.38,{"v":3E-32,"d":"3.00E-32"},1,4,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17, 1.1.1.35","2 : Cytoplasmic","3.2 : Degradation ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",15758219,"2a : Function from experimental evidences in other organisms",10,212,259,19,218,707]
[]
["CLOSTRIBL3_v1_12502","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_20310","_","Clostridiaceae BL-3","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24004 ;",0.5937,0.99472,57.56,{"v":1E-146,"d":"1.00E-146"},1,1,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286","1c : Function from experimental evidences in the studied genus",1,377,635,1,377,379]
[null,"BSU24150","_","Bacillus subtilis 168","mmgC","propionyl-CoA dehydrogenase subunit","_",0.58898,0.98681,55.35,{"v":2e-142,"d":"2.00E-142"},1,1,"2.4 : Metabolism of lipids ;","1.3.99.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",28956599,"1a : Function from experimental evidences in the studied strain",6,379,635,4,377,379]
[null,"PSEEN3546","_","Pseudomonas entomophila L48","fadFx","acyl-CoA dehydrogenase protein FadFx","_",0.58583,0.992,47.31,{"v":2E-119,"d":"2.00E-119"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",11251808,"2a : Function from experimental evidences in other organisms",6,377,635,4,375,375]
[null,"PP_2216","_","Pseudomonas putida KT2440","acd","short-chain acyl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24007 ;",0.58425,0.98933,47.17,{"v":6e-118,"d":"6.00E-118"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","1.3.99.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","16024185, 11251808, 24317404","1a : Function from experimental evidences in the studied strain",7,377,635,5,375,375]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.5874,0.98939,45.31,{"v":7e-112,"d":"7.00E-112"},1,2,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","1.3.99.-","2 : Cytoplasmic","3.2 : Degradation ; 6.2 : Amino acids and amines ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",6,378,635,4,376,377]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.5811,0.98138,45.53,{"v":3e-111,"d":"3.00E-111"},1,2,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,374,635,4,372,376]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.5811,0.98138,44.72,{"v":6e-109,"d":"6.00E-109"},1,2,"_","1.3.99.2","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,374,635,4,372,376]
[null,"CMR15v5_0672",null,"Ralstonia solanacearum CMR15","_","putative acyl CoA dehydrogenase oxidoreductase protein","_",0.5811,0.98138,44.44,{"v":4e-105,"d":"4.00E-105"},1,2,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,374,635,4,372,376]
[null,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.5811,0.984,45.26,{"v":5e-103,"d":"5.00E-103"},1,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.2","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","11812788, 2777793, 8655474","2a : Function from experimental evidences in other organisms",6,374,635,4,372,375]
[null,"BN12v2_410044","_","Tetrasphaera japonica T1-X7","_","putative acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.60787,0.98721,44.56,{"v":3e-96,"d":"3.00E-96"},1,1,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,377,635,2,386,391]
[null,"BN13v1_430010","_","Tetrasphaera jenkinsii Ben74","_","putative acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.6126,0.98731,42.42,{"v":6e-94,"d":"6.00E-94"},1,1,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,377,635,2,390,394]
[null,"MARHY1166",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","ivdA","Isovaleryl-coenzyme A dehydrogenase","_",0.59055,0.96649,40.8,{"v":7e-91,"d":"7.00E-91"},1,3,"1.1.3 : Amino acids ;","1.3.99.10","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",14612443,"2a : Function from experimental evidences in other organisms",3,377,635,10,384,388]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.59055,0.96154,39.2,{"v":4e-89,"d":"4.00E-89"},2,3,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,377,635,11,385,390]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.59843,0.96692,40.26,{"v":2E-85,"d":"2.00E-85"},2,2,"1.1.3.12 : Leucine degradation ;","1.3.99.10","2 : Cytoplasmic","6 : Energy metabolism ; 1 : Amino acid biosynthesis ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,377,635,9,388,393]
[null,"CMR15v5_0667",null,"Ralstonia solanacearum CMR15","_","putative acyl-CoA dehydrogenase oxidoreductase","_",0.59843,0.96692,39.74,{"v":7e-85,"d":"7.00E-85"},2,2,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,377,635,9,388,393]
[null,"RALTA_A0110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL-COA DEHYDROGENASE OXIDOREDUCTASE","_",0.59843,0.96692,40,{"v":1E-84,"d":"1.00E-84"},2,2,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,377,635,9,388,393]
[null,"VIBNIv4_A0948","_","Vibrio nigripulchritudo SFn1","ACAD8","Isobutyryl-CoA dehydrogenase","_",0.59685,0.98698,40.37,{"v":9e-84,"d":"9.00E-84"},1,1,"1.1.3.14 : Valine degradation ;","1.3.99.-","1 : Unknown","6.2 : Amino acids and amines ;","e : enzyme","10524212, 11013134, 14702039, 15489334, 10235267, 14752098, 12359132, 15505379, 16857760","2a : Function from experimental evidences in other organisms",1,378,635,1,377,384]
[null,"THI_3281",null,"Thiomonas sp. 3As","ivd","Isovaleryl-CoA dehydrogenase","_",0.59843,0.96939,38.68,{"v":3e-82,"d":"3.00E-82"},2,3,"1.1.3.12 : Leucine degradation ;","1.3.99.10","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","10677295, 12477932, 12665801, 1310317, 2318964, 7640268, 8468053, 921428","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,377,635,8,387,392]
[null,"Rmet_2530",null,"Cupriavidus metallidurans CH34","ivd","isovaleryl-CoA dehydrogenase (IVDHase)","_",0.59055,0.99206,36.53,{"v":2e-64,"d":"2.00E-64"},6,1,"1.1.1 : Carbohydrates/Carbon compounds ;","1.3.99.10","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,373,635,10,374,378]
[null,"Rmet_2531",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase (IVDHase)","_",0.58425,0.97889,36.39,{"v":6e-64,"d":"6.00E-64"},7,2,"1.1.1 : Carbohydrates/Carbon compounds ;","1.3.99.10","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,374,635,10,376,379]
[]
["CLOSTRIBL3_v1_11587","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_08030",null,"Clostridium difficile 630","_","Putative acyl-CoA dehydrogenase","_",0.99737,1,47.23,{"v":8e-114,"d":"8.00E-114"},2,3,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,377,379,1,378,380]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.98417,0.98939,41.29,{"v":8e-105,"d":"8.00E-105"},1,4,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","1.3.99.-","2 : Cytoplasmic","3.2 : Degradation ; 6.2 : Amino acids and amines ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",5,377,379,3,375,377]
[null,"BN13v1_350002","_","Tetrasphaera jenkinsii Ben74","_","Acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.96883,0.98417,41.02,{"v":3e-94,"d":"3.00E-94"},1,1,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",6,374,379,9,379,385]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.97179,1,35.88,{"v":6e-92,"d":"6.00E-92"},2,2,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,379,379,9,387,390]
[null,"PSEEN0120",null,"Pseudomonas entomophila L48","gcdH","glutaryl-CoA dehydrogenase","_",0.94148,0.97625,35.68,{"v":2E-78,"d":"2.00E-78"},4,1,"_","1.3.99.7","Unknown","6 : Energy metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",4,373,379,18,382,393]
[null,"PP_0158",null,"Pseudomonas putida KT2440","gcdH","glutaryl-CoA dehydrogenase","_",0.94148,0.97625,35.68,{"v":2E-78,"d":"2.00E-78"},4,1,"_","1.3.8.6","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","18177371, 8439237","2a : Function from experimental evidences in other organisms",4,373,379,18,382,393]
[null,"MARHY2089",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","fadE","acyl-CoA dehydrogenase","_",0.96114,0.97889,36.12,{"v":1e-76,"d":"1.00E-76"},4,5,"_","1.3.99.-","1 : Unknown","_","e : enzyme",12359260,"2a : Function from experimental evidences in other organisms",11,379,379,10,380,386]
[null,"ABAYE2315",null,"Acinetobacter baumannii AYE","dcaA","acyl-CoA dehydrogenase","_",0.98956,1,36.15,{"v":2e-76,"d":"2.00E-76"},5,5,"1.1.1 : carbon compounds ;","1.3.99.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",5,379,379,2,380,383]
[null,"RALTA_B1742",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.9397,0.98681,37.43,{"v":1e-75,"d":"1.00E-75"},2,4,"1.4 : Energy production/transport ;","1.3.99.-","2 : Cytoplasmic","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",12,377,379,2,372,398]
[null,"RALTA_B0786",null,"Cupriavidus taiwanensis LMG19424","_","ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN; putative Butyryl-CoA dehydrogenase","_",0.97889,0.97889,35.85,{"v":4e-72,"d":"4.00E-72"},3,4,"1.4 : Energy production/transport ; 1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3.14 : Valine degradation ; 1.1.3.12 : Leucine degradation ;","1.3.99.-, 1.3.99.2","2 : Cytoplasmic","3.2 : Degradation ;  6.2 : Amino acids and amines ;  6.5 : Electron transport ;","e : enzyme",8655474,"2b : Function from indirect experimental evidences (e.g. phenotypes)",11,377,379,13,377,379]
[null,"AZCBGv1_p140072",null,"Azospirillum brasilense CBG497","gcdH","glutaryl-CoA dehydrogenase","_",0.935,0.98681,35.56,{"v":4e-71,"d":"4.00E-71"},1,1,"1.1.3.10 : Lysine cleavage ; 1.1.3.8 : Tryptophan utilization ; 7.1 : Cytoplasm ;","1.3.99.7","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",8541831,"2a : Function from experimental evidences in other organisms",4,377,379,26,393,400]
[null,"RM41v1_pld1870126",null,"Sinorhizobium sp. Rm41","_","putative glutaryl-CoA dehydrogenase","_",0.93671,0.97625,35.41,{"v":1E-70,"d":"1.00E-70"},4,1,"1.5 : Building block biosynthesis ;","1.3.99.7","2 : Cytoplasmic","3.1 : Biosynthesis ; 6.2 : Amino acids and amines ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,373,379,18,384,395]
[null,"AZCBGv1_p430008",null,"Azospirillum brasilense CBG497","_","Putative Acyl-CoA dehydrogenase","_",0.62456,0.92612,36.47,{"v":9e-58,"d":"9.00E-58"},2,3,"_","1.3.8.1","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",38,374,379,209,554,562]
[]
["CLOSTRIBL3_v1_12012","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"LEPBIa0057","_","Leptospira biflexa serovar Patoc Patoc 1","acdA2","Acyl-CoA dehydrogenase","_",0.95619,0.97632,48.25,{"v":3e-106,"d":"3.00E-106"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.3.8.-","1 : Unknown","16.2 : Construct biomass (Anabolism) ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",6,375,380,7,377,388]
[null,"CD630_10540",null,"Clostridium difficile 630","bcd2","Butyryl-CoA dehydrogenase","_",0.98684,0.99206,43.47,{"v":3e-97,"d":"3.00E-97"},1,5,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",4,375,380,3,376,378]
[null,"CD630_03990",null,"Clostridium difficile 630","acdB","Acyl-CoA dehydrogenase, short-chain specific","_",0.98158,0.98939,42.63,{"v":1e-95,"d":"1.00E-95"},2,5,"7.1 : Cytoplasm ;","1.3.99.-","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","16802151, 16233311","2a : Function from experimental evidences in other organisms",3,372,380,1,372,377]
[null,"CLOSTRIBL3_v1_20310",null,"Clostridiaceae BL-3","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24004 ;",0.99474,0.99736,41.53,{"v":4E-95,"d":"4.00E-95"},1,4,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286","1c : Function from experimental evidences in the studied genus",1,375,380,1,377,379]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.98684,0.99734,38.93,{"v":2E-91,"d":"2.00E-91"},1,5,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,375,380,1,375,376]
[null,"CD630_08030",null,"Clostridium difficile 630","_","Putative acyl-CoA dehydrogenase","_",0.98684,0.98684,42.13,{"v":4e-91,"d":"4.00E-91"},3,5,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,372,380,1,375,380]
[null,"SCFA_v1_500014",null,"Ca. Phosphitivorax anaerolimi F81","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.96084,0.96842,41.58,{"v":3e-88,"d":"3.00E-88"},3,5,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",16,378,380,16,381,383]
[null,"CLOSTRIBL3_v1_10853",null,"Clostridiaceae BL-3","carC","Caffeyl-CoA reductase-Etf complex subunit CarC","RHEA:46956 ;",0.98421,0.98681,41.18,{"v":2E-87,"d":"2.00E-87"},4,4,"_","1.3.1.108","2 : Cytoplasmic","_","e : enzyme",23479729,"2a : Function from experimental evidences in other organisms",3,372,380,1,373,379]
[null,"SCFA_v1_1080002",null,"Ca. Phosphitivorax butyraticus R76","acdA","Acyl-CoA dehydrogenase","_",0.96084,0.96842,41.3,{"v":2E-87,"d":"2.00E-87"},4,5,"_","1.3.8.-","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",16,378,380,16,381,383]
[null,"ACIAD1607",null,"Acinetobacter baylyi ADP1","acads","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; RXN0-2301 ; RHEA:24007 ; RHEA:12277 ;",0.97368,0.98667,39.19,{"v":2e-82,"d":"2.00E-82"},2,5,"1.1.3.12 : Leucine degradation ; 1.1.3.14 : Valine degradation ; 1.1.5.1 : Phenylacetic acid degradation ;","1.3.8.1","1 : Unknown","3 : Fatty acid and phospholipid metabolism ; 5 : Central intermediary metabolism ;","e : enzyme","6712627, 16024185, 6261796, 11571189","2a : Function from experimental evidences in other organisms",5,372,380,3,372,375]
[null,"VIBNIv4_B0452",null,"Vibrio nigripulchritudo SFn1","_","putative Acyl-CoA dehydrogenase","_",0.93264,0.94737,37.22,{"v":3e-73,"d":"3.00E-73"},1,5,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",17,372,380,20,376,386]
[null,"SCFA_v1_30011",null,"Ca. Phosphitivorax anaerolimi F81","bcd","Acyl-CoA dehydrogenase (fragment)","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24004 ; RHEA:47196 ;",0.61842,0.96311,48.09,{"v":8e-71,"d":"8.00E-71"},5,4,"_","1.3.8.1","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",139,372,380,5,239,244]
[null,"CMR15v5_mp0370",null,"Ralstonia solanacearum CMR15","_","putative acyl-coa dehydrogenase oxidoreductase protein (abmD)","_",0.80549,0.85,36.84,{"v":5e-60,"d":"5.00E-60"},3,5,"_","1.3.99.2","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",58,377,380,66,386,401]
[null,"Rmet_6103","_","Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase-like protein (fragment)","_",0.55526,0.98598,39.81,{"v":3e-46,"d":"3.00E-46"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",170,372,380,4,205,214]
[]
["CLOSTRIBL3_v1_12013","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"ACIAD1607",null,"Acinetobacter baylyi ADP1","acads","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; RXN0-2301 ; RHEA:24007 ; RHEA:12277 ;",0.88918,0.92,36.52,{"v":2e-59,"d":"2.00E-59"},1,6,"1.1.3.12 : Leucine degradation ; 1.1.3.14 : Valine degradation ; 1.1.5.1 : Phenylacetic acid degradation ;","1.3.8.1","1 : Unknown","3 : Fatty acid and phospholipid metabolism ; 5 : Central intermediary metabolism ;","e : enzyme","6712627, 16024185, 6261796, 11571189","2a : Function from experimental evidences in other organisms",37,380,388,35,375,375]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.85309,0.88032,36.25,{"v":1e-57,"d":"1.00E-57"},1,6,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",51,380,388,49,375,376]
[null,"SCFA_v1_30011",null,"Ca. Phosphitivorax anaerolimi F81","bcd","Acyl-CoA dehydrogenase (fragment)","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24004 ; RHEA:47196 ;",0.63144,1.0041,35.51,{"v":7e-40,"d":"7.00E-40"},8,6,"_","1.3.8.1","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",138,381,388,3,243,244]
[]
["CLOSTRIBL3_v1_20310","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_10540",null,"Clostridium difficile 630","bcd2","Butyryl-CoA dehydrogenase","_",0.98681,0.98942,70.32,0,1,1,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",6,379,379,5,378,378]
[null,"BSU37170","_","Bacillus subtilis 168","acdA","acyl-CoA dehydrogenase","ACYLCOADEHYDROG-RXN ;",0.98681,0.98681,58.29,{"v":2e-156,"d":"2.00E-156"},1,1,"2.4 : Metabolism of lipids ;","1.3.99.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","1a : Function from experimental evidences in the studied strain",1,374,379,1,374,379]
[null,"CLOSTRIBL3_v1_12502","_","Clostridiaceae BL-3","bcd","Acyl-CoA dehydrogenase, short-chain specific","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47199 ; RHEA:24004 ;",0.5937,0.99472,57.56,{"v":8e-147,"d":"8.00E-147"},1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286, 8399220, 7857927","2a : Function from experimental evidences in other organisms",1,377,379,1,377,635]
[null,"CD630_08030",null,"Clostridium difficile 630","_","Putative acyl-CoA dehydrogenase","_",0.98947,0.99208,56.91,{"v":1e-145,"d":"1.00E-145"},2,1,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,374,379,1,375,380]
[null,"BSU24150",null,"Bacillus subtilis 168","mmgC","propionyl-CoA dehydrogenase subunit","_",0.97625,0.97625,52.16,{"v":4e-139,"d":"4.00E-139"},2,2,"2.4 : Metabolism of lipids ;","1.3.99.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",28956599,"1a : Function from experimental evidences in the studied strain",5,374,379,3,372,379]
[null,"CD630_03990",null,"Clostridium difficile 630","acdB","Acyl-CoA dehydrogenase, short-chain specific","_",0.98417,0.98939,53.89,{"v":8e-138,"d":"8.00E-138"},3,1,"7.1 : Cytoplasm ;","1.3.99.-","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","16802151, 16233311","2a : Function from experimental evidences in other organisms",7,379,379,5,377,377]
[null,"SCFA_v1_190035","_","Ca. Phosphitivorax anaerolimi F81","bcd","acyl-CoA dehydrogenase, short-chain specific (Butyryl-CoA dehydrogenase)","_",0.98953,0.99736,49.74,{"v":6e-135,"d":"6.00E-135"},1,1,"_","1.3.8.1","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,377,379,1,378,382]
[null,"BSU18260",null,"Bacillus subtilis 168","ldeJ","isovaleryl-CoA dehydrogenase (leucine degradation)","RXN0-2301 ;",1,1.00264,51.84,{"v":1e-132,"d":"1.00E-132"},3,1,"2.4 : Metabolism of lipids ;","1.3.8.4","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 17085570, 19935659","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,1,380,380]
[null,"SCFA_v1_500014",null,"Ca. Phosphitivorax anaerolimi F81","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.97911,0.98945,48.8,{"v":2e-129,"d":"2.00E-129"},3,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,374,379,1,375,383]
[null,"SCFA_v1_1080002",null,"Ca. Phosphitivorax butyraticus R76","acdA","Acyl-CoA dehydrogenase","_",0.97911,0.98945,49.07,{"v":1e-128,"d":"1.00E-128"},3,1,"_","1.3.8.-","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,374,379,1,375,383]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.97625,0.98143,45.41,{"v":3e-119,"d":"3.00E-119"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","1.3.99.-","2 : Cytoplasmic","3.2 : Degradation ; 6.2 : Amino acids and amines ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",5,374,379,3,372,377]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.97625,0.98404,45.14,{"v":3e-117,"d":"3.00E-117"},1,1,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,374,379,3,372,376]
[null,"ACIAD1607",null,"Acinetobacter baylyi ADP1","acads","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; RXN0-2301 ; RHEA:24007 ; RHEA:12277 ;",0.97625,0.98667,46.49,{"v":6e-117,"d":"6.00E-117"},1,1,"1.1.3.12 : Leucine degradation ; 1.1.3.14 : Valine degradation ; 1.1.5.1 : Phenylacetic acid degradation ;","1.3.8.1","1 : Unknown","3 : Fatty acid and phospholipid metabolism ; 5 : Central intermediary metabolism ;","e : enzyme","6712627, 16024185, 6261796, 11571189","2a : Function from experimental evidences in other organisms",8,377,379,6,375,375]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.97625,0.98404,45.14,{"v":4E-116,"d":"4.00E-116"},1,1,"_","1.3.99.2","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,374,379,3,372,376]
[null,"PSEEN3546",null,"Pseudomonas entomophila L48","fadFx","acyl-CoA dehydrogenase protein FadFx","_",0.98417,0.99467,44.77,{"v":2e-115,"d":"2.00E-115"},1,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",11251808,"2a : Function from experimental evidences in other organisms",5,377,379,3,375,375]
[null,"PP_2216",null,"Pseudomonas putida KT2440","acd","short-chain acyl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24007 ;",0.97625,0.98667,45.14,{"v":2e-115,"d":"2.00E-115"},1,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","1.3.99.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","16024185, 11251808, 24317404","1a : Function from experimental evidences in the studied strain",8,377,379,6,375,375]
[null,"CLOSTRIBL3_v1_10853",null,"Clostridiaceae BL-3","carC","Caffeyl-CoA reductase-Etf complex subunit CarC","RHEA:46956 ;",0.99208,0.99208,45.48,{"v":9e-115,"d":"9.00E-115"},3,1,"_","1.3.1.108","2 : Cytoplasmic","_","e : enzyme",23479729,"2a : Function from experimental evidences in other organisms",5,379,379,3,378,379]
[null,"RSK60v3_mp750032",null,"Ralstonia solanacearum K60","_","putative Butyryl-CoA dehydrogenase","_",0.98681,0.99204,46.26,{"v":3e-114,"d":"3.00E-114"},1,1,"1 : Metabolism ;","1.3.8.1","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,374,379,1,374,377]
[null,"CMR15v5_mp0941",null,"Ralstonia solanacearum CMR15","_","putative Butyryl-CoA dehydrogenase","_",0.98681,0.99204,45.99,{"v":1e-113,"d":"1.00E-113"},1,1,"1 : Metabolism ;","1.3.99.2","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,374,379,1,374,377]
[null,"RALSYv5_mp0315",null,"Ralstonia syzygii R24","_","putative Butyryl-CoA dehydrogenase","_",0.98681,0.99204,45.99,{"v":1e-113,"d":"1.00E-113"},1,1,"1 : Metabolism ;","1.3.99.2","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,374,379,1,374,377]
[null,"MGMSRv2_0193","_","Magnetospirillum gryphiswaldense MSR-1 v2","_","Acyl-CoA dehydrogenase","_",0.97368,0.97625,44.05,{"v":3e-111,"d":"3.00E-111"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","1.3.99.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","10524212, 8759838, 8969508, 17189250","2a : Function from experimental evidences in other organisms",5,374,379,3,372,380]
[null,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.97625,0.98667,44.86,{"v":3e-111,"d":"3.00E-111"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.2","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","11812788, 2777793, 8655474","2a : Function from experimental evidences in other organisms",5,374,379,3,372,375]
[null,"ACIAD1613",null,"Acinetobacter baylyi ADP1","_","putative acyl-CoA dehydrogenase protein (acdB-like)","2-METHYLACYL-COA-DEHYDROGENASE-RXN ; RXN-8568 ; RXN-12572 ;",0.98417,0.99467,42.9,{"v":9e-111,"d":"9.00E-111"},2,2,"_","1.3.8.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,377,379,3,375,375]
[null,"RALTA_B1110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.9657,0.99728,45.36,{"v":4e-110,"d":"4.00E-110"},1,1,"1 : Metabolism ;","1.3.99.-","2 : Cytoplasmic","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",12,377,379,2,367,367]
[null,"BN873v1_590034","_","Candidatus Competibacter denitrificans Run_A_D11","_","putative acyl-CoA dehydrogenase","_",0.97361,0.97361,43.36,{"v":5E-110,"d":"5.00E-110"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.8.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,373,379,3,371,379]
[null,"CMR15v5_0672",null,"Ralstonia solanacearum CMR15","_","putative acyl CoA dehydrogenase oxidoreductase protein","_",0.97625,0.98404,43.51,{"v":3e-109,"d":"3.00E-109"},1,1,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,374,379,3,372,376]
[null,"BN45v3_60311","_","Mycobacterium canettii STB-J","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.97172,0.99736,44.44,{"v":3e-107,"d":"3.00E-107"},1,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","10510226, 12775759, 15525680","3 : Putative function from multiple computational evidences",3,379,379,13,389,389]
[null,"BN44v3_70065","_","Mycobacterium canettii STB-D","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.97172,0.99736,44.44,{"v":3e-107,"d":"3.00E-107"},1,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","10510226, 12775759, 15525680","3 : Putative function from multiple computational evidences",3,379,379,13,389,389]
[null,"BN42v3_41331","_","Mycobacterium canettii STB-K","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.97172,0.99736,44.44,{"v":3e-107,"d":"3.00E-107"},1,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","10510226, 12775759, 15525680","3 : Putative function from multiple computational evidences",3,379,379,13,389,389]
[null,"BN43v3_60289","_","Mycobacterium canettii STB-L","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.97172,0.99736,44.44,{"v":5e-107,"d":"5.00E-107"},1,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","10510226, 12775759, 15525680","3 : Putative function from multiple computational evidences",3,379,379,13,389,389]
[null,"BN12v2_410006","_","Tetrasphaera japonica T1-X7","_","acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.98191,1.00264,44.47,{"v":2e-106,"d":"2.00E-106"},1,1,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme",17189250,"2a : Function from experimental evidences in other organisms",3,379,379,10,387,387]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.97179,1,42.22,{"v":4e-106,"d":"4.00E-106"},2,1,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,379,379,9,387,390]
[null,"BN13v1_920006","_","Tetrasphaera jenkinsii Ben74","_","putative acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.98705,1.00528,44.09,{"v":3e-105,"d":"3.00E-105"},1,1,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,379,379,8,386,386]
[null,"MARHY1166",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","ivdA","Isovaleryl-coenzyme A dehydrogenase","_",0.97423,0.99736,41.27,{"v":9e-104,"d":"9.00E-104"},1,1,"1.1.3 : Amino acids ;","1.3.99.10","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",14612443,"2a : Function from experimental evidences in other organisms",1,378,379,8,385,388]
[null,"BRADO1447","_","Bradyrhizobium sp. ORS278","ivd2","isovaleryl-CoA dehydrogenase","_",0.96667,0.99472,41.91,{"v":1e-101,"d":"1.00E-101"},1,1,"1.1.3.12 : Leucine degradation ;","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,378,379,10,386,390]
[null,"lpg1824","_","Legionella pneumophila subsp. pneumophila Philadelphia 1","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.97429,1,41.16,{"v":1E-100,"d":"1.00E-100"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,8,386,389]
[null,"lpl1788","_","Legionella pneumophila Lens","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.97429,1,41.16,{"v":1E-100,"d":"1.00E-100"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,8,386,389]
[null,"LPVv2_2096","_","Legionella pneumophila subsp. pneumophila HL06041035","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.98187,1,41.16,{"v":1E-100,"d":"1.00E-100"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,5,383,386]
[null,"LPOv2_1885","_","Legionella pneumophila subsp. pneumophila Lorraine","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.98187,1,41.16,{"v":1E-100,"d":"1.00E-100"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,5,383,386]
[null,"LPC_1268","_","Legionella pneumophila Corby","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.98187,1,41.16,{"v":1E-100,"d":"1.00E-100"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,5,383,386]
[null,"lpp1787","_","Legionella pneumophila Paris","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.97429,1,41.16,{"v":2E-100,"d":"2.00E-100"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,8,386,389]
[null,"AZOLI_p40074","_","Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.98425,0.98945,42.13,{"v":8e-96,"d":"8.00E-96"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.-","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,374,379,1,373,381]
[null,"MGMSRv2_0204",null,"Magnetospirillum gryphiswaldense MSR-1 v2","_","acyl-CoA dehydrogenase","_",0.98681,0.98681,40.11,{"v":1e-95,"d":"1.00E-95"},3,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","1.3.99.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","10524212, 8759838, 8969508, 17189250","2a : Function from experimental evidences in other organisms",1,373,379,1,372,379]
[null,"CLOSTRIBL3_v1_12012",null,"Clostridiaceae BL-3","carC","Caffeyl-CoA reductase-Etf complex subunit CarC","RHEA:46956 ;",0.99474,0.99736,41.53,{"v":4E-95,"d":"4.00E-95"},4,1,"_","1.3.1.108","2 : Cytoplasmic","_","e : enzyme",23479729,"2a : Function from experimental evidences in other organisms",1,377,379,1,375,380]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.97455,1.01055,40.47,{"v":1e-94,"d":"1.00E-94"},2,1,"1.1.3.12 : Leucine degradation ;","1.3.99.10","2 : Cytoplasmic","6 : Energy metabolism ; 1 : Amino acid biosynthesis ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,378,379,7,389,393]
[null,"THI_3281",null,"Thiomonas sp. 3As","ivd","Isovaleryl-CoA dehydrogenase","_",0.97704,1.01055,39.95,{"v":1e-94,"d":"1.00E-94"},2,1,"1.1.3.12 : Leucine degradation ;","1.3.99.10","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","10677295, 12477932, 12665801, 1310317, 2318964, 7640268, 8468053, 921428","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,378,379,6,388,392]
[null,"RALTA_A0110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL-COA DEHYDROGENASE OXIDOREDUCTASE","_",0.97455,1.01055,39.95,{"v":6e-94,"d":"6.00E-94"},2,1,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,378,379,7,389,393]
[null,"ACIAD1693",null,"Acinetobacter baylyi ADP1","acads4","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; GLUTARYL-COA-DEHYDROG-RXN ; RXN0-2301 ; RHEA:24007 ; RHEA:12277 ;",0.98958,1.00264,39.47,{"v":5E-91,"d":"5.00E-91"},3,2,"1.1.3.12 : Leucine degradation ; 1.1.3.14 : Valine degradation ; 1.1.5.1 : Phenylacetic acid degradation ;","1.3.8.1","1 : Unknown","3 : Fatty acid and phospholipid metabolism ; 5 : Central intermediary metabolism ;","e : enzyme","6712627, 16024185, 6261796, 11571189","1a : Function from experimental evidences in the studied strain",5,379,379,1,380,384]
[null,"ABAYE2303",null,"Acinetobacter baumannii AYE","dcaA","acyl-CoA dehydrogenase","_",0.98958,1.00264,38.68,{"v":8e-91,"d":"8.00E-91"},4,2,"1.1.1 : carbon compounds ;","1.3.99.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",5,379,379,1,380,384]
[null,"MARHY1099",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","_","acyl-CoA dehydrogenase","_",0.9768,1,38.79,{"v":3e-90,"d":"3.00E-90"},2,1,"_","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,377,379,1,378,388]
[null,"CMR15v5_0667",null,"Ralstonia solanacearum CMR15","_","putative acyl-CoA dehydrogenase oxidoreductase","_",0.96947,1.00528,37.53,{"v":6e-88,"d":"6.00E-88"},2,1,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,378,379,9,389,393]
[null,"VIBNIv4_B0452",null,"Vibrio nigripulchritudo SFn1","_","putative Acyl-CoA dehydrogenase","_",0.95855,0.97625,39.46,{"v":1e-86,"d":"1.00E-86"},1,3,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",10,379,379,13,381,386]
[null,"NBG4_v1_200003",null,"Candidatus Sulfobium mesophilum","acdA","Acyl-CoA dehydrogenase","RHEA:47196 ; RHEA:24004 ;",0.95116,0.97625,39.46,{"v":6e-84,"d":"6.00E-84"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.8.1","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",23468890,"2a : Function from experimental evidences in other organisms",7,374,379,19,382,389]
[null,"Npun_R3440",null,"Nostoc punctiforme ATCC 29133; PCC 73102","_","putative acyl-CoA dehydrogenase","_",0.95431,0.99208,39.63,{"v":2e-82,"d":"2.00E-82"},1,1,"_","1.3.99.2","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,374,379,1,370,394]
[null,"Rmet_4427","_","Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase(Butyryl-CoA dehydrogenase)","_",0.97423,0.99736,36.51,{"v":4e-81,"d":"4.00E-81"},1,1,"_","_","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,374,379,4,379,388]
[null,"MARHY2089",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","fadE","acyl-CoA dehydrogenase","_",0.97668,0.99472,35.81,{"v":2e-80,"d":"2.00E-80"},3,2,"_","1.3.99.-","1 : Unknown","_","e : enzyme",12359260,"2a : Function from experimental evidences in other organisms",8,379,379,4,380,386]
[null,"LEPBIa1138",null,"Leptospira biflexa serovar Patoc Patoc 1","_","Putative acyl-CoA dehydrogenase, short-chain specific (SCAD) (Butyryl-CoA dehydrogenase)","_",0.96193,1,37.99,{"v":7e-80,"d":"7.00E-80"},4,1,"_","1.3.8.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,379,379,14,390,394]
[null,"SCFA_v1_1630002",null,"Ca. Propionivorax syntrophicum F70","acdB","Acyl-CoA dehydrogenase, short-chain specific","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47196 ; RHEA:24004 ;",0.94898,0.98153,38.71,{"v":1E-79,"d":"1.00E-79"},1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,375,379,18,387,392]
[null,"XNC1_1707",null,"Xenorhabdus nematophila ATCC19061","xcnE","Acyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",0.94517,0.95515,37.85,{"v":3e-77,"d":"3.00E-77"},1,1,"_","1.3.99.2","1 : Unknown","_","e : enzyme","16349198, 1955881","1a : Function from experimental evidences in the studied strain",15,374,379,12,368,383]
[null,"XDD1v4_1795",null,"Xenorhabdus doucetiae FRM16","xcnE","Acyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",0.94517,0.95515,38.4,{"v":4e-77,"d":"4.00E-77"},1,1,"_","1.3.8.1","1 : Unknown","_","e : enzyme","16349198, 1955881","2a : Function from experimental evidences in other organisms",15,374,379,12,368,383]
[null,"Rmet_2599",null,"Cupriavidus metallidurans CH34","acdA","acyl-CoA dehydrogenase","_",0.97644,0.98417,37,{"v":2e-76,"d":"2.00E-76"},4,1,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,373,379,1,371,382]
[null,"SCATv2_5101",null,"Streptomyces cattleya NRRL 8057","_","putative Acyl-CoA dehydrogenase","_",0.97105,0.97361,36.59,{"v":6e-75,"d":"6.00E-75"},7,1,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",6,373,379,7,374,380]
[null,"BN381v2_250102","_","Candidatus Microthrix parvicella RN1","_","putative Acyl-CoA dehydrogenase","_",0.96585,1.04485,37.12,{"v":8e-74,"d":"8.00E-74"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.3.8.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",17189250,"3 : Putative function from multiple computational evidences",5,374,379,8,401,410]
[null,"MARHY1169",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","fadE","long chain acyl coenzyme A dehydrogenase","_",0.96859,0.97625,35.95,{"v":3e-73,"d":"3.00E-73"},6,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.13","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,374,379,9,376,382]
[null,"META1_2223","_","Methylobacterium extorquens AM1","mcd","methylsuccinyl-CoA dehydrogenase, putative isobutyryl-CoA dehydrogenase","_",0.68861,1.02111,36.69,{"v":1e-68,"d":"1.00E-68"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","16856937, 17548827","2a : Function from experimental evidences in other organisms",5,379,379,177,561,562]
[null,"Rmet_5152",null,"Cupriavidus metallidurans CH34","_","putative acyl-CoA dehydrogenase","_",0.9895,0.99472,35.28,{"v":5e-67,"d":"5.00E-67"},4,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.-, 1.3.99.13","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,377,379,8,381,381]
[]
["CLOSTRIBL3_v1_20311","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_04000",null,"Clostridium difficile 630","etfB1","Beta-subunit of electron transfer flavoprotein","_",1,1.00772,60.15,{"v":3e-106,"d":"3.00E-106"},1,2,"4.2 : Electrochemical potential driven transporters ;","_","1 : Unknown","7 : Transport and binding proteins ;","c : carrier","20195860, 18060402, 8655474","2a : Function from experimental evidences in other organisms",1,259,259,1,261,261]
[null,"CD630_10550",null,"Clostridium difficile 630","etfB","Electron transfer flavoproteins subunit beta","_",0.98113,1.00386,59.23,{"v":1e-104,"d":"1.00E-104"},2,1,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",1,259,259,6,265,265]
[null,"CD630_08040",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein beta-subunit, core","_",0.91667,0.93436,59.92,{"v":1e-90,"d":"1.00E-90"},3,2,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","c : carrier","17941859, 2326318","2a : Function from experimental evidences in other organisms",1,238,259,1,242,264]
[null,"CLOSTRIBL3_v1_12011",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1,1.01158,49.62,{"v":1e-80,"d":"1.00E-80"},2,2,"1.3 : Energy metabolism (carbon) ;","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,259,259,1,262,262]
[null,"SBF1_v1_470015",null,"Desulfosporosinus sp. SbF1","fixA","electron-transferring flavoprotein, subunit FixA","_",0.96029,1.02703,46.99,{"v":5e-75,"d":"5.00E-75"},1,3,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,259,259,1,266,277]
[null,"CLOSTRIBL3_v1_20124",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.89811,0.91892,46.64,{"v":6e-71,"d":"6.00E-71"},3,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,236,259,1,238,265]
[null,"AZOLI_0535",null,"Azospirillum lipoferum 4B","fixA","electron transfer flavoprotein beta subunit","_",0.81979,0.89575,43.97,{"v":6e-67,"d":"6.00E-67"},1,2,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ; 5.6 : Nitrogen fixation ;","c : carrier",15028689,"2a : Function from experimental evidences in other organisms",1,225,259,1,232,283]
[null,"BRADO5386",null,"Bradyrhizobium sp. ORS278","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.9573,1.03861,43.49,{"v":6E-65,"d":"6.00E-65"},1,2,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,256,259,1,269,281]
[null,"BURPHP2_0599",null,"Burkholderia phymatum STM815","fixA","protein fixA, electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.82624,0.89961,43.35,{"v":1E-62,"d":"1.00E-62"},1,3,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ; 6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",1,225,259,1,233,282]
[null,"MGMSRv2_1063",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.97122,1.04247,41.85,{"v":4e-62,"d":"4.00E-62"},1,3,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,257,259,1,269,278]
[null,"CLOSTRIBL3_v1_11115",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1,1.01158,44.27,{"v":1E-61,"d":"1.00E-61"},4,5,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,259,259,1,262,262]
[null,"pRALTA_0381",null,"Cupriavidus taiwanensis LMG19424","fixA","Electron transfer flavoprotein beta-subunit","_",0.86879,0.94595,42.04,{"v":4e-61,"d":"4.00E-61"},1,3,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ;  6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",1,234,259,1,245,282]
[null,"RM41v1_psym670028",null,"Sinorhizobium sp. Rm41","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.88014,0.99228,41.25,{"v":4e-59,"d":"4.00E-59"},1,2,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ; 16.15 : Symbiosis ;","c : carrier","15028689, 16453824","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,244,259,1,257,292]
[null,"MGMSRv2_0362",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","Electron transfer flavoprotein, beta-subunit","_",0.82394,0.90347,43.16,{"v":2e-58,"d":"2.00E-58"},2,4,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier","15028689, 3216855, 1850088, 9163424, 8369342, 8599534, 6317191, 3029021","2a : Function from experimental evidences in other organisms",1,225,259,1,234,284]
[null,"SCFA_v1_1630003",null,"Ca. Propionivorax syntrophicum F70","FixA","Electron transfer flavoproteins subunit beta","_",0.85606,0.87259,43.36,{"v":4e-58,"d":"4.00E-58"},1,3,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,222,259,1,226,264]
[null,"SCFA_v1_500013",null,"Ca. Phosphitivorax anaerolimi F81","etfB","Electron transfer flavoprotein, beta subunit","_",0.94872,1,37.84,{"v":5e-58,"d":"5.00E-58"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,256,259,2,260,273]
[null,"CLOSTRIBL3_v1_11488",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1,1.02317,40,{"v":2e-57,"d":"2.00E-57"},5,4,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,259,259,1,264,265]
[null,"SBF1_v1_6700003",null,"Desulfosporosinus sp. SbF1","etfB_2","electron-transferring flavoprotein, beta subunit EtfB (lutD-associated)","_",0.88031,0.90119,43.86,{"v":4e-57,"d":"4.00E-57"},2,6,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,225,259,1,228,253]
[null,"CD630_11710",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein subunit alpha","_",0.98868,1.01158,40.46,{"v":2E-55,"d":"2.00E-55"},4,6,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",1,259,259,4,265,265]
[null,"BN11v3_3200005",null,"Tetrasphaera australiensis Ben110","etfB","Electron transfer flavoprotein subunit beta","_",0.90909,0.92664,37.92,{"v":3e-48,"d":"3.00E-48"},1,1,"_","_","2 : Cytoplasmic","6.5 : Electron transport ;","e : enzyme","10026281, 9694853","2a : Function from experimental evidences in other organisms",1,238,259,5,244,264]
[null,"SCFA_v1_3390002",null,"Ca. Phosphitivorax butyraticus R76","etfB","Electron transfer flavoprotein subunit beta","_",0.93436,0.93798,41.74,{"v":3e-47,"d":"3.00E-47"},1,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,238,259,1,235,258]
[null,"SCFA_v1_130010",null,"Ca. Phosphitivorax anaerolimi F81","etfB","Electron transfer flavoprotein subunit beta","_",0.93822,0.94186,43.62,{"v":2E-46,"d":"2.00E-46"},2,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,238,259,1,235,258]
[null,"BN42v3_41032",null,"Mycobacterium canettii STB-K","fixA","Putative electron transfer flavoprotein (beta-subunit) FixA (beta-ETF) (electron transfer flavoprotein small subunit) (ETFSS)","_",0.91635,0.9305,37.34,{"v":5e-46,"d":"5.00E-46"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,238,259,3,243,263]
[null,"FRAAL5878",null,"Frankia alni ACN14a","fixA","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.92337,0.9305,35.68,{"v":1e-45,"d":"1.00E-45"},1,2,"1.4.3 : Electron carrier ;","_","1 : Unknown","16.1 : Circulate ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,238,259,1,241,261]
[null,"BN44v3_60523",null,"Mycobacterium canettii STB-D","fixA","Putative electron transfer flavoprotein (beta-subunit) FixA (beta-ETF) (electron transfer flavoprotein small subunit) (ETFSS)","_",0.91729,0.94208,36.89,{"v":5e-45,"d":"5.00E-45"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,238,259,3,246,266]
[null,"BN43v3_60008",null,"Mycobacterium canettii STB-L","fixA","Putative electron transfer flavoprotein (beta-subunit) FixA (beta-ETF) (electron transfer flavoprotein small subunit) (ETFSS)","_",0.91729,0.94208,36.89,{"v":5e-45,"d":"5.00E-45"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,238,259,3,246,266]
[null,"BN45v3_60006",null,"Mycobacterium canettii STB-J","fixA","Putative electron transfer flavoprotein (beta-subunit) FixA (beta-ETF) (electron transfer flavoprotein small subunit) (ETFSS)","_",0.91729,0.94208,36.89,{"v":6e-45,"d":"6.00E-45"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,238,259,3,246,266]
[null,"SCFA_v1_1080001",null,"Ca. Phosphitivorax butyraticus R76","etfB","Electron transfer flavoprotein subunit beta (fragment)","_",0.6834,0.9779,41.81,{"v":2e-44,"d":"2.00E-44"},2,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,175,259,2,178,181]
[null,"SBF1_v1_550001",null,"Desulfosporosinus sp. SbF1","etfB","electron-transferring flavoprotein, beta subunit EtfB","_",0.88417,0.89105,37.99,{"v":4e-44,"d":"4.00E-44"},3,1,"_","_","2 : Cytoplasmic","_","c : carrier",23468890,"2a : Function from experimental evidences in other organisms",1,229,259,1,222,257]
[null,"LEPBIa1133",null,"Leptospira biflexa serovar Patoc Patoc 1","etfB","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.92278,0.94466,37.66,{"v":1E-41,"d":"1.00E-41"},1,2,"1.4.3 : Electron carrier ;","_","1 : Unknown","16.10 : Respire ;","c : carrier","_","2a : Function from experimental evidences in other organisms",1,235,259,1,237,253]
[null,"BSU28530",null,"Bacillus subtilis 168","etfB","electron transfer flavoprotein (beta subunit)","_",0.81853,0.8249,36.79,{"v":1e-40,"d":"1.00E-40"},1,1,"1.4 : Membrane bioenergetics (electron transport chain and ATP synthase) ;","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","10026281, 17189250, 21398533","1a : Function from experimental evidences in the studied strain",1,211,259,1,211,257]
[null,"BBta_1140",null,"Bradyrhizobium sp. BTAi1","etfB","Electron transfer flavoprotein beta-subunit","_",0.96525,1.00402,35.2,{"v":5e-33,"d":"5.00E-33"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,245,259,1,246,249]
[null,"BRADO6492",null,"Bradyrhizobium sp. ORS278","etfB","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.96525,1.00402,35.2,{"v":1e-32,"d":"1.00E-32"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8599534,"2a : Function from experimental evidences in other organisms",1,245,259,1,246,249]
[null,"BURPHK2_1886",null,"Burkholderia phymatum STM815","_","putative electron transfer flavoprotein, beta subunit; FixA-like","_",0.8251,0.83784,36.87,{"v":4e-31,"d":"4.00E-31"},1,2,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier","_","3 : Putative function from multiple computational evidences",1,209,259,1,216,263]
[null,"AZOLI_0088",null,"Azospirillum lipoferum 4B","etfB3","Electron transfer flavoprotein beta-subunit","_",0.83012,0.86345,36.74,{"v":2e-28,"d":"2.00E-28"},2,3,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,210,259,1,210,249]
[null,"AZOLI_1605",null,"Azospirillum lipoferum 4B","etfB1","Electron transfer flavoprotein beta-subunit","_",0.82625,0.85944,35.51,{"v":2e-28,"d":"2.00E-28"},3,3,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,210,259,1,210,249]
[null,"BN77v1_0452",null,"Rhizobium mesoamericanum STM3625","etfB","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.66023,0.855,37.43,{"v":9e-23,"d":"9.00E-23"},1,2,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier",10026281,"2a : Function from experimental evidences in other organisms",1,166,259,34,199,200]
[]
["CLOSTRIBL3_v1_20312","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_04010",null,"Clostridium difficile 630","etfA1","Alpha-subunit of electron transfer flavoprotein","_",0.95942,0.99399,58.61,{"v":1e-140,"d":"1.00E-140"},1,2,"4.2 : Electrochemical potential driven transporters ;","_","1 : Unknown","7 : Transport and binding proteins ;","c : carrier","20195860, 18060402, 8655474","2a : Function from experimental evidences in other organisms",2,332,333,6,336,345]
[null,"CD630_08050",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein alpha-subunit","_",0.96765,0.98799,55.93,{"v":1e-129,"d":"1.00E-129"},2,2,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","c : carrier","17941859, 2326318","2a : Function from experimental evidences in other organisms",1,329,333,10,338,340]
[null,"CD630_10560",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.96726,0.97598,55.08,{"v":4e-124,"d":"4.00E-124"},3,1,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",9,333,333,4,328,336]
[null,"CLOSTRIBL3_v1_12010",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.99405,1.003,50.3,{"v":2e-111,"d":"2.00E-111"},2,2,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,333,333,1,334,336]
[null,"SBF1_v1_470014",null,"Desulfosporosinus sp. SbF1","fixB","electron-transferring flavoprotein, subunit FixB","_",0.73363,0.97598,49.85,{"v":3e-104,"d":"3.00E-104"},1,2,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,330,333,110,434,443]
[null,"AZOLI_0536",null,"Azospirillum lipoferum 4B","fixB","electron transfer flavoprotein alpha chain","_",0.90251,0.97297,49.69,{"v":6e-101,"d":"6.00E-101"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ; 5.6 : Nitrogen fixation ;","c : carrier",15028689,"2a : Function from experimental evidences in other organisms",6,325,333,21,344,359]
[null,"CLOSTRIBL3_v1_11487",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.97898,0.9939,50.61,{"v":1E-100,"d":"1.00E-100"},3,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",5,330,333,4,323,328]
[null,"CLOSTRIBL3_v1_20125",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.98498,0.98498,46.95,{"v":4e-100,"d":"4.00E-100"},4,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",7,333,333,2,329,333]
[null,"SBF1_v1_550002",null,"Desulfosporosinus sp. SbF1","etfA","electron-transferring flavoprotein, alpha subunit EtfA","_",0.97898,0.9939,47.24,{"v":2e-98,"d":"2.00E-98"},2,1,"_","_","2 : Cytoplasmic","_","c : carrier",23468890,"2a : Function from experimental evidences in other organisms",7,332,333,3,326,328]
[null,"BRADO5385",null,"Bradyrhizobium sp. ORS278","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.89674,0.99099,47.27,{"v":4e-93,"d":"4.00E-93"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",6,331,333,28,356,368]
[null,"pRALTA_0380",null,"Cupriavidus taiwanensis LMG19424","fixB","Electron transfer flavoprotein, alpha subunit","_",0.87467,0.98498,46.65,{"v":6e-93,"d":"6.00E-93"},1,3,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ;  6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",2,325,333,28,355,375]
[null,"MGMSRv2_1064",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.90984,1,44.14,{"v":1e-92,"d":"1.00E-92"},1,2,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",2,330,333,24,356,366]
[null,"BURPHP2_0598",null,"Burkholderia phymatum STM815","fixB","Protein fixB, Electron transfer flavoprotein, alpha subunit","_",0.86631,0.97297,46.3,{"v":2E-92,"d":"2.00E-92"},1,3,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ; 6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",6,325,333,32,355,374]
[null,"MGMSRv2_0361",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","Electron transfer flavoprotein, alpha subunit","_",0.88315,0.97598,46.77,{"v":7e-91,"d":"7.00E-91"},2,2,"1.4.3 : Electron carrier ;","_","1 : Unknown","5.6 : Nitrogen fixation ;","c : carrier","15028689, 3029021, 7875566, 8796346, 9163424, 8599534, 2503674","2a : Function from experimental evidences in other organisms",5,325,333,30,353,368]
[null,"CD630_11720",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.81281,0.99099,43.33,{"v":1e-90,"d":"1.00E-90"},4,3,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",1,330,333,64,391,406]
[null,"CLOSTRIBL3_v1_11114",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.81931,0.99399,44.41,{"v":3e-89,"d":"3.00E-89"},5,3,"_","_","2 : Cytoplasmic","_","c : carrier",17189250,"2a : Function from experimental evidences in other organisms",6,333,333,71,398,404]
[null,"RM41v1_psym670029",null,"Sinorhizobium sp. Rm41","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.92351,0.97898,45.09,{"v":4e-88,"d":"4.00E-88"},1,2,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ; 7.1 : Cytoplasm ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ; 16.15 : Symbiosis ;","c : carrier","15028689, 3029021","1c : Function from experimental evidences in the studied genus",5,325,333,11,335,353]
[null,"BSU28520",null,"Bacillus subtilis 168","etfA","electron transfer flavoprotein (alpha subunit)","_",0.98198,1.00615,44.34,{"v":1E-87,"d":"1.00E-87"},1,1,"1.4 : Membrane bioenergetics (electron transport chain and ATP synthase) ;","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 20059546, 21398533","1a : Function from experimental evidences in the studied strain",7,332,333,3,321,325]
[null,"SBF1_v1_6700004",null,"Desulfosporosinus sp. SbF1","etfA_2","electron-transferring flavoprotein, alpha subunit EtfA (lutD-associated)","_",0.81592,0.98498,44.51,{"v":7e-85,"d":"7.00E-85"},3,4,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",6,330,333,71,393,402]
[null,"SCFA_v1_500012",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",0.97898,0.97898,40.18,{"v":1e-82,"d":"1.00E-82"},1,2,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,330,333,6,328,333]
[null,"SCFA_v1_130009",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",0.98498,1.01863,42.38,{"v":1E-78,"d":"1.00E-78"},2,3,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,333,333,3,321,322]
[null,"LEPBIa1132",null,"Leptospira biflexa serovar Patoc Patoc 1","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.97297,1.01567,39.2,{"v":4E-70,"d":"4.00E-70"},1,3,"1.4.3 : Electron carrier ;","_","1 : Unknown","16.10 : Respire ;","c : carrier","_","2a : Function from experimental evidences in other organisms",9,332,333,4,317,319]
[null,"FRAAL5877",null,"Frankia alni ACN14a","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.98198,1.02188,40.98,{"v":5e-61,"d":"5.00E-61"},1,2,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","16.1 : Circulate ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,333,333,4,318,320]
[null,"BN44v3_60522",null,"Mycobacterium canettii STB-D","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97898,1.02516,38.04,{"v":2e-56,"d":"2.00E-56"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",9,333,333,4,317,318]
[null,"BN43v3_60007",null,"Mycobacterium canettii STB-L","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97898,1.02516,38.65,{"v":2e-56,"d":"2.00E-56"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",9,333,333,4,317,318]
[null,"MARHY1802",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","etfA","electron transfer flavoprotein alpha-subunit","_",0.97297,1.03514,35.8,{"v":3e-56,"d":"3.00E-56"},1,3,"1.4.3 : Electron carrier ;","_","1 : Unknown","6 : Energy metabolism ;","c : carrier",3415685,"2a : Function from experimental evidences in other organisms",9,332,333,3,312,313]
[null,"BN42v3_41031",null,"Mycobacterium canettii STB-K","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97898,1.02516,38.04,{"v":4e-56,"d":"4.00E-56"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",9,333,333,4,317,318]
[null,"BN45v3_60005",null,"Mycobacterium canettii STB-J","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97898,1.02516,38.34,{"v":5E-56,"d":"5.00E-56"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",9,333,333,4,317,318]
[null,"AZOLI_p50300",null,"Azospirillum lipoferum 4B","etfA2","Electron transfer flavoprotein alpha-subunit","_",0.96697,1.03205,38.82,{"v":2e-54,"d":"2.00E-54"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier","10984043, 16159782, 8599534","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,329,333,4,311,312]
[null,"ACIAD2654",null,"Acinetobacter baylyi ADP1","etfA","electron transfer flavoprotein alpha-subunit","_",0.97898,1.04823,38.34,{"v":8e-54,"d":"8.00E-54"},1,1,"1.4.3 : electron carrier ;","_","1 : Unknown","_","f : factor","_","2a : Function from experimental evidences in other organisms",9,329,333,3,311,311]
[null,"BURPHP2_0676",null,"Burkholderia phymatum STM815","etfA","electron transfer flavoprotein, alpha subunit","_",0.96096,1.0356,37.5,{"v":1E-53,"d":"1.00E-53"},2,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","10026281, 1576992, 8376381, 8599534","2b : Function from indirect experimental evidences (e.g. phenotypes)",11,329,333,5,309,309]
[null,"BURPHK2_1883",null,"Burkholderia phymatum STM815","etfA","electron transfer flavoprotein, alpha subunit","_",0.96396,1.02885,38.94,{"v":2e-53,"d":"2.00E-53"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","4 : Biosynthesis of cofactors, prosthetic groups, and carriers ;","c : carrier",10026281,"2a : Function from experimental evidences in other organisms",9,325,333,3,306,312]
[null,"AZCBGv1_p190001",null,"Azospirillum brasilense CBG497","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.8048,0.86452,42.54,{"v":4e-53,"d":"4.00E-53"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier","10984043, 16159782, 8599534","2b : Function from indirect experimental evidences (e.g. phenotypes)",62,329,333,51,307,310]
[null,"MGMSRv2_3943",null,"Magnetospirillum gryphiswaldense MSR-1 v2","etfA","electron transfer flavoprotein (alpha subunit)","_",0.96697,1.03537,37.58,{"v":1E-52,"d":"1.00E-52"},3,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",17189250,"2b : Function from indirect experimental evidences (e.g. phenotypes)",9,329,333,3,308,311]
[null,"Rmet_5518",null,"Cupriavidus metallidurans CH34","etfA","electron transfer flavoprotein, alpha subunit","_",0.96096,1.03226,38.44,{"v":4E-52,"d":"4.00E-52"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier","10026281, 1576992, 8376381, 8599534","2a : Function from experimental evidences in other organisms",11,329,333,5,310,310]
[null,"AZOLI_1606",null,"Azospirillum lipoferum 4B","etfA1","Electron transfer flavoprotein alpha-subunit","_",0.87988,0.9513,38.57,{"v":5E-52,"d":"5.00E-52"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",35,325,333,25,304,308]
[null,"Rmet_0738",null,"Cupriavidus metallidurans CH34","etfA","Electron transfer flavoprotein subunit alpha (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.96096,1.02894,38.44,{"v":7e-52,"d":"7.00E-52"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",11,329,333,5,310,311]
[null,"BN11v3_3200004",null,"Tetrasphaera australiensis Ben110","etfA","Electron transfer flavoprotein subunit alpha","_",0.97898,1.02516,35.58,{"v":1E-51,"d":"1.00E-51"},1,3,"_","_","1 : Unknown","6.5 : Electron transport ;","e : enzyme","10026281, 9694853","2a : Function from experimental evidences in other organisms",9,333,333,4,317,318]
[null,"MGMSRv2_1555",null,"Magnetospirillum gryphiswaldense MSR-1 v2","etfA","electron transfer flavoprotein (alpha subunit)","_",0.96997,1.0487,38.08,{"v":1E-51,"d":"1.00E-51"},4,1,"1.4 : Energy production/transport ; 1.4.3 : Electron carrier ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme",17189250,"2a : Function from experimental evidences in other organisms",9,329,333,3,308,308]
[null,"AZOLI_0089",null,"Azospirillum lipoferum 4B","etfA3","Electron transfer flavoprotein alpha-subunit","_",0.87988,0.9513,38.23,{"v":3E-51,"d":"3.00E-51"},3,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",35,325,333,25,304,308]
[null,"PSHAa1617","_","Pseudoalteromonas haloplanktis TAC125","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.94895,1.02597,37.03,{"v":8e-51,"d":"8.00E-51"},1,1,"2.5.4 : Menaquinone and ubiquinone ;","_","unknown","_","u : unknown",8599534,"2a : Function from experimental evidences in other organisms",11,325,333,5,304,308]
[null,"RALTA_A0796",null,"Cupriavidus taiwanensis LMG19424","etfA","ELECTRON TRANSFER FLAVOPROTEIN, ALPHA-SUBUNIT","_",0.89189,0.95498,39.73,{"v":9e-51,"d":"9.00E-51"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",35,329,333,25,310,311]
[null,"METDI2208",null,"Methylobacterium extorquens DM4","etfA","electron transfer flavoprotein, NAD/FAD-binding domain and ETFP adenine nucleotide-binding domain-like","_",0.97598,1.02524,36.62,{"v":2E-50,"d":"2.00E-50"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","15188393, 16926146, 8599534","2a : Function from experimental evidences in other organisms",11,333,333,5,315,317]
[null,"Mchl_1823",null,"Methylobacterium extorquens CM4","etfA","electron transfer flavoprotein alpha subunit","_",0.97598,1.02524,36.92,{"v":3e-50,"d":"3.00E-50"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","15188393, 16926146, 8599534","2a : Function from experimental evidences in other organisms",11,333,333,5,315,317]
[null,"THI_1679","_","Thiomonas sp. 3As","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF)(Electron transfer flavoprotein large subunit) (ETFLS)","_",0.81381,0.87419,42.8,{"v":1e-49,"d":"1.00E-49"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6 : Energy metabolism ;","c : carrier","10026281, 1576992, 8376381, 8599534","2a : Function from experimental evidences in other organisms",60,329,333,51,310,310]
[null,"CMR15v5_3436","_","Ralstonia solanacearum CMR15","etfA","Electron transfer flavoprotein, alpha-subunit","_",0.81081,0.86817,41.48,{"v":2e-49,"d":"2.00E-49"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",62,329,333,53,310,311]
[null,"NMV_2368",null,"Neisseria meningitidis NEM8013","etfA","electron transfer flavoprotein alpha-subunit (alpha-ETF; electron transfer flavoprotein large subunit; ETFLS)","_",0.9039,0.96785,41.2,{"v":2e-48,"d":"2.00E-48"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","f : factor","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",35,330,333,25,310,311]
[null,"RM41v1_680008",null,"Sinorhizobium sp. Rm41","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.89489,0.9644,36.24,{"v":3e-47,"d":"3.00E-47"},3,1,"1.4.3 : Electron carrier ; 7.1 : Cytoplasm ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",30,325,333,20,305,309]
[null,"NT26v4_3414",null,"Rhizobium sp. NT-26","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.89489,0.9644,38.26,{"v":5e-47,"d":"5.00E-47"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",30,325,333,20,305,309]
[null,"PSEEN3657",null,"Pseudomonas entomophila L48","etfA","electron transfer flavoprotein alpha-subunit","_",0.83784,1.01087,39.43,{"v":2E-46,"d":"2.00E-46"},1,2,"1.4.3 : Electron carrier ;","_","Unknown","6 : Energy metabolism ;","c : carrier","_","2a : Function from experimental evidences in other organisms",47,325,333,8,272,276]
[null,"BBta_1141",null,"Bradyrhizobium sp. BTAi1","etfA","Electron transfer flavoprotein alpha-subunit","_",0.89489,0.94904,36.91,{"v":8e-43,"d":"8.00E-43"},2,2,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",30,325,333,20,305,314]
[null,"BRADO6491",null,"Bradyrhizobium sp. ORS278","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.9009,0.96463,37,{"v":1E-41,"d":"1.00E-41"},2,3,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",30,325,333,20,305,311]
[null,"SCFA_v1_1630004",null,"Ca. Propionivorax syntrophicum F70","FixB","Electron transfer flavoprotein, alpha subunit (partial)","_",0.13514,0.81818,51.11,4e-06,1,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,52,333,8,52,55]
[]
["CLOSTRIBL3_v1_11710","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_23790","_","Clostridium difficile 630","buk","Butyrate kinase (Branched-chain carboxylic acid kinase) (BK)","_",0.99162,0.99719,62.54,{"v":2e-164,"d":"2.00E-164"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ; 7.1 : Cytoplasm ;","2.7.2.7","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","19222573, 17077990, 15640230, 10937485, 10855714, 8244020","1c : Function from experimental evidences in the studied genus",1,355,358,1,353,356]
[null,"CD630_01130",null,"Clostridium difficile 630","buk","Butyrate kinase (BK) (Branched-chain carboxylic acid kinase)","_",0.99164,0.99441,55.62,{"v":3e-133,"d":"3.00E-133"},2,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.7.2.7","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","20382813, 19222573, 18767192, 18725313, 17349085, 15028695, 12324374","2a : Function from experimental evidences in other organisms",3,356,358,5,358,359]
[null,"BSU24070",null,"Bacillus subtilis 168","buk","branched-chain fatty-acid kinase","BRANCHED-CHAIN-FATTY-ACID-KINASE-RXN ; BUTYRATE-KINASE-RXN ; RHEA:13585 ;",0.98347,0.99721,46.78,{"v":5e-119,"d":"5.00E-119"},1,3,"2.4 : Metabolism of lipids ;","2.7.2.7, 2.7.2.-","6 : Inner membrane-associated","16.2 : Construct biomass (Anabolism) ; 16.8 : Protect ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","10094682, 12427936, 15241682","1a : Function from experimental evidences in the studied strain",4,358,358,9,363,363]
[null,"CD630_24260",null,"Clostridium difficile 630","buk1","Butyrate kinase 1 (BK 1) (Branched-chain carboxylic acid kinase 1)","_",0.98603,1.00284,47.88,{"v":6e-117,"d":"6.00E-117"},3,2,"_","2.7.2.7","2 : Cytoplasmic","_","e : enzyme","15028695, 3027059, 13923331","2a : Function from experimental evidences in other organisms",4,355,358,2,352,352]
[null,"CLOSTRIBL3_v1_20086",null,"Clostridiaceae BL-3","buk2","Butyrate kinase 2","BUTYRATE-KINASE-RXN ; RHEA:13585 ;",0.97784,0.98603,49.01,{"v":2e-112,"d":"2.00E-112"},1,1,"_","2.7.2.7","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ; 16.8 : Protect ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","11466286, 10937485","2a : Function from experimental evidences in other organisms",5,356,358,5,355,361]
[null,"CLOSTRIBL3_v1_20087",null,"Clostridiaceae BL-3","buk","Butyrate kinase","BUTYRATE-KINASE-RXN ; RHEA:13585 ;",1.00279,1.00279,48.47,{"v":7e-109,"d":"7.00E-109"},2,1,"_","2.7.2.7","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ; 16.8 : Protect ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",12552129,"2a : Function from experimental evidences in other organisms",1,357,358,1,356,358]
[]
["CLOSTRIBL3_v1_11711","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_12308","_","Clostridiaceae BL-3","ptb","Phosphate butyryltransferase","PHOSPHATE-BUTYRYLTRANSFERASE-RXN ; RHEA:20892 ;",0.97674,0.98658,47.28,{"v":1e-85,"d":"1.00E-85"},1,1,"_","2.3.1.19","2 : Cytoplasmic","_","e : enzyme",11466286,"2a : Function from experimental evidences in other organisms",4,297,301,3,295,298]
[null,"CD630_24250",null,"Clostridium difficile 630","ptb","Phosphate butyryltransferase (Phosphotransbutyrylase)","_",0.99003,1.00337,43.62,{"v":6e-78,"d":"6.00E-78"},1,2,"1.1.4 : Amines ;","2.3.1.19","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","10855714, 11400055","2a : Function from experimental evidences in other organisms",2,299,301,1,295,297]
[null,"CD630_01120",null,"Clostridium difficile 630","ptb","phosphate butyryltransferase","_",0.9701,0.97333,43.84,{"v":6e-76,"d":"6.00E-76"},3,3,"1.1 : Carbon compound utilization ;","2.3.1.19","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","10094682, 12427936, 15241682","2a : Function from experimental evidences in other organisms",4,295,301,2,292,300]
[null,"BSU24090",null,"Bacillus subtilis 168","ptb","phosphate BCFA and butyryl coenzyme A transferase","PHOSPHATE-BUTYRYLTRANSFERASE-RXN ; RHEA:20892 ;",0.93688,0.94314,41.49,{"v":3e-67,"d":"3.00E-67"},1,3,"2.4 : Metabolism of lipids ;","2.3.1.19, 2.3.1.-","6 : Inner membrane-associated","16.2 : Construct biomass (Anabolism) ; 16.8 : Protect ;","e : enzyme","10094682, 12427936, 15241682, 22720735, 28165735","1a : Function from experimental evidences in the studied strain",18,299,301,14,293,299]
[null,"LFAv2_pA0055",null,"Legionella-Like Amoebal Pathogens 10","_","Phosphate butyryltransferase","_",0.60981,0.95017,40.56,{"v":3e-59,"d":"3.00E-59"},1,2,"_","2.3.1.19","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",21,301,301,179,464,469]
[]
["CLOSTRIBL3_v1_12016","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_24250",null,"Clostridium difficile 630","ptb","Phosphate butyryltransferase (Phosphotransbutyrylase)","_",1.01333,1.02357,39.8,{"v":3e-70,"d":"3.00E-70"},2,3,"1.1.4 : Amines ;","2.3.1.19","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","10855714, 11400055","2a : Function from experimental evidences in other organisms",1,300,300,1,296,297]
[null,"p2METDI0001","_","Methylobacterium extorquens DM4","pta","phosphate acetyltransferase","_",0.81416,0.92,43.84,{"v":6e-69,"d":"6.00E-69"},1,1,"_","2.3.1.8","1 : Unknown","_","e : enzyme",10094701,"2a : Function from experimental evidences in other organisms",23,297,300,47,322,339]
[]
["CLOSTRIBL3_v1_12308","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_07150",null,"Clostridium difficile 630","ptb","Phosphate butyryltransferase (Phosphotransbutyrylase)","_",0.9868,1.00336,51.17,{"v":2E-92,"d":"2.00E-92"},1,1,"1.1.3.7 : Threonine catabolism ; 1.3.5 : Fermentation ; 1.7.28 : Pyruvate catabolism ; 1.7.29 : Acetate catabolism ; 1.7.35 : Lactate oxidation ;","2.3.1.19","1 : Unknown","6.2 : Amino acids and amines ; 6.7 : Fermentation ;","e : enzyme","10855714, 8244020, 2317039, 11400055, 2844725","2a : Function from experimental evidences in other organisms",1,298,298,1,299,303]
[null,"BSU24090","_","Bacillus subtilis 168","ptb","phosphate BCFA and butyryl coenzyme A transferase","PHOSPHATE-BUTYRYLTRANSFERASE-RXN ; RHEA:20892 ;",0.98662,0.98993,48.47,{"v":5e-86,"d":"5.00E-86"},1,1,"2.4 : Metabolism of lipids ;","2.3.1.19, 2.3.1.-","6 : Inner membrane-associated","16.2 : Construct biomass (Anabolism) ; 16.8 : Protect ;","e : enzyme","10094682, 12427936, 15241682, 22720735, 28165735","1a : Function from experimental evidences in the studied strain",4,298,298,2,294,299]
[null,"CLOSTRIBL3_v1_11711","_","Clostridiaceae BL-3","ptb","Phosphate butyryltransferase","PHOSPHATE-BUTYRYLTRANSFERASE-RXN ; RHEA:20892 ;",0.97674,0.98658,47.28,{"v":1e-85,"d":"1.00E-85"},1,1,"_","2.3.1.19","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ; 16.8 : Protect ;","e : enzyme","10094682, 12427936, 15241682, 22720735, 28165735","2a : Function from experimental evidences in other organisms",3,295,298,4,297,301]
[null,"Rmet_0563","_","Cupriavidus metallidurans CH34","ptb","Phosphate acetyltransferase (Phosphotransacetylase)","_",0.87975,0.93289,45.32,{"v":7e-77,"d":"7.00E-77"},1,1,"_","2.3.1.19","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",21,298,298,26,303,316]
[null,"BN874v1_390023","_","Candidatus Contendobacter odensis Run_B_J11","_","putative Phosphate acetyl/butyryltransferase","_",0.94569,0.99329,42.91,{"v":2e-72,"d":"2.00E-72"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.-","1 : Unknown","_","e : enzyme","10094682, 12427936, 15241682","3 : Putative function from multiple computational evidences",3,298,298,6,301,313]
[null,"AZOLI_p20460","_","Azospirillum lipoferum 4B","pta2","phosphate acetyltransferase","_",0.58333,0.9396,43.93,{"v":1e-71,"d":"1.00E-71"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.8","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme","10094701, 8226623","2a : Function from experimental evidences in other organisms",19,298,298,188,467,480]
[null,"RCFBPv5_mp0811","_","Ralstonia solanacearum CFBP2957","ptb","phosphate butyryl coenzyme A transferase (Phosphotransacetylase)","_",0.94569,0.99329,42.91,{"v":1e-71,"d":"1.00E-71"},1,1,"_","2.3.1.19","6 : Inner membrane-associated","16.2 : Construct biomass (Anabolism) ; 16.8 : Protect ;","e : enzyme","10094682, 12427936, 15241682","2a : Function from experimental evidences in other organisms",3,298,298,6,301,313]
[null,"MGMSRv2_1018","_","Magnetospirillum gryphiswaldense MSR-1 v2","_","putative phosphate acetyltransferase containing a MaoC like domain","_",0.58849,0.92617,43.84,{"v":7e-71,"d":"7.00E-71"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.19","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme",10094701,"3 : Putative function from multiple computational evidences",20,293,298,177,452,469]
[null,"RALTA_A1396","_","Cupriavidus taiwanensis LMG19424","_","putative Phosphate acetyl/butyryltransferase","_",0.94872,0.99329,41.22,{"v":7e-71,"d":"7.00E-71"},1,1,"1 : Metabolism ;","2.3.1.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,298,298,6,301,312]
[null,"BN77v1_3276","_","Rhizobium mesoamericanum STM3625","pta","Phosphate acetyltransferase","_",0.90062,0.97315,40.34,{"v":3e-69,"d":"3.00E-69"},1,1,"_","2.3.1.8","1 : Unknown","_","e : enzyme",10094701,"2a : Function from experimental evidences in other organisms",11,298,298,21,310,322]
[null,"AZOLI_0598","_","Azospirillum lipoferum 4B","pta1","phosphate acetyltransferase","_",0.54601,0.89597,43.07,{"v":4e-69,"d":"4.00E-69"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.-","2 : Cytoplasmic","3.1 : Biosynthesis ;","e : enzyme",10094701,"2b : Function from indirect experimental evidences (e.g. phenotypes)",27,293,298,206,472,489]
[null,"BN873v1_140032","_","Candidatus Competibacter denitrificans Run_A_D11","_","putative Phosphate acetyl/butyryltransferase","_",0.58723,0.92617,43.84,{"v":7e-69,"d":"7.00E-69"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10094682, 12427936, 15241682, 10094701","3 : Putative function from multiple computational evidences",20,293,298,176,451,470]
[null,"HEAR1516","_","Herminiimonas arsenicoxydans","_","putative phosphate acetyltransferase","_",0.66366,0.98658,40.82,{"v":5e-67,"d":"5.00E-67"},1,1,"1.1 : Carbon compound utilization ; 1.7.28 : Pyruvate catabolism ;","2.3.1.8","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,298,298,143,435,443]
[null,"RM41v1_580007","_","Sinorhizobium sp. Rm41","pta","Phosphate acetyltransferase","_",0.92767,0.98993,40,{"v":5e-67,"d":"5.00E-67"},1,1,"7.1 : Cytoplasm ;","2.3.1.8","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",10094701,"2a : Function from experimental evidences in other organisms",4,298,298,13,307,318]
[null,"RPSI07_mp1365","_","Ralstonia solanacearum PSI07","_","putative phosphate butyryltransferase (pta)","_",0.85797,0.99329,41.22,{"v":6e-67,"d":"6.00E-67"},1,1,"_","2.3.1.19","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,298,298,38,333,345]
[null,"Mchl_1294","_","Methylobacterium extorquens CM4","pta","phosphate acetyltransferase","_",0.86111,0.93624,43.01,{"v":1e-65,"d":"1.00E-65"},1,1,"1.1 : Carbon compound utilization ;","2.3.1.8","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",10094701,"2a : Function from experimental evidences in other organisms",20,296,298,32,310,324]
[null,"BRADO6360","_","Bradyrhizobium sp. ORS278","_","putative phosphate acetyltransferase containing a MaoC like domain","_",0.61099,0.9698,39.79,{"v":9e-64,"d":"9.00E-64"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.19","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme",10094701,"3 : Putative function from multiple computational evidences",8,296,298,164,452,473]
[null,"LFAv2_pA0055","_","Legionella-Like Amoebal Pathogens 10","_","Phosphate butyryltransferase","_",0.56716,0.89262,41.35,{"v":1E-62,"d":"1.00E-62"},1,1,"_","2.3.1.19","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",30,293,298,190,455,469]
[null,"METDI0294","_","Methylobacterium extorquens DM4","_","putative phosphate butyryltransferase","_",0.62151,0.9698,41.18,{"v":3e-62,"d":"3.00E-62"},1,1,"_","2.3.1.19","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",11,297,298,170,458,465]
[null,"THI_1475","_","Thiomonas sp. 3As","_","phosphate butyltransferase","_",0.61458,0.98993,38.64,{"v":4e-62,"d":"4.00E-62"},1,1,"1 : Metabolism ;","2.3.1.19","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,293,298,162,456,480]
[]
["CLOSTRIBL3_v1_20086","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_01130",null,"Clostridium difficile 630","buk","Butyrate kinase (BK) (Branched-chain carboxylic acid kinase)","_",0.97507,0.9805,53.69,{"v":5e-133,"d":"5.00E-133"},1,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.7.2.7","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","20382813, 19222573, 18767192, 18725313, 17349085, 15028695, 12324374","2a : Function from experimental evidences in other organisms",5,355,361,7,358,359]
[null,"BSU24070",null,"Bacillus subtilis 168","buk","branched-chain fatty-acid kinase","BRANCHED-CHAIN-FATTY-ACID-KINASE-RXN ; BUTYRATE-KINASE-RXN ; RHEA:13585 ;",0.96694,0.9723,49.86,{"v":3E-124,"d":"3.00E-124"},1,1,"2.4 : Metabolism of lipids ;","2.7.2.7, 2.7.2.-","6 : Inner membrane-associated","16.2 : Construct biomass (Anabolism) ; 16.8 : Protect ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","10094682, 12427936, 15241682","1a : Function from experimental evidences in the studied strain",5,354,361,10,360,363]
[null,"CD630_24260",null,"Clostridium difficile 630","buk1","Butyrate kinase 1 (BK 1) (Branched-chain carboxylic acid kinase 1)","_",0.96953,0.99432,48.29,{"v":2e-117,"d":"2.00E-117"},2,1,"_","2.7.2.7","2 : Cytoplasmic","_","e : enzyme","15028695, 3027059, 13923331","2a : Function from experimental evidences in other organisms",5,354,361,3,352,352]
[null,"CLOSTRIBL3_v1_11710",null,"Clostridiaceae BL-3","buk","Butyrate kinase","BUTYRATE-KINASE-RXN ; RHEA:13585 ;",0.97784,0.98603,49.01,{"v":2e-112,"d":"2.00E-112"},1,1,"_","2.7.2.7","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ; 16.8 : Protect ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","10585557, 16825665","2a : Function from experimental evidences in other organisms",5,355,361,5,356,358]
[null,"CD630_23790",null,"Clostridium difficile 630","buk","Butyrate kinase (Branched-chain carboxylic acid kinase) (BK)","_",0.97507,0.98876,46.31,{"v":9e-108,"d":"9.00E-108"},3,3,"1.1.1 : Carbohydrates/Carbon compounds ; 7.1 : Cytoplasm ;","2.7.2.7","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","19222573, 17077990, 15640230, 10937485, 10855714, 8244020","1c : Function from experimental evidences in the studied genus",5,356,361,5,355,356]
[null,"CLOSTRIBL3_v1_20087",null,"Clostridiaceae BL-3","buk","Butyrate kinase","BUTYRATE-KINASE-RXN ; RHEA:13585 ;",0.96953,0.97765,47.43,{"v":1e-105,"d":"1.00E-105"},2,2,"_","2.7.2.7","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ; 16.8 : Protect ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",12552129,"2a : Function from experimental evidences in other organisms",1,349,361,1,350,358]
[null,"BTCD_v1_1767",null,"Brochothrix thermosphacta CD337","buk","branched-chain fatty-acid kinase","BRANCHED-CHAIN-FATTY-ACID-KINASE-RXN ; BUTYRATE-KINASE-RXN ;",0.96694,0.9723,45.3,{"v":5e-105,"d":"5.00E-105"},1,3,"_","2.7.2.7","6 : Inner membrane-associated","16.2 : Construct biomass (Anabolism) ; 16.8 : Protect ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","10094682, 12427936, 15241682","2a : Function from experimental evidences in other organisms",5,354,361,5,355,363]
[null,"BTCD_v1_0750",null,"Brochothrix thermosphacta CD337","_","putative butyrate kinase","BUTYRATE-KINASE-RXN ;",0.96175,0.97507,35.8,{"v":1e-67,"d":"1.00E-67"},2,3,"_","2.7.2.7","2 : Cytoplasmic","_","e : enzyme",12552129,"3 : Putative function from multiple computational evidences",5,354,361,7,357,366]
[]
["CLOSTRIBL3_v1_20087","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_01130",null,"Clostridium difficile 630","buk","Butyrate kinase (BK) (Branched-chain carboxylic acid kinase)","_",0.96936,0.97207,54.02,{"v":8e-131,"d":"8.00E-131"},1,3,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.7.2.7","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","20382813, 19222573, 18767192, 18725313, 17349085, 15028695, 12324374","2a : Function from experimental evidences in other organisms",3,350,358,5,352,359]
[null,"BSU24070",null,"Bacillus subtilis 168","buk","branched-chain fatty-acid kinase","BRANCHED-CHAIN-FATTY-ACID-KINASE-RXN ; BUTYRATE-KINASE-RXN ; RHEA:13585 ;",0.98072,0.99441,49.44,{"v":2e-122,"d":"2.00E-122"},1,2,"2.4 : Metabolism of lipids ;","2.7.2.7, 2.7.2.-","6 : Inner membrane-associated","16.2 : Construct biomass (Anabolism) ; 16.8 : Protect ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","10094682, 12427936, 15241682","1a : Function from experimental evidences in the studied strain",2,356,358,7,362,363]
[null,"CLOSTRIBL3_v1_11710",null,"Clostridiaceae BL-3","buk","Butyrate kinase","BUTYRATE-KINASE-RXN ; RHEA:13585 ;",1.00279,1.00279,48.47,{"v":7e-109,"d":"7.00E-109"},1,2,"_","2.7.2.7","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ; 16.8 : Protect ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","10585557, 16825665","2a : Function from experimental evidences in other organisms",1,356,358,1,357,358]
[null,"CD630_23790",null,"Clostridium difficile 630","buk","Butyrate kinase (Branched-chain carboxylic acid kinase) (BK)","_",0.97765,0.98315,50,{"v":2e-108,"d":"2.00E-108"},2,2,"1.1.1 : Carbohydrates/Carbon compounds ; 7.1 : Cytoplasm ;","2.7.2.7","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","19222573, 17077990, 15640230, 10937485, 10855714, 8244020","1c : Function from experimental evidences in the studied genus",1,350,358,1,348,356]
[null,"BTCD_v1_1767",null,"Brochothrix thermosphacta CD337","buk","branched-chain fatty-acid kinase","BRANCHED-CHAIN-FATTY-ACID-KINASE-RXN ; BUTYRATE-KINASE-RXN ;",0.96419,0.97765,47.71,{"v":2E-107,"d":"2.00E-107"},1,1,"_","2.7.2.7","6 : Inner membrane-associated","16.2 : Construct biomass (Anabolism) ; 16.8 : Protect ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","10094682, 12427936, 15241682","2a : Function from experimental evidences in other organisms",1,350,358,1,350,363]
[null,"CLOSTRIBL3_v1_20086",null,"Clostridiaceae BL-3","buk2","Butyrate kinase 2","BUTYRATE-KINASE-RXN ; RHEA:13585 ;",0.96953,0.97765,47.43,{"v":1e-105,"d":"1.00E-105"},2,2,"_","2.7.2.7","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ; 16.8 : Protect ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","11466286, 10937485","2a : Function from experimental evidences in other organisms",1,350,358,1,349,361]
[null,"CD630_24260",null,"Clostridium difficile 630","buk1","Butyrate kinase 1 (BK 1) (Branched-chain carboxylic acid kinase 1)","_",0.97207,0.98864,44.54,{"v":1e-104,"d":"1.00E-104"},3,3,"_","2.7.2.7","2 : Cytoplasmic","_","e : enzyme","15028695, 3027059, 13923331","2a : Function from experimental evidences in other organisms",4,351,358,2,348,352]
[null,"BTCD_v1_0750",null,"Brochothrix thermosphacta CD337","_","putative butyrate kinase","BUTYRATE-KINASE-RXN ;",0.95082,0.97207,37.93,{"v":3e-73,"d":"3.00E-73"},2,1,"_","2.7.2.7","2 : Cytoplasmic","_","e : enzyme",12552129,"3 : Putative function from multiple computational evidences",4,350,358,6,352,366]
[]
["CLOSTRIBL3_v1_13110","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"SCFA_v1_780005","_","Ca. Propionivorax syntrophicum F70","ACH1","Acetyl-CoA hydrolase","ACETYL-COA-HYDROLASE-RXN ; RHEA:20289 ;",0.97566,0.99549,47.39,{"v":4e-139,"d":"4.00E-139"},1,1,"_","3.1.2.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",10,449,452,6,442,443]
[]
["CLOSTRIBL3_v1_11114","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"SBF1_v1_6700004",null,"Desulfosporosinus sp. SbF1","etfA_2","electron-transferring flavoprotein, alpha subunit EtfA (lutD-associated)","_",0.97772,0.98259,71.65,0,1,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,395,404,1,393,402]
[null,"CD630_11720",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.9803,0.98515,63.32,0,1,1,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",1,398,404,1,394,406]
[null,"CLOSTRIBL3_v1_11487",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.81683,1.0061,45.76,{"v":9e-90,"d":"9.00E-90"},2,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",71,397,404,5,325,328]
[null,"CLOSTRIBL3_v1_20312",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.81931,0.99399,44.41,{"v":3e-89,"d":"3.00E-89"},3,5,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","c : carrier","17189250, 20059546, 21398533, 8655474, 11466286","2a : Function from experimental evidences in other organisms",71,398,404,6,333,333]
[null,"CD630_08050",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein alpha-subunit","_",0.81188,0.96471,41.77,{"v":2e-88,"d":"2.00E-88"},2,6,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","c : carrier","17941859, 2326318","2a : Function from experimental evidences in other organisms",71,394,404,15,338,340]
[null,"CD630_04010",null,"Clostridium difficile 630","etfA1","Alpha-subunit of electron transfer flavoprotein","_",0.84158,0.98551,40.59,{"v":7e-88,"d":"7.00E-88"},3,6,"4.2 : Electrochemical potential driven transporters ;","_","1 : Unknown","7 : Transport and binding proteins ;","c : carrier","20195860, 18060402, 8655474","2a : Function from experimental evidences in other organisms",67,402,404,6,341,345]
[null,"CD630_10560",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.81436,0.97917,43.77,{"v":2E-87,"d":"2.00E-87"},4,5,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",74,398,404,4,328,336]
[null,"SBF1_v1_470014",null,"Desulfosporosinus sp. SbF1","fixB","electron-transferring flavoprotein, subunit FixB","_",0.74718,0.81931,40.79,{"v":2e-81,"d":"2.00E-81"},2,5,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",69,397,404,108,436,443]
[null,"CLOSTRIBL3_v1_12010",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.82426,0.99107,39.04,{"v":1E-78,"d":"1.00E-78"},4,5,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",71,400,404,6,336,336]
[null,"BURPHP2_0598",null,"Burkholderia phymatum STM815","fixB","Protein fixB, Electron transfer flavoprotein, alpha subunit","_",0.80198,0.86631,37.65,{"v":2e-77,"d":"2.00E-77"},1,6,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ; 6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",71,390,404,32,355,374]
[null,"CLOSTRIBL3_v1_20125",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.7896,0.95796,40.13,{"v":5e-77,"d":"5.00E-77"},5,5,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",83,398,404,13,329,333]
[null,"pRALTA_0380",null,"Cupriavidus taiwanensis LMG19424","fixB","Electron transfer flavoprotein, alpha subunit","_",0.80693,0.86933,38.34,{"v":9e-77,"d":"9.00E-77"},1,5,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ;  6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",71,392,404,32,357,375]
[null,"AZOLI_0536",null,"Azospirillum lipoferum 4B","fixB","electron transfer flavoprotein alpha chain","_",0.81436,0.91643,39.82,{"v":1e-76,"d":"1.00E-76"},1,6,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ; 5.6 : Nitrogen fixation ;","c : carrier",15028689,"2a : Function from experimental evidences in other organisms",70,392,404,20,346,359]
[null,"BRADO5385",null,"Bradyrhizobium sp. ORS278","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.81683,0.89674,38.48,{"v":2e-75,"d":"2.00E-75"},1,5,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",71,397,404,28,357,368]
[null,"MGMSRv2_0361",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","Electron transfer flavoprotein, alpha subunit","_",0.81683,0.89674,36.97,{"v":3e-74,"d":"3.00E-74"},1,5,"1.4.3 : Electron carrier ;","_","1 : Unknown","5.6 : Nitrogen fixation ;","c : carrier","15028689, 3029021, 7875566, 8796346, 9163424, 8599534, 2503674","2a : Function from experimental evidences in other organisms",71,397,404,31,360,368]
[null,"MGMSRv2_1064",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.83416,0.92077,37.69,{"v":4E-73,"d":"4.00E-73"},2,6,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",67,397,404,24,358,366]
[null,"RM41v1_psym670029",null,"Sinorhizobium sp. Rm41","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.80693,0.92351,36.81,{"v":2e-68,"d":"2.00E-68"},1,6,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ; 7.1 : Cytoplasm ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ; 16.15 : Symbiosis ;","c : carrier","15028689, 3029021","1c : Function from experimental evidences in the studied genus",71,392,404,12,337,353]
[null,"SCFA_v1_500012",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",0.81931,0.99399,35.65,{"v":2E-66,"d":"2.00E-66"},1,4,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",68,397,404,6,330,333]
[]
["CLOSTRIBL3_v1_11115","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"SBF1_v1_6700003",null,"Desulfosporosinus sp. SbF1","etfB_2","electron-transferring flavoprotein, beta subunit EtfB (lutD-associated)","_",1,1.03557,75.19,{"v":7e-144,"d":"7.00E-144"},1,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,262,262,1,253,253]
[null,"CD630_11710",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein subunit alpha","_",0.98868,1,67.94,{"v":8e-132,"d":"8.00E-132"},1,1,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",1,262,262,4,265,265]
[null,"CLOSTRIBL3_v1_20124",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.95094,0.96183,44.44,{"v":6e-69,"d":"6.00E-69"},1,3,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,252,262,1,251,265]
[null,"CLOSTRIBL3_v1_12011",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1.00382,1.00382,41.44,{"v":1e-66,"d":"1.00E-66"},3,3,"1.3 : Energy metabolism (carbon) ;","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,262,262,1,262,262]
[null,"CD630_08040",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein beta-subunit, core","_",1.00758,1.01527,43.23,{"v":7e-65,"d":"7.00E-65"},2,5,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","c : carrier","17941859, 2326318","2a : Function from experimental evidences in other organisms",1,262,262,1,264,264]
[null,"CLOSTRIBL3_v1_11488",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.99623,1.00763,39.39,{"v":2e-63,"d":"2.00E-63"},4,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,262,262,1,264,265]
[null,"CD630_04000",null,"Clostridium difficile 630","etfB1","Beta-subunit of electron transfer flavoprotein","_",1.00382,1.00766,41.44,{"v":3e-63,"d":"3.00E-63"},3,5,"4.2 : Electrochemical potential driven transporters ;","_","1 : Unknown","7 : Transport and binding proteins ;","c : carrier","20195860, 18060402, 8655474","2a : Function from experimental evidences in other organisms",1,262,262,1,261,261]
[null,"CLOSTRIBL3_v1_20311",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1,1.01158,44.27,{"v":1E-61,"d":"1.00E-61"},5,4,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286, 9694853","2a : Function from experimental evidences in other organisms",1,262,262,1,259,259]
[null,"AZOLI_0535",null,"Azospirillum lipoferum 4B","fixA","electron transfer flavoprotein beta subunit","_",0.85866,0.92748,40.33,{"v":4e-60,"d":"4.00E-60"},1,5,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ; 5.6 : Nitrogen fixation ;","c : carrier",15028689,"2a : Function from experimental evidences in other organisms",1,238,262,1,242,283]
[null,"SBF1_v1_470015",null,"Desulfosporosinus sp. SbF1","fixA","electron-transferring flavoprotein, subunit FixA","_",0.90975,0.96183,41.67,{"v":2e-59,"d":"2.00E-59"},2,5,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,246,262,1,248,277]
[null,"MGMSRv2_0362",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","Electron transfer flavoprotein, beta-subunit","_",0.93662,1.01527,39.85,{"v":9e-59,"d":"9.00E-59"},1,3,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier","15028689, 3216855, 1850088, 9163424, 8369342, 8599534, 6317191, 3029021","2a : Function from experimental evidences in other organisms",1,256,262,1,266,284]
[null,"CD630_10550",null,"Clostridium difficile 630","etfB","Electron transfer flavoproteins subunit beta","_",0.98491,0.99618,42.53,{"v":1E-58,"d":"1.00E-58"},4,5,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",1,258,262,6,261,265]
[null,"BRADO5386",null,"Bradyrhizobium sp. ORS278","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.93594,1.00382,39.54,{"v":4e-58,"d":"4.00E-58"},1,4,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,256,262,1,263,281]
[null,"pRALTA_0381",null,"Cupriavidus taiwanensis LMG19424","fixA","Electron transfer flavoprotein beta-subunit","_",0.93972,1.01145,37.36,{"v":9e-57,"d":"9.00E-57"},1,4,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ;  6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",1,256,262,1,265,282]
[null,"SCFA_v1_500013",null,"Ca. Phosphitivorax anaerolimi F81","etfB","Electron transfer flavoprotein, beta subunit","_",0.97802,1.01908,40.07,{"v":1E-54,"d":"1.00E-54"},1,3,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,259,262,2,264,273]
[null,"BURPHP2_0599",null,"Burkholderia phymatum STM815","fixA","protein fixA, electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.84043,0.90458,37.97,{"v":2e-54,"d":"2.00E-54"},1,4,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ; 6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",1,232,262,1,237,282]
[null,"MGMSRv2_1063",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.93885,0.99618,38.7,{"v":4e-54,"d":"4.00E-54"},2,4,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,252,262,1,261,278]
[null,"RM41v1_psym670028",null,"Sinorhizobium sp. Rm41","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.91096,1.01527,38.35,{"v":4e-48,"d":"4.00E-48"},1,5,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ; 16.15 : Symbiosis ;","c : carrier","15028689, 16453824","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,252,262,1,262,292]
[]
["CLOSTRIBL3_v1_11486","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"SBF1_v1_6700005",null,"Desulfosporosinus sp. SbF1","lutD_2","L-lactate, D-lactate, and/or glycolate dehydrogenase, FAD-linked subunit (etfBA associated, with TM domain)","_",0.98726,0.99785,36.13,{"v":2e-97,"d":"2.00E-97"},1,3,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",10,469,471,6,464,466]
[null,"CD630_11730",null,"Clostridium difficile 630","_","Putative FAD-linked oxidase","_",0.97665,0.99352,37.83,{"v":2e-96,"d":"2.00E-96"},1,3,"_","1.1.-.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",16,469,471,10,462,463]
[null,"SBF1_v1_1830012",null,"Desulfosporosinus sp. SbF1","glcD","glycolate, D-lactate, or L-lactate dehydrogenase, FAD-linked subunit","GLYCOLATEDEHYDRO-RXN ; RHEA:21264 ;",0.98938,1.00648,36.27,{"v":1e-85,"d":"1.00E-85"},2,5,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",11,469,471,1,460,463]
[]
["CLOSTRIBL3_v1_11487","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_20312",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.97898,0.9939,50.61,{"v":1E-100,"d":"1.00E-100"},1,3,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","c : carrier","17189250, 20059546, 21398533, 8655474, 11466286","2a : Function from experimental evidences in other organisms",4,323,328,5,330,333]
[null,"CD630_08050",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein alpha-subunit","_",0.95882,0.9939,47.24,{"v":9e-94,"d":"9.00E-94"},1,5,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","c : carrier","17941859, 2326318","2a : Function from experimental evidences in other organisms",4,322,328,14,338,340]
[null,"CD630_04010",null,"Clostridium difficile 630","etfA1","Alpha-subunit of electron transfer flavoprotein","_",0.94203,0.99085,48.31,{"v":3e-93,"d":"3.00E-93"},2,5,"4.2 : Electrochemical potential driven transporters ;","_","1 : Unknown","7 : Transport and binding proteins ;","c : carrier","20195860, 18060402, 8655474","2a : Function from experimental evidences in other organisms",5,322,328,10,333,345]
[null,"CD630_11720",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.80049,0.99085,47.08,{"v":4E-90,"d":"4.00E-90"},3,4,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",4,324,328,68,392,406]
[null,"CLOSTRIBL3_v1_11114",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.81683,1.0061,45.76,{"v":8E-90,"d":"8.00E-90"},2,2,"_","_","2 : Cytoplasmic","_","c : carrier",17189250,"2a : Function from experimental evidences in other organisms",5,325,328,71,397,404]
[null,"SBF1_v1_6700004",null,"Desulfosporosinus sp. SbF1","etfA_2","electron-transferring flavoprotein, alpha subunit EtfA (lutD-associated)","_",0.80597,0.9878,46.91,{"v":1e-86,"d":"1.00E-86"},1,3,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",5,324,328,71,394,402]
[null,"CLOSTRIBL3_v1_20125",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.97898,0.9939,47.85,{"v":3e-86,"d":"3.00E-86"},4,4,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",6,323,328,2,326,333]
[null,"CLOSTRIBL3_v1_12010",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.98214,1.0061,43.33,{"v":5e-82,"d":"5.00E-82"},5,4,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",3,324,328,4,332,336]
[null,"BURPHP2_0598",null,"Burkholderia phymatum STM815","fixB","Protein fixB, Electron transfer flavoprotein, alpha subunit","_",0.87166,0.9939,44.48,{"v":5E-80,"d":"5.00E-80"},1,5,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ; 6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",3,318,328,30,355,374]
[null,"CD630_10560",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.96131,0.98476,44.89,{"v":1E-78,"d":"1.00E-78"},4,6,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",8,322,328,4,324,336]
[null,"BRADO5385",null,"Bradyrhizobium sp. ORS278","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.89674,1.0061,41.52,{"v":7e-77,"d":"7.00E-77"},1,4,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",3,323,328,26,355,368]
[null,"AZOLI_0536",null,"Azospirillum lipoferum 4B","fixB","electron transfer flavoprotein alpha chain","_",0.93593,1.02439,42.26,{"v":9e-77,"d":"9.00E-77"},1,5,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ; 5.6 : Nitrogen fixation ;","c : carrier",15028689,"2a : Function from experimental evidences in other organisms",3,328,328,19,354,359]
[null,"pRALTA_0380",null,"Cupriavidus taiwanensis LMG19424","fixB","Electron transfer flavoprotein, alpha subunit","_",0.86933,0.9939,43.56,{"v":2e-75,"d":"2.00E-75"},1,6,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ;  6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",3,318,328,30,355,375]
[null,"MGMSRv2_1064",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.90437,1.00915,39.88,{"v":1e-74,"d":"1.00E-74"},1,5,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",5,325,328,28,358,366]
[null,"MGMSRv2_0361",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","Electron transfer flavoprotein, alpha subunit","_",0.91033,1.02134,37.91,{"v":3e-73,"d":"3.00E-73"},2,6,"1.4.3 : Electron carrier ;","_","1 : Unknown","5.6 : Nitrogen fixation ;","c : carrier","15028689, 3029021, 7875566, 8796346, 9163424, 8599534, 2503674","2a : Function from experimental evidences in other organisms",3,328,328,29,363,368]
[null,"SBF1_v1_470014",null,"Desulfosporosinus sp. SbF1","fixB","electron-transferring flavoprotein, subunit FixB","_",0.73815,0.99695,40.06,{"v":3E-68,"d":"3.00E-68"},3,6,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,325,328,110,436,443]
[null,"SCFA_v1_500012",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",0.99399,1.00915,37.46,{"v":5e-64,"d":"5.00E-64"},1,5,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,325,328,1,330,333]
[]
["CLOSTRIBL3_v1_11488","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_20124",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.96226,0.96226,45.49,{"v":5E-71,"d":"5.00E-71"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,255,265,1,252,265]
[null,"CD630_08040",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein beta-subunit, core","_",1.00755,1.01136,44.57,{"v":5e-69,"d":"5.00E-69"},1,4,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","c : carrier","17941859, 2326318","2a : Function from experimental evidences in other organisms",1,264,265,1,264,264]
[null,"SBF1_v1_6700003",null,"Desulfosporosinus sp. SbF1","etfB_2","electron-transferring flavoprotein, beta subunit EtfB (lutD-associated)","_",0.86792,0.90909,43.91,{"v":4e-64,"d":"4.00E-64"},1,5,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,230,265,1,229,253]
[null,"CLOSTRIBL3_v1_11115",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.99623,1.00763,39.39,{"v":2e-63,"d":"2.00E-63"},2,4,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,264,265,1,262,262]
[null,"CD630_11710",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein subunit alpha","_",0.99623,0.99623,42.42,{"v":2e-63,"d":"2.00E-63"},2,4,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",1,264,265,4,265,265]
[null,"CLOSTRIBL3_v1_12011",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.96226,0.97328,42.75,{"v":4e-63,"d":"4.00E-63"},3,5,"1.3 : Energy metabolism (carbon) ;","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,255,265,1,252,262]
[null,"CD630_04000",null,"Clostridium difficile 630","etfB1","Beta-subunit of electron transfer flavoprotein","_",1,1.01533,39.62,{"v":2e-59,"d":"2.00E-59"},3,6,"4.2 : Electrochemical potential driven transporters ;","_","1 : Unknown","7 : Transport and binding proteins ;","c : carrier","20195860, 18060402, 8655474","2a : Function from experimental evidences in other organisms",1,264,265,1,261,261]
[null,"CLOSTRIBL3_v1_20311",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1,1.02317,40,{"v":2e-57,"d":"2.00E-57"},4,5,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286, 9694853","2a : Function from experimental evidences in other organisms",1,264,265,1,259,259]
[null,"CD630_10550",null,"Clostridium difficile 630","etfB","Electron transfer flavoproteins subunit beta","_",1,1,39.62,{"v":3e-55,"d":"3.00E-55"},4,6,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",1,264,265,6,265,265]
[null,"SBF1_v1_470015",null,"Desulfosporosinus sp. SbF1","fixA","electron-transferring flavoprotein, subunit FixA","_",0.85199,0.89057,41.1,{"v":1E-54,"d":"1.00E-54"},2,6,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,233,265,1,234,277]
[null,"BRADO5386",null,"Bradyrhizobium sp. ORS278","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.9573,1.01509,36.43,{"v":6E-49,"d":"6.00E-49"},1,6,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,261,265,1,267,281]
[null,"AZOLI_0535",null,"Azospirillum lipoferum 4B","fixA","electron transfer flavoprotein beta subunit","_",0.87986,0.93962,37.75,{"v":1e-47,"d":"1.00E-47"},1,6,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ; 5.6 : Nitrogen fixation ;","c : carrier",15028689,"2a : Function from experimental evidences in other organisms",1,242,265,1,245,283]
[null,"MGMSRv2_1063",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.92446,0.96981,36.58,{"v":2E-46,"d":"2.00E-46"},1,6,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,245,265,1,256,278]
[null,"MGMSRv2_0362",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","Electron transfer flavoprotein, beta-subunit","_",0.87676,0.93962,37.75,{"v":3e-45,"d":"3.00E-45"},2,6,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier","15028689, 3216855, 1850088, 9163424, 8369342, 8599534, 6317191, 3029021","2a : Function from experimental evidences in other organisms",1,242,265,1,247,284]
[null,"pRALTA_0381",null,"Cupriavidus taiwanensis LMG19424","fixA","Electron transfer flavoprotein beta-subunit","_",0.95035,1.01132,35.07,{"v":5e-43,"d":"5.00E-43"},1,6,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ;  6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",1,255,265,1,262,282]
[null,"BURPHP2_0599",null,"Burkholderia phymatum STM815","fixA","protein fixA, electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.8617,0.91698,37.04,{"v":3e-42,"d":"3.00E-42"},1,6,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ; 6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",1,233,265,1,237,282]
[null,"SCFA_v1_500013",null,"Ca. Phosphitivorax anaerolimi F81","etfB","Electron transfer flavoprotein, beta subunit","_",0.96703,0.99623,35.23,{"v":3e-40,"d":"3.00E-40"},1,6,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,261,265,2,260,273]
[]
["CLOSTRIBL3_v1_12010","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_20312",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.99405,1.003,50.3,{"v":2e-111,"d":"2.00E-111"},2,2,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","c : carrier","17189250, 20059546, 21398533, 8655474, 11466286","2a : Function from experimental evidences in other organisms",1,334,336,1,333,333]
[null,"CD630_04010",null,"Clostridium difficile 630","etfA1","Alpha-subunit of electron transfer flavoprotein","_",0.95942,0.98512,48.94,{"v":1E-107,"d":"1.00E-107"},1,3,"4.2 : Electrochemical potential driven transporters ;","_","1 : Unknown","7 : Transport and binding proteins ;","c : carrier","20195860, 18060402, 8655474","2a : Function from experimental evidences in other organisms",6,336,336,10,339,345]
[null,"CD630_08050",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein alpha-subunit","_",0.97059,0.98214,44.55,{"v":1e-98,"d":"1.00E-98"},2,3,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","c : carrier","17941859, 2326318","2a : Function from experimental evidences in other organisms",1,330,336,10,338,340]
[null,"pRALTA_0380",null,"Cupriavidus taiwanensis LMG19424","fixB","Electron transfer flavoprotein, alpha subunit","_",0.864,0.96429,45.06,{"v":1e-95,"d":"1.00E-95"},1,2,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ;  6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",6,326,336,32,355,375]
[null,"SBF1_v1_470014",null,"Desulfosporosinus sp. SbF1","fixB","electron-transferring flavoprotein, subunit FixB","_",0.73589,0.97024,46.32,{"v":3e-95,"d":"3.00E-95"},1,3,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,331,336,110,434,443]
[null,"BURPHP2_0598",null,"Burkholderia phymatum STM815","fixB","Protein fixB, Electron transfer flavoprotein, alpha subunit","_",0.86631,0.96429,43.52,{"v":1e-92,"d":"1.00E-92"},1,2,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ; 6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",6,326,336,32,355,374]
[null,"MGMSRv2_0361",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","Electron transfer flavoprotein, alpha subunit","_",0.90217,0.9881,42.47,{"v":8e-91,"d":"8.00E-91"},1,3,"1.4.3 : Electron carrier ;","_","1 : Unknown","5.6 : Nitrogen fixation ;","c : carrier","15028689, 3029021, 7875566, 8796346, 9163424, 8599534, 2503674","2a : Function from experimental evidences in other organisms",3,331,336,28,358,368]
[null,"BRADO5385",null,"Bradyrhizobium sp. ORS278","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.90489,0.99107,43.84,{"v":1e-90,"d":"1.00E-90"},1,3,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",3,332,336,25,356,368]
[null,"CD630_10560",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.97321,0.97321,43.73,{"v":6e-90,"d":"6.00E-90"},3,4,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",8,334,336,3,328,336]
[null,"CLOSTRIBL3_v1_20125",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.97917,0.98799,42.55,{"v":9e-88,"d":"9.00E-88"},3,3,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",7,334,336,2,329,333]
[null,"MGMSRv2_1064",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.89891,0.97917,40.43,{"v":5e-87,"d":"5.00E-87"},2,3,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",6,331,336,28,356,366]
[null,"SBF1_v1_550002",null,"Desulfosporosinus sp. SbF1","etfA","electron-transferring flavoprotein, alpha subunit EtfA","_",0.97321,0.99695,42.51,{"v":3e-85,"d":"3.00E-85"},2,3,"_","_","2 : Cytoplasmic","_","c : carrier",23468890,"2a : Function from experimental evidences in other organisms",7,333,336,3,326,328]
[null,"RM41v1_psym670029",null,"Sinorhizobium sp. Rm41","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.92918,0.97619,42.68,{"v":2e-84,"d":"2.00E-84"},1,3,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ; 7.1 : Cytoplasm ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ; 16.15 : Symbiosis ;","c : carrier","15028689, 3029021","1c : Function from experimental evidences in the studied genus",3,326,336,9,335,353]
[null,"CLOSTRIBL3_v1_11487",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.98214,1.0061,43.33,{"v":5e-82,"d":"5.00E-82"},4,5,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",4,332,336,3,324,328]
[null,"AZOLI_0536",null,"Azospirillum lipoferum 4B","fixB","electron transfer flavoprotein alpha chain","_",0.90251,0.96429,41.36,{"v":2e-81,"d":"2.00E-81"},1,3,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ; 5.6 : Nitrogen fixation ;","c : carrier",15028689,"2a : Function from experimental evidences in other organisms",6,326,336,21,344,359]
[null,"SCFA_v1_130009",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",0.97024,1.01242,42.94,{"v":7e-79,"d":"7.00E-79"},1,2,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",11,334,336,6,321,322]
[null,"CLOSTRIBL3_v1_11114",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.82426,0.99107,39.04,{"v":1E-78,"d":"1.00E-78"},5,4,"_","_","2 : Cytoplasmic","_","c : carrier",17189250,"2a : Function from experimental evidences in other organisms",6,336,336,71,400,404]
[null,"CD630_11720",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.81773,0.9881,37.05,{"v":2E-78,"d":"2.00E-78"},4,5,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",4,335,336,67,395,406]
[null,"SBF1_v1_6700004",null,"Desulfosporosinus sp. SbF1","etfA_2","electron-transferring flavoprotein, alpha subunit EtfA (lutD-associated)","_",0.81095,0.97024,39.88,{"v":2e-77,"d":"2.00E-77"},3,5,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",6,331,336,71,393,402]
[null,"LEPBIa1132","_","Leptospira biflexa serovar Patoc Patoc 1","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.97024,1.02194,41.1,{"v":1e-74,"d":"1.00E-74"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","16.10 : Respire ;","c : carrier","_","2a : Function from experimental evidences in other organisms",8,333,336,3,317,319]
[null,"FRAAL5877",null,"Frankia alni ACN14a","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.97321,1.02188,39.14,{"v":1e-66,"d":"1.00E-66"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","16.1 : Circulate ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,334,336,3,318,320]
[null,"SCFA_v1_500012",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",0.97619,0.98498,35.37,{"v":3e-63,"d":"3.00E-63"},2,6,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,331,336,3,328,333]
[null,"BN45v3_60005","_","Mycobacterium canettii STB-J","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97321,1.0283,37.92,{"v":2e-61,"d":"2.00E-61"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",8,334,336,3,317,318]
[null,"BN43v3_60007","_","Mycobacterium canettii STB-L","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97321,1.0283,37.92,{"v":2e-61,"d":"2.00E-61"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",8,334,336,3,317,318]
[null,"BN44v3_60522","_","Mycobacterium canettii STB-D","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97321,1.0283,37.31,{"v":6e-61,"d":"6.00E-61"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",8,334,336,3,317,318]
[null,"BN42v3_41031","_","Mycobacterium canettii STB-K","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97321,1.0283,37.31,{"v":1e-60,"d":"1.00E-60"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",8,334,336,3,317,318]
[null,"MARHY1802","_","Marinobacter hydrocarbonoclasticus ATCC 49840","etfA","electron transfer flavoprotein alpha-subunit","_",0.82143,0.88179,40.22,{"v":4e-57,"d":"4.00E-57"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6 : Energy metabolism ;","c : carrier",3415685,"2a : Function from experimental evidences in other organisms",58,333,336,49,312,313]
[null,"HEAR0620","_","Herminiimonas arsenicoxydans","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.81845,0.88997,41.09,{"v":1E-53,"d":"1.00E-53"},1,1,"1.4.3 : electron carrier ;","_","1 : Unknown","6 : Energy metabolism ;","c : carrier","10026281, 1576992, 8376381, 8599534","2a : Function from experimental evidences in other organisms",56,330,336,47,308,309]
[null,"AZOLI_0089",null,"Azospirillum lipoferum 4B","etfA3","Electron transfer flavoprotein alpha-subunit","_",0.8244,0.89935,38.27,{"v":8e-51,"d":"8.00E-51"},2,2,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",54,330,336,45,308,308]
[null,"BURPHK2_1883",null,"Burkholderia phymatum STM815","etfA","electron transfer flavoprotein, alpha subunit","_",0.87798,0.94551,39.32,{"v":3e-50,"d":"3.00E-50"},1,2,"1.4.3 : Electron carrier ;","_","1 : Unknown","4 : Biosynthesis of cofactors, prosthetic groups, and carriers ;","c : carrier",10026281,"2a : Function from experimental evidences in other organisms",35,326,336,25,306,312]
[null,"METDI2208",null,"Methylobacterium extorquens DM4","etfA","electron transfer flavoprotein, NAD/FAD-binding domain and ETFP adenine nucleotide-binding domain-like","_",0.97321,1.03155,36.09,{"v":5e-50,"d":"5.00E-50"},1,2,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","15188393, 16926146, 8599534","2a : Function from experimental evidences in other organisms",11,335,336,5,316,317]
[null,"Mchl_1823",null,"Methylobacterium extorquens CM4","etfA","electron transfer flavoprotein alpha subunit","_",0.97321,1.03155,36.7,{"v":7e-50,"d":"7.00E-50"},1,2,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","15188393, 16926146, 8599534","2a : Function from experimental evidences in other organisms",11,335,336,5,316,317]
[null,"PSEEN3657","_","Pseudomonas entomophila L48","etfA","electron transfer flavoprotein alpha-subunit","_",0.8244,1.00362,40.07,{"v":4e-48,"d":"4.00E-48"},1,1,"1.4.3 : Electron carrier ;","_","Unknown","6 : Energy metabolism ;","c : carrier","_","2a : Function from experimental evidences in other organisms",54,330,336,12,276,276]
[null,"NT26v4_3414",null,"Rhizobium sp. NT-26","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.84524,0.91909,38.73,{"v":4e-45,"d":"4.00E-45"},1,2,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",45,326,336,35,305,309]
[null,"VIBNIv4_B0455",null,"Vibrio nigripulchritudo SFn1","etfA","Electron transfer flavoprotein subunit alpha","_",0.8631,0.93548,35.86,{"v":2e-42,"d":"2.00E-42"},1,4,"1.4.1 : Electron donor ;","_","1 : Unknown","5.8 : Electron carrier regeneration ;","c : carrier","8599534, 12597275","2a : Function from experimental evidences in other organisms",46,332,336,34,309,310]
[]
["CLOSTRIBL3_v1_12011","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_08040",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein beta-subunit, core","_",1.00379,1.01145,50.94,{"v":2E-90,"d":"2.00E-90"},1,3,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","c : carrier","17941859, 2326318","2a : Function from experimental evidences in other organisms",1,262,262,1,264,264]
[null,"CLOSTRIBL3_v1_20311",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1,1.01158,49.62,{"v":1e-80,"d":"1.00E-80"},2,2,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286, 9694853","2a : Function from experimental evidences in other organisms",1,262,262,1,259,259]
[null,"SBF1_v1_470015",null,"Desulfosporosinus sp. SbF1","fixA","electron-transferring flavoprotein, subunit FixA","_",0.9639,1.01908,45.32,{"v":6e-78,"d":"6.00E-78"},1,1,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,262,262,1,266,277]
[null,"CD630_04000",null,"Clostridium difficile 630","etfB1","Beta-subunit of electron transfer flavoprotein","_",0.97328,0.97701,47.45,{"v":6e-78,"d":"6.00E-78"},2,3,"4.2 : Electrochemical potential driven transporters ;","_","1 : Unknown","7 : Transport and binding proteins ;","c : carrier","20195860, 18060402, 8655474","2a : Function from experimental evidences in other organisms",1,254,262,1,254,261]
[null,"CD630_10550",null,"Clostridium difficile 630","etfB","Electron transfer flavoproteins subunit beta","_",0.98868,1,44.66,{"v":2E-73,"d":"2.00E-73"},3,3,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",1,262,262,6,265,265]
[null,"pRALTA_0381",null,"Cupriavidus taiwanensis LMG19424","fixA","Electron transfer flavoprotein beta-subunit","_",0.94326,1.01527,43.98,{"v":4E-73,"d":"4.00E-73"},1,1,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ;  6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",1,257,262,1,266,282]
[null,"BURPHP2_0599",null,"Burkholderia phymatum STM815","fixA","protein fixA, electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.87943,0.94656,45.16,{"v":9e-71,"d":"9.00E-71"},1,1,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ; 6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",1,241,262,1,248,282]
[null,"MGMSRv2_0362",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","Electron transfer flavoprotein, beta-subunit","_",0.90141,0.9771,44.92,{"v":3e-69,"d":"3.00E-69"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier","15028689, 3216855, 1850088, 9163424, 8369342, 8599534, 6317191, 3029021","2a : Function from experimental evidences in other organisms",1,248,262,1,256,284]
[null,"AZOLI_0535",null,"Azospirillum lipoferum 4B","fixA","electron transfer flavoprotein beta subunit","_",0.85159,0.91985,47.72,{"v":5e-68,"d":"5.00E-68"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ; 5.6 : Nitrogen fixation ;","c : carrier",15028689,"2a : Function from experimental evidences in other organisms",1,232,262,1,237,283]
[null,"CLOSTRIBL3_v1_11115",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1.00382,1.00382,41.44,{"v":1e-66,"d":"1.00E-66"},3,3,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,262,262,1,262,262]
[null,"BRADO5386",null,"Bradyrhizobium sp. ORS278","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.93594,1.00382,41.83,{"v":2E-66,"d":"2.00E-66"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,256,262,1,263,281]
[null,"MGMSRv2_1063",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.94245,1,43.13,{"v":3e-66,"d":"3.00E-66"},2,2,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,253,262,1,262,278]
[null,"SBF1_v1_6700003",null,"Desulfosporosinus sp. SbF1","etfB_2","electron-transferring flavoprotein, beta subunit EtfB (lutD-associated)","_",0.87786,0.90909,45.22,{"v":2e-65,"d":"2.00E-65"},2,4,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,229,262,1,230,253]
[null,"CLOSTRIBL3_v1_20124",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.95472,0.96565,41.11,{"v":4e-64,"d":"4.00E-64"},4,4,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,252,262,1,252,265]
[null,"CLOSTRIBL3_v1_11488",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.96226,0.97328,42.75,{"v":4e-63,"d":"4.00E-63"},5,3,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,252,262,1,255,265]
[null,"RM41v1_psym670028",null,"Sinorhizobium sp. Rm41","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.86301,0.96183,42.06,{"v":1E-61,"d":"1.00E-61"},1,1,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ; 16.15 : Symbiosis ;","c : carrier","15028689, 16453824","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,244,262,1,252,292]
[null,"CD630_11710",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein subunit alpha","_",0.99245,1.00382,39.54,{"v":4e-60,"d":"4.00E-60"},4,5,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",1,262,262,4,265,265]
[null,"SCFA_v1_500013",null,"Ca. Phosphitivorax anaerolimi F81","etfB","Electron transfer flavoprotein, beta subunit","_",0.94139,0.98092,35.8,{"v":6E-51,"d":"6.00E-51"},1,5,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,255,262,2,256,273]
[null,"FRAAL5878",null,"Frankia alni ACN14a","fixA","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.9313,0.93487,38.93,{"v":1e-47,"d":"1.00E-47"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","16.1 : Circulate ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,241,262,1,242,261]
[null,"SCFA_v1_130010",null,"Ca. Phosphitivorax anaerolimi F81","etfB","Electron transfer flavoprotein subunit beta","_",1.00763,1.02326,36.74,{"v":7e-44,"d":"7.00E-44"},2,2,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,258,262,1,253,258]
[null,"SBF1_v1_550001",null,"Desulfosporosinus sp. SbF1","etfB","electron-transferring flavoprotein, beta subunit EtfB","_",0.79389,0.80934,36.06,{"v":2E-41,"d":"2.00E-41"},3,2,"_","_","2 : Cytoplasmic","_","c : carrier",23468890,"2a : Function from experimental evidences in other organisms",1,208,262,1,207,257]
[null,"SCFA_v1_1080001",null,"Ca. Phosphitivorax butyraticus R76","etfB","Electron transfer flavoprotein subunit beta (fragment)","_",0.67939,0.98343,37.64,{"v":9e-39,"d":"9.00E-39"},2,5,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,177,262,2,179,181]
[null,"AZOLI_p50299","_","Azospirillum lipoferum 4B","etfB2","Electron transfer flavoprotein beta-subunit","_",0.78626,0.85833,36.41,{"v":2e-30,"d":"2.00E-30"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier","12597275, 16303747, 17449609, 8599534","2b : Function from indirect experimental evidences (e.g. phenotypes)",34,235,262,26,219,240]
[null,"AZOLI_0088",null,"Azospirillum lipoferum 4B","etfB3","Electron transfer flavoprotein beta-subunit","_",0.82824,0.87149,35.02,{"v":4e-30,"d":"4.00E-30"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,214,262,1,212,249]
[null,"NT26v4_3413",null,"Rhizobium sp. NT-26","etfB","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.78244,0.82329,35.12,{"v":1e-29,"d":"1.00E-29"},1,2,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6 : Energy metabolism ;","c : carrier",8599534,"2a : Function from experimental evidences in other organisms",1,202,262,1,201,249]
[null,"BN77v1_0452","_","Rhizobium mesoamericanum STM3625","etfB","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.65649,0.86,40.12,{"v":2e-25,"d":"2.00E-25"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier",10026281,"2a : Function from experimental evidences in other organisms",1,167,262,34,199,200]
[]
["CLOSTRIBL3_v1_20124","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_11488",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.96226,0.96226,45.49,{"v":5E-71,"d":"5.00E-71"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,252,265,1,255,265]
[null,"CLOSTRIBL3_v1_20311",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.89811,0.91892,46.64,{"v":6e-71,"d":"6.00E-71"},2,3,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286, 9694853","2a : Function from experimental evidences in other organisms",1,238,265,1,236,259]
[null,"CD630_04000",null,"Clostridium difficile 630","etfB1","Beta-subunit of electron transfer flavoprotein","_",0.95472,0.96935,42.29,{"v":4e-69,"d":"4.00E-69"},1,4,"4.2 : Electrochemical potential driven transporters ;","_","1 : Unknown","7 : Transport and binding proteins ;","c : carrier","20195860, 18060402, 8655474","2a : Function from experimental evidences in other organisms",1,252,265,1,252,261]
[null,"CLOSTRIBL3_v1_11115",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.95094,0.96183,44.44,{"v":6e-69,"d":"6.00E-69"},3,1,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,251,265,1,252,262]
[null,"SBF1_v1_6700003",null,"Desulfosporosinus sp. SbF1","etfB_2","electron-transferring flavoprotein, beta subunit EtfB (lutD-associated)","_",0.86415,0.90514,44.54,{"v":3e-66,"d":"3.00E-66"},1,2,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,228,265,1,229,253]
[null,"CD630_11710",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein subunit alpha","_",0.87925,0.87925,43.35,{"v":3E-65,"d":"3.00E-65"},2,3,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",1,232,265,4,236,265]
[null,"CD630_10550",null,"Clostridium difficile 630","etfB","Electron transfer flavoproteins subunit beta","_",1.00377,1.00377,44.36,{"v":2e-64,"d":"2.00E-64"},3,4,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",1,265,265,6,265,265]
[null,"CD630_08040",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein beta-subunit, core","_",0.96604,0.9697,40.62,{"v":3e-64,"d":"3.00E-64"},4,6,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","c : carrier","17941859, 2326318","2a : Function from experimental evidences in other organisms",1,252,265,1,255,264]
[null,"CLOSTRIBL3_v1_12011",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.95472,0.96565,41.11,{"v":4e-64,"d":"4.00E-64"},4,4,"1.3 : Energy metabolism (carbon) ;","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,252,265,1,252,262]
[null,"AZOLI_0535",null,"Azospirillum lipoferum 4B","fixA","electron transfer flavoprotein beta subunit","_",0.89753,0.95849,39.37,{"v":3e-60,"d":"3.00E-60"},1,4,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ; 5.6 : Nitrogen fixation ;","c : carrier",15028689,"2a : Function from experimental evidences in other organisms",1,249,265,1,254,283]
[null,"SBF1_v1_470015",null,"Desulfosporosinus sp. SbF1","fixA","electron-transferring flavoprotein, subunit FixA","_",0.84477,0.88302,42.31,{"v":2e-59,"d":"2.00E-59"},2,4,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,231,265,1,234,277]
[null,"pRALTA_0381",null,"Cupriavidus taiwanensis LMG19424","fixA","Electron transfer flavoprotein beta-subunit","_",0.87943,0.93585,38.71,{"v":3e-56,"d":"3.00E-56"},1,5,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ;  6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",1,242,265,1,246,282]
[null,"BRADO5386",null,"Bradyrhizobium sp. ORS278","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.879,0.93208,39.27,{"v":8e-54,"d":"8.00E-54"},1,5,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,240,265,1,247,281]
[null,"BURPHP2_0599",null,"Burkholderia phymatum STM815","fixA","protein fixA, electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.84043,0.89434,38.4,{"v":3e-53,"d":"3.00E-53"},1,5,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ; 6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",1,231,265,1,237,282]
[null,"MGMSRv2_1063",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.92806,0.97358,37.6,{"v":5E-52,"d":"5.00E-52"},1,5,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,248,265,1,257,278]
[null,"MGMSRv2_0362",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","Electron transfer flavoprotein, beta-subunit","_",0.84155,0.90189,39.75,{"v":6E-52,"d":"6.00E-52"},2,5,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier","15028689, 3216855, 1850088, 9163424, 8369342, 8599534, 6317191, 3029021","2a : Function from experimental evidences in other organisms",1,232,265,1,239,284]
[null,"SCFA_v1_500013",null,"Ca. Phosphitivorax anaerolimi F81","etfB","Electron transfer flavoprotein, beta subunit","_",0.87179,0.89811,37.82,{"v":2E-51,"d":"2.00E-51"},1,4,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,236,265,2,238,273]
[null,"RM41v1_psym670028",null,"Sinorhizobium sp. Rm41","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.81507,0.89811,38.24,{"v":4e-49,"d":"4.00E-49"},1,4,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ; 16.15 : Symbiosis ;","c : carrier","15028689, 16453824","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,231,265,1,238,292]
[null,"FRAAL5878",null,"Frankia alni ACN14a","fixA","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.86038,0.87356,35.96,{"v":2E-41,"d":"2.00E-41"},1,4,"1.4.3 : Electron carrier ;","_","1 : Unknown","16.1 : Circulate ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,226,265,1,227,261]
[]
["CLOSTRIBL3_v1_20125","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_20312",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.98498,0.98498,46.95,{"v":4e-100,"d":"4.00E-100"},1,4,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","c : carrier","17189250, 20059546, 21398533, 8655474, 11466286","2a : Function from experimental evidences in other organisms",2,329,333,7,333,333]
[null,"CD630_04010",null,"Clostridium difficile 630","etfA1","Alpha-subunit of electron transfer flavoprotein","_",0.93333,0.96697,47.83,{"v":1E-99,"d":"1.00E-99"},1,4,"4.2 : Electrochemical potential driven transporters ;","_","1 : Unknown","7 : Transport and binding proteins ;","c : carrier","20195860, 18060402, 8655474","2a : Function from experimental evidences in other organisms",2,323,333,11,331,345]
[null,"CD630_08050",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein alpha-subunit","_",0.95294,0.97297,45.68,{"v":2E-95,"d":"2.00E-95"},2,4,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","c : carrier","17941859, 2326318","2a : Function from experimental evidences in other organisms",4,325,333,18,338,340]
[null,"SBF1_v1_470014",null,"Desulfosporosinus sp. SbF1","fixB","electron-transferring flavoprotein, subunit FixB","_",0.74041,0.98498,45.12,{"v":3e-91,"d":"3.00E-91"},1,4,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,331,333,113,436,443]
[null,"CD630_10560",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.98512,0.99399,44.11,{"v":4E-90,"d":"4.00E-90"},3,3,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",1,331,333,1,330,336]
[null,"CLOSTRIBL3_v1_12010",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.97917,0.98799,42.55,{"v":8e-88,"d":"8.00E-88"},3,3,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",2,329,333,7,334,336]
[null,"CLOSTRIBL3_v1_11487",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.97898,0.9939,47.85,{"v":3e-86,"d":"3.00E-86"},4,4,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",2,326,333,6,323,328]
[null,"MGMSRv2_0361",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","Electron transfer flavoprotein, alpha subunit","_",0.8913,0.98498,41.77,{"v":3e-83,"d":"3.00E-83"},1,4,"1.4.3 : Electron carrier ;","_","1 : Unknown","5.6 : Nitrogen fixation ;","c : carrier","15028689, 3029021, 7875566, 8796346, 9163424, 8599534, 2503674","2a : Function from experimental evidences in other organisms",2,326,333,32,358,368]
[null,"MGMSRv2_1064",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.89344,0.98198,40.67,{"v":2e-80,"d":"2.00E-80"},2,4,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",4,327,333,31,357,366]
[null,"AZOLI_0536",null,"Azospirillum lipoferum 4B","fixB","electron transfer flavoprotein alpha chain","_",0.90529,0.97598,42.46,{"v":4e-80,"d":"4.00E-80"},1,4,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ; 5.6 : Nitrogen fixation ;","c : carrier",15028689,"2a : Function from experimental evidences in other organisms",2,321,333,22,344,359]
[null,"BURPHP2_0598",null,"Burkholderia phymatum STM815","fixB","Protein fixB, Electron transfer flavoprotein, alpha subunit","_",0.86364,0.96997,42.11,{"v":4e-80,"d":"4.00E-80"},1,4,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ; 6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",4,321,333,35,355,374]
[null,"pRALTA_0380",null,"Cupriavidus taiwanensis LMG19424","fixB","Electron transfer flavoprotein, alpha subunit","_",0.88,0.99099,40.3,{"v":1e-77,"d":"1.00E-77"},1,4,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ;  6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",2,328,333,33,362,375]
[null,"CLOSTRIBL3_v1_11114",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.7896,0.95796,40.13,{"v":4e-77,"d":"4.00E-77"},5,5,"_","_","2 : Cytoplasmic","_","c : carrier",17189250,"2a : Function from experimental evidences in other organisms",13,329,333,83,398,404]
[null,"SBF1_v1_6700004",null,"Desulfosporosinus sp. SbF1","etfA_2","electron-transferring flavoprotein, alpha subunit EtfA (lutD-associated)","_",0.79353,0.95796,40.44,{"v":2e-75,"d":"2.00E-75"},2,6,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",13,331,333,83,398,402]
[null,"SCFA_v1_500012",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",0.97898,0.97898,36.2,{"v":3e-75,"d":"3.00E-75"},1,3,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,327,333,6,329,333]
[null,"BRADO5385",null,"Bradyrhizobium sp. ORS278","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.8913,0.98498,40.24,{"v":7e-75,"d":"7.00E-75"},1,6,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",2,326,333,29,355,368]
[null,"RM41v1_psym670029",null,"Sinorhizobium sp. Rm41","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.91785,0.97297,40.12,{"v":7e-75,"d":"7.00E-75"},1,4,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ; 7.1 : Cytoplasm ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ; 16.15 : Symbiosis ;","c : carrier","15028689, 3029021","1c : Function from experimental evidences in the studied genus",2,321,333,13,335,353]
[null,"CD630_11720",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.7931,0.96697,37.58,{"v":9e-73,"d":"9.00E-73"},4,6,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",9,329,333,77,394,406]
[null,"FRAAL5877",null,"Frankia alni ACN14a","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.99099,1.03125,36.97,{"v":5e-59,"d":"5.00E-59"},1,4,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","16.1 : Circulate ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,329,333,1,318,320]
[]
["CLOSTRIBL3_v1_10629","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"SCFA_v1_420042",null,"Ca. Phosphitivorax anaerolimi F81","rnfC","Electron transport complex subunit RnfC","_",0.96061,1.00688,54.67,{"v":2e-172,"d":"2.00E-172"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,439,457,1,436,436]
[null,"SCFA_v1_1220012",null,"Ca. Phosphitivorax butyraticus R76","rnfC","Electron transport complex subunit RnfC","_",0.9628,1.00228,53.86,{"v":4e-171,"d":"4.00E-171"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,440,457,1,437,439]
[null,"NBG4_v1_240018",null,"Candidatus Sulfobium mesophilum","rnfC","Electron transport complex protein RnfC","_",0.94311,0.9908,55.45,{"v":3e-161,"d":"3.00E-161"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 21747791","2a : Function from experimental evidences in other organisms",2,430,457,3,431,435]
[null,"CD630_11370",null,"Clostridium difficile 630","rnfC","Electron transport complex protein","_",0.97155,0.99775,49.1,{"v":1E-150,"d":"1.00E-150"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 12773378, 11160111","2a : Function from experimental evidences in other organisms",2,442,457,3,444,445]
[null,"MAGMOv5_3971",null,"Magnetotactic ovoidal bacterium MO-1","rnfC","Electron transport complex protein rnfC. 4Fe-4S","_",0.75484,1.02407,44.02,{"v":2e-133,"d":"2.00E-133"},1,1,"6.1 : Membrane ; 7.3 : Inner membrane ;","_","6 : Inner membrane-associated","6 : Energy metabolism ;","c : carrier",9492268,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,457,457,7,471,620]
[null,"MARHY2352",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","rnfC","Electron transport complex, RnfABCDGE type, C subunit. Required for the reduction of SoxR","_",0.76355,1.01751,41.08,{"v":1e-122,"d":"1.00E-122"},1,1,"_","_","11 : Membrane","_","t : transporter","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,457,457,4,466,609]
[null,"MALCv4_3938",null,"Methylomicrobium alcaliphilum 20Z","rnfC","electron transport complex protein RnfC","_",0.94092,0.96413,41.16,{"v":4e-113,"d":"4.00E-113"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8264535,"2b : Function from indirect experimental evidences (e.g. phenotypes)",4,429,457,8,433,446]
[null,"PSHAa1103",null,"Pseudoalteromonas haloplanktis TAC125","rsxC","Electron transport complex protein rnfC","_",0.54728,1.01313,40.39,{"v":2e-104,"d":"2.00E-104"},1,1,"1.4.2 : Electron transport ;","_","inner membrane associated","_","t : transporter","_","2a : Function from experimental evidences in other organisms",1,457,457,12,469,846]
[null,"VIBNIv4_A0907",null,"Vibrio nigripulchritudo SFn1","_","putative Electron transport complex protein rnfC","_",0.45034,1.00219,39.52,{"v":4e-101,"d":"4.00E-101"},1,1,"1.4.3 : Electron carrier ; 7.5 : Extracellular ;","_","10 : Secreted","6.5 : Electron transport ;","c : carrier","_","3 : Putative function from multiple computational evidences",2,454,457,13,464,1017]
[null,"ECK1625",null,"Escherichia coli K12","rsxC","putative 4Fe-4S ferredoxin-type protein fused with unknown protein","_",0.62297,1.00875,36.23,{"v":9e-92,"d":"9.00E-92"},1,1,"6.1 : Membrane ; 7.3 : Inner membrane ;","_","6 : Inner membrane-associated","18.1 : Enzymes of unknown specificity ;","c : carrier","_","3 : Putative function from multiple computational evidences",5,457,457,16,469,740]
[null,"VS_0976",null,"Vibrio tasmaniensis LGP32","_","Putative membrane protein","_",0.54048,0.89493,38.06,{"v":2E-52,"d":"2.00E-52"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","18 : Unknown function ;","m : membrane component","_","3 : Putative function from multiple computational evidences",4,248,457,27,271,276]
[]
["CLOSTRIBL3_v1_10630","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"NBG4_v1_240019",null,"Candidatus Sulfobium mesophilum","_","Putative electron transport complex protein RnfD","_",0.97101,1.01208,48.96,{"v":8e-111,"d":"8.00E-111"},1,1,"1.4.3 : Electron carrier ;","_","5 : Inner membrane protein","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 21747791","3 : Putative function from multiple computational evidences",3,329,331,2,336,345]
[null,"SCFA_v1_420043",null,"Ca. Phosphitivorax anaerolimi F81","rnfD","Electron transport complex subunit D","_",0.96522,1.00604,48.05,{"v":1e-98,"d":"1.00E-98"},1,1,"_","_","5 : Inner membrane protein","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,331,331,14,345,345]
[null,"SCFA_v1_190017",null,"Ca. Phosphitivorax butyraticus R76","rnfD","putative Ion-translocating oxidoreductase complex subunit D","_",0.89426,1.0137,50.34,{"v":1E-89,"d":"1.00E-89"},1,1,"6.1 : Membrane ;","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","e : enzyme","10637328, 12773378","3 : Putative function from multiple computational evidences",43,331,331,2,292,292]
[null,"CD630_11380",null,"Clostridium difficile 630","rnfD","Electron transport complex protein","_",0.96677,0.98462,46.25,{"v":3e-85,"d":"3.00E-85"},1,1,"6.1 : Membrane ;","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","e : enzyme","9492268, 9154934, 8264535, 12773378, 11160111","2a : Function from experimental evidences in other organisms",13,328,331,7,321,325]
[null,"MAGMOv5_3970",null,"Magnetotactic ovoidal bacterium MO-1","rnfD","Electron transport complex protein rnfD","_",0.96657,1.04834,40.92,{"v":1e-82,"d":"1.00E-82"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","18.1 : Enzymes of unknown specificity ;","c : carrier","10637328, 12773378","2b : Function from indirect experimental evidences (e.g. phenotypes)",14,331,331,6,349,359]
[null,"MALCv4_3937",null,"Methylomicrobium alcaliphilum 20Z","rnfD","electron transport complex protein RnfD","_",1.00602,1.00906,43.11,{"v":2e-80,"d":"2.00E-80"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier",8264535,"2a : Function from experimental evidences in other organisms",13,328,331,8,331,332]
[null,"ECK1626",null,"Escherichia coli K12","rsxD","putative inner membrane oxidoreductase","_",1.02273,1.08761,36.67,{"v":5e-60,"d":"5.00E-60"},1,1,"6.1 : Membrane ;","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","e : enzyme","10637328, 12773378","3 : Putative function from multiple computational evidences",10,331,331,2,351,352]
[null,"ECUMN_1921",null,"Escherichia coli UMN026","rsxD","putative inner membrane oxidoreductase","_",1.02273,1.08761,36.39,{"v":1E-59,"d":"1.00E-59"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","18.1 : Enzymes of unknown specificity ;","e : enzyme","10637328, 12773378, 15849754, 16850406","3 : Putative function from multiple computational evidences",10,331,331,2,351,352]
[null,"EFER_1413",null,"Escherichia fergusonii ATCC 35469T","rsxD","putative inner membrane oxidoreductase","_",1.01705,1.08157,35.47,{"v":1E-59,"d":"1.00E-59"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","18.1 : Enzymes of unknown specificity ;","e : enzyme","10637328, 12773378, 15849754, 16850406","3 : Putative function from multiple computational evidences",10,331,331,2,351,352]
[null,"ECS88_1678",null,"Escherichia coli S88","rsxD","putative inner membrane oxidoreductase","_",1.02273,1.08761,35.83,{"v":6e-59,"d":"6.00E-59"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","18.1 : Enzymes of unknown specificity ;","e : enzyme","10637328, 12773378, 15849754, 16850406","3 : Putative function from multiple computational evidences",10,331,331,2,351,352]
[null,"VC1014",null,"Vibrio cholerae N16961","rfnD","Electron transport complex protein rnfD","_",1.00575,1.0574,35.43,{"v":2e-53,"d":"2.00E-53"},1,1,"1.4.3 : Electron carrier ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","6.5 : Electron transport ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",11,328,331,3,347,348]
[]
["CLOSTRIBL3_v1_10631","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_11390",null,"Clostridium difficile 630","rnfG","Electron transport complex protein","_",0.94709,0.96757,35.2,{"v":1e-30,"d":"1.00E-30"},1,1,"_","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","e : enzyme","11160111, 12773378, 8264535, 9154934, 9492268","2a : Function from experimental evidences in other organisms",8,175,185,2,180,189]
[null,"NBG4_v1_240020",null,"Candidatus Sulfobium mesophilum","_","Putative electron transport complex protein RnfG","_",0.89796,0.95135,39.2,{"v":3e-30,"d":"3.00E-30"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 21747791","3 : Putative function from multiple computational evidences",10,175,185,6,176,196]
[]
["CLOSTRIBL3_v1_10632","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_11400",null,"Clostridium difficile 630","rnfE","Electron transport complex protein","_",0.88208,0.94924,50.8,{"v":4e-65,"d":"4.00E-65"},1,1,"_","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","c : carrier","11160111, 12773378, 8264535, 9154934, 9492268","2a : Function from experimental evidences in other organisms",1,187,212,1,187,197]
[null,"SCFA_v1_420045",null,"Ca. Phosphitivorax anaerolimi F81","rnfE","Ion-translocating oxidoreductase complex subunit E (Predicted NADH:ubiquinone oxidoreductase, subunit RnfE)","_",0.83721,0.84906,50.56,{"v":1E-61,"d":"1.00E-61"},1,1,"6.1 : Membrane ;","1.18.1.-","5 : Inner membrane protein","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,188,212,9,188,215]
[null,"SCFA_v1_190015",null,"Ca. Phosphitivorax butyraticus R76","rnfE","Ion-translocating oxidoreductase complex subunit E (Predicted NADH:ubiquinone oxidoreductase, subunit RnfE)","_",0.82569,0.84906,49.44,{"v":2e-60,"d":"2.00E-60"},1,1,"6.1 : Membrane ;","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","c : carrier","10411911, 10637328, 12773378","3 : Putative function from multiple computational evidences",9,188,212,9,188,218]
[null,"NBG4_v1_240021",null,"Candidatus Sulfobium mesophilum","rnfE","Electron transport complex protein RnfE","_",0.91667,0.93396,45.45,{"v":1E-54,"d":"1.00E-54"},1,1,"1.4.3 : Electron carrier ;","_","5 : Inner membrane protein","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 21747791","2a : Function from experimental evidences in other organisms",3,193,212,9,206,216]
[null,"MALCv4_3935",null,"Methylomicrobium alcaliphilum 20Z","rnfE","electron transport complex protein RnfE","_",0.93427,0.93868,42.71,{"v":8e-51,"d":"8.00E-51"},1,1,"1.4.3 : Electron carrier ;","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","c : carrier",8264535,"2b : Function from indirect experimental evidences (e.g. phenotypes)",5,203,212,19,212,213]
[null,"VIBNIv4_A0904",null,"Vibrio nigripulchritudo SFn1","rnfE","Electron transport complex protein rnfE","_",0.93043,1.00943,40.65,{"v":3E-49,"d":"3.00E-49"},1,1,"1.4.3 : Electron carrier ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","6.5 : Electron transport ;","c : carrier","9097039, 9278503, 16738553, 10411911, 15919996","2a : Function from experimental evidences in other organisms",6,206,212,7,219,230]
[null,"MARHY2355",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","rsxE","Electron transport complex protein rnfE. Required for the reduction of SoxR","_",0.88655,0.99528,39.81,{"v":4e-49,"d":"4.00E-49"},1,1,"6.1 : Membrane ;","_","11 : Membrane","_","t : transporter","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,202,212,8,218,238]
[null,"MAGMOv5_3968",null,"Magnetotactic ovoidal bacterium MO-1","rnfE","Electron transport complex protein rnfE","_",0.91071,0.96226,40.2,{"v":8e-48,"d":"8.00E-48"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","18.1 : Enzymes of unknown specificity ;","c : carrier","10411911, 10637328, 12773378","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,206,212,9,209,224]
[null,"PSHAa1100",null,"Pseudoalteromonas haloplanktis TAC125","rsxE","Electron transport complex protein rnfE","_",0.96552,1.0566,38.84,{"v":4e-47,"d":"4.00E-47"},1,1,"1.4.2 : Electron transport ;","_","integral inner membrane","_","t : transporter","_","2a : Function from experimental evidences in other organisms",2,212,212,3,226,232]
[null,"VC2292",null,"Vibrio cholerae N16961","nqrD","Na(+)-translocating NADH-quinone reductase subunit D","_",0.96226,0.97143,37.25,{"v":1E-41,"d":"1.00E-41"},2,1,"4.S.130 : Na+ ; 7.3 : Inner membrane ;","1.6.5.-","5 : Inner membrane protein","7.4 : Cations and iron carrying compounds ;","t : transporter","7805867, 7729558, 9490015, 10549856, 11248187, 11248188","2a : Function from experimental evidences in other organisms",8,200,212,8,209,210]
[null,"ECK1628",null,"Escherichia coli K12","rsxE","putative inner membrane NADH-quinone reductase","_",0.84848,0.92453,38.27,{"v":2E-41,"d":"2.00E-41"},1,1,"6.1 : Membrane ;","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","c : carrier","10411911, 10637328, 12773378","3 : Putative function from multiple computational evidences",5,187,212,6,201,231]
[null,"ECS88_1680",null,"Escherichia coli S88","rsxE","putative inner membrane NADH-quinone reductase","_",0.84848,0.92453,38.27,{"v":2E-41,"d":"2.00E-41"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","18.1 : Enzymes of unknown specificity ;","c : carrier","10411911, 10637328, 12773378, 15849754, 16850406","3 : Putative function from multiple computational evidences",5,187,212,6,201,231]
[null,"ECUMN_1923",null,"Escherichia coli UMN026","rsxE","putative inner membrane NADH-quinone reductase","_",0.84848,0.92453,38.27,{"v":2E-41,"d":"2.00E-41"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","18.1 : Enzymes of unknown specificity ;","c : carrier","10411911, 10637328, 12773378, 15849754, 16850406","3 : Putative function from multiple computational evidences",5,187,212,6,201,231]
[null,"EFER_1411",null,"Escherichia fergusonii ATCC 35469T","rsxE","putative inner membrane NADH-quinone reductase","_",0.85217,0.92453,37.76,{"v":2e-40,"d":"2.00E-40"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","18.1 : Enzymes of unknown specificity ;","c : carrier","10411911, 10637328, 12773378, 15849754, 16850406","3 : Putative function from multiple computational evidences",5,187,212,6,201,230]
[null,"VIBNIv4_A0569",null,"Vibrio nigripulchritudo SFn1","nqrD","Na(+)-translocating NADH-quinone reductase subunit D","_",0.96226,0.97143,36.76,{"v":3e-40,"d":"3.00E-40"},2,1,"4.S.130 : Na+ ; 7.3 : Inner membrane ;","1.6.5.-","5 : Inner membrane protein","7.4 : Cations and iron carrying compounds ;","t : transporter","7805867, 7729558, 9490015, 10549856, 11248187, 11248188","1c : Function from experimental evidences in the studied genus",8,200,212,8,209,210]
[null,"NMV_1857",null,"Neisseria meningitidis NEM8013","nqrD","Na(+)-translocating NADH-quinone reductase subunit D (Na(+)-translocating NQR subunit D; Na(+)-NQR subunit D; NQR complex subunit D; NQR-1 subunit D)","_",0.85849,0.875,36.81,{"v":2e-36,"d":"2.00E-36"},1,1,"_","1.6.5.8","11 : Membrane","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",12,186,212,16,195,208]
[]
["CLOSTRIBL3_v1_10633","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"NBG4_v1_240022",null,"Candidatus Sulfobium mesophilum","rnfA","Electron transport complex protein RnfA","_",0.94924,0.96891,52.94,{"v":3e-73,"d":"3.00E-73"},1,1,"1.4.3 : Electron carrier ;","_","5 : Inner membrane protein","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 21747791","2a : Function from experimental evidences in other organisms",7,193,193,11,197,197]
[null,"ECK1623",null,"Escherichia coli K12","rsxA","putative inner membrane subunit of an electron transport system","_",1,1,47.67,{"v":2e-65,"d":"2.00E-65"},1,1,"6.1 : Membrane ;","_","11 : Membrane","14 : Cell envelope ;","m : membrane component","10411911, 10637328, 12773378","3 : Putative function from multiple computational evidences",1,193,193,1,193,193]
[null,"ECS88_1675",null,"Escherichia coli S88","rsxA","putative inner membrane subunit of an electron transport system","_",1,1,47.67,{"v":2e-65,"d":"2.00E-65"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","14 : Cell envelope ;","m : membrane component","10411911, 10637328, 12773378, 15849754, 16850406","3 : Putative function from multiple computational evidences",1,193,193,1,193,193]
[null,"ECUMN_1918",null,"Escherichia coli UMN026","rsxA","putative inner membrane subunit of an electron transport system","_",1,1,47.67,{"v":2e-65,"d":"2.00E-65"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","14 : Cell envelope ;","m : membrane component","10411911, 10637328, 12773378, 15849754, 16850406","3 : Putative function from multiple computational evidences",1,193,193,1,193,193]
[null,"EFER_1416",null,"Escherichia fergusonii ATCC 35469T","rsxA","putative inner membrane subunit of an electron transport system","_",1,1,47.15,{"v":1e-64,"d":"1.00E-64"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","14 : Cell envelope ;","m : membrane component","10411911, 10637328, 12773378, 15849754, 16850406","3 : Putative function from multiple computational evidences",1,193,193,1,193,193]
[null,"VIBNIv4_A0909",null,"Vibrio nigripulchritudo SFn1","rnfA","Electron transport complex protein rnfA","_",1,1,45.6,{"v":4e-63,"d":"4.00E-63"},1,1,"1.4.3 : Electron carrier ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","6.5 : Electron transport ;","c : carrier","9278503, 16738553, 10411911, 15919996","2a : Function from experimental evidences in other organisms",1,193,193,1,193,193]
[null,"SCFA_v1_1220010",null,"Ca. Phosphitivorax butyraticus R76","rnfA","Electron transport complex protein rnfA","_",0.97409,0.98429,46.28,{"v":5e-62,"d":"5.00E-62"},1,1,"6.1 : Membrane ;","_","11 : Membrane","14 : Cell envelope ;","m : membrane component","10411911, 10637328, 12773378","3 : Putative function from multiple computational evidences",4,191,193,3,190,191]
[null,"PSHAa1105",null,"Pseudoalteromonas haloplanktis TAC125","rsxA","Electron transport complex protein rnfA, inner membrane protein","_",0.98964,0.98964,45.03,{"v":8e-62,"d":"8.00E-62"},1,1,"1.4.2 : Electron transport ;","_","integral inner membrane","_","t : transporter",10411911,"2a : Function from experimental evidences in other organisms",1,191,193,1,191,193]
[null,"SCFA_v1_420040",null,"Ca. Phosphitivorax anaerolimi F81","rnfA","Electron transport complex protein rnfA","_",0.89952,0.97409,45.74,{"v":5e-61,"d":"5.00E-61"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","14 : Cell envelope ;","m : membrane component","10411911, 10637328, 12773378","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,191,193,21,208,209]
[null,"CD630_11410",null,"Clostridium difficile 630","rnfA","Electron transport complex protein","_",0.97927,0.98953,44.44,{"v":7e-61,"d":"7.00E-61"},1,1,"6.1 : Membrane ;","_","11 : Membrane","14 : Cell envelope ;","m : membrane component","9492268, 9154934, 8264535, 12773378, 11160111","2a : Function from experimental evidences in other organisms",5,193,193,4,191,191]
[null,"MARHY2350",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","rsxA","Electron transport complex protein rnfA","_",1,1,43.52,{"v":8e-61,"d":"8.00E-61"},1,1,"6.1 : Membrane ;","_","11 : Membrane","_","t : transporter","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,193,193,1,193,193]
[null,"MAGMOv5_3973",null,"Magnetotactic ovoidal bacterium MO-1","rnfA","Electron transport complex protein rnfA","_",0.95431,0.97409,43.09,{"v":1E-59,"d":"1.00E-59"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","14 : Cell envelope ;","c : carrier","10411911, 10637328, 12773378","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,191,193,9,196,197]
[null,"MALCv4_3934",null,"Methylomicrobium alcaliphilum 20Z","rnfA","electron transport complex protein RnfA","_",0.97409,0.97409,40.43,{"v":1E-50,"d":"1.00E-50"},2,1,"1.4.3 : Electron carrier ;","_","11 : Membrane","14 : Cell envelope ;","m : membrane component","8264535, 9154934","2a : Function from experimental evidences in other organisms",3,190,193,5,191,193]
[null,"NMV_1858",null,"Neisseria meningitidis NEM8013","nqrE","Na(+)-translocating NADH-quinone reductase subunit E (Na(+)-translocating NQR subunit E; Na(+)-NQR subunit E; NQR complex subunit E; NQR-1 subunit E)","_",0.98985,1.01036,43.59,{"v":1E-50,"d":"1.00E-50"},1,1,"_","1.6.5.8","11 : Membrane","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,190,193,1,195,197]
[null,"VIBNIv4_A0570",null,"Vibrio nigripulchritudo SFn1","nqrE","Na(+)-translocating NADH-quinone reductase subunit E","_",0.9899,1.01554,40.31,{"v":1E-46,"d":"1.00E-46"},2,1,"4.S.130 : Na+ ; 7.3 : Inner membrane ;","1.6.5.-","5 : Inner membrane protein","7.4 : Cations and iron carrying compounds ;","t : transporter",10587447,"1c : Function from experimental evidences in the studied genus",1,190,193,1,196,198]
[]
["CLOSTRIBL3_v1_10634","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"NBG4_v1_240023",null,"Candidatus Sulfobium mesophilum","_","Putative electron transport complex protein RnfB","_",0.65404,0.90244,49.42,{"v":2E-91,"d":"2.00E-91"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 21747791","3 : Putative function from multiple computational evidences",9,266,287,58,311,396]
[null,"CD630_11420",null,"Clostridium difficile 630","rnfB","Electron transport complex protein","_",0.80308,0.90941,44.06,{"v":1e-75,"d":"1.00E-75"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 12773378, 11160111","2a : Function from experimental evidences in other organisms",6,266,287,6,260,325]
[null,"SCFA_v1_420041",null,"Ca. Phosphitivorax anaerolimi F81","RnfB","electron transport complex protein RnfB","_",0.81481,0.91986,39.39,{"v":5e-64,"d":"5.00E-64"},1,1,"_","1.18.1.-","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,269,287,2,261,324]
[null,"SCFA_v1_1220011",null,"Ca. Phosphitivorax butyraticus R76","rnfB","Electron transport complex protein RnfB","_",0.82407,0.93031,38.2,{"v":4e-61,"d":"4.00E-61"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,269,287,2,261,324]
[]
["CLOSTRIBL3_v1_10096","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_33130",null,"Clostridium difficile 630","hydN1","Putative oxidoreductase, Fe-S subunit","_",0.95745,1.05263,45,{"v":3e-56,"d":"3.00E-56"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,180,188,2,165,171]
[null,"CD630_33150",null,"Clostridium difficile 630","hydN2","Putative oxidoreductase, Fe-S subunit","_",0.99468,1.02186,41.71,{"v":5e-48,"d":"5.00E-48"},2,2,"_","_","11 : Membrane","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,182,188,1,175,183]
[null,"ECK3562",null,"Escherichia coli K12","yiaI","putative hydrogenase, 4Fe-4S ferredoxin-type component","_",0.87234,1.04459,46.34,{"v":2e-47,"d":"2.00E-47"},2,1,"_","_","1 : Unknown","18.1 : Enzymes of unknown specificity ;","c : carrier","_","3 : Putative function from multiple computational evidences",3,166,188,2,140,157]
[null,"AZOLI_p30032",null,"Azospirillum lipoferum 4B","hydN","formate dehydrogenase-H, [4Fe-4S] ferredoxin subunit","_",0.95213,0.99444,43.02,{"v":7e-47,"d":"7.00E-47"},1,1,"1.3.7 : Anaerobic respiration ;","_","2 : Cytoplasmic","6.3 : Anaerobic ;","c : carrier",8661925,"2a : Function from experimental evidences in other organisms",3,180,188,2,167,180]
[null,"Ent638_0146",null,"Enterobacter sp. 638","ysaA","Putative hydrogenase, 4Fe-4S ferredoxin-type component","_",0.88298,1.08497,42.17,{"v":8e-44,"d":"8.00E-44"},2,1,"_","_","1 : Unknown","18 : Unknown function ;","c : carrier","_","3 : Putative function from multiple computational evidences",3,168,188,2,142,153]
[null,"ECK2463",null,"Escherichia coli K12","aegA","fused putative oxidoreductase: FeS binding subunit ; NAD/FAD-binding subunit","_",0.25341,0.8883,43.11,{"v":5e-43,"d":"5.00E-43"},3,5,"_","_","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme",8955321,"3 : Putative function from multiple computational evidences",3,169,188,2,146,659]
[null,"ECK2881",null,"Escherichia coli K12","ygfS","putative oxidoreductase, 4Fe-4S ferredoxin-type subunit","_",0.87234,1.01235,41.46,{"v":2E-41,"d":"2.00E-41"},4,1,"_","_","1 : Unknown","18.1 : Enzymes of unknown specificity ;","c : carrier","_","3 : Putative function from multiple computational evidences",6,169,188,5,142,162]
[null,"AZOLI_p30030",null,"Azospirillum lipoferum 4B","hyfA","hydrogenase 4, 4Fe-4S subunit","_",0.73191,0.91489,40.12,{"v":1e-38,"d":"1.00E-38"},2,1,"1.3.5 : Fermentation ; 1.3.7 : Anaerobic respiration ;","_","1 : Unknown","6.3 : Anaerobic ; 6.7 : Fermentation ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,171,188,40,203,235]
[null,"EFER_0694",null,"Escherichia fergusonii ATCC 35469T","_","putative hydrogenase 4, 4Fe-4S subunit","_",0.90732,0.98936,39.25,{"v":2e-38,"d":"2.00E-38"},5,1,"_","_","1 : Unknown","_","c : carrier","_","3 : Putative function from multiple computational evidences",3,169,188,2,171,205]
[null,"ECK2882",null,"Escherichia coli K12","ygfT","fused putative oxidoreductase: Fe-S subunit ; nucleotide-binding subunit","_",0.27074,0.92021,39.31,{"v":3E-37,"d":"3.00E-37"},7,5,"_","_","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,174,188,2,141,639]
[null,"Pars_0924","_","Pyrobaculum arsenaticum DSM 13514","_","putative polysulfide reductase chain B (Sulfur reductase chain B) PsrB","_",0.83621,1.03191,36.6,{"v":1E-26,"d":"1.00E-26"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,162,188,1,189,232]
[null,"SCFA_v1_1550009",null,"Ca. Phosphitivorax anaerolimi F81","_","putative ferredoxin","_",0.26064,0.85965,40.82,7e-09,7,9,"_","_","9 : Periplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",60,108,188,10,56,57]
[]
[]
[]
["CLOSTRIBL3_v1_10095","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_33140",null,"Clostridium difficile 630","hydA","Iron hydrogenase","_",0.97186,0.97397,64.37,0,1,1,"_","1.12.7.2","2 : Cytoplasmic","_","e : enzyme","10529166, 15899410, 7894709, 10585557","1c : Function from experimental evidences in the studied genus",7,455,462,5,453,461]
[null,"SCFA_v1_560006","_","Ca. Propionivorax syntrophicum F70","hydA","Ferredoxin hydrogenase, Fe-only","_",0.7987,0.99461,52.57,{"v":3e-137,"d":"3.00E-137"},1,1,"_","1.12.7.2","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",92,460,462,1,365,371]
[null,"SBF1_v1_5500002",null,"Desulfosporosinus sp. SbF1","hndD_2","hydrogen dehydrogenase (NADP+), delta subunit (hydrogenase active site)","1.12.1.3-RXN ; RHEA:18640 ;",0.8,1.00433,43.32,{"v":3e-127,"d":"3.00E-127"},1,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",11,460,462,148,579,580]
[null,"CD630_34070",null,"Clostridium difficile 630","_","Putative iron-only hydrogenase, catalytic subunit HymC-like","_",0.77403,0.99351,43.57,{"v":6e-126,"d":"6.00E-126"},2,1,"1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.99.5","2 : Cytoplasmic","6.3 : Anaerobic ; 6.5 : Electron transport ; 7.4 : Cations and iron carrying compounds ;","c : carrier","12560990, 11891051","3 : Putative function from multiple computational evidences",11,455,462,147,573,593]
[null,"SBF1_v1_40032",null,"Desulfosporosinus sp. SbF1","hndD_1","hydrogen dehydrogenase (NADP+), delta subunit (hydrogenase active site)","1.12.1.3-RXN ; RHEA:18640 ;",0.8,1.00433,42.03,{"v":1E-119,"d":"1.00E-119"},2,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",11,460,462,148,579,580]
[null,"SBF1_v1_3630004",null,"Desulfosporosinus sp. SbF1","hndD_3b","fragment of hydrogen dehydrogenase (NADP+), delta subunit (hydrogenase active site) (part 2/3)","1.12.1.3-RXN ; RHEA:18640 ;",0.34632,0.99379,44.38,{"v":6e-39,"d":"6.00E-39"},3,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",211,365,462,1,160,161]
[null,"SCFA_v1_620002",null,"Ca. Propionivorax syntrophicum F70","hydA","Hydrogenase, Fe-only","_",0.24459,0.94958,53.1,{"v":2e-31,"d":"2.00E-31"},3,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",211,316,462,1,113,119]
[null,"SCFA_v1_620001",null,"Ca. Propionivorax syntrophicum F70","hydA","Hydrogenase, Fe-only","_",0.23593,0.90083,42.2,{"v":3E-23,"d":"3.00E-23"},4,1,"_","1.12.7.2","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",350,458,462,4,109,121]
[null,"SBF1_v1_3630005",null,"Desulfosporosinus sp. SbF1","hndD_3c","fragment of hydrogen dehydrogenase (NADP+), delta subunit (hydrogenase active site) (part 3/3)","1.12.1.3-RXN ; RHEA:18640 ;",0.17965,1.0122,48.19,{"v":2E-19,"d":"2.00E-19"},6,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",378,460,462,2,81,82]
[null,"SCFA_v1_1550009",null,"Ca. Phosphitivorax anaerolimi F81","_","putative ferredoxin","_",0.09957,0.80702,52.17,3E-11,1,3,"_","_","9 : Periplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",10,55,462,5,49,57]
[]
["CLOSTRIBL3_v1_10094","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_33150",null,"Clostridium difficile 630","hydN2","Putative oxidoreductase, Fe-S subunit","_",0.98919,1,53.01,{"v":8e-64,"d":"8.00E-64"},1,1,"_","_","11 : Membrane","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,182,185,1,182,183]
[null,"CD630_33130",null,"Clostridium difficile 630","hydN1","Putative oxidoreductase, Fe-S subunit","_",0.94595,1.02339,39.43,{"v":7e-44,"d":"7.00E-44"},2,2,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,179,185,1,171,171]
[null,"CLOSTRIBL3_v1_10096",null,"Clostridiaceae BL-3","hydN","Electron transport protein HydN","_",0.97872,0.99459,39.13,{"v":2e-42,"d":"2.00E-42"},1,1,"1.3.7 : Anaerobic respiration ;","_","2 : Cytoplasmic","6.3 : Anaerobic ;","c : carrier",8661925,"2a : Function from experimental evidences in other organisms",6,177,185,3,184,188]
[null,"AZOLI_p30032",null,"Azospirillum lipoferum 4B","hydN","formate dehydrogenase-H, [4Fe-4S] ferredoxin subunit","_",0.97838,1.00556,38.67,{"v":2E-41,"d":"2.00E-41"},1,2,"1.3.7 : Anaerobic respiration ;","_","2 : Cytoplasmic","6.3 : Anaerobic ;","c : carrier",8661925,"2a : Function from experimental evidences in other organisms",5,181,185,1,178,180]
[null,"ECK3562",null,"Escherichia coli K12","yiaI","putative hydrogenase, 4Fe-4S ferredoxin-type component","_",0.8973,1.05732,39.16,{"v":4e-37,"d":"4.00E-37"},2,2,"_","_","1 : Unknown","18.1 : Enzymes of unknown specificity ;","c : carrier","_","3 : Putative function from multiple computational evidences",5,170,185,1,151,157]
[null,"Ent638_0146",null,"Enterobacter sp. 638","ysaA","Putative hydrogenase, 4Fe-4S ferredoxin-type component","_",0.8973,1.08497,35.54,{"v":7e-37,"d":"7.00E-37"},2,2,"_","_","1 : Unknown","18 : Unknown function ;","c : carrier","_","3 : Putative function from multiple computational evidences",5,170,185,1,151,153]
[null,"ECK2463",null,"Escherichia coli K12","aegA","fused putative oxidoreductase: FeS binding subunit ; NAD/FAD-binding subunit","_",0.23824,0.84865,39.49,{"v":9e-36,"d":"9.00E-36"},3,6,"_","_","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme",8955321,"3 : Putative function from multiple computational evidences",5,161,185,1,145,659]
[null,"AZOLI_p30030",null,"Azospirillum lipoferum 4B","hyfA","hydrogenase 4, 4Fe-4S subunit","_",0.80851,1.02703,35.79,{"v":1e-34,"d":"1.00E-34"},2,2,"1.3.5 : Fermentation ; 1.3.7 : Anaerobic respiration ;","_","1 : Unknown","6.3 : Anaerobic ; 6.7 : Fermentation ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,176,185,38,215,235]
[null,"ECK2882",null,"Escherichia coli K12","ygfT","fused putative oxidoreductase: Fe-S subunit ; nucleotide-binding subunit","_",0.25196,0.87027,35.4,{"v":2e-31,"d":"2.00E-31"},6,6,"_","_","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,164,185,1,140,639]
[null,"EFER_0694",null,"Escherichia fergusonii ATCC 35469T","_","putative hydrogenase 4, 4Fe-4S subunit","_",0.8878,0.98378,35.16,{"v":5e-30,"d":"5.00E-30"},5,2,"_","_","1 : Unknown","_","c : carrier","_","3 : Putative function from multiple computational evidences",5,161,185,1,170,205]
[]
["CLOSTRIBL3_v1_10091","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"SCFA_v1_560028",null,"Ca. Phosphitivorax anaerolimi F81","hydC","Fe-hydrogenase gamma subunit (NADP-reducing hydrogenase subunit HndA)","_",0.88344,0.94118,45.14,{"v":1e-44,"d":"1.00E-44"},1,1,"_","1.6.5.11","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",18,160,163,10,153,153]
[null,"NBG4_v1_170016",null,"Candidatus Sulfobium mesophilum","_","Putative NADH dehydrogenase (Ubiquinone) 24 kDa subunit","NADH-DEHYDROG-A-RXN ;",0.88957,0.90062,42.07,{"v":6e-43,"d":"6.00E-43"},1,1,"1.4 : Energy production/transport ;","1.6.5.3","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","9446680, 20505720, 22392981","3 : Putative function from multiple computational evidences",17,161,163,16,160,161]
[null,"SCFA_v1_220024",null,"Ca. Phosphitivorax anaerolimi F81","hndA","NADP-reducing hydrogenase subunit HndA (Putative NADH dehydrogenase (Ubiquinone) 24 kDa subunit)","_",0.51237,0.88957,44.83,{"v":5E-42,"d":"5.00E-42"},2,1,"_","1.6.5.11","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",18,162,163,8,152,283]
[null,"SBF1_v1_40019",null,"Desulfosporosinus sp. SbF1","fdhC","putative formate dehydrogenase, gamma subunit","_",0.87117,0.8875,45.07,{"v":8e-42,"d":"8.00E-42"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",18,159,163,18,159,160]
[null,"SBF1_v1_210026",null,"Desulfosporosinus sp. SbF1","nuoE","putative NADH:quinone oxidoreductase, subunit E","_",0.83523,0.90184,42.86,{"v":2e-40,"d":"2.00E-40"},2,1,"_","1.6.5.-","5 : Inner membrane protein","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",13,158,163,19,165,176]
[null,"SCFA_v1_1110002",null,"Ca. Phosphitivorax butyraticus R76","hndA","NADP-reducing hydrogenase subunit HndA (Putative NADH dehydrogenase (Ubiquinone) 24 kDa subunit)","_",0.51237,0.88957,43.45,{"v":4e-40,"d":"4.00E-40"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",18,162,163,8,152,283]
[null,"SBF1_v1_1490002",null,"Desulfosporosinus sp. SbF1","hndA_2","hydrogen dehydrogenase (NADP+), alpha subunit (NADP+-reducing)","1.12.1.3-RXN ; RHEA:18640 ;",0.83237,0.88344,40.97,{"v":3E-37,"d":"3.00E-37"},3,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",18,160,163,16,159,173]
[null,"SCFA_v1_120014",null,"Ca. Phosphitivorax anaerolimi F81","hydC","NADP-reducing hydrogenase subunit HndA","_",0.85119,0.8773,35.66,{"v":2e-34,"d":"2.00E-34"},3,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",18,160,163,26,168,168]
[null,"SBF1_v1_3630001",null,"Desulfosporosinus sp. SbF1","hndA_3","hydrogen dehydrogenase (NADP+), alpha subunit (NADP+-reducing)","1.12.1.3-RXN ; RHEA:18640 ;",0.88344,0.88889,36.11,{"v":2e-32,"d":"2.00E-32"},4,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",18,160,163,16,159,162]
[null,"CD630_34050",null,"Clostridium difficile 630","_","Putative iron-only hydrogenase,electron-transferring subunit HymA-like","_",0.85455,0.86503,37.59,{"v":2e-31,"d":"2.00E-31"},1,1,"1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.99.5","2 : Cytoplasmic","6.3 : Anaerobic ; 6.5 : Electron transport ; 7.4 : Cations and iron carrying compounds ;","c : carrier","12560990, 11891051","3 : Putative function from multiple computational evidences",20,160,163,19,159,165]
[null,"LEPBIa1300",null,"Leptospira biflexa serovar Patoc Patoc 1","nuoE","NADH-quinone oxidoreductase, chain E (NADH dehydrogenase I, chain E) (NDH-1, chain E) (NUO5)","_",0.86585,0.87117,35.92,{"v":1e-29,"d":"1.00E-29"},1,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.5.11","2 : Cytoplasmic","16.10 : Respire ;","e : enzyme","12923180, 8774714","2a : Function from experimental evidences in other organisms",19,158,163,18,159,164]
[null,"SCFA_v1_100025",null,"Ca. Phosphitivorax anaerolimi F81","nuoE","NADH-quinone oxidoreductase subunit E 2","_",0.85276,0.87975,36.69,{"v":6e-28,"d":"6.00E-28"},4,1,"_","7.1.1.2","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",24,161,163,18,156,158]
[]
["CLOSTRIBL3_v1_10092","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"SCFA_v1_560027",null,"Ca. Phosphitivorax anaerolimi F81","hydB","Fe-hydrogenase beta subunit (NADP-reducing hydrogenase subunit HndC)","_",0.95491,0.98998,58.52,0,1,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,598,599,31,620,621]
[null,"CD630_34060",null,"Clostridium difficile 630","_","Putative iron-only hydrogenase,electron-transferring subunit HymB-like","_",0.94108,0.98664,51.95,0,1,1,"1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.99.5","2 : Cytoplasmic","6.3 : Anaerobic ; 6.5 : Electron transport ; 7.4 : Cations and iron carrying compounds ;","c : carrier","12560990, 11891051","3 : Putative function from multiple computational evidences",9,596,599,39,625,628]
[null,"SBF1_v1_40018",null,"Desulfosporosinus sp. SbF1","fdhB","putative formate dehydrogenase, beta subunit","_",0.99499,1.00168,51.85,0,1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,596,599,1,592,595]
[null,"SBF1_v1_3630002",null,"Desulfosporosinus sp. SbF1","hndC_3","hydrogen dehydrogenase (NADP+), gamma HndC-like subunit (NADP+-reducing)","1.12.1.3-RXN ; RHEA:18640 ;",0.87073,0.9783,51.71,0,2,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",7,592,599,86,665,673]
[null,"NBG4_v1_170017",null,"Candidatus Sulfobium mesophilum","_","Putative hydrogen hydrogenase (HndC)","1.12.1.3-RXN ;",0.94436,0.99165,53.7,0,1,1,"1.4 : Energy production/transport ;","1.12.1.3","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","9703971, 2538471, 8389482, 18156274","3 : Putative function from multiple computational evidences",7,598,599,29,616,629]
[null,"SBF1_v1_40033",null,"Desulfosporosinus sp. SbF1","hndC_1","hydrogen dehydrogenase (NADP+), gamma HndC-like subunit (NADP+-reducing)","1.12.1.3-RXN ; RHEA:18640 ;",0.94268,0.98831,50,0,3,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,592,599,35,620,628]
[null,"SBF1_v1_210025",null,"Desulfosporosinus sp. SbF1","nuoF","putative NADH:quinone oxidoreductase, subunit F","_",0.96327,0.98632,51.65,0,4,1,"_","1.6.5.-","5 : Inner membrane protein","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",25,598,599,17,584,585]
[null,"SCFA_v1_120012",null,"Ca. Phosphitivorax anaerolimi F81","hndC","NADP-reducing hydrogenase subunit HndC","_",0.52616,0.88982,52.91,0,2,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,541,599,10,539,1013]
[null,"SCFA_v1_2590004",null,"Ca. Phosphitivorax butyraticus R76","hydB","Fe-hydrogenase beta subunit (NADP-reducing hydrogenase subunit HndC)","_",0.65776,1,65.99,0,1,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",205,598,599,1,393,394]
[null,"SCFA_v1_220025",null,"Ca. Phosphitivorax anaerolimi F81","hndC","hydrogen dehydrogenase (NADP+), gamma HndC-like subunit (NADP+-reducing)","_",0.49675,0.89316,49.35,{"v":6e-178,"d":"6.00E-178"},3,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,542,599,30,560,1077]
[null,"ADVE02_v2_11630",null,"Methylosinus trichosporium OB3b","fdsB","NAD-linked formate dehydrogenase molybdenum containing, beta subunit","_",0.85643,0.99226,40.74,{"v":1E-125,"d":"1.00E-125"},1,1,"1.3 : Energy metabolism (carbon) ; 1.3.6 : Aerobic respiration ; 4.S.59 : formate ;","1.2.1.2, 1.2.1.43, 1.6.99.5","2 : Cytoplasmic","5 : Central intermediary metabolism ; 5.2 : One-carbon metabolism ;","e : enzyme","1657982, 204923","1a : Function from experimental evidences in the studied strain",16,526,599,13,509,517]
[null,"MSPATv1_360031",null,"Methylocystis sp. ATCC 49242","fdhB","NAD-linked formate dehydrogenase, molybdenum containing, beta subunit","_",0.83806,0.97099,41.63,{"v":8e-125,"d":"8.00E-125"},1,1,"1.1 : Carbon compound utilization ; 1.4 : Energy production/transport ;","1.2.1.2","2 : Cytoplasmic","5.2 : One-carbon metabolism ;","e : enzyme",9756865,"2a : Function from experimental evidences in other organisms",27,526,599,20,509,517]
[null,"BRADO4976",null,"Bradyrhizobium sp. ORS278","fdsB","Putative formate dehydrogenase beta subunit","_",0.86144,0.99614,40.89,{"v":3e-123,"d":"3.00E-123"},1,1,"1.3.7 : Anaerobic respiration ; 1.4.3 : Electron carrier ; 4.S.59 : formate ;","1.2.1.2","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",9,524,599,7,507,518]
[null,"METBGv2_11586",null,"Methylomicrobium album BG8","fdsB","NAD-dependent formate dehydrogenase, beta subunit","_",0.82805,0.95938,39.52,{"v":6e-123,"d":"6.00E-123"},1,1,"4.S.59 : formate ;","1.2.1.2","2 : Cytoplasmic","5.2 : One-carbon metabolism ;","e : enzyme",9756865,"2a : Function from experimental evidences in other organisms",31,524,599,25,508,517]
[null,"SCFA_v1_100026",null,"Ca. Phosphitivorax anaerolimi F81","nuoF","NADH:ubiquinone oxidoreductase, chain F","RXN0-5388 ; NADH-DEHYDROG-A-RXN ;",0.69282,0.9976,44.82,{"v":5e-121,"d":"5.00E-121"},4,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 4.S.130 : Na+ ; 7.1 : Cytoplasm ;","7.1.1.2","2 : Cytoplasmic","6.1 : Aerobic ; 6.3 : Anaerobic ; 6.5 : Electron transport ; 7.4 : Cations and iron carrying compounds ;","c : carrier","7690854, 8157582, 8366049, 9593861","2a : Function from experimental evidences in other organisms",115,529,599,3,414,416]
[null,"AZOLI_p10069",null,"Azospirillum lipoferum 4B","fdsB","formate dehydrogenase beta subunit","_",0.86144,0.98099,37.79,{"v":1E-119,"d":"1.00E-119"},1,1,"_","1.2.1.2","2 : Cytoplasmic","5.2 : One-carbon metabolism ;","e : enzyme",9756865,"2a : Function from experimental evidences in other organisms",13,526,599,14,513,526]
[null,"HEAR3433",null,"Herminiimonas arsenicoxydans","fdsB","NAD-dependent formate dehydrogenase beta subunit","_",0.83639,0.95429,38.72,{"v":3e-119,"d":"3.00E-119"},1,1,"1.1 : Carbon compound utilization ; 1.4 : Energy production/transport ;","1.2.1.2","1 : Unknown","6 : Energy metabolism ; 5 : Central intermediary metabolism ;","e : enzyme",9756865,"2a : Function from experimental evidences in other organisms",26,524,599,24,516,525]
[null,"MGMSRv2_1755",null,"Magnetospirillum gryphiswaldense MSR-1 v2","nuoF","NADH-quinone oxidoreductase subunit F, NuoF","_",0.87646,1.0274,37.33,{"v":4e-118,"d":"4.00E-118"},1,1,"1.3.7 : Anaerobic respiration ; 1.4.3 : Electron carrier ; 4.S.59 : formate ;","1.6.99.5","2 : Cytoplasmic","6.5 : Electron transport ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",9,524,599,9,510,511]
[null,"METUNv2_520263",null,"Methyloversatilis universalis FAM5","fdsB","NAD-dependent formate dehydrogenase beta subunit","_",0.85309,0.99031,38.75,{"v":5E-117,"d":"5.00E-117"},1,1,"1.1 : Carbon compound utilization ; 1.4 : Energy production/transport ;","1.2.1.2","2 : Cytoplasmic","5 : Central intermediary metabolism ; 5.2 : One-carbon metabolism ; 6 : Energy metabolism ;","e : enzyme","9521673, 9756865","2a : Function from experimental evidences in other organisms",16,524,599,14,508,516]
[null,"NIDE1931",null,"Candidatus Nitrospira defluvii","fdsB","Formate dehydrogenase, beta subunit","_",0.69783,0.83936,42.58,{"v":9e-117,"d":"9.00E-117"},1,1,"7.1 : Cytoplasm ; 1.4.3 : Electron carrier ;","1.2.1.2","2 : Cytoplasmic","6.5 : Electron transport ; 5.2 : One-carbon metabolism ;","e : enzyme","15862094, 2181145, 9756865","2b : Function from indirect experimental evidences (e.g. phenotypes)",112,529,599,86,497,498]
[null,"MAGMOv5_3364",null,"Magnetotactic ovoidal bacterium MO-1","nuoF","NADH-quinone oxidoreductase chain F (NADH dehydrogenase I, chain F) (NDH-1, chain F)","_",0.70284,0.98826,42.99,{"v":2E-116,"d":"2.00E-116"},1,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.99.5, 1.6.5.3","2 : Cytoplasmic","16.10 : Respire ; 16.7 : Manage energy ; 6.1 : Aerobic ; 6.3 : Anaerobic ; 6.5 : Electron transport ;","e : enzyme","12118882, 12923180, 12975362, 15175326, 15368583, 7565112, 9219542","2a : Function from experimental evidences in other organisms",115,533,599,5,423,426]
[null,"Rmet_0554",null,"Cupriavidus metallidurans CH34","fdsB","NAD-dependent formate dehydrogenase beta subunit","_",0.83639,0.96718,38.72,{"v":1e-115,"d":"1.00E-115"},1,1,"_","1.2.1.2","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",9756865,"2b : Function from indirect experimental evidences (e.g. phenotypes)",26,524,599,20,508,518]
[null,"NIDE0611",null,"Candidatus Nitrospira defluvii","nuoF","NADH-quinone oxidoreductase, subunit F","_",0.65776,0.90575,42.39,{"v":2e-115,"d":"2.00E-115"},2,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ; 4.S.132 : Na+/ H+ ;","1.6.99.5","6 : Inner membrane-associated","6 : Energy metabolism ; 6.1 : Aerobic ; 6.3 : Anaerobic ; 6.5 : Electron transport ;","e : enzyme","12730198, 17157874, 1903537, 7690854, 8366049, 8566820, 9030257, 9593861","2a : Function from experimental evidences in other organisms",131,524,599,20,413,435]
[null,"METDI5438",null,"Methylobacterium extorquens DM4","fdh2B","NAD-dependent formate dehydrogenase, Molybdenum containing, beta subunit","_",0.8197,0.94605,38.7,{"v":9e-115,"d":"9.00E-115"},1,1,"1.4.3 : Electron carrier ; 7.1 : Cytoplasm ;","1.2.1.2","2 : Cytoplasmic","6.5 : Electron transport ; 5.2 : One-carbon metabolism ;","e : enzyme",12730156,"1c : Function from experimental evidences in the studied genus",36,524,599,30,508,519]
[null,"RALTA_A0598",null,"Cupriavidus taiwanensis LMG19424","fdsB","NAD-dependent formate dehydrogenase beta subunit","_",0.85309,0.98269,38.55,{"v":1e-114,"d":"1.00E-114"},1,1,"1.7.21 : Glyoxylate degradation ;","1.6.99.5, 1.2.1.2","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9756865,"2b : Function from indirect experimental evidences (e.g. phenotypes)",16,524,599,16,510,520]
[null,"LEPBIa1301",null,"Leptospira biflexa serovar Patoc Patoc 1","nuoF","NADH-quinone oxidoreductase, chain F (NADH dehydrogenase I, chain F) (NDH-1, chain F) (NUO6)","_",0.6778,0.95981,41.38,{"v":5e-109,"d":"5.00E-109"},1,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.5.11","2 : Cytoplasmic","16.10 : Respire ;","e : enzyme","12923180, 8774714","2a : Function from experimental evidences in other organisms",128,531,599,15,418,423]
[null,"THI_2634",null,"Thiomonas sp. 3As","nuoF","NADH-quinone oxidoreductase chain F (NADH dehydrogenase I, chain F) (NDH-1, chain F)","_",0.67446,0.91403,43.07,{"v":7e-108,"d":"7.00E-108"},1,1,"1.4 : Energy production/transport ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ;","1.6.99.5","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9108316,"2a : Function from experimental evidences in other organisms",132,533,599,35,436,442]
[null,"NMV_0272",null,"Neisseria meningitidis NEM8013","nuoF","NADH-quinone oxidoreductase chain F (NADH dehydrogenase I, chain F; NDH-1, chain F)","_",0.67613,0.93968,42.47,{"v":1E-107,"d":"1.00E-107"},1,1,"1.3.6 : Aerobic respiration ;","1.6.5.11","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",128,530,599,19,421,431]
[null,"CAGGBEG34_v5_20009",null,"Candidatus Glomeribacter gigasporarum BEG34","nuoF","NADH-quinone oxidoreductase subunit F (NADH dehydrogenase I subunit F) (NDH-1 subunit F)","_",0.67446,0.93735,43.56,{"v":1E-107,"d":"1.00E-107"},1,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.99.5","2 : Cytoplasmic","6.1 : Aerobic ; 6.3 : Anaerobic ; 6.5 : Electron transport ; 7.4 : Cations and iron carrying compounds ;","e : enzyme","1605643, 1905152, 1909571, 7690854, 8157582, 19061856","2a : Function from experimental evidences in other organisms",132,533,599,24,425,431]
[null,"CMR15v5_2233",null,"Ralstonia solanacearum CMR15","nuoF","NADH-quinone oxidoreductase subunit F","_",0.68114,0.94664,41.67,{"v":7e-107,"d":"7.00E-107"},1,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.99.5","2 : Cytoplasmic","6.1 : Aerobic ; 6.3 : Anaerobic ; 6.5 : Electron transport ; 7 : Transport and binding proteins ;","e : enzyme","15368583, 15922336, 7565112, 9219542, 9593861","2a : Function from experimental evidences in other organisms",128,533,599,20,425,431]
[null,"Rmet_0932",null,"Cupriavidus metallidurans CH34","nuoF","NADH:ubiquinone oxidoreductase, chain F","_",0.67446,0.93735,41.83,{"v":2e-106,"d":"2.00E-106"},2,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.99.5","2 : Cytoplasmic","6.1 : Aerobic ; 6.3 : Anaerobic ; 6.5 : Electron transport ; 7.4 : Cations and iron carrying compounds ;","e : enzyme","7690854, 8157582, 8366049, 9593861","2a : Function from experimental evidences in other organisms",132,533,599,24,425,431]
[null,"SBF1_v1_5500001",null,"Desulfosporosinus sp. SbF1","hndC_2b","fragment of hydrogen dehydrogenase (NADP+), gamma HndC-like subunit (NADP+-reducing) (part 2/2)","1.12.1.3-RXN ; RHEA:18640 ;",0.4424,0.97426,54.72,{"v":4e-106,"d":"4.00E-106"},5,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",328,592,599,2,264,272]
[null,"RALTA_A1039",null,"Cupriavidus taiwanensis LMG19424","nuoF","NADH:ubiquinone oxidoreductase complex I, chain F","_",0.67446,0.93735,41.83,{"v":5e-106,"d":"5.00E-106"},2,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.5.3","2 : Cytoplasmic","6.1 : Aerobic ;  6.3 : Anaerobic ;  6.5 : Electron transport ;  7 : Transport and binding proteins ;","e : enzyme",9593861,"2a : Function from experimental evidences in other organisms",132,533,599,24,425,431]
[null,"PSEEN1827","_","Pseudomonas entomophila L48","_","putative formate dehydrogenase, beta subunit","_",0.82471,0.95551,38.26,{"v":3e-105,"d":"3.00E-105"},1,1,"1.4.3 : Electron carrier ;","1.6.99.5","Unknown","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",36,524,599,29,508,517]
[null,"ACIAD0735",null,"Acinetobacter baylyi ADP1","nuoF","NADH dehydrogenase I chain F","NADH-DEHYDROG-A-RXN ; NADH-DEHYDROGENASE-RXN ;",0.66778,0.90293,40.5,{"v":9e-104,"d":"9.00E-104"},1,1,"1.3.6 : aerobic respiration ; 1.4.1 : electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ;","1.6.5.3","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",131,528,599,31,429,443]
[null,"PP_4123",null,"Pseudomonas putida KT2440","nuoF","NADH-quinone oxidoreductase subunit F","NADH-DEHYDROGENASE-QUINONE-RXN ; 1.6.99.5-RXN ;",0.68114,0.90066,40.44,{"v":5e-101,"d":"5.00E-101"},2,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ;","1.6.5.11","2 : Cytoplasmic","6.1 : Aerobic ; 6.3 : Anaerobic ; 6.5 : Electron transport ; 7.4 : Cations and iron carrying compounds ;","c : carrier","8157582, 9593861","2a : Function from experimental evidences in other organisms",121,525,599,25,430,453]
[null,"PSEEN3488",null,"Pseudomonas entomophila L48","nuoF","NADH dehydrogenase I chain F","_",0.68114,0.89868,40.44,{"v":7e-101,"d":"7.00E-101"},2,1,"1.3.6 : Aerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ;","1.6.5.3","Inner membrane protein","6 : Energy metabolism ; 7 : Transport and binding proteins ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",121,525,599,25,430,454]
[null,"BN44v3_60657",null,"Mycobacterium canettii STB-D","nuoF","Putative NADH dehydrogenase I (chain F) NuoF (NADH-ubiquinone oxidoreductase chain F)","_",0.66444,0.89438,41.96,{"v":3e-100,"d":"3.00E-100"},1,1,"7 : intermediary metabolism and respiration ;","1.6.5.3, 1.6.99.5","2 : Cytoplasmic","_","e : enzyme","11929527, 12657046","3 : Putative function from multiple computational evidences",140,533,599,35,429,445]
[null,"BN43v3_60136",null,"Mycobacterium canettii STB-L","nuoF","Putative NADH dehydrogenase I (chain F) NuoF (NADH-ubiquinone oxidoreductase chain F)","_",0.66444,0.89438,41.96,{"v":3e-100,"d":"3.00E-100"},1,1,"7 : intermediary metabolism and respiration ;","1.6.5.3, 1.6.99.5","2 : Cytoplasmic","_","e : enzyme","11929527, 12657046","3 : Putative function from multiple computational evidences",140,533,599,35,429,445]
[null,"BN45v3_60156",null,"Mycobacterium canettii STB-J","nuoF","Putative NADH dehydrogenase I (chain F) NuoF (NADH-ubiquinone oxidoreductase chain F)","_",0.66444,0.89438,41.71,{"v":5e-99,"d":"5.00E-99"},1,1,"7 : intermediary metabolism and respiration ;","1.6.5.3, 1.6.99.5","2 : Cytoplasmic","_","e : enzyme","11929527, 12657046","3 : Putative function from multiple computational evidences",140,533,599,35,429,445]
[null,"BN42v3_41193",null,"Mycobacterium canettii STB-K","nuoF","Putative NADH dehydrogenase I (chain F) NuoF (NADH-ubiquinone oxidoreductase chain F)","_",0.66444,0.89438,41.71,{"v":5e-99,"d":"5.00E-99"},1,1,"7 : intermediary metabolism and respiration ;","1.6.5.3, 1.6.99.5","2 : Cytoplasmic","_","e : enzyme","11929527, 12657046","3 : Putative function from multiple computational evidences",140,533,599,35,429,445]
[null,"AZOLI_2201",null,"Azospirillum lipoferum 4B","nuoF","NADH-quinone oxidoreductase, subunit F","_",0.63439,0.88578,39.21,{"v":4e-87,"d":"4.00E-87"},1,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.99.5, 1.6.5.3","2 : Cytoplasmic","6.1 : Aerobic ; 6.3 : Anaerobic ; 6.5 : Electron transport ; 7 : Transport and binding proteins ;","e : enzyme",7690854,"2a : Function from experimental evidences in other organisms",156,532,599,43,421,429]
[null,"BBta_4556",null,"Bradyrhizobium sp. BTAi1","nuoF","NADH-quinone oxidoreductase chain F","_",0.68447,0.92971,38.05,{"v":5e-84,"d":"5.00E-84"},2,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.99.5, 1.6.5.3","2 : Cytoplasmic","16.10 : Respire ; 16.7 : Manage energy ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",132,537,599,20,426,441]
[null,"BRADO4179",null,"Bradyrhizobium sp. ORS278","nuoF","NADH-quinone oxidoreductase chain F (NADH dehydrogenase I, chain F) (NDH-1, chain F)","_",0.6995,0.95011,37.47,{"v":2e-83,"d":"2.00E-83"},2,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.99.5, 1.6.5.3","2 : Cytoplasmic","16.10 : Respire ; 16.7 : Manage energy ;","e : enzyme","12118882, 12923180, 12975362, 15175326, 15368583, 7565112, 9219542","2a : Function from experimental evidences in other organisms",123,537,599,11,426,441]
[null,"MGMSRv2_1322",null,"Magnetospirillum gryphiswaldense MSR-1 v2","nqo1","NADH-quinone oxidoreductase chain 1","_",0.65609,0.92254,38.68,{"v":5e-83,"d":"5.00E-83"},2,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.99.3","2 : Cytoplasmic","6.1 : Aerobic ; 6.3 : Anaerobic ; 16.7 : Manage energy ; 16.10 : Respire ;","e : enzyme","1905152, 1909571, 1605643","2b : Function from indirect experimental evidences (e.g. phenotypes)",146,535,599,34,425,426]
[null,"METDI1561",null,"Methylobacterium extorquens DM4","nuoF","NADH-quinone oxidoreductase chain F (NADH dehydrogenase I, chain F)","_",0.6828,0.94457,38.14,{"v":1e-82,"d":"1.00E-82"},2,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.5.3","2 : Cytoplasmic","6.1 : Aerobic ; 6.3 : Anaerobic ; 6.5 : Electron transport ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",123,528,599,11,416,433]
[null,"Mchl_1209",null,"Methylobacterium extorquens CM4","nuoF","NADH-quinone oxidoreductase chain F","_",0.6828,0.94457,38.14,{"v":1e-82,"d":"1.00E-82"},2,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.5.3","2 : Cytoplasmic","6.1 : Aerobic ; 6.3 : Anaerobic ; 6.5 : Electron transport ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",123,528,599,11,416,433]
[null,"ADVE02_v2_14053",null,"Methylosinus trichosporium OB3b","nuoF","NADH-quinone oxidoreductase subunit F","_",0.68447,0.9447,36.83,{"v":6e-81,"d":"6.00E-81"},2,1,"_","1.6.99.5","5 : Inner membrane protein","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",130,528,599,10,417,434]
[null,"RM41v1_500061",null,"Sinorhizobium sp. Rm41","nuoF","NADH-quinone oxidoreductase chain F (NADH dehydrogenase I, chain F) (NDH-1, chain F)","_",0.68447,0.9447,36.83,{"v":1e-80,"d":"1.00E-80"},3,1,"1.3.6 : Aerobic respiration ; 1.3.7 : Anaerobic respiration ; 1.4.1 : Electron donor ; 4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ; 7.1 : Cytoplasm ;","1.6.99.5, 1.6.5.3","2 : Cytoplasmic","16.7 : Manage energy ; 16.10 : Respire ;","e : enzyme","12118882, 12923180, 12975362, 15175326, 15368583, 7565112, 9219542","2a : Function from experimental evidences in other organisms",123,528,599,11,416,434]
[null,"RCFBPv5_mp0830",null,"Ralstonia solanacearum CFBP2957","nuoF","NADH-quinone oxidoreductase subunit F","_",0.67947,0.85504,36.12,{"v":1e-74,"d":"1.00E-74"},1,1,"_","1.6.99.5","2 : Cytoplasmic","6.1 : Aerobic ; 6.3 : Anaerobic ; 6.5 : Electron transport ;","e : enzyme","7690854, 8157582, 8366049, 9593861","2a : Function from experimental evidences in other organisms",119,523,599,78,470,476]
[null,"SCFA_v1_1110001",null,"Ca. Phosphitivorax butyraticus R76","hndC","hydrogen dehydrogenase (NADP+), gamma HndC-like subunit (NADP+-reducing)","_",0.42404,0.90391,39.76,{"v":2e-57,"d":"2.00E-57"},4,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,261,599,30,280,281]
[null,"SBF1_v1_1490001",null,"Desulfosporosinus sp. SbF1","hndC_2a","fragment of hydrogen dehydrogenase (NADP+), gamma HndC-like subunit (NADP+-reducing) (part 1/2)","1.12.1.3-RXN ; RHEA:18640 ;",0.36561,0.87952,44.29,{"v":2e-57,"d":"2.00E-57"},6,1,"_","1.12.1.3","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,219,599,35,248,249]
[]
["CLOSTRIBL3_v1_10093","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"SCFA_v1_2590003",null,"Ca. Phosphitivorax butyraticus R76","hydA","NADH dehydrogenase","_",0.88048,0.91322,43.44,{"v":3E-57,"d":"3.00E-57"},1,1,"_","1.12.7.2","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,217,251,6,223,242]
[null,"SCFA_v1_560026",null,"Ca. Phosphitivorax anaerolimi F81","hydA","putative [Fe] hydrogenase (or NADP-reducing hydrogenase subunit HndC)","_",0.91235,0.94628,43.23,{"v":9e-57,"d":"9.00E-57"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,225,251,6,231,242]
[]
["CLOSTRIBL3_v1_13020","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_32580","_","Clostridium difficile 630","_","Iron hydrogenase","_",0.95816,1.02004,41.92,{"v":9e-109,"d":"9.00E-109"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","10368269, 9836629","2a : Function from experimental evidences in other organisms",8,447,449,18,463,478]
[]
["CLOSTRIBL3_v1_20317","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_08940",null,"Clostridium difficile 630","_","Putative iron-dependent hydrogenase","_",1.00201,1.00605,55.91,0,1,1,"_","1.12.7.2","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,496,496,1,498,498]
[null,"CD630_08930",null,"Clostridium difficile 630","_","Putative iron-dependent hydrogenase","_",0.97642,1.00202,54.53,0,2,1,"_","1.12.7.2","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,496,496,14,509,509]
[]
["CLOSTRIBL3_v1_12009","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"ECK1699","_","Escherichia coli K12","ydiD","short chain acyl-CoA synthetase, anaerobic","ACYLCOASYN-RXN ;",0.96113,0.97143,44.49,{"v":2E-169,"d":"2.00E-169"},1,1,"_","_","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","12535077, 15213221, 7984428","1a : Function from experimental evidences in the studied strain",5,548,560,23,563,566]
[]
["CLOSTRIBL3_v1_10745","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"RALTA_B1570","_","Cupriavidus taiwanensis LMG19424","pta","phosphate acetyltransferase (taurine catabolism pathway)","_",0.9593,0.99698,47.27,{"v":2E-99,"d":"2.00E-99"},1,1,"1.8.2 : Sulfur metabolism ;","2.3.1.8","2 : Cytoplasmic","5.5 : Sulfur metabolism ;","e : enzyme","12358600, 8702268","2a : Function from experimental evidences in other organisms",1,330,331,1,330,344]
[null,"VIBNIv4_B0182","_","Vibrio nigripulchritudo SFn1","pta","Phosphate acetyltransferase","_",0.99398,0.99698,45.45,{"v":2e-98,"d":"2.00E-98"},1,1,"7.1 : Cytoplasm ; 1 : Metabolism ;","2.3.1.8","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","8702268, 11466286","2a : Function from experimental evidences in other organisms",1,330,331,1,330,332]
[null,"HELPY_0889",null,"Helicobacter pylori B38","pta","Phosphotransacetylase","_",0.61776,0.96677,49.38,{"v":1e-96,"d":"1.00E-96"},1,1,"1.1.3.7 : Threonine catabolism ; 1.3.5 : Fermentation ; 1.7.28 : Pyruvate catabolism ; 1.7.29 : Acetate catabolism ; 1.7.35 : Lactate oxidation ;","2.3.1.8","1 : Unknown","6.7 : Fermentation ;","e : enzyme","15048838, 15062079, 16552088, 16678422","2a : Function from experimental evidences in other organisms",11,330,331,205,517,518]
[null,"BSU37660","_","Bacillus subtilis 168","pta","phosphotransacetylase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.94562,0.96904,49.84,{"v":2e-96,"d":"2.00E-96"},1,1,"2.1.1 : Specific pathways ;","2.3.1.8","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme","4201530, 10559153, 10809684, 16283428, 17183215, 17233734, 21453533, 23468065, 25355936","1a : Function from experimental evidences in the studied strain",17,329,331,18,322,323]
[null,"CDIV41_v1_140089","_","Carnobacterium divergens V41","pta","Phosphate acetyltransferase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.9577,0.97239,49.84,{"v":3e-94,"d":"3.00E-94"},1,1,"_","2.3.1.8","2 : Cytoplasmic","6.2 : Amino acids and amines ; 6.7 : Fermentation ;","e : enzyme",7883769,"2a : Function from experimental evidences in other organisms",15,329,331,13,323,326]
[null,"NMV_1777","_","Neisseria meningitidis NEM8013","pta","phosphate acetyltransferase (phosphotransacetylase)","_",0.646,0.97583,50.15,{"v":1e-93,"d":"1.00E-93"},1,1,"1.3.5 : Fermentation ;","2.3.1.8","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",9,330,331,183,496,500]
[null,"BN44v3_10449",null,"Mycobacterium canettii STB-D","pta","Putative phosphate acetyltransferase Pta (phosphotransacetylase)","_",0.45915,0.98489,47.85,{"v":2e-93,"d":"2.00E-93"},1,1,"7 : intermediary metabolism and respiration ;","2.3.1.8","1 : Unknown","_","e : enzyme",17443846,"3 : Putative function from multiple computational evidences",6,331,331,389,707,710]
[null,"NMCC_0579","_","Neisseria meningitidis 053442","_","putative phosphate acetyltransferase (phosphotransacetylase)","_",0.59375,0.97583,50.15,{"v":2e-93,"d":"2.00E-93"},1,1,"_","2.3.1.8","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",9,330,331,227,540,544]
[null,"BN45v3_10446",null,"Mycobacterium canettii STB-J","pta","Putative phosphate acetyltransferase Pta (phosphotransacetylase)","_",0.45915,0.98489,47.85,{"v":4e-93,"d":"4.00E-93"},1,1,"7 : intermediary metabolism and respiration ;","2.3.1.8","1 : Unknown","_","e : enzyme",17443846,"3 : Putative function from multiple computational evidences",6,331,331,389,707,710]
[null,"BN43v3_10441",null,"Mycobacterium canettii STB-L","pta","Putative phosphate acetyltransferase Pta (phosphotransacetylase)","_",0.47246,0.98489,47.55,{"v":4e-93,"d":"4.00E-93"},1,1,"7 : intermediary metabolism and respiration ;","2.3.1.8","1 : Unknown","_","e : enzyme",17443846,"3 : Putative function from multiple computational evidences",6,331,331,369,687,690]
[null,"BN13v1_910015",null,"Tetrasphaera jenkinsii Ben74","pta","Phosphate acetyltransferase","_",0.47238,0.98187,46.15,{"v":9e-93,"d":"9.00E-93"},1,1,"_","2.3.1.8","2 : Cytoplasmic","5 : Central intermediary metabolism ; 6 : Energy metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",5,329,331,367,684,688]
[null,"BN42v3_20129",null,"Mycobacterium canettii STB-K","pta","Putative phosphate acetyltransferase Pta (phosphotransacetylase)","_",0.47246,0.98489,47.24,{"v":1e-92,"d":"1.00E-92"},1,1,"7 : intermediary metabolism and respiration ;","2.3.1.8","1 : Unknown","_","e : enzyme",17443846,"3 : Putative function from multiple computational evidences",6,331,331,369,687,690]
[null,"SSV_v1_1079","_","Streptococcus sanguinis 2908","pta","phosphate acetyltransferase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ;",1.00302,1.02154,46.99,{"v":1E-91,"d":"1.00E-91"},1,1,"_","2.3.1.8","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme","4201530, 10559153, 10809684, 16283428, 17183215, 17233734, 21453533","2a : Function from experimental evidences in other organisms",1,331,331,1,323,325]
[null,"VIBNIv4_A2402",null,"Vibrio nigripulchritudo SFn1","pta","phosphate acetyltransferase","_",0.45467,0.98489,50.31,{"v":3e-91,"d":"3.00E-91"},1,1,"1.3.5 : Fermentation ; 1.7.28 : Pyruvate catabolism ; 1.7.29 : Acetate catabolism ;","2.3.1.8","1 : Unknown","6.7 : Fermentation ;","e : enzyme","7883769, 7918659, 9205837, 9278503, 16738553, 2536666","2a : Function from experimental evidences in other organisms",6,330,331,394,710,717]
[null,"BTCD_v1_2175","_","Brochothrix thermosphacta CD337","pta","phosphotransacetylase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ;",0.94562,0.96308,46.96,{"v":4E-90,"d":"4.00E-90"},1,1,"_","2.3.1.8","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","4201530, 10559153, 10809684, 16283428, 17183215, 17233734, 21453533","2a : Function from experimental evidences in other organisms",17,329,331,18,322,325]
[null,"BN424_559","_","Carnobacterium maltaromaticum LMA28 v1","pta","phosphate acetyltransferase","PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.89124,1.01027,50.85,{"v":4E-90,"d":"4.00E-90"},1,1,"_","2.3.1.8","1 : Unknown","6.2 : Amino acids and amines ; 6.7 : Fermentation ;","e : enzyme","7883769, 7918659, 21796982","2a : Function from experimental evidences in other organisms",35,329,331,1,289,292]
[null,"BN10v3_560038",null,"Tetrasphaera elongata Lp2","pta","Phosphate acetyltransferase","_",0.47025,0.97885,46.3,{"v":4e-89,"d":"4.00E-89"},1,1,"_","2.3.1.8","2 : Cytoplasmic","5 : Central intermediary metabolism ; 6 : Energy metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",6,329,331,370,686,689]
[null,"RM41v1_pld1620006","_","Sinorhizobium sp. Rm41","pta","Phosphate acetyltransferase","_",0.99396,0.99697,45.29,{"v":5e-87,"d":"5.00E-87"},1,1,"1.1 : Carbon compound utilization ; 1.3.5 : Fermentation ; 1.7 : Central intermediary metabolism ;","2.3.1.8","1 : Unknown","6.2 : Amino acids and amines ; 6.7 : Fermentation ;","e : enzyme",8226623,"2a : Function from experimental evidences in other organisms",1,329,331,1,329,330]
[null,"MARHY2149",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","pta","phosphate acetyltransferase","_",0.49317,0.98187,47.69,{"v":7e-87,"d":"7.00E-87"},1,1,"1.1.3.7 : Threonine catabolism ; 1.3.5 : Fermentation ; 1.7.28 : Pyruvate catabolism ; 1.7.29 : Acetate catabolism ; 1.7.35 : Lactate oxidation ;","2.3.1.8","1 : Unknown","6.2 : Amino acids and amines ; 6.7 : Fermentation ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",6,330,331,335,651,659]
[null,"BN874v1_910011","_","Candidatus Contendobacter odensis Run_B_J11","pta","Phosphate acetyltransferase","_",0.44444,0.96677,46.56,{"v":1e-86,"d":"1.00E-86"},1,1,"1.7.29 : Acetate catabolism ;","2.3.1.8","2 : Cytoplasmic","_","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",11,330,331,398,709,720]
[null,"BN12v2_1100006",null,"Tetrasphaera japonica T1-X7","pta","phosphate acetyltransferase (fragment)","_",0.67532,0.9426,45.51,{"v":2e-86,"d":"2.00E-86"},1,1,"_","2.3.1.8","2 : Cytoplasmic","5 : Central intermediary metabolism ; 6 : Energy metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",18,329,331,155,459,462]
[null,"BN11v3_1350009",null,"Tetrasphaera australiensis Ben110","pta","Phosphate acetyltransferase","_",0.47445,0.98187,44.62,{"v":6e-84,"d":"6.00E-84"},1,1,"_","2.3.1.8","2 : Cytoplasmic","5 : Central intermediary metabolism ; 6 : Energy metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",5,329,331,366,683,685]
[null,"SBF1_v1_1100027","_","Desulfosporosinus sp. SbF1","pta","phosphate acetyltransferase","PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.98187,1.00619,44.31,{"v":2e-82,"d":"2.00E-82"},1,1,"_","2.3.1.8","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,327,331,1,321,323]
[null,"BN873v1_210146","_","Candidatus Competibacter denitrificans Run_A_D11","pta","Phosphate acetyltransferase","_",0.44506,0.96677,45.62,{"v":1e-81,"d":"1.00E-81"},1,1,"1.7.29 : Acetate catabolism ;","2.3.1.8","2 : Cytoplasmic","_","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",11,330,331,398,709,719]
[null,"ABAYE3283",null,"Acinetobacter baumannii AYE","pta","phosphate acetyltransferase","_",0.44678,0.96375,47.02,{"v":3e-81,"d":"3.00E-81"},1,1,"1.1.1 : carbon compounds ; 1.1.3 : amino acids ; 1.7.28 : pyruvate oxidation ; 1.7.29 : acetate catabolism ; 1.7.30 : threonine catabolism ;","2.3.1.8","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",13,330,331,400,708,714]
[null,"ACIAD0540",null,"Acinetobacter baylyi ADP1","pta","phosphate acetyltransferase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ; RHEA:19524 ; RHEA:28049 ;",0.44306,0.96375,46.71,{"v":4e-81,"d":"4.00E-81"},1,1,"1.1.3.7 : Threonine catabolism ; 1.7.28 : Pyruvate catabolism ; 1.7.29 : Acetate catabolism ; 1.7.35 : Lactate oxidation ;","2.3.1.8","2 : Cytoplasmic","6.2 : Amino acids and amines ; 16.2 : Construct biomass (Anabolism) ;","e : enzyme","7765811, 15231792, 10542166, 16272400, 19852855","2a : Function from experimental evidences in other organisms",13,330,331,400,708,720]
[null,"PSEEN0916","_","Pseudomonas entomophila L48","pta","phosphate acetyltransferase","_",0.45904,0.98187,43.69,{"v":1e-76,"d":"1.00E-76"},1,1,"1.7.28 : Pyruvate catabolism ; 1.3.5 : Fermentation ; 1.3.7 : Anaerobic respiration ; 1.7.29 : Acetate catabolism ;","2.3.1.8","Unknown","5 : Central intermediary metabolism ; 6 : Energy metabolism ;","e : enzyme",15231792,"2a : Function from experimental evidences in other organisms",6,329,331,389,704,708]
[null,"HPP12_0902",null,"Helicobacter pylori P12","pta-2","Fragment of phosphotransacetylase (Part 2)","_",0.55891,1.03352,54.59,{"v":4e-57,"d":"4.00E-57"},1,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",146,330,331,1,178,179]
[null,"HPAG1_0885",null,"Helicobacter pylori HPAG1","_","Fragment of phosphotransacetylase (Part 3)","_",0.55891,1.03352,54.59,{"v":6E-57,"d":"6.00E-57"},1,1,"_","2.3.1.8","1 : Unknown","_","u : unknown","_","5 : Unknown function",146,330,331,1,178,179]
[null,"HP0904",null,"Helicobacter pylori 26695","pta","Fragment of putative phosphotransacetylase (Part 4)","_",0.2145,0.9726,67.61,{"v":3e-26,"d":"3.00E-26"},1,1,"6.7 : Fermentation ;","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",260,330,331,2,72,73]
[null,"HP0904",null,"Helicobacter pylori 26695","pta","Fragment of putative phosphotransacetylase (Part 3)","_",0.36858,0.99187,45.9,{"v":2e-24,"d":"2.00E-24"},2,1,"6.7 : Fermentation ;","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",146,267,331,1,115,123]
[null,"HP0904",null,"Helicobacter pylori 26695","pta","Fragment of putative phosphotransacetylase (Part 2)","_",0.32326,0.96396,38.32,{"v":8e-19,"d":"8.00E-19"},3,1,"6.7 : Fermentation ;","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",22,128,331,7,111,111]
[]
["CLOSTRIBL3_v1_10746","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_11750",null,"Clostridium difficile 630","ackA","Acetate kinase (Acetokinase)","_",0.99749,1,63.07,0,1,1,"1.1.3.7 : Threonine catabolism ; 1.3.5 : Fermentation ; 1.7.28 : Pyruvate catabolism ; 1.7.29 : Acetate catabolism ; 7.1 : Cytoplasm ;","2.7.2.1","2 : Cytoplasmic","6.2 : Amino acids and amines ; 6.7 : Fermentation ;","e : enzyme","18055595, 19026742, 19019159","2a : Function from experimental evidences in other organisms",1,396,399,1,398,398]
[null,"SBF1_v1_800074",null,"Desulfosporosinus sp. SbF1","ackA","acetate kinase","ACETATEKIN-RXN ; RHEA:11355 ;",0.99499,1,57.43,{"v":9e-173,"d":"9.00E-173"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,396,399,1,397,397]
[null,"BSU29470","_","Bacillus subtilis 168","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ; RHEA:11352 ;",0.98997,1,55.7,{"v":4E-160,"d":"4.00E-160"},1,1,"2.1.1 : Specific pathways ;","2.7.2.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8226682, 9811655, 11244084, 16995897, 19019159, 26098117","1a : Function from experimental evidences in the studied strain",2,396,399,3,395,395]
[null,"SSV_v1_0105","_","Streptococcus sanguinis 2908","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ;",0.98496,0.98992,54.45,{"v":9e-144,"d":"9.00E-144"},1,1,"_","2.7.2.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8226682, 9811655, 11244084, 16995897, 19019159","2a : Function from experimental evidences in other organisms",2,392,399,3,392,397]
[null,"BTCD_v1_0691","_","Brochothrix thermosphacta CD337","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ;",0.98005,0.98496,50.64,{"v":2e-139,"d":"2.00E-139"},1,1,"_","2.7.2.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8226682, 9811655, 11244084, 16995897, 19019159","2a : Function from experimental evidences in other organisms",2,390,399,3,393,401]
[null,"EFER_2027","_","Escherichia fergusonii ATCC 35469T","_","putative acetate/propionate kinase pduW","_",0.97277,0.98496,47.84,{"v":1e-133,"d":"1.00E-133"},1,1,"_","2.7.2.1","1 : Unknown","_","e : enzyme",10498708,"3 : Putative function from multiple computational evidences",2,394,399,4,392,404]
[null,"NMA1718","_","Neisseria meningitidis Z2491","ackA1","acetate kinase 1 (acetokinase 1)","_",0.96078,0.98246,51.53,{"v":2e-133,"d":"2.00E-133"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,391,399,16,402,408]
[null,"NMV_0875","_","Neisseria meningitidis NEM8013","ackA1","acetate kinase 1 (acetokinase 1)","_",0.98246,0.98492,51.28,{"v":5e-132,"d":"5.00E-132"},1,1,"1.3.5 : Fermentation ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,391,399,6,392,398]
[null,"VIBNIv4_A2401",null,"Vibrio nigripulchritudo SFn1","ackA","acetate kinase","_",0.98747,0.98995,47.21,{"v":3e-121,"d":"3.00E-121"},1,1,"1.3.5 : Fermentation ; 1.7.28 : Pyruvate catabolism ; 1.7.29 : Acetate catabolism ; 7.1 : Cytoplasm ;","2.7.2.1","2 : Cytoplasmic","6.7 : Fermentation ;","e : enzyme","2536666, 7883769, 9205837, 9278503, 16738553","2a : Function from experimental evidences in other organisms",3,391,399,5,392,398]
[null,"VC1098",null,"Vibrio cholerae N16961","ackA","acetate kinase","_",0.98747,0.98995,46.45,{"v":2E-118,"d":"2.00E-118"},1,1,"1.3.5 : Fermentation ; 1.7.28 : Pyruvate catabolism ; 1.7.29 : Acetate catabolism ; 7.1 : Cytoplasm ;","2.7.2.1","2 : Cytoplasmic","6.7 : Fermentation ;","e : enzyme","2536666, 7883769, 9205837, 9278503, 16738553","2a : Function from experimental evidences in other organisms",3,391,399,5,392,398]
[null,"BN12v2_1100005",null,"Tetrasphaera japonica T1-X7","ackA","Acetate kinase","_",0.98496,0.98992,45.29,{"v":2e-114,"d":"2.00E-114"},1,1,"_","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",3,395,399,6,395,397]
[null,"BN13v1_910016",null,"Tetrasphaera jenkinsii Ben74","ackA","Acetate kinase","_",0.97995,0.99239,47.31,{"v":5e-114,"d":"5.00E-114"},1,1,"_","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",2,390,399,3,387,394]
[null,"BN11v3_1350008",null,"Tetrasphaera australiensis Ben110","ackA","acetate kinase A and propionate kinase 2","_",0.97744,0.97744,46.67,{"v":5e-112,"d":"5.00E-112"},1,1,"_","2.7.2.-, 2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",2,390,399,7,391,399]
[null,"ECS88_4678","_","Escherichia coli S88","_","Putative Acetate/propionate kinase","_",0.91264,0.99499,43.58,{"v":1e-110,"d":"1.00E-110"},1,1,"_","2.7.2.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,396,399,43,433,435]
[null,"ECED1_3455","_","Escherichia coli ED1a","_","Putative Acetate/propionate kinase","_",0.91264,0.99499,43.58,{"v":1e-110,"d":"1.00E-110"},1,1,"_","2.7.2.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,396,399,43,433,435]
[null,"MARHY2148",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","ackA","acetate kinase A and propionate kinase 2","_",0.97506,0.97995,44.76,{"v":2E-107,"d":"2.00E-107"},1,1,"1.1.3.7 : Threonine catabolism ; 1.7.28 : Pyruvate catabolism ; 1.7.29 : Acetate catabolism ;","2.7.2.1, 2.7.2.-","2 : Cytoplasmic","6.2 : Amino acids and amines ; 6.7 : Fermentation ;","e : enzyme","2536666, 7883769","2a : Function from experimental evidences in other organisms",3,390,399,5,387,401]
[null,"VIBNIv4_B1211","_","Vibrio nigripulchritudo SFn1","ackA","Acetate kinase","_",0.99749,1.00252,44.72,{"v":2e-106,"d":"2.00E-106"},1,1,"7.1 : Cytoplasm ; 1.7.29 : Acetate catabolism ; 1.3.7 : Anaerobic respiration ; 1.5.3.5 : Coenzyme A ;","2.7.2.1","2 : Cytoplasmic","6.3 : Anaerobic ; 4 : Biosynthesis of cofactors, prosthetic groups, and carriers ;","e : enzyme","2536666, 7883769","2a : Function from experimental evidences in other organisms",3,395,399,6,397,397]
[null,"VS_II1135","_","Vibrio tasmaniensis LGP32","ackA-2","Acetate kinase","ACETATEKIN-RXN ; RXN-7958 ;",1.00501,1.01008,41.9,{"v":8e-105,"d":"8.00E-105"},1,1,"1.3.5 : Fermentation ; 1.5.3.5 : Coenzyme A ;","2.7.2.1","2 : Cytoplasmic","6.3 : Anaerobic ; 6.7 : Fermentation ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,395,399,6,397,397]
[null,"BN45v3_10447",null,"Mycobacterium canettii STB-J","ackA","Putative acetate kinase AckA (acetokinase)","_",0.97494,1.01039,42.93,{"v":7e-103,"d":"7.00E-103"},1,1,"7 : intermediary metabolism and respiration ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",3,390,399,5,375,385]
[null,"BN44v3_10450",null,"Mycobacterium canettii STB-D","ackA","Putative acetate kinase AckA (acetokinase)","_",0.97494,1.01039,42.93,{"v":8e-102,"d":"8.00E-102"},1,1,"7 : intermediary metabolism and respiration ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",3,390,399,5,375,385]
[null,"BN10v3_560037",null,"Tetrasphaera elongata Lp2","ackA","Acetate kinase","_",0.99248,1.05319,42.17,{"v":2e-101,"d":"2.00E-101"},1,1,"_","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",3,395,399,5,370,376]
[null,"BN43v3_10442",null,"Mycobacterium canettii STB-L","ackA","Putative acetate kinase AckA (acetokinase)","_",0.97494,1.01039,42.67,{"v":3e-101,"d":"3.00E-101"},1,1,"7 : intermediary metabolism and respiration ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",3,390,399,5,375,385]
[null,"BN42v3_20130",null,"Mycobacterium canettii STB-K","ackA","Putative acetate kinase AckA (acetokinase)","_",0.97494,1.01039,42.67,{"v":6e-101,"d":"6.00E-101"},1,1,"7 : intermediary metabolism and respiration ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",3,390,399,5,375,385]
[null,"ABAYE3282",null,"Acinetobacter baumannii AYE","ack","acetate kinase (propionate kinase)","_",0.9925,0.99499,41.56,{"v":8e-98,"d":"8.00E-98"},1,1,"1.1.1 : carbon compounds ; 1.1.3 : amino acids ; 1.7.28 : pyruvate oxidation ; 1.7.29 : acetate catabolism ; 1.7.30 : threonine catabolism ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,396,399,5,388,400]
[null,"MGMSRv2_1019","_","Magnetospirillum gryphiswaldense MSR-1 v2","ackA","Acetate kinase","_",0.95923,1.00251,41.25,{"v":1E-97,"d":"1.00E-97"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 1.7.29 : Acetate catabolism ; 7.1 : Cytoplasm ;","2.7.2.1","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme",10094701,"2a : Function from experimental evidences in other organisms",3,399,399,22,413,417]
[null,"ACIAD0541",null,"Acinetobacter baylyi ADP1","ack","acetate kinase (propionate kinase)","ACETATEKIN-RXN ; PROPKIN-RXN ; RXN-7958 ; RHEA:11355 ; RHEA:23151 ;",1,1.00501,41.4,{"v":2e-97,"d":"2.00E-97"},1,1,"1.1.3.7 : Threonine catabolism ; 1.7.28 : Pyruvate catabolism ; 1.7.29 : Acetate catabolism ;","2.7.2.1","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","2844264, 6252971, 3020034","1b : Function from experimental evidences in the studied species",3,399,399,5,392,401]
[null,"MT37II_v2_a0110",null,"Ca. Spiroplasma holothuricola MT37","ackA","acetate kinase (possibly promiscuous)","RXN-7958 ; ACETATEKIN-RXN ; RHEA:11352 ;",0.97778,0.99248,40.15,{"v":5e-95,"d":"5.00E-95"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,391,399,7,394,405]
[null,"BN874v1_640030","_","Candidatus Contendobacter odensis Run_B_J11","ackA","Acetate/propionate kinase","_",1.01253,1.03061,40.1,{"v":7e-92,"d":"7.00E-92"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.3 : Propionate degradation ;","2.7.2.1, 2.7.2.-","2 : Cytoplasmic","_","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",3,396,399,5,392,392]
[null,"HELPY_0888",null,"Helicobacter pylori B38","_","Fragment of putative acetate kinase AckA (Part 1)","_",0.7218,0.96,47.57,{"v":5E-91,"d":"5.00E-91"},1,1,"1.3.5 : Fermentation ;","2.7.2.1","1 : Unknown","6.7 : Fermentation ;","e : enzyme","12634340, 15755952, 17465479, 18223085","5 : Unknown function",1,284,399,1,286,300]
[null,"NIDE3516","_","Candidatus Nitrospira defluvii","ackA","Acetate kinase","_",0.96535,0.97744,42.31,{"v":1E-89,"d":"1.00E-89"},1,1,"1.3.5 : Fermentation ; 1.7.28 : Pyruvate catabolism ; 1.7.29 : Acetate catabolism ; 7.1 : Cytoplasm ; 1.1.3.7 : Threonine catabolism ;","2.7.2.1","2 : Cytoplasmic","6.2 : Amino acids and amines ; 6.7 : Fermentation ; 6.8 : Glycolysis/gluconeogenesis ;","e : enzyme","10074080, 10075432, 10094701, 11133963, 7883769, 8226623, 8226682, 8702268, 9805396","2a : Function from experimental evidences in other organisms",3,389,399,11,392,404]
[null,"AZOLI_p20461","_","Azospirillum lipoferum 4B","ackA2","Acetate kinase","_",0.98529,1.00752,40.3,{"v":2e-89,"d":"2.00E-89"},1,1,"7.1 : Cytoplasm ; 1.5.4 : Fatty acid and phosphatidic acid ; 1.7.29 : Acetate catabolism ;","2.7.2.1","2 : Cytoplasmic","3.1 : Biosynthesis ; 6 : Energy metabolism ;","e : enzyme","10094701, 2536666, 3053659, 7883769, 9484901","2a : Function from experimental evidences in other organisms",4,395,399,13,399,408]
[null,"HP0903",null,"Helicobacter pylori 26695","ackA","Fragment of putative acetate kinase (Part 1)","_",0.7218,0.9863,47.22,{"v":5e-89,"d":"5.00E-89"},1,1,"6.7 : Fermentation ;","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,284,399,1,286,292]
[null,"BN873v1_460010","_","Candidatus Competibacter denitrificans Run_A_D11","ackA","Acetate/propionate kinase","_",1.01425,1.07018,36.07,{"v":2e-88,"d":"2.00E-88"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.3 : Propionate degradation ; 1.7.29 : Acetate catabolism ;","2.7.2.1, 2.7.2.-","2 : Cytoplasmic","_","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",3,395,399,5,419,421]
[null,"BRADO6361","_","Bradyrhizobium sp. ORS278","ackA","Acetate kinase","_",0.98526,1.00501,39.4,{"v":3e-88,"d":"3.00E-88"},1,1,"7.1 : Cytoplasm ; 1.5.4 : Fatty acid and phosphatidic acid ; 1.7.29 : Acetate catabolism ;","2.7.2.1","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme",10094701,"2a : Function from experimental evidences in other organisms",3,395,399,5,391,407]
[null,"p2METDI0002","_","Methylobacterium extorquens DM4","ackA","acetate kinase","_",0.98747,1.00767,39.34,{"v":5e-88,"d":"5.00E-88"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme",10094701,"2a : Function from experimental evidences in other organisms",4,392,399,7,388,391]
[null,"BN77v1_3277","_","Rhizobium mesoamericanum STM3625","ackA","Acetate kinase","_",0.99749,1.02051,38.19,{"v":6e-85,"d":"6.00E-85"},1,1,"5.5 : Adaptation to stress ; 5.5.6 : Other stresses (mechanical, nutritional, oxidative) ;","2.7.2.1","1 : Unknown","_","e : enzyme","10094701, 9805396","2a : Function from experimental evidences in other organisms",3,395,399,4,388,390]
[null,"RALTA_A1397","_","Cupriavidus taiwanensis LMG19424","_","Acetate kinase","_",1.01754,1.02525,38.92,{"v":6e-85,"d":"6.00E-85"},1,1,"1.1.3.7 : Threonine catabolism ; 1.7.28 : Pyruvate catabolism ; 1.7.29 : Acetate catabolism ;","2.7.2.1","1 : Unknown","6.2 : Amino acids and amines ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,395,399,5,391,396]
[null,"AZOLI_0599","_","Azospirillum lipoferum 4B","ackA1","Acetate kinase","_",1.00501,1.01777,39.65,{"v":2e-84,"d":"2.00E-84"},1,1,"7.1 : Cytoplasm ; 1.5.4 : Fatty acid and phosphatidic acid ; 1.7.29 : Acetate catabolism ;","2.7.2.1","2 : Cytoplasmic","3.1 : Biosynthesis ; 6 : Energy metabolism ; 6.2 : Amino acids and amines ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,395,399,5,391,394]
[null,"HEAR1515","_","Herminiimonas arsenicoxydans","ackA","Acetate kinase (Acetokinase)","_",0.94903,0.97995,39.64,{"v":1E-83,"d":"1.00E-83"},1,1,"1.7.28 : Pyruvate catabolism ; 7.1 : Cytoplasm ;","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",10094701,"2b : Function from indirect experimental evidences (e.g. phenotypes)",3,388,399,21,400,412]
[null,"RCFBPv5_mp0810","_","Ralstonia solanacearum CFBP2957","ackA","acetate kinase","_",0.98246,1,40.56,{"v":3e-83,"d":"3.00E-83"},1,1,"_","2.7.2.1","2 : Cytoplasmic","6.2 : Amino acids and amines ; 5 : Central intermediary metabolism ;","e : enzyme",10094701,"2a : Function from experimental evidences in other organisms",3,389,399,4,384,392]
[null,"METDI0790","_","Methylobacterium extorquens DM4","_","putative acetate kinase (ackA)","_",1.00501,1.01777,38.4,{"v":8e-83,"d":"8.00E-83"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,395,399,9,391,394]
[null,"RM41v1_pld1870123","_","Sinorhizobium sp. Rm41","ackA","Acetate kinase","_",1.00251,1.02041,38,{"v":1e-81,"d":"1.00E-81"},1,1,"1.3.5 : Fermentation ; 1.5.4 : Fatty acid and phosphatidic acid ; 1.7.29 : Acetate catabolism ; 7.1 : Cytoplasm ;","2.7.2.1","2 : Cytoplasmic","6.2 : Amino acids and amines ; 6.7 : Fermentation ;","e : enzyme",10094701,"1b : Function from experimental evidences in the studied species",3,396,399,4,390,392]
[null,"Rmet_0562","_","Cupriavidus metallidurans CH34","ackA2","acetate kinase","_",1.00988,1.02506,40.59,{"v":2e-81,"d":"2.00E-81"},1,1,"_","2.7.2.1","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,397,399,8,403,405]
[null,"RPSI07_mp1366","_","Ralstonia solanacearum PSI07","ackA","Acetate kinase","_",0.98496,1.00255,39.44,{"v":1E-79,"d":"1.00E-79"},1,1,"_","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",10094701,"2a : Function from experimental evidences in other organisms",3,389,399,4,384,392]
[null,"THI_1474","_","Thiomonas sp. 3As","ackA","Acetate kinase AckA","_",1,1.00251,35.75,{"v":2e-69,"d":"2.00E-69"},1,1,"1 : Metabolism ; 1.7.28 : Pyruvate catabolism ; 7.1 : Cytoplasm ;","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,391,399,6,395,400]
[null,"HPP12_0900",null,"Helicobacter pylori P12","ackA-2","Fragment of acetate kinase (Part 2)","_",0.48622,0.9604,50,{"v":6e-66,"d":"6.00E-66"},1,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",94,287,399,5,198,202]
[null,"HPB8_649",null,"Helicobacter pylori B8","_","Fragment of acetate kinase AckA (Part 2)","_",0.41855,0.91257,55.09,{"v":9e-63,"d":"9.00E-63"},1,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",118,284,399,10,176,183]
[null,"HPAG1_0884",null,"Helicobacter pylori HPAG1","_","Fragment of acetate kinase (Part 1)","_",0.38847,0.89595,40.65,{"v":4e-32,"d":"4.00E-32"},1,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,151,399,2,154,173]
[null,"HPB8_650",null,"Helicobacter pylori B8","_","Fragment of acetate kinase AckA (Part 3)","_",0.29323,0.99153,49.57,{"v":7e-29,"d":"7.00E-29"},2,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",284,399,399,2,118,118]
[null,"HPG27_856","_","Helicobacter pylori G27","_","Fragment of putative acetate kinase AckA (Part 2)","_",0.28571,0.94215,45.61,{"v":2e-26,"d":"2.00E-26"},1,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",284,396,399,5,118,121]
[null,"HPP12_0899",null,"Helicobacter pylori P12","ackA-3","Fragment of acetate kinase (Part 3)","_",0.28571,0.9661,44.74,{"v":1E-25,"d":"1.00E-25"},2,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",284,396,399,2,115,118]
[null,"HP0903",null,"Helicobacter pylori 26695","ackA","Fragment of putative acetate kinase (Part 2)","_",0.28571,0.9661,44.74,{"v":3e-25,"d":"3.00E-25"},2,1,"6.7 : Fermentation ;","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",284,396,399,2,115,118]
[null,"HPAG1_0883",null,"Helicobacter pylori HPAG1","_","Fragment of actetate kinase (Part 3)","_",0.20551,0.93182,46.34,{"v":3e-18,"d":"3.00E-18"},2,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",284,365,399,5,86,88]
[null,"HELPY_0887",null,"Helicobacter pylori B38","_","Fragment of putative acetate kinase AckA (Part 2)","_",0.20551,0.93182,45.12,{"v":2e-17,"d":"2.00E-17"},2,1,"1.3.5 : Fermentation ;","2.7.2.1","1 : Unknown","6.7 : Fermentation ;","e : enzyme","12634340, 15755952, 17465479, 18223085","5 : Unknown function",284,365,399,5,86,88]
[null,"HPP12_0901",null,"Helicobacter pylori P12","ackA-1","Fragment of acetate kinase (Part 1)","_",0.24812,1.0102,39.39,2e-15,3,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,95,399,1,97,98]
[null,"HPB8_648",null,"Helicobacter pylori B8","_","Fragment of acetate kinase AckA (Part 1)","_",0.24812,0.95192,39.39,3e-15,3,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,95,399,1,97,104]
[]
["CLOSTRIBL3_v1_11881","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"RCFBPv5_mp0504",null,"Ralstonia solanacearum CFBP2957","_","putative iron-containing alcohol dehydrogenase","_",0.99743,1.00258,54.38,{"v":2E-140,"d":"2.00E-140"},1,1,"_","1.1.1.1","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,386,387,1,388,389]
[null,"p1METDI0061","_","Methylobacterium extorquens DM4","_","putative iron-containing alcohol dehydrogenase","_",0.98966,0.99481,37.86,{"v":2e-76,"d":"2.00E-76"},1,1,"_","1.1.1.-","1 : Unknown","_","e : enzyme",2935393,"3 : Putative function from multiple computational evidences",3,382,387,2,381,385]
[null,"Rmet_4943","_","Cupriavidus metallidurans CH34","_","putative iron-containing alcohol dehydrogenase","_",0.98191,0.98701,35.79,{"v":3e-74,"d":"3.00E-74"},1,1,"1.7.1 : Unassigned reversible reactions ;","1.1.1.1","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,383,387,4,382,385]
[null,"plu1563","_","Photorhabdus luminescens TT01","yiaY","_","_",0.91214,0.92167,35.41,{"v":1E-70,"d":"1.00E-70"},1,1,"_","_","_","_","_","_","_",31,382,387,28,379,383]
[null,"ECS88_0712",null,"Escherichia coli S88","_","putative alcohol dehydrogenase","_",0.96641,0.97143,35.56,{"v":6e-69,"d":"6.00E-69"},1,1,"_","1.1.1.1","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",13,385,387,8,377,385]
[null,"PSEEN2959","_","Pseudomonas entomophila L48","adhB","alcohol dehydrogenase II (","_",0.94315,0.9555,37.53,{"v":2e-68,"d":"2.00E-68"},1,1,"1.7.1 : Unassigned reversible reactions ;","1.1.1.1","Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",20,382,387,15,378,382]
[]
["CLOSTRIBL3_v1_20137","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_19070",null,"Clostridium difficile 630","eutG","Ethanolamine iron-dependent Alcohol dehydrogenase","_",0.99476,1.01064,53.68,{"v":2e-145,"d":"2.00E-145"},1,1,"1.1.4 : Amines ;","1.1.1.1","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","19246383, 18776017, 10464203, 8113167, 18689481, 18790863, 20234377","2a : Function from experimental evidences in other organisms",1,380,382,1,375,376]
[null,"BTCD_v1_1443",null,"Brochothrix thermosphacta CD337","eutG","Ethanolamine iron-dependent Alcohol dehydrogenase","_",0.99476,1.00796,51.32,{"v":4e-128,"d":"4.00E-128"},1,1,"1.1.4 : Amines ;","1.1.1.1","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","19246383, 18776017, 10464203, 8113167, 18689481, 18790863, 20234377","2a : Function from experimental evidences in other organisms",1,380,382,1,376,377]
[null,"SSV_v1_0411",null,"Streptococcus sanguinis 2908","pduQ","NADPH-dependent butanol dehydrogenase","_",0.98953,0.99474,50.26,{"v":1e-122,"d":"1.00E-122"},1,1,"_","1.1.1.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,381,382,7,380,380]
[null,"EFER_1994","_","Escherichia fergusonii ATCC 35469T","_","putative Alcohol dehydrogenase, iron-dependent","_",0.98196,0.99738,44.09,{"v":3e-106,"d":"3.00E-106"},1,1,"_","1.1.1.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,381,382,5,380,388]
[null,"ECIAI39_4210","_","Escherichia coli IAI39","_","putative Alcohol dehydrogenase, iron-dependent","_",0.98196,0.99738,44.09,{"v":7E-106,"d":"7.00E-106"},1,1,"1.1.5.2 : Ethanol degradation ; 1.3.5 : Fermentation ;","1.1.1.1","1 : Unknown","6.7 : Fermentation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,381,382,5,380,388]
[null,"ECED1_3448","_","Escherichia coli ED1a","_","putative propanol dehydrogenase","_",0.96335,0.98925,41.85,{"v":8e-94,"d":"8.00E-94"},1,1,"_","1.1.1.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",9,376,382,10,366,372]
[null,"ECS88_4685","_","Escherichia coli S88","_","putative propanol dehydrogenase","_",0.96335,0.98925,41.58,{"v":3e-93,"d":"3.00E-93"},1,1,"_","1.1.1.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",9,376,382,10,366,372]
[null,"EFER_2022",null,"Escherichia fergusonii ATCC 35469T","_","putative Propanediol utilization propanol dehydrogenase pduQ","_",1,1.03243,40.84,{"v":7e-87,"d":"7.00E-87"},2,1,"_","1.1.1.1","1 : Unknown","6 : Energy metabolism ;","e : enzyme",10498708,"3 : Putative function from multiple computational evidences",1,380,382,1,369,370]
[null,"VIBNIv4_B2100","_","Vibrio nigripulchritudo SFn1","_","putative Alcohol dehydrogenase, iron-type","_",0.93782,0.94764,37.85,{"v":3e-72,"d":"3.00E-72"},1,1,"1.1.5.2 : Ethanol degradation ; 1.3.5 : Fermentation ; 7.1 : Cytoplasm ;","1.1.1.1","2 : Cytoplasmic","6.7 : Fermentation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",30,381,382,35,385,386]
[]
["CLOSTRIBL3_v1_12484","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"SSV_v1_0420",null,"Streptococcus sanguinis 2908","_","putative acetaldehyde dehydrogenase","_",0.85283,0.9187,52.88,{"v":1e-162,"d":"1.00E-162"},1,1,"_","1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,454,530,5,455,492]
[null,"CD630_19170",null,"Clostridium difficile 630","eutE","Ethanolamine acetaldehyde oxydoreductase","_",0.86415,0.93661,50,{"v":3e-147,"d":"3.00E-147"},1,1,"1.1.4 : Amines ;","1.2.1.10","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","19246383, 18776017, 10464203, 8113167, 18689481, 18790863, 20234377","2a : Function from experimental evidences in other organisms",4,457,530,4,459,489]
[null,"EFER_1992",null,"Escherichia fergusonii ATCC 35469T","_","putative Aldehyde dehydrogenase","_",0.85366,0.85849,47.69,{"v":4e-147,"d":"4.00E-147"},1,2,"_","1.2.1.10","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,456,530,9,462,533]
[null,"ECIAI39_4208",null,"Escherichia coli IAI39","_","putative Aldehyde dehydrogenase","_",0.85366,0.85849,47.69,{"v":9e-147,"d":"9.00E-147"},1,2,"_","_","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,456,530,9,462,533]
[null,"BTCD_v1_1434",null,"Brochothrix thermosphacta CD337","eutE","Ethanolamine acetaldehyde oxydoreductase","_",0.86038,0.94606,46.93,{"v":5e-146,"d":"5.00E-146"},1,2,"_","1.2.1.10","2 : Cytoplasmic","_","e : enzyme","19246383, 18776017, 10464203, 8113167, 18689481, 18790863, 20234377","2a : Function from experimental evidences in other organisms",4,457,530,3,457,482]
[null,"BTCD_v1_1042",null,"Brochothrix thermosphacta CD337","_","putative succinate-semialdehyde dehydrogenase (acetylating)","RXN-8891 ;",0.83208,0.98879,47.85,{"v":6e-135,"d":"6.00E-135"},2,1,"_","1.2.1.76","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",13,447,530,10,445,446]
[null,"BTCD_v1_1045",null,"Brochothrix thermosphacta CD337","_","putative acetaldehyde dehydrogenase (Acetylating)","_",0.85094,1.00222,45.9,{"v":2E-131,"d":"2.00E-131"},3,1,"_","1.2.1.10","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,448,530,2,450,450]
[null,"AZOLI_p10253","_","Azospirillum lipoferum 4B","adhE2","Aldehyde-alcohol dehydrogenase","_",0.49889,0.84906,46.44,{"v":9e-128,"d":"9.00E-128"},1,1,"1.1.5.2 : Ethanol degradation ; 1.3.5 : Fermentation ; 5.5.6 : Other stresses (mechanical, nutritional, oxidative) ;","1.2.1.10, 1.1.1.1","2 : Cytoplasmic","6.7 : Fermentation ; 15.10 : Adaptations to atypical conditions ;","e : enzyme","12783863, 4301680","2a : Function from experimental evidences in other organisms",8,450,530,5,452,902]
[null,"AZOLI_p20688","_","Azospirillum lipoferum 4B","adhE","Aldehyde-alcohol dehydrogenase","_",0.47598,0.82264,47.48,{"v":1E-127,"d":"1.00E-127"},1,1,"1.1.5.2 : Ethanol degradation ; 1.3.5 : Fermentation ; 5.5.6 : Other stresses (mechanical, nutritional, oxidative) ;","1.2.1.10, 1.1.1.1","1 : Unknown","6.7 : Fermentation ; 15.10 : Adaptations to atypical conditions ;","e : enzyme","2695398, 2015910","2a : Function from experimental evidences in other organisms",22,450,530,47,480,916]
[null,"VIBNIv4_A0888","_","Vibrio nigripulchritudo SFn1","adhE","Aldehyde-alcohol dehydrogenase [Includes: Alcohol dehydrogenase ; Acetaldehyde dehydrogenase [acetylating] ; Pyruvate-formate-lyase deactivase]","_",0.48287,0.82453,45.77,{"v":2e-117,"d":"2.00E-117"},1,1,"1.1.5.2 : Ethanol degradation ; 1.3.5 : Fermentation ; 7.1 : Cytoplasm ;","1.2.1.10, 1.1.1.1","2 : Cytoplasmic","6.7 : Fermentation ;","e : enzyme","2695398, 2015910, 8905232, 9278503, 16738553, 7773397, 7521508, 12783863, 18723842","2a : Function from experimental evidences in other organisms",22,450,530,17,451,905]
[null,"VS_0958","_","Vibrio tasmaniensis LGP32","adhE","Fused acetaldehyde-CoA dehydrogenase ; iron-dependent alcohol dehydrogenase","ACETALD-DEHYDROG-RXN ; ALCOHOL-DEHYDROG-RXN ; RHEA:10736 ; RHEA:23288 ;",0.48448,0.82453,44.62,{"v":1e-113,"d":"1.00E-113"},1,1,"1.1.5.2 : Ethanol degradation ;","1.2.1.10, 1.1.1.1","2 : Cytoplasmic","6 : Energy metabolism ; 6.7 : Fermentation ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",22,450,530,17,451,902]
[]
["CLOSTRIBL3_v1_12496","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"EFER_1992",null,"Escherichia fergusonii ATCC 35469T","_","putative Aldehyde dehydrogenase","_",0.84803,0.91129,54.2,{"v":1E-173,"d":"1.00E-173"},1,1,"_","1.2.1.10","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,455,496,9,460,533]
[null,"ECIAI39_4208",null,"Escherichia coli IAI39","_","putative Aldehyde dehydrogenase","_",0.84803,0.91129,54.2,{"v":5e-173,"d":"5.00E-173"},1,1,"_","_","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,455,496,9,460,533]
[null,"SSV_v1_0420",null,"Streptococcus sanguinis 2908","_","putative acetaldehyde dehydrogenase","_",0.91734,0.9248,49.23,{"v":2e-157,"d":"2.00E-157"},1,2,"_","1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,455,496,1,455,492]
[null,"BTCD_v1_1434",null,"Brochothrix thermosphacta CD337","eutE","Ethanolamine acetaldehyde oxydoreductase","_",0.92339,0.95021,47.6,{"v":1E-146,"d":"1.00E-146"},1,1,"_","1.2.1.10","2 : Cytoplasmic","_","e : enzyme","19246383, 18776017, 10464203, 8113167, 18689481, 18790863, 20234377","2a : Function from experimental evidences in other organisms",3,460,496,2,459,482]
[null,"CD630_19170",null,"Clostridium difficile 630","eutE","Ethanolamine acetaldehyde oxydoreductase","_",0.91935,0.93252,44.3,{"v":6e-142,"d":"6.00E-142"},1,2,"1.1.4 : Amines ;","1.2.1.10","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","19246383, 18776017, 10464203, 8113167, 18689481, 18790863, 20234377","2a : Function from experimental evidences in other organisms",1,455,496,1,456,489]
[null,"BTCD_v1_1042",null,"Brochothrix thermosphacta CD337","_","putative succinate-semialdehyde dehydrogenase (acetylating)","RXN-8891 ;",0.87097,0.96861,43.52,{"v":6e-122,"d":"6.00E-122"},2,2,"_","1.2.1.76","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",17,448,496,14,445,446]
[null,"CLOSTRIBL3_v1_12484",null,"Clostridiaceae BL-3","_","putative acetaldehyde dehydrogenase","ACETALD-DEHYDROG-RXN ; RHEA:23288 ;",0.84528,0.90323,43.08,{"v":8e-122,"d":"8.00E-122"},1,1,"_","1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",4,450,496,4,449,530]
[null,"BTCD_v1_1045",null,"Brochothrix thermosphacta CD337","_","putative acetaldehyde dehydrogenase (Acetylating)","_",0.89315,0.98444,41.08,{"v":3e-121,"d":"3.00E-121"},3,2,"_","1.2.1.10","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",7,449,496,8,450,450]
[]
["CLOSTRIBL3_v1_12732","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"RALTA_B0400",null,"Cupriavidus taiwanensis LMG19424","mhpF","acetaldehyde dehydrogenase, NAD-binding","_",0.95681,0.9931,54.17,{"v":3e-105,"d":"3.00E-105"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","1.2.1.10","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",12902278,"2a : Function from experimental evidences in other organisms",1,281,290,1,288,301]
[null,"Rmet_1320",null,"Cupriavidus metallidurans CH34","mhpF","Acetaldehyde-CoA dehydrogenase II, NAD-binding (gene belongs to CMGI-2)(ICE Tn4371 6054)","_",0.967,1.01034,53.92,{"v":6e-105,"d":"6.00E-105"},1,1,"1.1.2.2 : 3-phenylpropionate and 3-(3-hydroxyphenyl)propionate degradation ; 1.1.5.2 : Ethanol degradation ; 7.1 : Cytoplasm ;","1.2.1.10","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,286,290,1,293,303]
[null,"METUNv2_590024",null,"Methyloversatilis universalis FAM5","_","Acetaldehyde dehydrogenase 1","_",0.96393,1.01379,52.38,{"v":6e-100,"d":"6.00E-100"},1,1,"_","1.2.1.10","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,285,290,1,294,305]
[null,"BN42v3_90030",null,"Mycobacterium canettii STB-K","_","Putative acetaldehyde dehydrogenase (Acetaldehyde dehydrogenase)","_",0.9835,1.02759,50.34,{"v":2e-97,"d":"2.00E-97"},1,1,"7 : intermediary metabolism and respiration ;","1.2.1.10","1 : Unknown","_","e : enzyme","12657046, 17264217, 17635188, 7496535","3 : Putative function from multiple computational evidences",3,289,290,4,301,303]
[null,"BN45v3_100030",null,"Mycobacterium canettii STB-J","hsaG","Putative acetaldehyde dehydrogenase (Acetaldehyde dehydrogenase)","_",0.9835,1.02759,50,{"v":3e-97,"d":"3.00E-97"},1,1,"7 : intermediary metabolism and respiration ;","1.2.1.10","1 : Unknown","_","e : enzyme","12657046, 17264217, 17635188, 7496535","3 : Putative function from multiple computational evidences",3,289,290,4,301,303]
[null,"BN44v3_110027",null,"Mycobacterium canettii STB-D","hsaG","Putative acetaldehyde dehydrogenase (Acetaldehyde dehydrogenase)","_",0.9835,1.02759,50,{"v":3e-97,"d":"3.00E-97"},1,1,"7 : intermediary metabolism and respiration ;","1.2.1.10","1 : Unknown","_","e : enzyme","12657046, 17264217, 17635188, 7496535","3 : Putative function from multiple computational evidences",3,289,290,4,301,303]
[null,"BN43v3_90033",null,"Mycobacterium canettii STB-L","hsaG","Putative acetaldehyde dehydrogenase (Acetaldehyde dehydrogenase)","_",0.9835,1.02759,50,{"v":3e-97,"d":"3.00E-97"},1,1,"7 : intermediary metabolism and respiration ;","1.2.1.10","1 : Unknown","_","e : enzyme","12657046, 17264217, 17635188, 7496535","3 : Putative function from multiple computational evidences",3,289,290,4,301,303]
[null,"EC55989_0358",null,"Escherichia coli 55989","mhpF","acetaldehyde-CoA dehydrogenase II, NAD-binding","_",0.99367,1.08276,50.96,{"v":4e-97,"d":"4.00E-97"},1,1,"1.1.2.2 : 3-phenylpropionate and 3-(3-hydroxyphenyl)propionate degradation ; 1.1.5.2 : Ethanol degradation ; 7.1 : Cytoplasm ;","1.2.1.10","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","9098055, 9603882","1b : Function from experimental evidences in the studied species",1,290,290,1,314,316]
[null,"Rmet_5208",null,"Cupriavidus metallidurans CH34","mhpF","acetaldehyde-CoA dehydrogenase II, NAD-binding","_",0.96815,1.04828,52.63,{"v":1e-96,"d":"1.00E-96"},1,1,"1.1.2.2 : 3-phenylpropionate and 3-(3-hydroxyphenyl)propionate degradation ; 1.1.5.2 : Ethanol degradation ; 7.1 : Cytoplasm ;","1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,284,290,1,304,314]
[null,"CMR15v5_mp1210",null,"Ralstonia solanacearum CMR15","mhpF","acetaldehyde dehydrogenase, NAD-binding","_",0.9902,1.04483,50.5,{"v":3e-93,"d":"3.00E-93"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","1.2.1.10","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,286,290,3,305,306]
[null,"BN11v3_400013",null,"Tetrasphaera australiensis Ben110","mhpF","acetaldehyde dehydrogenase","_",0.88788,1.01034,49.83,{"v":2e-89,"d":"2.00E-89"},1,1,"1.1.2.2 : 3-phenylpropionate and 3-(3-hydroxyphenyl)propionate degradation ; 1.1.5.2 : Ethanol degradation ; 7.1 : Cytoplasm ;","1.2.1.10","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",9098055,"2a : Function from experimental evidences in other organisms",3,278,290,4,296,330]
[null,"Spro_3026",null,"Serratia proteamaculans 568","nahO","Acetaldehyde dehydrogenase","_",0.94915,0.96552,36.79,{"v":2e-56,"d":"2.00E-56"},1,1,"1.1.2.2 : 3-phenylpropionate and 3-(3-hydroxyphenyl)propionate degradation ; 1.1.5.2 : Ethanol degradation ;","1.2.1.10","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,281,290,3,281,295]

{"sheet":"SwissProt","index":5,"n_rows":1150,"n_cols":22,"rows_kept":1150}
[" CLOSTRIBL3_v1_11086","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"D9TQ02","IPMed?",0.99061,0.99764,30.57,{"v":3e-50,"d":"3.00E-50"},1,3,"larA","Lactate racemase","5.1.2.1","3D-structure, Complete proteome, Isomerase, Metal-binding, Nickel, Reference proteome",24710389,"Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",8,417,423,8,418,426]
[null,"F9USS9","IPMed?",0.97406,0.97636,28.57,{"v":4e-43,"d":"4.00E-43"},2,3,"larA","Lactate racemase","5.1.2.1","3D-structure, Complete proteome, Isomerase, Metal-binding, Nickel, Reference proteome","12566566, 22156394, 16166538, 24710389, 25349156, 27114550, 26138974","Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)","ATCC BAA-793 / NCIMB 8826 / WCFS1 / ATCC BAA-793 / NCIMB 8826 / WCFS1 / ATCC BAA-793 / NCIMB 8826 / WCFS1 / ATCC BAA-793 / NCIMB 8826 / WCFS1 / ATCC BAA-793 / NCIMB 8826 / WCFS1",16,417,423,21,418,424]
[]
["CLOSTRIBL3_v1_11116","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"F9USS9","IPMed?",0.99764,0.99764,64.3,0,1,1,"larA","Lactate racemase","5.1.2.1","3D-structure, Complete proteome, Isomerase, Metal-binding, Nickel, Reference proteome","12566566, 22156394, 16166538, 24710389, 25349156, 27114550, 26138974","Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)","ATCC BAA-793 / NCIMB 8826 / WCFS1 / ATCC BAA-793 / NCIMB 8826 / WCFS1 / ATCC BAA-793 / NCIMB 8826 / WCFS1 / ATCC BAA-793 / NCIMB 8826 / WCFS1 / ATCC BAA-793 / NCIMB 8826 / WCFS1",1,423,424,1,423,424]
[null,"D9TQ02","IPMed?",0.99296,0.99764,60.28,0,2,1,"larA","Lactate racemase","5.1.2.1","3D-structure, Complete proteome, Isomerase, Metal-binding, Nickel, Reference proteome",24710389,"Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",1,423,424,1,423,426]
[null,"P13626","IPMed?",0.4434,0.56456,21.28,0.016,3,1,"petA","Cytochrome f","_","Electron transport, Heme, Iron, Membrane, Metal-binding, Photosynthesis, Signal, Thylakoid, Transmembrane, Transmembrane helix, Transport",2842748,"Desmonostoc sp. (strain PCC 7906)","_",2,169,424,92,266,333]
[null,"Q5IR70","IPMed?",0.08716,0.17453,31.08,0.85,4,4,"Cage1","Cancer-associated gene 1 protein homolog","_","Alternative splicing, Coiled coil, Complete proteome, Direct protein sequencing, Phosphoprotein, Reference proteome","15819420, 19468303, 15489334, 21183079","Mus musculus","C57BL/6N / C57BL/6J / C57BL/6J",2,72,424,317,386,849]
[]
["CLOSTRIBL3_v1_11117","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O33654","IPMed?",0.86417,0.92616,56.72,{"v":4e-173,"d":"4.00E-173"},1,1,"lctP","L-lactate permease","_","Cell membrane, Membrane, Transmembrane, Transmembrane helix, Transport",10508058,"Streptococcus iniae","_",9,446,508,6,444,474]
[null,"Q46839","IPMed?",0.94464,1.04134,36.86,{"v":3e-100,"d":"3.00E-100"},2,1,"glcA","Glycolate permease GlcA","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport","9278503, 16738553, 11283302, 11785976, 15919996","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / MG1655 / ATCC 47076",9,497,508,20,546,560]
[null,"Q8Z2E3","_",0.96007,1.04134,35.16,{"v":4e-100,"d":"4.00E-100"},3,1,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Transmembrane, Transmembrane helix, Transport","11677608, 12644504","Salmonella typhi","CT18 / ATCC 700931 / Ty2",2,497,508,13,538,551]
[null,"Q8ZL63","_",0.96007,1.04134,35.16,{"v":6e-100,"d":"6.00E-100"},4,1,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport",11677609,"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720",2,497,508,13,538,551]
[null,"P33231","IPMed?",0.96007,1.04134,35.35,{"v":1e-98,"d":"1.00E-98"},5,1,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport","8407843, 8041620, 9278503, 16738553, 11283302, 11785976, 15919996","Escherichia coli (strain K12)","K12 / K12 / MG1655 / ATCC 47076 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / MG1655 / ATCC 47076",2,497,508,13,538,551]
[null,"P65254","_",0.96007,1.04134,35.16,{"v":3E-98,"d":"3.00E-98"},6,1,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",2,497,508,13,538,551]
[null,"P65253","_",0.96007,1.04134,35.16,{"v":3E-98,"d":"3.00E-98"},6,1,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Transmembrane, Transmembrane helix, Transport",12471157,"Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","CFT073 / ATCC 700928 / UPEC",2,497,508,13,538,551]
[null,"P71067","IPMed?",0.9627,1.06693,35.42,{"v":3e-95,"d":"3.00E-95"},7,1,"lutP","L-lactate permease","_","Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport","9384377, 8969506, 19201793","Bacillus subtilis (strain 168)","168 / 168 / 3610",2,499,508,13,552,563]
[null,"P55910","IPMed?",0.98336,1.04724,31.39,{"v":2e-76,"d":"2.00E-76"},8,1,"lctP","L-lactate permease","_","Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport","8969502, 9384377, 19383706, 10809684","Bacillus subtilis (strain 168)","168 / 168",2,504,508,11,539,541]
[null,"Q9K5Z9","_",0.96183,0.99213,32.74,{"v":5E-74,"d":"5.00E-74"},9,1,"lctP","L-lactate permease","_","Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport",11058132,"Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)","ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125",8,499,508,17,518,524]
[null,"Q57251","_",1.01504,1.06299,23.89,{"v":5e-37,"d":"5.00E-37"},10,1,"_","Putative L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",5,504,508,2,528,532]
[null,"P45428","IPMed?",0.63189,0.70549,19.94,0.033,11,1,"dcuD","Putative cryptic C4-dicarboxylate transporter DcuD","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport","9278503, 16738553, 10525738, 15919996","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",180,474,508,131,425,455]
[null,"P46921","IPMed?",0.3622,0.65248,23.91,0.23,12,14,"opuAB","Glycine betaine transport system permease protein OpuAB","_","Amino-acid transport, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport","7622480, 8969502, 9384377, 8752321","Bacillus subtilis (strain 168)","168 / JH642 / 168 / 168 / 168 / JH642",35,203,508,100,269,282]
[null,"P36062","IPMed?",0.25867,0.35236,21.23,0.26,13,1,"AVT3","Vacuolar amino acid transporter 3","_","Amino-acid transport, Complete proteome, Membrane, Phosphoprotein, Reference proteome, Transmembrane, Transmembrane helix, Transport, Vacuole","8091859, 8196765, 24374639, 11274162, 17330950, 18407956, 19779198, 22814378","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 204508 / S288c / ADR376",35,201,508,415,584,692]
[null,"Q5VRB2","IPMed?",0.55315,0.67064,26.33,0.9,14,6,"BASS2","Probable sodium/metabolite cotransporter BASS2, chloroplastic","_","Chloroplast, Complete proteome, Membrane, Plastid, Reference proteome, Symport, Transit peptide, Transmembrane, Transmembrane helix, Transport","12447438, 16100779, 18089549, 24280374, 15685292, 12869764, 12177140","Oryza sativa subsp. japonica","cv. Nipponbare / cv. Nipponbare / cv. Nipponbare / cv. Nipponbare / cv. Nipponbare / cv. Nipponbare",16,275,508,146,419,419]
[]
["CLOSTRIBL3_v1_30024","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"F9USS9","IPMed?",1,1,61.08,{"v":4e-177,"d":"4.00E-177"},1,2,"larA","Lactate racemase","5.1.2.1","3D-structure, Complete proteome, Isomerase, Metal-binding, Nickel, Reference proteome","12566566, 22156394, 16166538, 24710389, 25349156, 27114550, 26138974","Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)","ATCC BAA-793 / NCIMB 8826 / WCFS1 / ATCC BAA-793 / NCIMB 8826 / WCFS1 / ATCC BAA-793 / NCIMB 8826 / WCFS1 / ATCC BAA-793 / NCIMB 8826 / WCFS1 / ATCC BAA-793 / NCIMB 8826 / WCFS1",1,424,424,1,424,424]
[null,"D9TQ02","IPMed?",0.99296,0.99764,55.08,{"v":9e-164,"d":"9.00E-164"},2,2,"larA","Lactate racemase","5.1.2.1","3D-structure, Complete proteome, Isomerase, Metal-binding, Nickel, Reference proteome",24710389,"Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",1,423,424,1,423,426]
[]
["CLOSTRIBL3_v1_10010","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"A6QK89","IPMed?",0.44203,0.57367,27.32,4e-07,1,2,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Stress response","17951380, 18356528","Staphylococcus aureus (strain Newman)","Newman",124,305,414,8,180,319]
[null,"Q5HCV0","IPMed?",0.44203,0.57367,27.32,4e-07,1,2,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Stress response","15774886, 18356528","Staphylococcus aureus (strain COL)","COL",124,305,414,8,180,319]
[null,"P42123","IPMed?",0.50725,0.62874,27.62,1E-4,2,2,"Ldhb","L-lactate dehydrogenase B chain","1.1.1.27","Acetylation, Complete proteome, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","7937776, 15489334, 22673903","Rattus norvegicus","_",104,308,414,6,199,334]
[null,"P00336","IPMed?",0.50725,0.62874,26.67,1E-3,3,2,"LDHB","L-lactate dehydrogenase B chain","1.1.1.27","3D-structure, Acetylation, Complete proteome, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","7937776, 838465, 7338899","Sus scrofa","_",104,308,414,6,199,334]
[null,"P07195","IPMed?",0.50725,0.62874,26.67,2E-3,4,2,"LDHB","L-lactate dehydrogenase B chain","1.1.1.27","3D-structure, Acetylation, Complete proteome, Cytoplasm, Direct protein sequencing, Disease mutation, NAD, Oxidoreductase, Phosphoprotein, Polymorphism, Reference proteome","2930497, 3435492, 15489334, 10508479, 15592455, 19690332, 19608861, 20068231, 21269460, 23186163, 24275569, 25944712, 11276087, 8314553, 8462975, 1587525, 2334429, 8611651, 10211631, 9929983, 11509017","Homo sapiens","_",104,308,414,6,199,334]
[null,"P0C0J3","IPMed?",0.45894,0.60317,23.16,2E-3,5,2,"ldh","L-lactate dehydrogenase","1.1.1.27","Complete proteome, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","7679720, 16077101","Mycoplasma hyopneumoniae (strain J / ATCC 25934 / NCTC 10110)","J / ATCC 25934 / NCTC 10110",124,312,414,6,185,315]
[null,"P13714","IPMed?",0.44686,0.57812,25.41,0.004,6,2,"ldh","L-lactate dehydrogenase","1.1.1.27","3D-structure, Allosteric enzyme, Complete proteome, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","8969502, 9384377, 19383706, 3098260, 10809684, 17218307","Bacillus subtilis (strain 168)","168 / 168 / 168",124,305,414,8,180,320]
[null,"D8KFT1","IPMed?",0.36473,0.48089,28.48,0.006,7,2,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","12867459, 20639323","Lactococcus lactis subsp. cremoris (strain NZ9000)","NZ9000 / NZ9000",124,274,414,8,147,314]
[null,"A6QDL6","IPMed?",0.39614,0.51735,24.39,0.009,8,2,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Stress response","17951380, 18356528","Staphylococcus aureus (strain Newman)","Newman",119,279,414,4,155,317]
[null,"Q5HJD7","IPMed?",0.39614,0.51735,24.39,0.009,8,2,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","3D-structure, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Stress response","15774886, 18356528","Staphylococcus aureus (strain COL)","COL",119,279,414,4,155,317]
[null,"O32765","IPMed?",0.48068,0.6161,24.12,0.009,9,2,"ldh","L-lactate dehydrogenase","1.1.1.27","Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein",9212432,"Lactobacillus helveticus","1953-07-01",196,389,414,74,262,323]
[null,"P00343","IPMed?",0.3744,0.47546,27.74,0.012,10,2,"ldh","L-lactate dehydrogenase","1.1.1.27","3D-structure, Allosteric enzyme, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","1768113, 6411465, 14601, 7766183, 19787773","Lactobacillus casei","ATCC 393 / DSM 20011 / JCM 1134 / NBRC 15883 / NCIMB 11970 / NCDO 161 / ATCC 393 / DSM 20011 / JCM 1134 / NBRC 15883 / NCIMB 11970 / NCDO 161 / ATCC 393 / DSM 20011 / JCM 1134 / NBRC 15883 / NCIMB 11970 / NCDO 161",126,279,414,14,157,326]
[]
["CLOSTRIBL3_v1_10012","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q97DC6","_",1,1,58.13,{"v":1e-133,"d":"1.00E-133"},1,1,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Reference proteome",11466286,"Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,320,320,1,320,320]
[null,"Q9EVR0","IPMed?",0.98125,0.98742,51.59,{"v":2e-110,"d":"2.00E-110"},2,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",11821921,"Selenomonas ruminantium","HD4",5,318,320,4,317,318]
[null,"Q8KQC4","_",0.95625,0.9653,38.89,{"v":1E-73,"d":"1.00E-73"},3,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","_","Hungateiclostridium thermocellum (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)","_",7,311,320,9,309,317]
[null,"Q892U0","_",0.94063,0.95253,39.87,{"v":2e-71,"d":"2.00E-71"},4,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome",12552129,"Clostridium tetani (strain Massachusetts / E88)","Massachusetts / E88",7,306,320,7,303,316]
[null,"Q63CN1","_",0.97813,0.99682,37.7,{"v":2e-69,"d":"2.00E-69"},5,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",16621833,"Bacillus cereus (strain ZK / E33L)","ZK / E33L",1,313,320,1,310,314]
[null,"Q6HK31","_",0.97813,0.99682,37.7,{"v":2e-69,"d":"2.00E-69"},5,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",16621833,"Bacillus thuringiensis subsp. konkukian (strain 97-27)","97-27",1,313,320,1,310,314]
[null,"P62047","_",0.97813,0.99682,37.7,{"v":2e-69,"d":"2.00E-69"},5,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",14960714,"Bacillus cereus (strain ATCC 10987 / NRS 248)","ATCC 10987 / NRS 248",1,313,320,1,310,314]
[null,"Q81RW4","_",0.97813,0.99682,37.7,{"v":2e-69,"d":"2.00E-69"},5,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","12721629, 18952800","Bacillus anthracis","Ames / isolate Porton / Ames ancestor",1,313,320,1,310,314]
[null,"C3KVF0","_",1.00937,1.01572,36.84,{"v":3e-69,"d":"3.00E-69"},6,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","_","Clostridium botulinum (strain 657 / Type Ba4)","_",2,318,320,4,318,318]
[null,"B1L1N3","_",1.00937,1.01572,36.53,{"v":6e-69,"d":"6.00E-69"},7,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",18060065,"Clostridium botulinum (strain Loch Maree / Type A3)","Loch Maree / Type A3",2,318,320,4,318,318]
[null,"A7GDK3","_",1.00937,1.01572,36.53,{"v":9e-69,"d":"9.00E-69"},8,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","_","Clostridium botulinum (strain Langeland / NCTC 10281 / Type F)","_",2,318,320,4,318,318]
[null,"B1IKX1","_",1.00937,1.01572,36.53,{"v":9e-69,"d":"9.00E-69"},8,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",18060065,"Clostridium botulinum (strain Okra / Type B1)","Okra / Type B1",2,318,320,4,318,318]
[null,"Q81EP4","_",0.97813,0.99682,37.38,{"v":1e-68,"d":"1.00E-68"},10,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","3D-structure, Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome",12721630,"Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)","ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711",1,313,320,1,310,314]
[null,"Q7X5C9","IPMed?",0.98125,1.00965,39.17,{"v":1e-68,"d":"1.00E-68"},9,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",15007569,"Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485)","DSM 8691 / JW/SL-YS485",6,314,320,2,307,311]
[null,"P00345","IPMed?",0.98125,0.98742,36.62,{"v":4e-67,"d":"4.00E-67"},11,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","3122782, 3118900","Bacillus megaterium","DSM 090",3,316,320,7,316,318]
[null,"P00343","IPMed?",0.96012,0.97813,35.46,{"v":4e-66,"d":"4.00E-66"},12,1,"ldh","L-lactate dehydrogenase","1.1.1.27","3D-structure, Allosteric enzyme, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","1768113, 6411465, 14601, 7766183, 19787773","Lactobacillus casei","ATCC 393 / DSM 20011 / JCM 1134 / NBRC 15883 / NCIMB 11970 / NCDO 161 / ATCC 393 / DSM 20011 / JCM 1134 / NBRC 15883 / NCIMB 11970 / NCDO 161 / ATCC 393 / DSM 20011 / JCM 1134 / NBRC 15883 / NCIMB 11970 / NCDO 161",7,316,320,11,316,326]
[null,"P13714","IPMed?",0.96562,0.96562,35.92,{"v":6e-66,"d":"6.00E-66"},13,1,"ldh","L-lactate dehydrogenase","1.1.1.27","3D-structure, Allosteric enzyme, Complete proteome, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","8969502, 9384377, 19383706, 3098260, 10809684, 17218307","Bacillus subtilis (strain 168)","168 / 168 / 168",6,311,320,6,311,320]
[null,"P14561","IPMed?",0.96875,0.97484,35.81,{"v":2e-64,"d":"2.00E-64"},14,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Allosteric enzyme, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","2334516, 3435642","Bacillus psychrosaccharolyticus","_",6,315,320,7,312,318]
[null,"Q01462","IPMed?",0.94769,0.9625,34.42,{"v":4e-64,"d":"4.00E-64"},16,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","1400245, 1452029, 8081494, 9023947, 11337471","Lactococcus lactis subsp. lactis (strain IL1403)","LM0230 / BU2-60 / 1117M / IL1403",5,309,320,6,306,325]
[null,"P04034","IPMed?",0.94769,0.9625,34.74,{"v":4e-64,"d":"4.00E-64"},15,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Allosteric enzyme, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","8081494, 9023947, 518918","Lactococcus lactis subsp. cremoris","ML1 / AM4 / US3",5,309,320,6,306,325]
[null,"O32765","IPMed?",0.96285,0.97188,35.05,{"v":6e-64,"d":"6.00E-64"},17,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein",9212432,"Lactobacillus helveticus","1953-07-01",7,316,320,9,313,323]
[null,"P56511","IPMed?",1.00625,1.00625,35.4,{"v":3e-63,"d":"3.00E-63"},18,1,"ldh","L-lactate dehydrogenase","1.1.1.27","3D-structure, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","1840590, 1425707, 11807949","Lactobacillus pentosus","ATCC 8041 / DSM 20314 / JCM 1558 / NCDO 363 / NCIMB 8026 / ATCC 8041 / DSM 20314 / JCM 1558 / NCDO 363 / NCIMB 8026",3,313,320,5,310,320]
[]
["CLOSTRIBL3_v1_12309","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O52792","IPMed?",0.94398,0.94663,32.34,{"v":1e-36,"d":"1.00E-36"},1,1,"hmo","4-hydroxymandelate oxidase","1.1.3.46","3D-structure, Antibiotic biosynthesis, Flavoprotein, FMN, Oxidoreductase","9545426, 11137816, 12240298","Amycolatopsis orientalis","_",54,345,356,27,344,357]
[null,"Q54E41","_",0.84278,0.91854,31.5,{"v":9e-36,"d":"9.00E-36"},2,1,"haox","Hydroxyacid oxidase","1.1.3.15","Complete proteome, Flavoprotein, FMN, Oxidoreductase, Reference proteome",15875012,"Dictyostelium discoideum","AX4",64,356,356,65,382,388]
[null,"Q9LJH5","IPMed?",0.9146,0.93258,29.52,{"v":4E-35,"d":"4.00E-35"},3,1,"GLO4","Peroxisomal (S)-2-hydroxy-acid oxidase GLO4","1.1.3.15","Complete proteome, Flavoprotein, FMN, Glycolate pathway, Oxidoreductase, Peroxisome, Photorespiration, Reference proteome","10907853, 27862469, 14593172, 19264754","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia",54,348,356,28,347,363]
[null,"Q3ZBW2","_",0.41854,0.4221,44.3,{"v":2e-33,"d":"2.00E-33"},4,1,"HAO2","Hydroxyacid oxidase 2","1.1.3.15","Complete proteome, Flavoprotein, FMN, Oxidoreductase, Peroxisome, Reference proteome","_","Bos taurus","_",206,353,356,200,348,353]
[null,"Q24JJ8","IPMed?",0.9146,0.93258,27.41,{"v":5e-33,"d":"5.00E-33"},5,1,"GLO3","Peroxisomal (S)-2-hydroxy-acid oxidase GLO3","1.1.3.15","Complete proteome, Flavoprotein, FMN, Glycolate pathway, Oxidoreductase, Peroxisome, Photorespiration, Reference proteome","10907853, 27862469, 19264754, 19329564","Arabidopsis thaliana","cv. Columbia / cv. Columbia",54,348,356,28,347,363]
[null,"Q9UJM8","IPMed?",0.38378,0.39888,47.18,{"v":6e-33,"d":"6.00E-33"},6,1,"HAO1","Hydroxyacid oxidase 1","1.1.3.15","3D-structure, Complete proteome, Flavoprotein, FMN, Oxidoreductase, Peroxisome, Phosphoprotein, Reference proteome","10978532, 10777549, 11780052, 15489334, 24275569, 18215067, 20054120","Homo sapiens","_",213,353,356,220,360,370]
[null,"Q9HV37","_",0.37008,0.39607,48.23,{"v":8e-32,"d":"8.00E-32"},7,1,"lldD","L-lactate dehydrogenase","1.1.-.-","Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Membrane, Oxidoreductase, Reference proteome",10984043,"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1",210,350,356,235,372,381]
[null,"Q02FQ1","_",0.37008,0.39607,48.23,{"v":8e-32,"d":"8.00E-32"},7,1,"lldD","L-lactate dehydrogenase","1.1.-.-","Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Membrane, Oxidoreductase",17038190,"Pseudomonas aeruginosa (strain UCBPP-PA14)","UCBPP-PA14",210,350,356,235,372,381]
[null,"B7V1I3","_",0.37008,0.39607,48.23,{"v":8e-32,"d":"8.00E-32"},7,1,"lldD","L-lactate dehydrogenase","1.1.-.-","Cell inner membrane, Cell membrane, Flavoprotein, FMN, Membrane, Oxidoreductase",19047519,"Pseudomonas aeruginosa (strain LESB58)","LESB58",210,350,356,235,372,381]
[null,"Q9WU19","IPMed?",0.38378,0.39888,45.07,{"v":9e-32,"d":"9.00E-32"},8,1,"Hao1","Hydroxyacid oxidase 1","1.1.3.15","Complete proteome, Flavoprotein, FMN, Oxidoreductase, Peroxisome, Phosphoprotein, Reference proteome","9891009, 17242355, 21183079, 23806337","Mus musculus","_",213,353,356,220,360,370]
[null,"A6VCM8","_",0.37008,0.39607,48.23,{"v":1e-31,"d":"1.00E-31"},10,1,"lldD","L-lactate dehydrogenase","1.1.-.-","Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Membrane, Oxidoreductase","_","Pseudomonas aeruginosa (strain PA7)","_",210,350,356,235,372,381]
[null,"Q6DAY3","_",0.35751,0.38764,49.28,{"v":1e-31,"d":"1.00E-31"},9,1,"lldD","L-lactate dehydrogenase","1.1.-.-","Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Membrane, Oxidoreductase, Reference proteome",15263089,"Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)","SCRI 1043 / ATCC BAA-672",213,350,356,235,372,386]
[null,"Q9NYQ2","IPMed?",0.94944,0.95751,27.22,{"v":1e-31,"d":"1.00E-31"},11,1,"Hao2","Hydroxyacid oxidase 2","1.1.3.15","Complete proteome, Flavoprotein, FMN, Oxidoreductase, Peroxisome, Phosphoprotein, Reference proteome","10777549, 16141072, 21183079","Mus musculus","C57BL/6J",54,353,356,27,348,353]
[null,"Q8H3I4","IPMed?",0.92896,0.95506,29.71,{"v":2e-31,"d":"2.00E-31"},12,1,"GLO4","Peroxisomal (S)-2-hydroxy-acid oxidase GLO4","1.1.3.15","Complete proteome, Flavoprotein, FMN, Glycolate pathway, Host-virus interaction, Oxidoreductase, Peroxisome, Photorespiration, Reference proteome","16100779, 18089549, 24280374, 15685292, 12869764, 19264754, 26900141","Oryza sativa subsp. japonica","cv. Nipponbare / cv. Nipponbare / cv. Nipponbare / cv. Nipponbare / cv. Nipponbare / cv. Zhonghua 11",54,348,356,30,350,366]
[null,"Q9LRR9","IPMed?",0.89646,0.92416,25.84,{"v":6e-31,"d":"6.00E-31"},13,1,"GLO1","(S)-2-hydroxy-acid oxidase GLO1","1.1.3.15","Acetylation, Alternative splicing, Complete proteome, Flavoprotein, FMN, Glycolate pathway, Oxidoreductase, Photorespiration, Reference proteome","10819329, 27862469, 14593172, 19423640, 17951448, 19264754","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia",61,348,356,34,349,367]
[null,"O49506","IPMed?",0.8913,0.92135,27.13,{"v":8e-31,"d":"8.00E-31"},14,1,"GLO5","Peroxisomal (S)-2-hydroxy-acid oxidase GLO5","1.1.3.15","Acetylation, Alternative splicing, Complete proteome, Flavoprotein, FMN, Glycolate pathway, Oxidoreductase, Photorespiration, Reference proteome","10617198, 27862469, 14593172, 19264754, 22223895","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia",61,348,356,34,349,368]
[null,"Q07523","IPMed?",0.94663,0.95467,28.49,{"v":9e-31,"d":"9.00E-31"},15,1,"Hao2","Hydroxyacid oxidase 2","1.1.3.15","3D-structure, Complete proteome, Direct protein sequencing, Flavoprotein, FMN, Oxidoreductase, Peroxisome, Phosphoprotein, Reference proteome","8508789, 15489334, 1939137, 3061453, 22673903, 15683236","Rattus norvegicus","Wistar",54,353,356,27,348,353]
[]
[" CLOSTRIBL3_v1_12417","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q2RMD6","IPMed?",0.99829,1,60.63,0,1,3,"_","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Reference proteome, Transport","18631365, 9214293, 10878009, 29581263","Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320 / ATCC 39073 / JCM 9320",6,1171,1173,4,1170,1171]
[null,"P19543","IPMed?",1.00256,1.00256,60.2,0,2,3,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Plasmid, Repeat, Transport","2504647, 1708766","Enterobacter agglomerans","333 / 333",1,1170,1173,1,1171,1173]
[null,"P03833","IPMed?",0.99915,1.00085,58.53,0,3,3,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","3062178, 3060860, 8483412, 6306580","Klebsiella pneumoniae","_",1,1170,1173,1,1168,1171]
[null,"P94692","IPMed?",0.93669,0.9838,58.32,0,4,2,"por","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Calcium, Cytoplasm, Direct protein sequencing, Disulfide bond, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Thiamine pyrophosphate, Transport","9294422, 7612653, 10048931, 11752578, 16472741","Desulfocurvibacter africanus","ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi / ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi",1,1151,1173,1,1148,1232]
[null,"Q94IN5","IPMed?",0.64947,0.99829,50.56,0,5,2,"PNO","Pyruvate dehydrogenase [NADP(+)], mitochondrial","1.2.1.51","4Fe-4S, Direct protein sequencing, Electron transport, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, Mitochondrion, NADP, Oxidoreductase, Repeat, Thiamine pyrophosphate, Transit peptide, Transport","11023353, 11319255, 1910287, 8373179, 3110154, 12623066","Euglena gracilis","SAG1224-5/25",6,1169,1173,70,1232,1803]
[null,"Q968X7","IPMed?",0.64168,1.05797,49.15,0,6,2,"PFOR","Pyruvate dehydrogenase [NADP(+)]","1.2.1.51","4Fe-4S, Electron transport, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat, Thiamine pyrophosphate, Transport",11319255,"Cryptosporidium parvum","KSU-1",8,1171,1173,7,1242,1934]
[null,"Q3M8N0","IPMed?",0.99832,1.01279,49.58,0,7,1,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","25197444, 8352652","Trichormus variabilis (strain ATCC 29413 / PCC 7937)","ATCC 29413 / PCC 7937",3,1170,1173,4,1183,1190]
[null,"P52965","_",0.97915,1.00085,48.64,0,8,1,"nifJ","Putative pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8590279, 8905231","Synechocystis sp. (strain PCC 6803 / Kazusa)","ATCC 27184 / PCC 6803 / N-1 / PCC 6803 / Kazusa",7,1171,1173,8,1174,1199]
[null,"Q06879","IPMed?",1.00167,1.02387,47.88,0,9,1,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8415612, 11759840","Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)","PCC 7120 / SAG 25.82 / UTEX 2576",1,1170,1173,1,1197,1199]
[null,"Q53046","IPMed?",0.9958,1.01108,46.8,0,10,1,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8736535, 21886856","Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)","ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1",2,1172,1173,3,1180,1191]
[null,"P52647","IPMed?",1.01022,1.01108,47.13,0,11,1,"ydbK","Probable pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","9097039, 9278503, 16738553, 9025293","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",5,1170,1173,1,1165,1174]
[]
["CLOSTRIBL3_v1_12774","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q56317","IPMed?",0.96296,1.00971,51.28,{"v":5e-106,"d":"5.00E-106"},1,1,"porB","Pyruvate synthase subunit PorB","1.2.7.1","4Fe-4S, Complete proteome, Direct protein sequencing, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome","8550425, 10360571","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 / ATCC 43589 / MSB8 / DSM 3109 / JCM 10099",1,304,309,1,312,324]
[null,"Q57714","_",0.91586,0.94966,50.88,{"v":1e-90,"d":"1.00E-90"},2,2,"porB","Pyruvate synthase subunit PorB","1.2.7.1","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome",8688087,"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440",18,298,309,15,291,298]
[null,"O27771","_",0.93528,1.00347,48.1,{"v":2e-83,"d":"2.00E-83"},3,2,"porB","Pyruvate synthase subunit PorB","1.2.7.1","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome",9371463,"Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)","ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H",15,303,309,9,286,288]
[null,"P80522","IPMed?",0.95469,0.99662,46.78,{"v":2e-82,"d":"2.00E-82"},4,1,"porB","Pyruvate synthase subunit PorB","1.2.7.1","4Fe-4S, Complete proteome, Direct protein sequencing, Iron, Iron-sulfur, Metal-binding, Oxidoreductase","16980466, 8620891","Methanosarcina barkeri (strain Fusaro / DSM 804)","Fusaro / DSM 804",8,299,309,1,289,296]
[null,"P80901","IPMed?",0.93528,1.00347,47.75,{"v":5e-82,"d":"5.00E-82"},5,2,"porB","Pyruvate synthase subunit PorB","1.2.7.1","4Fe-4S, Complete proteome, Direct protein sequencing, Iron, Iron-sulfur, Metal-binding, Oxidoreductase","20802048, 9108258","Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)","ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg / ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg",15,303,309,9,286,288]
[null,"O58417","_",0.9426,1.00971,45.83,{"v":4E-78,"d":"4.00E-78"},6,2,"porB","Pyruvate synthase subunit PorB","1.2.7.1","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Oxidoreductase",9679194,"Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)","ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3",18,303,309,17,320,331]
[null,"Q51805","IPMed?",0.9426,1.00971,44.23,{"v":3e-76,"d":"3.00E-76"},7,1,"porB","Pyruvate synthase subunit PorB","1.2.7.1","4Fe-4S, Complete proteome, Direct protein sequencing, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome","8550425, 10430560, 8380721","Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)","ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 / ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 / ATCC 43587 / DSM 3638 / JCM 8422 / Vc1",18,303,309,17,320,331]
[null,"Q9UYZ5","_",0.9426,1.00971,43.59,{"v":7e-75,"d":"7.00E-75"},8,2,"porB","Pyruvate synthase subunit PorB","1.2.7.1","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Oxidoreductase","12622808, 22057919","Pyrococcus abyssi (strain GE5 / Orsay)","GE5 / Orsay / GE5 / Orsay",18,303,309,17,320,331]
[null,"Q9UYZ2","_",0.93569,0.94175,43.99,{"v":2e-74,"d":"2.00E-74"},9,1,"vorB","Ketoisovalerate oxidoreductase subunit VorB","1.2.7.7","Complete proteome, Oxidoreductase","12622808, 22057919","Pyrococcus abyssi (strain GE5 / Orsay)","GE5 / Orsay / GE5 / Orsay",17,305,309,21,305,311]
[null,"O58414","_",0.93569,0.94175,43.64,{"v":4e-74,"d":"4.00E-74"},10,1,"vorB","Ketoisovalerate oxidoreductase subunit VorB","1.2.7.7","Complete proteome, Oxidoreductase",9679194,"Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)","ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3",17,305,309,21,305,311]
[null,"Q51802","IPMed?",0.93569,0.94175,43.64,{"v":6e-74,"d":"6.00E-74"},11,2,"vorB","Ketoisovalerate oxidoreductase subunit VorB","1.2.7.7","Complete proteome, Direct protein sequencing, Oxidoreductase, Reference proteome","8550425, 10430560","Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)","ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 / ATCC 43587 / DSM 3638 / JCM 8422 / Vc1",17,305,309,21,305,311]
[null,"Q2RI42","IPMed?",0.8535,0.86731,41.79,{"v":6e-64,"d":"6.00E-64"},12,2,"_","Oxalate oxidoreductase subunit beta","1.2.7.10","3D-structure, 4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome","18631365, 20956531","Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320",18,280,309,20,284,314]
[null,"Q8L3A9","IPMed?",0.66816,0.9644,32.21,{"v":3e-40,"d":"3.00E-40"},13,2,"padI","NADH-dependent phenylglyoxylate dehydrogenase subunit beta","1.2.1.58","4Fe-4S, Direct protein sequencing, Iron, Iron-sulfur, Metal-binding, NAD, Oxidoreductase, Repeat",9490067,"Azoarcus evansii","KB740 / DSM 6898",7,299,309,147,432,446]
[null,"Q53046","IPMed?",0.1738,0.6699,32.85,3e-15,14,5,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8736535, 21886856","Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)","ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1",107,300,309,975,1171,1191]
[null,"Q968X7","IPMed?",0.1122,0.70227,27.19,1e-12,15,6,"PFOR","Pyruvate dehydrogenase [NADP(+)]","1.2.1.51","4Fe-4S, Electron transport, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat, Thiamine pyrophosphate, Transport",11319255,"Cryptosporidium parvum","KSU-1",107,303,309,1027,1237,1934]
[null,"P94692","IPMed?",0.16964,0.67638,29.19,7e-12,16,6,"por","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Calcium, Cytoplasm, Direct protein sequencing, Disulfide bond, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Thiamine pyrophosphate, Transport","9294422, 7612653, 10048931, 11752578, 16472741","Desulfocurvibacter africanus","ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi / ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi",106,303,309,960,1163,1232]
[]
["CLOSTRIBL3_v1_12775","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O05651","IPMed?",1.0051,1.00767,56.09,{"v":1E-139,"d":"1.00E-139"},1,1,"porA","Pyruvate synthase subunit PorA","1.2.7.1","Complete proteome, Direct protein sequencing, Oxidoreductase, Reference proteome","8550425, 10360571, 8305426","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 / ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 / ATCC 43589 / MSB8 / DSM 3109 / JCM 10099",1,391,391,4,392,392]
[null,"P56810","_",0.92583,0.94517,47.51,{"v":1e-109,"d":"1.00E-109"},2,1,"porA","Pyruvate synthase subunit PorA","1.2.7.1","Complete proteome, Oxidoreductase, Reference proteome",9371463,"Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)","ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H",7,368,391,6,362,383]
[null,"P80900","IPMed?",0.98465,1.00522,44.42,{"v":4E-107,"d":"4.00E-107"},3,1,"porA","Pyruvate synthase subunit PorA","1.2.7.1","Complete proteome, Direct protein sequencing, Oxidoreductase","20802048, 9108258","Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)","ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg / ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg",7,391,391,6,380,383]
[null,"Q9UYZ4","_",0.99494,1.00512,46.31,{"v":1e-105,"d":"1.00E-105"},4,1,"porA","Pyruvate synthase subunit PorA","1.2.7.1","Complete proteome, Oxidoreductase","12622808, 22057919","Pyrococcus abyssi (strain GE5 / Orsay)","GE5 / Orsay / GE5 / Orsay",1,391,391,1,392,395]
[null,"Q57715","_",0.96419,0.96915,47.21,{"v":2e-105,"d":"2.00E-105"},5,1,"porA","Pyruvate synthase subunit PorA","1.2.7.1","Complete proteome, Oxidoreductase, Reference proteome",8688087,"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440",7,378,391,10,382,389]
[null,"Q51804","IPMed?",0.9899,1.00256,45.15,{"v":2e-103,"d":"2.00E-103"},6,1,"porA","Pyruvate synthase subunit PorA","1.2.7.1","Complete proteome, Direct protein sequencing, Oxidoreductase, Reference proteome","8550425, 10430560, 8305426, 8380721","Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)","ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 / ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 / ATCC 43587 / DSM 3638 / JCM 8422 / Vc1",1,390,391,1,391,396]
[null,"O73986","_",0.99494,1.00512,45.55,{"v":1e-101,"d":"1.00E-101"},7,1,"porA","Pyruvate synthase subunit PorA","1.2.7.1","Complete proteome, Oxidoreductase",9679194,"Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)","ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3",1,391,391,1,392,395]
[null,"P80521","IPMed?",0.94279,0.96931,42.74,{"v":2E-95,"d":"2.00E-95"},8,1,"porA","Pyruvate synthase subunit PorA","1.2.7.1","Complete proteome, Direct protein sequencing, Oxidoreductase","16980466, 8620891","Methanosarcina barkeri (strain Fusaro / DSM 804)","Fusaro / DSM 804",3,379,391,9,387,402]
[null,"Q9UYZ1","_",0.95696,0.96675,43.39,{"v":4E-95,"d":"4.00E-95"},9,1,"vorA","Ketoisovalerate oxidoreductase subunit VorA","1.2.7.7","Complete proteome, Oxidoreductase","12622808, 22057919","Pyrococcus abyssi (strain GE5 / Orsay)","GE5 / Orsay / GE5 / Orsay",7,382,391,11,385,395]
[null,"Q51801","IPMed?",0.96701,0.97442,43.57,{"v":2e-94,"d":"2.00E-94"},10,1,"vorA","Ketoisovalerate oxidoreductase subunit VorA","1.2.7.7","Complete proteome, Direct protein sequencing, Oxidoreductase, Reference proteome","8550425, 10430560","Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)","ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 / ATCC 43587 / DSM 3638 / JCM 8422 / Vc1",4,382,391,7,384,394]
[null,"Q8L3B1","IPMed?",0.90647,0.96675,37.83,{"v":4e-82,"d":"4.00E-82"},11,1,"padG","NADH-dependent phenylglyoxylate dehydrogenase subunit alpha","1.2.1.58","Direct protein sequencing, NAD, Oxidoreductase",9490067,"Azoarcus evansii","KB740 / DSM 6898",3,371,391,19,396,417]
[null,"Q2RI41","IPMed?",0.98481,0.99488,35.22,{"v":1e-69,"d":"1.00E-69"},12,2,"_","Oxalate oxidoreductase subunit alpha","1.2.7.10","3D-structure, Complete proteome, Oxidoreductase, Reference proteome","18631365, 20956531","Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320",1,386,391,1,389,395]
[null,"Q3M8N0","IPMed?",0.32941,1.00256,30.36,{"v":5e-46,"d":"5.00E-46"},13,4,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","25197444, 8352652","Trichormus variabilis (strain ATCC 29413 / PCC 7937)","ATCC 29413 / PCC 7937",6,383,391,8,396,1190]
[null,"Q2RMD6","IPMed?",0.33219,0.99488,31.36,{"v":4e-44,"d":"4.00E-44"},14,4,"_","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Reference proteome, Transport","18631365, 9214293, 10878009, 29581263","Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320 / ATCC 39073 / JCM 9320",6,383,391,5,390,1171]
[null,"Q9APC2","IPMed?",0.96782,1,31.2,{"v":4e-44,"d":"4.00E-44"},15,4,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport",11167002,"Nostoc sp. (strain ATCC 29151 / PCC 7119)","_",7,383,391,1,385,404]
[]
["CLOSTRIBL3_v1_12776","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q56316","IPMed?",0.86869,0.87755,48.84,{"v":5e-27,"d":"5.00E-27"},1,1,"porD","Pyruvate synthase subunit PorD","_","4Fe-4S, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","8550425, 10360571","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 / ATCC 43589 / MSB8 / DSM 3109 / JCM 10099",13,98,98,6,91,99]
[null,"Q51803","IPMed?",0.78095,0.83673,45.12,{"v":1e-23,"d":"1.00E-23"},2,1,"porD","Pyruvate synthase subunit PorD","_","4Fe-4S, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","8550425, 10430560","Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)","ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 / ATCC 43587 / DSM 3638 / JCM 8422 / Vc1",17,98,98,22,103,105]
[null,"Q51800","IPMed?",0.72381,0.77551,46.05,{"v":2e-23,"d":"2.00E-23"},3,1,"vorD","Ketoisovalerate oxidoreductase subunit VorD","1.2.7.7","4Fe-4S, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","8550425, 10430560","Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)","ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 / ATCC 43587 / DSM 3638 / JCM 8422 / Vc1",23,98,98,28,103,105]
[null,"O58415","_",0.78095,0.83673,45.12,{"v":8e-23,"d":"8.00E-23"},4,1,"porD","Pyruvate synthase subunit PorD","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",9679194,"Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)","ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3",17,98,98,22,103,105]
[null,"Q9UYZ3","_",0.78095,0.83673,43.9,{"v":2e-22,"d":"2.00E-22"},5,1,"porD","Pyruvate synthase subunit PorD","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport","12622808, 22057919","Pyrococcus abyssi (strain GE5 / Orsay)","GE5 / Orsay / GE5 / Orsay",17,98,98,22,103,105]
[null,"Q9UYZ0","_",0.62857,0.67347,48.48,{"v":1e-21,"d":"1.00E-21"},6,1,"vorD","Ketoisovalerate oxidoreductase subunit VorD","1.2.7.7","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Repeat, Transport","12622808, 22057919","Pyrococcus abyssi (strain GE5 / Orsay)","GE5 / Orsay / GE5 / Orsay",33,98,98,38,103,105]
[null,"O58412","_",0.62857,0.67347,46.97,{"v":3e-21,"d":"3.00E-21"},7,1,"vorD","Ketoisovalerate oxidoreductase subunit VorD","1.2.7.7","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Repeat, Transport",9679194,"Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)","ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3",33,98,98,38,103,105]
[null,"Q57716","_",0.83673,0.95349,43.9,{"v":1e-18,"d":"1.00E-18"},8,1,"porD","Pyruvate synthase subunit PorD","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport",8688087,"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440",17,98,98,3,84,86]
[null,"P80524","IPMed?",0.82653,0.85263,41.98,{"v":2e-18,"d":"2.00E-18"},9,1,"porD","Pyruvate synthase subunit PorD","_","4Fe-4S, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport","16980466, 8620891","Methanosarcina barkeri (strain Fusaro / DSM 804)","Fusaro / DSM 804",18,98,98,20,93,95]
[null,"P80903","IPMed?",0.81633,0.98765,43.75,{"v":7e-18,"d":"7.00E-18"},10,2,"porD","Pyruvate synthase subunit PorD","_","4Fe-4S, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport","20802048, 9108258","Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)","ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg / ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg",19,98,98,5,80,81]
[null,"P56815","_",0.81633,0.98765,43.75,{"v":7e-18,"d":"7.00E-18"},10,2,"porD","Pyruvate synthase subunit PorD","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport",9371463,"Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)","ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H",19,98,98,5,80,81]
[null,"Q2RI40","IPMed?",0.20952,0.67347,43.94,4e-13,11,4,"_","Oxalate oxidoreductase subunit delta","1.2.7.10","3D-structure, 4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat","18631365, 20956531","Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320",33,98,98,246,310,315]
[null,"Q8L3B2","IPMed?",0.56122,0.5914,38.18,8e-11,12,2,"padF","NADH-dependent phenylglyoxylate dehydrogenase subunit delta","1.2.1.58","4Fe-4S, Direct protein sequencing, Iron, Iron-sulfur, Metal-binding, NAD, Oxidoreductase, Repeat",9490067,"Azoarcus evansii","KB740 / DSM 6898",34,88,98,34,87,93]
[null,"Q9HR73","IPMed?",0.29771,0.79592,32.05,8e-06,13,6,"dmsB","Putative dimethyl sulfoxide reductase iron-sulfur subunit B","_","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Transport","11016950, 15716436","Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)","ATCC 700922 / JCM 11081 / NRC-1 / ATCC 700922 / JCM 11081 / NRC-1",17,92,98,40,117,262]
[null,"P00202","IPMed?",0.56122,0.9322,36.36,1e-05,14,9,"_","Ferredoxin","_","4Fe-4S, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",6754724,"Methanosarcina barkeri","ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474",44,97,98,5,59,59]
[null,"P00197","IPMed?",0.5,0.89091,40.82,2e-05,15,7,"_","Ferredoxin","_","4Fe-4S, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",4433520,"Clostridium sp. (strain M-E)","_",45,93,98,5,52,55]
[]
["CLOSTRIBL3_v1_12777","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O05650","IPMed?",0.98964,0.99479,43.98,{"v":8e-48,"d":"8.00E-48"},1,1,"porC","Pyruvate synthase subunit PorC","1.2.7.1","3D-structure, Complete proteome, Direct protein sequencing, Oxidoreductase, Reference proteome","8550425, 10360571","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 / ATCC 43589 / MSB8 / DSM 3109 / JCM 10099",1,191,193,3,189,192]
[null,"Q5JIK2","_",0.8601,0.8973,46.39,{"v":1e-44,"d":"1.00E-44"},2,1,"porG","Pyruvate synthase subunit PorC / Ketoisovalerate oxidoreductase subunit VorC","1.2.7.1, 1.2.7.7","Complete proteome, Oxidoreductase, Reference proteome",15710748,"Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)","ATCC BAA-918 / JCM 12380 / KOD1",5,170,193,1,162,185]
[null,"Q51799","IPMed?",0.8601,0.8973,46.99,{"v":2e-44,"d":"2.00E-44"},3,1,"porG","Pyruvate synthase subunit PorC / Ketoisovalerate oxidoreductase subunit VorC","1.2.7.1, 1.2.7.7","Complete proteome, Direct protein sequencing, Oxidoreductase, Reference proteome","8550425, 10430560, 8380721","Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)","ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 / ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 / ATCC 43587 / DSM 3638 / JCM 8422 / Vc1",5,170,193,1,162,185]
[null,"O58411","_",0.87047,0.90811,45.83,{"v":7e-44,"d":"7.00E-44"},4,1,"porG","Pyruvate synthase subunit PorC / Ketoisovalerate oxidoreductase subunit VorC","1.2.7.1, 1.2.7.7","Complete proteome, Oxidoreductase",9679194,"Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)","ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3",5,172,193,1,168,185]
[null,"P84820","IPMed?",0.8601,0.8973,46.39,{"v":1e-43,"d":"1.00E-43"},5,1,"porG","Pyruvate synthase subunit PorC / Ketoisovalerate oxidoreductase subunit VorC","1.2.7.1, 1.2.7.7","Complete proteome, Direct protein sequencing, Oxidoreductase","22493191, 8550513","Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)","ATCC 51850 / DSM 5473 / JCM 8560 / NS-C / ATCC 51850 / DSM 5473 / JCM 8560 / NS-C",5,170,193,1,162,185]
[null,"Q9UYY9","_",0.8601,0.8973,46.39,{"v":5e-43,"d":"5.00E-43"},6,1,"porG","Pyruvate synthase subunit PorC / Ketoisovalerate oxidoreductase subunit VorC","1.2.7.1, 1.2.7.7","Complete proteome, Oxidoreductase","12622808, 22057919","Pyrococcus abyssi (strain GE5 / Orsay)","GE5 / Orsay / GE5 / Orsay",5,170,193,1,162,185]
[null,"O27772","_",0.99482,1.06667,42.71,{"v":7e-43,"d":"7.00E-43"},7,1,"porC","Pyruvate synthase subunit PorC","1.2.7.1","Complete proteome, Oxidoreductase, Reference proteome",9371463,"Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)","ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H",5,193,193,1,176,180]
[null,"P80902","IPMed?",0.87047,0.94915,45.24,{"v":3e-41,"d":"3.00E-41"},8,1,"porC","Pyruvate synthase subunit PorC","1.2.7.1","Complete proteome, Direct protein sequencing, Oxidoreductase","20802048, 9108258","Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)","ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg / ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg",5,172,193,1,161,177]
[null,"P80523","IPMed?",0.95855,1.01648,37.84,{"v":2e-39,"d":"2.00E-39"},9,1,"porC","Pyruvate synthase subunit PorC","1.2.7.1","Complete proteome, Direct protein sequencing, Oxidoreductase","16980466, 8620891","Methanosarcina barkeri (strain Fusaro / DSM 804)","Fusaro / DSM 804",7,191,193,3,178,182]
[null,"Q57717","_",0.87047,0.94382,44.64,{"v":7e-38,"d":"7.00E-38"},10,1,"porC","Pyruvate synthase subunit PorC","1.2.7.1","Complete proteome, Oxidoreductase, Reference proteome",8688087,"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440",5,172,193,1,161,178]
[null,"Q8L3B3","IPMed?",0.95337,0.96842,37.5,{"v":5e-28,"d":"5.00E-28"},11,1,"padE","NADH-dependent phenylglyoxylate dehydrogenase subunit gamma","1.2.1.58","Direct protein sequencing, NAD, Oxidoreductase",9490067,"Azoarcus evansii","KB740 / DSM 6898",7,190,193,3,179,190]
[null,"Q2RI40","IPMed?",0.66984,1.09326,29.38,6e-15,12,3,"_","Oxalate oxidoreductase subunit delta","1.2.7.10","3D-structure, 4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat","18631365, 20956531","Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320",4,191,193,11,204,315]
[null,"P52647","IPMed?",0.16865,1.02591,24.75,3E-10,13,6,"ydbK","Probable pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","9097039, 9278503, 16738553, 9025293","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",6,193,193,418,615,1174]
[null,"Q2RMD6","IPMed?",0.14688,0.89119,27.33,3E-9,14,6,"_","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Reference proteome, Transport","18631365, 9214293, 10878009, 29581263","Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320 / ATCC 39073 / JCM 9320",32,193,193,442,612,1171]
[null,"P19543","IPMed?",0.17562,1.06736,23.3,2e-07,15,7,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Plasmid, Repeat, Transport","2504647, 1708766","Enterobacter agglomerans","333 / 333",2,193,193,414,615,1173]
[]
["CLOSTRIBL3_v1_10343","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P19543","IPMed?",1.00085,1.00514,70.78,0,1,1,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Plasmid, Repeat, Transport","2504647, 1708766","Enterobacter agglomerans","333 / 333",3,1167,1168,4,1173,1173]
[null,"P03833","IPMed?",0.99744,1,67.81,0,2,1,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","3062178, 3060860, 8483412, 6306580","Klebsiella pneumoniae","_",3,1168,1168,4,1171,1171]
[null,"Q2RMD6","IPMed?",0.99915,1.00171,64.62,0,3,1,"_","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Reference proteome, Transport","18631365, 9214293, 10878009, 29581263","Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320 / ATCC 39073 / JCM 9320",5,1165,1168,4,1169,1171]
[null,"P94692","IPMed?",0.94886,1.00086,58.85,0,4,1,"por","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Calcium, Cytoplasm, Direct protein sequencing, Disulfide bond, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Thiamine pyrophosphate, Transport","9294422, 7612653, 10048931, 11752578, 16472741","Desulfocurvibacter africanus","ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi / ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi",3,1165,1168,4,1167,1232]
[null,"Q94IN5","IPMed?",0.64836,1.00086,50.9,0,5,1,"PNO","Pyruvate dehydrogenase [NADP(+)], mitochondrial","1.2.1.51","4Fe-4S, Direct protein sequencing, Electron transport, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, Mitochondrion, NADP, Oxidoreductase, Repeat, Thiamine pyrophosphate, Transit peptide, Transport","11023353, 11319255, 1910287, 8373179, 3110154, 12623066","Euglena gracilis","SAG1224-5/25",5,1164,1168,70,1232,1803]
[null,"Q968X7","IPMed?",0.64426,1.06678,49.76,0,6,1,"PFOR","Pyruvate dehydrogenase [NADP(+)]","1.2.1.51","4Fe-4S, Electron transport, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat, Thiamine pyrophosphate, Transport",11319255,"Cryptosporidium parvum","KSU-1",1,1165,1168,1,1241,1934]
[null,"Q3M8N0","IPMed?",1.00252,1.0214,49.79,0,7,2,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","25197444, 8352652","Trichormus variabilis (strain ATCC 29413 / PCC 7937)","ATCC 29413 / PCC 7937",6,1168,1168,8,1186,1190]
[null,"Q06879","IPMed?",1.00417,1.03082,48.09,0,9,2,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8415612, 11759840","Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)","PCC 7120 / SAG 25.82 / UTEX 2576",6,1166,1168,7,1198,1199]
[null,"P52965","_",0.98499,1.01113,49.36,0,8,2,"nifJ","Putative pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8590279, 8905231","Synechocystis sp. (strain PCC 6803 / Kazusa)","ATCC 27184 / PCC 6803 / N-1 / PCC 6803 / Kazusa",6,1165,1168,8,1173,1199]
[null,"Q53046","IPMed?",0.9958,1.01541,46.8,0,10,2,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8736535, 21886856","Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)","ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1",3,1165,1168,5,1178,1191]
[null,"P52647","IPMed?",1.00511,1.01027,47.03,0,11,2,"ydbK","Probable pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","9097039, 9278503, 16738553, 9025293","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",4,1165,1168,1,1165,1174]
[]
["CLOSTRIBL3_v1_20129","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P19543","IPMed?",1,1.00256,62.75,0,1,2,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Plasmid, Repeat, Transport","2504647, 1708766","Enterobacter agglomerans","333 / 333",7,1169,1170,4,1171,1173]
[null,"P03833","IPMed?",0.99744,0.99829,61.04,0,2,2,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","3062178, 3060860, 8483412, 6306580","Klebsiella pneumoniae","_",7,1169,1170,4,1168,1171]
[null,"Q2RMD6","IPMed?",1.00085,1.00171,60.49,0,3,2,"_","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Reference proteome, Transport","18631365, 9214293, 10878009, 29581263","Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320 / ATCC 39073 / JCM 9320",9,1170,1170,4,1170,1171]
[null,"P94692","IPMed?",0.93425,0.98376,57.86,0,4,3,"por","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Calcium, Cytoplasm, Direct protein sequencing, Disulfide bond, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Thiamine pyrophosphate, Transport","9294422, 7612653, 10048931, 11752578, 16472741","Desulfocurvibacter africanus","ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi / ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi",7,1150,1170,4,1148,1232]
[null,"Q94IN5","IPMed?",0.64892,1,49.32,0,5,3,"PNO","Pyruvate dehydrogenase [NADP(+)], mitochondrial","1.2.1.51","4Fe-4S, Direct protein sequencing, Electron transport, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, Mitochondrion, NADP, Oxidoreductase, Repeat, Thiamine pyrophosphate, Transit peptide, Transport","11023353, 11319255, 1910287, 8373179, 3110154, 12623066","Euglena gracilis","SAG1224-5/25",8,1168,1170,69,1232,1803]
[null,"Q968X7","IPMed?",0.62875,1.03932,49.26,0,6,3,"PFOR","Pyruvate dehydrogenase [NADP(+)]","1.2.1.51","4Fe-4S, Electron transport, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat, Thiamine pyrophosphate, Transport",11319255,"Cryptosporidium parvum","KSU-1",11,1147,1170,7,1219,1934]
[null,"Q3M8N0","IPMed?",0.99664,1.01368,49.24,0,7,3,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","25197444, 8352652","Trichormus variabilis (strain ATCC 29413 / PCC 7937)","ATCC 29413 / PCC 7937",10,1169,1170,8,1183,1190]
[null,"P52965","_",0.98499,1.0094,47.84,0,8,3,"nifJ","Putative pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8590279, 8905231","Synechocystis sp. (strain PCC 6803 / Kazusa)","ATCC 27184 / PCC 6803 / N-1 / PCC 6803 / Kazusa",8,1170,1170,6,1174,1199]
[null,"Q06879","IPMed?",0.99917,1.02393,46.58,0,9,3,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8415612, 11759840","Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)","PCC 7120 / SAG 25.82 / UTEX 2576",10,1169,1170,7,1197,1199]
[null,"Q53046","IPMed?",0.99328,1.01111,46.83,0,10,3,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8736535, 21886856","Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)","ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1",7,1169,1170,5,1178,1191]
[null,"P52647","IPMed?",1.00596,1.0094,46.32,0,11,3,"ydbK","Probable pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","9097039, 9278503, 16738553, 9025293","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",10,1169,1170,3,1165,1174]
[]
["CLOSTRIBL3_v1_12838","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P45359","IPMed?",1,1,73.47,0,1,1,"thlA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","7867955, 11075929, 11466286, 1685080","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,392,392,1,391,392]
[null,"Q18AR0","_",1,1.00256,69.9,0,2,1,"thlA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",16804543,"Peptoclostridium difficile (strain 630)",630,1,392,392,1,391,391]
[null,"P14611","IPMed?",0.99746,1,64.8,{"v":2E-174,"d":"2.00E-174"},4,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, PHB biosynthesis, Reference proteome, Transferase","2670935, 16964242, 2670936, 4198758, 1476773, 25152395","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337",1,392,392,1,392,393]
[null,"Q0AVM3","IPMed?",0.99495,1.0051,65.74,{"v":2E-174,"d":"2.00E-174"},3,1,"_","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",2,391,392,3,394,396]
[null,"Q9I2A8","_",0.99746,1,63.01,{"v":2E-171,"d":"2.00E-171"},5,1,"atoB","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase",10984043,"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1",1,392,392,1,392,393]
[null,"P45369","IPMed?",0.98985,0.9949,61.79,{"v":1E-169,"d":"1.00E-169"},6,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, PHB biosynthesis, Reference proteome, Transferase","1396692, 22675582, 1476773","Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)","ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D / ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D",3,392,392,4,393,394]
[null,"P45363","IPMed?",0.98731,0.99235,60.93,{"v":1E-166,"d":"1.00E-166"},7,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase","7763384, 1476773","Thiocystis violacea","2311 / DSM 208",4,392,392,5,393,394]
[null,"P44873","_",1,1.00255,61.83,{"v":6e-163,"d":"6.00E-163"},8,1,"atoB","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",1,392,392,1,392,393]
[null,"Q9ZHI1","IPMed?",0.9949,0.9949,60.51,{"v":3e-161,"d":"3.00E-161"},9,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, PHA biosynthesis, Reference proteome, Transferase","14500782, 10427049","Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)","ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757 / ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757",3,392,392,2,391,392]
[null,"P76461","_",0.99746,1.00255,61.32,{"v":2e-157,"d":"2.00E-157"},10,1,"atoB","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","9097040, 9278503, 16738553","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",1,392,392,1,392,394]
[null,"P54810","IPMed?",1,1.00256,59.18,{"v":6E-157,"d":"6.00E-157"},11,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase",8566717,"Paracoccus denitrificans","_",1,392,392,1,390,391]
[null,"P50174","IPMed?",0.98982,0.99235,59.38,{"v":7e-157,"d":"7.00E-157"},12,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, PHB biosynthesis, Reference proteome, Transferase","7582015, 11481430, 11474104","Rhizobium meliloti (strain 1021)","41 / 1021 / 1021",4,392,392,6,392,393]
[null,"P07097","IPMed?",0.98724,0.98724,58.4,{"v":2E-155,"d":"2.00E-155"},13,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase","2878929, 2670935, 1673680, 1476773, 10764581, 10545327, 12501183","Zoogloea ramigera","ATCC 19623 / I-16-M / NCIB 10340 / NCTC 10482",5,391,392,6,390,392]
[null,"Q8CAY6","IPMed?",0.98489,0.99745,55.75,{"v":1e-140,"d":"1.00E-140"},14,1,"Acat2","Acetyl-CoA acetyltransferase, cytosolic","2.3.1.9","Acetylation, Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","16141072, 15489334, 2055458, 21183079","Mus musculus","C57BL/6J / C57BL/6J / C57BL/6J",4,392,392,8,396,397]
[]
["CLOSTRIBL3_v1_13111","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q0AVM3","IPMed?",0.99495,1.00767,50.76,{"v":1e-132,"d":"1.00E-132"},1,2,"_","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",2,390,391,3,394,396]
[null,"Q9I2A8","_",1,1.00512,49.36,{"v":4e-123,"d":"4.00E-123"},2,2,"atoB","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase",10984043,"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1",1,387,391,1,388,393]
[null,"P45359","IPMed?",1.00765,1.01023,45.32,{"v":5e-122,"d":"5.00E-122"},3,2,"thlA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","7867955, 11075929, 11466286, 1685080","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,390,391,1,390,392]
[null,"Q18AR0","_",1,1,46.29,{"v":2E-118,"d":"2.00E-118"},4,2,"thlA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",16804543,"Peptoclostridium difficile (strain 630)",630,1,390,391,1,390,391]
[null,"Q9ZHI1","IPMed?",0.99235,0.99488,48.59,{"v":4e-118,"d":"4.00E-118"},5,2,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, PHA biosynthesis, Reference proteome, Transferase","14500782, 10427049","Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)","ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757 / ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757",4,390,391,3,390,392]
[null,"Q5HIU0","_",0.99491,1,45.78,{"v":4e-115,"d":"4.00E-115"},6,2,"_","Probable acetyl-CoA acyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Transferase",15774886,"Staphylococcus aureus (strain COL)","COL",1,389,391,1,389,393]
[null,"P44873","_",0.99746,1.00256,45.41,{"v":6e-115,"d":"6.00E-115"},7,2,"atoB","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",1,390,391,1,391,393]
[null,"Q8NY95","_",0.99491,1,45.52,{"v":2e-114,"d":"2.00E-114"},8,2,"_","Probable acetyl-CoA acyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Transferase",12044378,"Staphylococcus aureus (strain MW2)","MW2",1,389,391,1,389,393]
[null,"Q6GCB8","_",0.99491,1,45.52,{"v":2e-114,"d":"2.00E-114"},8,2,"_","Probable acetyl-CoA acyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, Transferase",15213324,"Staphylococcus aureus (strain MSSA476)","MSSA476",1,389,391,1,389,393]
[null,"Q2G124","_",0.99491,1,45.52,{"v":2e-114,"d":"2.00E-114"},8,2,"_","Probable acetyl-CoA acyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","_","Staphylococcus aureus (strain NCTC 8325)","_",1,389,391,1,389,393]
[null,"Q2FJQ9","_",0.99491,1,45.52,{"v":2e-114,"d":"2.00E-114"},8,2,"_","Probable acetyl-CoA acyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Transferase",16517273,"Staphylococcus aureus (strain USA300)","USA300",1,389,391,1,389,393]
[null,"Q7A7L2","_",0.99491,1,45.27,{"v":9e-114,"d":"9.00E-114"},9,2,"_","Probable acetyl-CoA acyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Transferase","11418146, 15590099","Staphylococcus aureus (strain N315)","N315 / N315",1,389,391,1,389,393]
[null,"Q99WM3","_",0.99491,1,45.27,{"v":9e-114,"d":"9.00E-114"},9,2,"_","Probable acetyl-CoA acyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Transferase",11418146,"Staphylococcus aureus (strain Mu50 / ATCC 700699)","Mu50 / ATCC 700699",1,389,391,1,389,393]
[null,"Q6GJW4","_",0.99491,1,45.27,{"v":1e-113,"d":"1.00E-113"},10,2,"_","Probable acetyl-CoA acyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, Transferase",15213324,"Staphylococcus aureus (strain MRSA252)","MRSA252",1,389,391,1,389,393]
[null,"P45369","IPMed?",1,1.00767,45.18,{"v":4e-113,"d":"4.00E-113"},11,2,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, PHB biosynthesis, Reference proteome, Transferase","1396692, 22675582, 1476773","Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)","ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D / ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D",3,390,391,4,392,394]
[null,"P50174","IPMed?",0.98982,0.99488,47.81,{"v":8e-112,"d":"8.00E-112"},12,2,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, PHB biosynthesis, Reference proteome, Transferase","7582015, 11481430, 11474104","Rhizobium meliloti (strain 1021)","41 / 1021 / 1021",3,390,391,5,391,393]
[null,"P14611","IPMed?",0.99746,1.00256,44.9,{"v":2e-111,"d":"2.00E-111"},13,2,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, PHB biosynthesis, Reference proteome, Transferase","2670935, 16964242, 2670936, 4198758, 1476773, 25152395","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337",1,390,391,1,391,393]
[null,"P45363","IPMed?",0.99746,1.00512,44.78,{"v":5e-111,"d":"5.00E-111"},14,2,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase","7763384, 1476773","Thiocystis violacea","2311 / DSM 208",4,390,391,5,392,394]
[null,"P54810","IPMed?",1.01023,1.01023,44.3,{"v":3e-109,"d":"3.00E-109"},15,2,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase",8566717,"Paracoccus denitrificans","_",1,390,391,1,389,391]
[null,"P42765","IPMed?",0.98489,1,45.52,{"v":5e-109,"d":"5.00E-109"},16,2,"ACAA2","3-ketoacyl-CoA thiolase, mitochondrial","2.3.1.16","3D-structure, Acetylation, Acyltransferase, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Hydrolase, Lipid metabolism, Mitochondrion, Phosphoprotein, Polymorphism, Reference proteome, Transferase, Transit peptide","8241273, 15489334, 15242332, 18371312, 18669648, 21269460, 24275569, 25944712, 25478839","Homo sapiens","_",1,390,391,4,394,397]
[null,"P07097","IPMed?",0.98724,0.98977,45.74,{"v":2e-108,"d":"2.00E-108"},17,2,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase","2878929, 2670935, 1673680, 1476773, 10764581, 10545327, 12501183","Zoogloea ramigera","ATCC 19623 / I-16-M / NCIB 10340 / NCTC 10482",5,390,391,6,390,392]
[]
["CLOSTRIBL3_v1_11283","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O26884","_",0.99248,1.03394,42.17,{"v":2E-92,"d":"2.00E-92"},1,1,"_","Uncharacterized protein MTH_793","_","Complete proteome, Reference proteome",9371463,"Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)","ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H",1,396,399,1,383,383]
[null,"Q58944","_",1.00752,1.02551,38.81,{"v":1e-71,"d":"1.00E-71"},2,1,"_","Uncharacterized protein MJ1549","_","Complete proteome, Reference proteome",8688087,"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440",1,395,399,1,389,392]
[null,"P32020","IPMed?",0.75137,1.03008,32.85,{"v":5e-45,"d":"5.00E-45"},3,1,"Scp2","Non-specific lipid-transfer protein","2.3.1.176","Acetylation, Acyltransferase, Alternative initiation, Complete proteome, Cytoplasm, Direct protein sequencing, Lipid transport, Lipid-binding, Mitochondrion, Peroxisome, Phosphoprotein, Reference proteome, Transferase, Transport","8428655, 16141072, 19468303, 15489334, 1709640, 8751375, 16916647, 17208939, 17242355, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / C57BL/6J / 129/Sv",1,393,399,11,402,547]
[null,"P22307","IPMed?",0.74589,1.02256,33.09,{"v":1e-44,"d":"1.00E-44"},4,1,"SCP2","Non-specific lipid-transfer protein","2.3.1.176","3D-structure, Acetylation, Acyltransferase, Alternative promoter usage, Alternative splicing, Complete proteome, Cytoplasm, Direct protein sequencing, Lipid transport, Lipid-binding, Mitochondrion, Peroxisome, Phosphoprotein, Polymorphism, Reference proteome, Transferase, Transport","7698762, 1718316, 1703300, 1483685, 14702039, 16710414, 15489334, 14563822, 16685654, 8300590, 19608861, 21269460, 24275569, 25944712, 8243660, 17157249, 16959974","Homo sapiens","_",1,393,399,11,402,547]
[null,"O62742","IPMed?",0.73492,1.00752,32.84,{"v":3e-42,"d":"3.00E-42"},5,1,"SCP2","Non-specific lipid-transfer protein","2.3.1.176","3D-structure, Acetylation, Acyltransferase, Alternative initiation, Complete proteome, Cytoplasm, Lipid transport, Lipid-binding, Mitochondrion, Peroxisome, Phosphoprotein, Reference proteome, Transferase, Transport","9711242, 10417421, 10684638","Oryctolagus cuniculus","_",4,390,399,14,400,547]
[null,"P07857","IPMed?",0.74401,1.01253,31.68,{"v":5E-42,"d":"5.00E-42"},6,1,"SCP2","Non-specific lipid-transfer protein","2.3.1.176","Acetylation, Acyltransferase, Alternative initiation, Complete proteome, Cytoplasm, Direct protein sequencing, Lipid transport, Lipid-binding, Mitochondrion, Peroxisome, Phosphoprotein, Reference proteome, Transferase, Transport",3977925,"Bos taurus","_",4,393,399,14,401,543]
[null,"P11915","IPMed?",0.73857,1.01253,31.93,{"v":7e-42,"d":"7.00E-42"},7,1,"Scp2","Non-specific lipid-transfer protein","2.3.1.176","Acetylation, Acyltransferase, Alternative initiation, Complete proteome, Cytoplasm, Direct protein sequencing, Lipid transport, Lipid-binding, Mitochondrion, Peroxisome, Phosphoprotein, Reference proteome, Transferase, Transport","1985920, 2034675, 1915369, 15489334, 2334427, 2340090, 3115977, 3395344, 22673903","Rattus norvegicus","Wistar / CD Charles River",4,390,399,14,400,547]
[null,"Q07598","IPMed?",0.74589,1.02256,32.84,{"v":1E-41,"d":"1.00E-41"},8,1,"SCP2","Non-specific lipid-transfer protein","2.3.1.176","Acyltransferase, Alternative initiation, Complete proteome, Cytoplasm, Lipid transport, Lipid-binding, Mitochondrion, Peroxisome, Reference proteome, Transferase, Transport",8323294,"Gallus gallus","White leghorn",2,393,399,16,405,547]
[null,"G5EDP2","IPMed?",0.99757,1.03008,32.12,{"v":8e-40,"d":"8.00E-40"},9,1,"daf-22","Non-specific lipid-transfer protein-like 2","2.3.1.176","Complete proteome, Lipid transport, Lipid-binding, Peroxisome, Reference proteome, Transferase, Transport","9151950, 9851916, 3859733, 19496754, 19174521","Caenorhabditis elegans","Bristol N2 / Bristol N2",3,390,399,7,397,412]
[null,"Q0AVM3","IPMed?",1.10526,1.11364,22.45,1e-11,10,3,"_","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",2,390,399,3,392,396]
[null,"Q04677","IPMed?",1.04715,1.05764,24.64,2e-10,11,3,"PACTB","Acetyl-CoA acetyltransferase IB","2.3.1.9","Acyltransferase, Direct protein sequencing, Peroxisome, Transferase",1362382,"Candida tropicalis","ATCC 20336 / pK233 / NCYC 997",15,390,399,21,393,403]
[null,"Q12598","IPMed?",1.00993,1.02005,24.57,2e-10,12,3,"PACTA","Acetyl-CoA acetyltransferase IA","2.3.1.9","Acyltransferase, Direct protein sequencing, Peroxisome, Transferase",1362382,"Candida tropicalis","ATCC 20336 / pK233 / NCYC 997",15,377,399,21,385,403]
[]
["CLOSTRIBL3_v1_11276","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P45856","IPMed?",0.92283,1,37.63,{"v":2e-53,"d":"2.00E-53"},1,2,"mmgB","Probable 3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",3,288,311,1,282,287]
[null,"P77851","_",0.9164,1.01423,37.19,{"v":9e-48,"d":"9.00E-48"},2,3,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",5,288,311,1,280,281]
[null,"P52041","IPMed?",0.9164,1.01064,36.14,{"v":2E-45,"d":"2.00E-45"},3,4,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",5,288,311,1,280,282]
[null,"Q8CUW0","_",0.76849,0.7785,39.75,{"v":2E-41,"d":"2.00E-41"},4,1,"lcdH","L-carnitine dehydrogenase","1.1.1.108","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Reference proteome",12235376,"Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831)","DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831",5,243,311,1,235,307]
[null,"P45364","IPMed?",0.90997,1.00712,33.22,{"v":1e-39,"d":"1.00E-39"},5,4,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase",8001771,"Clostridioides difficile","E",7,288,311,2,279,281]
[null,"Q9Y2S2","IPMed?",0.77429,0.79421,33.6,{"v":3e-39,"d":"3.00E-39"},6,1,"CRYL1","Lambda-crystallin homolog","1.1.1.45","3D-structure, Acetylation, Alternative splicing, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","12527201, 14702039, 15057823, 15489334, 15809331, 21269460, 24275569","Homo sapiens","_",8,253,311,9,255,319]
[null,"Q5RDZ2","_",0.77429,0.79421,33.6,{"v":3e-39,"d":"3.00E-39"},6,1,"CRYL1","Lambda-crystallin homolog","1.1.1.45","Acetylation, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","_","Pongo abelii","_",8,253,311,9,255,319]
[null,"P76083","IPMed?",0.61684,0.94212,34.13,{"v":6e-39,"d":"6.00E-39"},7,3,"paaH","3-hydroxyadipyl-CoA dehydrogenase","1.1.1.-","3D-structure, Complete proteome, NAD, Oxidoreductase, Reference proteome","9748275, 9097039, 9278503, 16738553, 10766858, 12846838, 20660314","Escherichia coli (strain K12)","W / ATCC 11105 / DSM 1900 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",1,291,311,1,288,475]
[null,"Q9RVG1","_",0.90997,1.01799,34.28,{"v":2e-38,"d":"2.00E-38"},8,3,"hbd","Probable 3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome",10567266,"Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)","ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422",7,288,311,2,278,278]
[null,"P9WNP6","_",0.93248,1.01399,31.72,{"v":3E-37,"d":"3.00E-37"},9,3,"fadB2","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",1,288,311,1,286,286]
[null,"P9WNP7","IPMed?",0.93248,1.01399,31.72,{"v":3E-37,"d":"3.00E-37"},9,3,"fadB2","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","9634230, 11489128, 12081975, 20378648, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",1,288,311,1,286,286]
[null,"Q0AVM2","IPMed?",0.90354,1.00717,32.03,{"v":4e-37,"d":"4.00E-37"},10,3,"_","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.35","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, NAD, Oxidoreductase, Reference proteome","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",7,286,311,2,277,279]
[null,"Q99KP3","IPMed?",0.77429,0.79421,33.2,{"v":6E-37,"d":"6.00E-37"},11,1,"Cryl1","Lambda-crystallin homolog","1.1.1.45","Acetylation, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","12527201, 16141072, 15489334, 21183079","Mus musculus","C57BL/6J / FVB/N",8,253,311,9,255,319]
[null,"Q811X6","IPMed?",0.77429,0.79421,31.98,{"v":2E-35,"d":"2.00E-35"},12,1,"Cryl1","Lambda-crystallin homolog","1.1.1.45","Acetylation, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","12527201, 15489334, 22673903","Rattus norvegicus","_",8,253,311,9,255,319]
[null,"P14755","IPMed?",0.77429,0.79421,31.98,{"v":3e-35,"d":"3.00E-35"},13,1,"CRYL1","Lambda-crystallin","1.1.1.45","3D-structure, Acetylation, Complete proteome, Cytoplasm, Direct protein sequencing, Eye lens protein, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","3170592, 15809331","Oryctolagus cuniculus","_",8,253,311,9,255,319]
[]
["CLOSTRIBL3_v1_13113","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P52041","IPMed?",0.98958,1.01064,40.7,{"v":4e-60,"d":"4.00E-60"},1,2,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",3,287,288,1,280,282]
[null,"P00348","IPMed?",0.93312,1.01736,39.25,{"v":3e-59,"d":"3.00E-59"},2,2,"HADH","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide","9593854, 7409145, 10064895, 3479790, 10548046","Sus scrofa","_",3,288,288,27,314,314]
[null,"Q16836","IPMed?",0.93312,1.01736,38.57,{"v":5e-59,"d":"5.00E-59"},3,2,"HADH","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","3D-structure, Acetylation, Alternative splicing, Complete proteome, Disease mutation, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Polymorphism, Reference proteome, Transit peptide","8687463, 15815621, 15489334, 19608861, 21269460, 24275569, 25944712, 10231530, 10840044, 16176262, 11489939","Homo sapiens","_",3,288,288,27,314,314]
[null,"P45364","IPMed?",0.98264,1.00712,40.28,{"v":2e-58,"d":"2.00E-58"},4,2,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase",8001771,"Clostridioides difficile","E",5,287,288,2,279,281]
[null,"Q9WVK7","IPMed?",0.93312,1.01736,38.57,{"v":1E-56,"d":"1.00E-56"},5,2,"Hadh","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","Acetylation, Complete proteome, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide",10064895,"Rattus norvegicus","Sprague-Dawley",3,288,288,27,314,314]
[null,"Q0AVM2","IPMed?",0.98264,1.01434,35.69,{"v":4e-56,"d":"4.00E-56"},6,2,"_","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.35","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, NAD, Oxidoreductase, Reference proteome","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",5,287,288,2,279,279]
[null,"Q61425","IPMed?",0.93312,1.01736,38.57,{"v":5E-56,"d":"5.00E-56"},7,2,"Hadh","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","Acetylation, Complete proteome, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide","7642117, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J",3,288,288,27,314,314]
[null,"P77851","_",0.99306,1.01779,37.06,{"v":1e-55,"d":"1.00E-55"},8,2,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",3,288,288,1,281,281]
[null,"P34439","_",0.99329,1.02778,37.5,{"v":2E-51,"d":"2.00E-51"},9,2,"_","Probable 3-hydroxyacyl-CoA dehydrogenase F54C8.1","1.1.1.35","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome","7906398, 9851916","Caenorhabditis elegans","Bristol N2 / Bristol N2",2,288,288,10,297,298]
[null,"P45856","IPMed?",1.00694,1.01045,34.83,{"v":5e-50,"d":"5.00E-50"},10,3,"mmgB","Probable 3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",1,288,288,1,283,287]
[null,"P76083","IPMed?",0.60842,1.00347,35.99,{"v":2E-41,"d":"2.00E-41"},11,2,"paaH","3-hydroxyadipyl-CoA dehydrogenase","1.1.1.-","3D-structure, Complete proteome, NAD, Oxidoreductase, Reference proteome","9748275, 9097039, 9278503, 16738553, 10766858, 12846838, 20660314","Escherichia coli (strain K12)","W / ATCC 11105 / DSM 1900 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",1,288,288,3,286,475]
[null,"P9WNP7","IPMed?",0.99306,1,32.52,{"v":2e-38,"d":"2.00E-38"},12,2,"fadB2","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","9634230, 11489128, 12081975, 20378648, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",3,287,288,5,286,286]
[]
["CLOSTRIBL3_v1_20313","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P52041","IPMed?",1,1,79.08,{"v":4e-162,"d":"4.00E-162"},1,1,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,282,282,1,282,282]
[null,"P77851","_",0.99645,1,67.97,{"v":9e-137,"d":"9.00E-137"},2,1,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",1,281,282,1,281,281]
[null,"Q0AVM2","IPMed?",0.98582,0.99642,63.31,{"v":5e-126,"d":"5.00E-126"},3,1,"_","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.35","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, NAD, Oxidoreductase, Reference proteome","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",3,280,282,2,279,279]
[null,"P45364","IPMed?",0.99291,0.99644,59.64,{"v":8e-113,"d":"8.00E-113"},4,1,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase",8001771,"Clostridioides difficile","E",3,282,282,2,281,281]
[null,"P45856","IPMed?",0.98258,1,53.55,{"v":9E-103,"d":"9.00E-103"},5,1,"mmgB","Probable 3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",1,282,282,3,284,287]
[null,"Q9RVG1","_",0.98582,1,54.32,{"v":1E-97,"d":"1.00E-97"},6,1,"hbd","Probable 3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome",10567266,"Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)","ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422",3,280,282,2,278,278]
[null,"Q45223","_",0.95904,0.99645,50.53,{"v":1e-95,"d":"1.00E-95"},7,1,"hbdA","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome",12597275,"Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110",1,281,282,5,285,293]
[null,"P9WNP7","IPMed?",0.98601,1,40.43,{"v":3e-72,"d":"3.00E-72"},8,1,"fadB2","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","9634230, 11489128, 12081975, 20378648, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",1,280,282,5,286,286]
[null,"P9WNP6","_",0.98601,1,40.43,{"v":3e-72,"d":"3.00E-72"},8,1,"fadB2","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",1,280,282,5,286,286]
[null,"Q16836","IPMed?",0.92038,1.02482,43.94,{"v":7E-72,"d":"7.00E-72"},9,1,"HADH","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","3D-structure, Acetylation, Alternative splicing, Complete proteome, Disease mutation, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Polymorphism, Reference proteome, Transit peptide","8687463, 15815621, 15489334, 19608861, 21269460, 24275569, 25944712, 10231530, 10840044, 16176262, 11489939","Homo sapiens","_",1,281,282,27,314,314]
[null,"P76083","IPMed?",0.59368,1,43.26,{"v":3e-71,"d":"3.00E-71"},10,1,"paaH","3-hydroxyadipyl-CoA dehydrogenase","1.1.1.-","3D-structure, Complete proteome, NAD, Oxidoreductase, Reference proteome","9748275, 9097039, 9278503, 16738553, 10766858, 12846838, 20660314","Escherichia coli (strain K12)","W / ATCC 11105 / DSM 1900 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",1,281,282,5,286,475]
[null,"Q9WVK7","IPMed?",0.92038,1.02482,43.94,{"v":4e-71,"d":"4.00E-71"},11,1,"Hadh","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","Acetylation, Complete proteome, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide",10064895,"Rattus norvegicus","Sprague-Dawley",1,281,282,27,314,314]
[null,"Q61425","IPMed?",0.92038,1.02482,43.94,{"v":4e-71,"d":"4.00E-71"},11,1,"Hadh","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","Acetylation, Complete proteome, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide","7642117, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J",1,281,282,27,314,314]
[null,"P00348","IPMed?",0.92038,1.02482,42.91,{"v":1E-70,"d":"1.00E-70"},12,1,"HADH","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide","9593854, 7409145, 10064895, 3479790, 10548046","Sus scrofa","_",1,281,282,27,314,314]
[null,"Q9ZPI6","IPMed?",0.39112,1,36.52,{"v":3e-53,"d":"3.00E-53"},13,1,"AIM1","Enoyl-CoA hydratase/3-2-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase / 3-hydroxyacyl-CoA dehydrogenase","4.2.1.17, 5.1.2.3, 5.3.3.8, 1.1.1.35","Complete proteome, Fatty acid metabolism, Isomerase, Lipid metabolism, Lyase, Multifunctional enzyme, NAD, Oxidoreductase, Peroxisome, Reference proteome","10521521, 10617198, 27862469, 14593172, 17544464, 17951448, 20463021, 24254312","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia",1,282,282,309,587,721]
[]
["CLOSTRIBL3_v1_13112","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P52046","IPMed?",0.96935,0.99216,45.85,{"v":6e-69,"d":"6.00E-69"},1,2,"crt","Short-chain-enoyl-CoA hydratase","4.2.1.150","3D-structure, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","8655474, 11466286, 5057466","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,249,255,3,254,261]
[null,"A4YI89","IPMed?",0.96139,0.97647,45.78,{"v":5e-64,"d":"5.00E-64"},2,2,"_","3-hydroxypropionyl-coenzyme A dehydratase","4.2.1.116","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","18083856, 19429610","Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)","ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2",10,255,255,12,259,259]
[null,"Q0AVM1","IPMed?",0.99231,1.01176,43.02,{"v":7e-64,"d":"7.00E-64"},3,2,"_","Crotonyl-CoA hydratase","4.2.1.150","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",2,255,255,4,260,260]
[null,"Q1ZXF1","_",0.90253,0.98039,40,{"v":3e-55,"d":"3.00E-55"},4,2,"echs1","Probable enoyl-CoA hydratase, mitochondrial","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide",15875012,"Dictyostelium discoideum","AX4",7,255,255,29,277,277]
[null,"Q8BH95","_",0.82414,0.93725,41.84,{"v":4E-55,"d":"4.00E-55"},5,2,"Echs1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Phosphoprotein, Reference proteome, Transit peptide","16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / C57BL/6J",12,249,255,47,284,290]
[null,"Q54HG7","_",0.81848,0.97255,40.73,{"v":5e-55,"d":"5.00E-55"},6,1,"auh","Methylglutaconyl-CoA hydratase, mitochondrial","4.2.1.18","Branched-chain amino acid catabolism, Complete proteome, Lyase, Mitochondrion, Reference proteome, Transit peptide",15875012,"Dictyostelium discoideum","AX4",12,255,255,57,303,303]
[null,"Q52995","IPMed?",0.96887,0.97647,40.96,{"v":1E-54,"d":"1.00E-54"},7,2,"fadB1","Probable enoyl-CoA hydratase","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","7751302, 11481430, 11474104","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",2,249,255,4,251,257]
[null,"P14604","IPMed?",0.82414,0.93725,41,{"v":1E-53,"d":"1.00E-53"},8,2,"Echs1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide","2806264, 15489334, 7883013, 8895557, 9480773, 11851409, 12445775","Rattus norvegicus","_",12,249,255,47,284,290]
[null,"F4JML5","IPMed?",0.82392,0.97255,43.95,{"v":2e-53,"d":"2.00E-53"},9,1,"_","Probable enoyl-CoA hydratase 2, mitochondrial","4.2.1.17","Complete proteome, Fatty acid metabolism, Hydrolase, Lipid metabolism, Lyase, Mitochondrion, Protease, Reference proteome, Transit peptide","9461215, 10617198, 27862469, 14593172, 10929101","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia",13,254,255,54,300,301]
[null,"P30084","IPMed?",0.82414,0.93725,39.75,{"v":6e-53,"d":"6.00E-53"},10,2,"ECHS1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Disease mutation, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Neurodegeneration, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","8012501, 9073515, 15164054, 15489334, 1286669, 11271497, 19608861, 21269460, 25125611, 24275569, 25393721, 25944712, 26000322, 26251176, 27221955, 26741492","Homo sapiens","_",12,249,255,47,284,290]
[null,"Q4PEN0","IPMed?",0.95985,1.03137,40.3,{"v":1E-51,"d":"1.00E-51"},11,1,"fer4","Enoyl-CoA isomerase/hydratase fer4","4.2.1.17","Coiled coil, Complete proteome, Isomerase, Lyase, Reference proteome, Virulence","17080091, 17138696, 20070524","Ustilago maydis (strain 521 / FGSC 9021)","521 / FGSC 9021 / 521 / FGSC 9021",5,255,255,14,274,274]
[null,"Q9JLZ3","IPMed?",0.80255,0.98824,40.48,{"v":1E-50,"d":"1.00E-50"},12,2,"Auh","Methylglutaconyl-CoA hydratase, mitochondrial","4.2.1.18","Acetylation, Alternative splicing, Branched-chain amino acid catabolism, Complete proteome, Lyase, Mitochondrion, Reference proteome, RNA-binding, Transit peptide","10072761, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","BALB/cJ / C57BL/6J",12,255,255,64,314,314]
[null,"F1LU71","IPMed?",0.8,0.98824,39.68,{"v":1e-49,"d":"1.00E-49"},13,2,"Auh","Methylglutaconyl-CoA hydratase, mitochondrial","4.2.1.18","Acetylation, Branched-chain amino acid catabolism, Complete proteome, Lyase, Mitochondrion, Reference proteome, RNA-binding, Transit peptide","15057822, 13783048","Rattus norvegicus","Brown Norway",12,255,255,65,315,315]
[]
["CLOSTRIBL3_v1_11087","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q1ZXF1","_",0.92419,1.00787,32.03,{"v":2e-27,"d":"2.00E-27"},1,3,"echs1","Probable enoyl-CoA hydratase, mitochondrial","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide",15875012,"Dictyostelium discoideum","AX4",7,254,254,29,277,277]
[null,"P52046","IPMed?",0.96552,0.99213,31.75,{"v":6e-27,"d":"6.00E-27"},2,3,"crt","Short-chain-enoyl-CoA hydratase","4.2.1.150","3D-structure, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","8655474, 11466286, 5057466","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,247,254,3,253,261]
[null,"P34559","_",0.86458,0.98031,30.12,{"v":3e-25,"d":"3.00E-25"},3,3,"ech-6","Probable enoyl-CoA hydratase, mitochondrial","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome","7906398, 9851916","Caenorhabditis elegans","Bristol N2 / Bristol N2",12,254,254,45,288,288]
[null,"O07137","_",1.01556,1.02756,28.74,{"v":1e-24,"d":"1.00E-24"},4,3,"echA8","Probable enoyl-CoA hydratase echA8","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome",11234002,"Mycobacterium leprae (strain TN)","TN",1,254,254,1,257,257]
[null,"Q8BH95","_",0.87931,1.00394,29.41,{"v":2e-24,"d":"2.00E-24"},5,3,"Echs1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Phosphoprotein, Reference proteome, Transit peptide","16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / C57BL/6J",9,253,254,44,289,290]
[null,"P30084","IPMed?",0.87586,1,29.13,{"v":3E-24,"d":"3.00E-24"},6,3,"ECHS1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Disease mutation, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Neurodegeneration, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","8012501, 9073515, 15164054, 15489334, 1286669, 11271497, 19608861, 21269460, 25125611, 24275569, 25393721, 25944712, 26000322, 26251176, 27221955, 26741492","Homo sapiens","_",9,254,254,44,290,290]
[null,"Q58DM8","_",0.87586,1,27.95,{"v":4e-24,"d":"4.00E-24"},7,3,"ECHS1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","Acetylation, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide",16305752,"Bos taurus","_",9,254,254,44,290,290]
[null,"P14604","IPMed?",0.87931,1.00394,29.41,{"v":1e-23,"d":"1.00E-23"},8,3,"Echs1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide","2806264, 15489334, 7883013, 8895557, 9480773, 11851409, 12445775","Rattus norvegicus","_",9,253,254,44,289,290]
[null,"P76082","IPMed?",0.96863,0.97244,29.96,{"v":4e-23,"d":"4.00E-23"},9,3,"paaF","2,3-dehydroadipyl-CoA hydratase","4.2.1.17","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","9748275, 9097039, 9278503, 16738553, 10766858, 12846838, 20660314","Escherichia coli (strain K12)","W / ATCC 11105 / DSM 1900 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",12,254,254,12,255,255]
[null,"A4YI89","IPMed?",0.96139,0.98031,31.73,{"v":5e-23,"d":"5.00E-23"},10,3,"_","3-hydroxypropionyl-coenzyme A dehydratase","4.2.1.116","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","18083856, 19429610","Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)","ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2",15,254,254,17,259,259]
[null,"Q0AVM1","IPMed?",0.98462,1.00787,28.12,{"v":5e-23,"d":"5.00E-23"},11,3,"_","Crotonyl-CoA hydratase","4.2.1.150","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",4,254,254,6,260,260]
[null,"Q4WF54","IPMed?",0.92593,0.98425,30,{"v":1E-22,"d":"1.00E-22"},12,3,"sidH","Mevalonyl-coenzyme A hydratase sidH","4.2.1.-","Complete proteome, Isomerase, Lyase, Peroxisome, Reference proteome","16372009, 15504822, 16113265, 17845073, 18721228, 21622789, 22106303, 23617799","Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)","ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100",11,251,254,20,265,270]
[null,"G4V4T7","IPMed?",0.96226,1.00394,30.59,{"v":6e-22,"d":"6.00E-22"},13,3,"dpgD","Enoyl-CoA-hydratase","4.2.1.17","Antibiotic biosynthesis, Lyase",11752437,"Amycolatopsis orientalis","NRRL18098",4,249,254,6,260,265]
[null,"O34893","IPMed?",0.95385,0.97638,32.66,{"v":4e-21,"d":"4.00E-21"},14,3,"yngF","Putative enoyl-CoA hydratase/isomerase YngF","_","Complete proteome, Lyase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",9,251,254,11,257,260]
[null,"P77467","IPMed?",1.01908,1.05118,29.96,{"v":7e-21,"d":"7.00E-21"},15,3,"paaG","1,2-epoxyphenylacetyl-CoA isomerase","5.3.3.18","3D-structure, Complete proteome, Isomerase, Lyase, Reference proteome","9748275, 9097039, 9278503, 16738553, 10766858, 12846838, 20660314","Escherichia coli (strain K12)","W / ATCC 11105 / DSM 1900 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",1,254,254,2,262,262]
[]
["CLOSTRIBL3_v1_20109","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q2RQ36","IPMed?",0.92361,0.96377,43.61,{"v":1e-29,"d":"1.00E-29"},1,1,"phaJ","(R)-specific enoyl-CoA hydratase","4.2.1.119","Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","10709984, 21886856","Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)","S1 / ATCC 25903 / S1H / ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1",7,138,138,12,143,144]
[null,"C5AZ74","IPMed?",0.89172,1.01449,43.57,{"v":1e-28,"d":"1.00E-28"},2,1,"croR","3-hydroxybutyryl-CoA dehydratase","4.2.1.55","Complete proteome, Lyase, Reference proteome","11872727, 19440302","Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)","ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1 / ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1",1,138,138,5,142,157]
[null,"O32472","IPMed?",0.97101,1,37.31,{"v":1e-23,"d":"1.00E-23"},3,1,"phaJ","(R)-specific enoyl-CoA hydratase","4.2.1.119","3D-structure, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase","9244271, 9457873, 12409309","Aeromonas caviae","FA440 / FA440",4,136,138,1,134,134]
[null,"P86397","IPMed?",0.77381,0.94203,38.46,{"v":2e-21,"d":"2.00E-21"},4,1,"HTD2","Hydroxyacyl-thioester dehydratase type 2, mitochondrial","4.2.1.-","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide","17898086, 16641997","Homo sapiens","_",9,136,138,36,163,168]
[null,"P77455","IPMed?",0.20705,1.02174,27.66,0.0003,5,1,"paaZ","2-oxepin-2(3H)-ylideneacetyl-CoA hydrolase / 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase","3.3.2.12, 1.2.1.91","Complete proteome, Hydrolase, Lyase, Multifunctional enzyme, NADP, Oxidoreductase, Reference proteome","9748275, 9097039, 9278503, 16738553, 10766858, 20660314, 21296885","Escherichia coli (strain K12)","W / ATCC 11105 / DSM 1900 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",1,123,138,514,647,681]
[null,"P49251","IPMed?",0.35224,0.85507,29.66,1E-3,6,1,"maoC","Protein MaoC","_","_",1556068,"Klebsiella aerogenes","W70",1,100,138,181,295,335]
[null,"Q54XZ0","IPMed?",0.42857,0.91304,27.78,0.004,7,1,"mfeB","Probable enoyl-CoA hydratase 2","4.2.1.119","Complete proteome, Lyase, Peroxisome, Reference proteome","15875012, 12796309","Dictyostelium discoideum","AX4 / AX4",15,138,138,170,290,294]
[null,"Q9VXJ0","IPMed?",0.18395,0.7971,24.55,0.012,8,8,"Mfe2","(3R)-hydroxyacyl-CoA dehydrogenase / Enoyl-CoA hydratase 2","4.2.1.119","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Multifunctional enzyme, NAD, Oxidoreductase, Peroxisome, Reference proteome","10731132, 12537572, 12537569, 21320074","Drosophila melanogaster","Berkeley / Berkeley / Berkeley",22,129,138,483,586,598]
[null,"Q02207","IPMed?",0.09111,0.5942,32.93,0.017,9,9,"FOX2","2-enoyl-CoA hydratase / (3R)-3-hydroxyacyl-CoA dehydrogenase","4.2.1.119","Complete proteome, Fatty acid metabolism, Isomerase, Lipid metabolism, Lyase, Multifunctional enzyme, NAD, Oxidoreductase, Peroxisome, Reference proteome, Repeat","1551874, 1441752, 8196765, 24374639","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 204508 / S288c",19,99,138,787,864,900]
[null,"Q8VYI3","IPMed?",0.22977,0.51449,30.99,0.32,10,1,"ECH2","Enoyl-CoA hydratase 2, peroxisomal","4.2.1.119","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Oxidoreductase, Peroxisome, Reference proteome","11130712, 27862469, 14593172, 16982622, 17951448","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia",32,100,138,205,275,309]
[]
["CLOSTRIBL3_v1_20308","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P52046","IPMed?",1,1.00772,75.1,{"v":4e-135,"d":"4.00E-135"},1,1,"crt","Short-chain-enoyl-CoA hydratase","4.2.1.150","3D-structure, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","8655474, 11466286, 5057466","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,259,259,1,261,261]
[null,"Q0AVM1","IPMed?",1,1.00386,65.38,{"v":3e-114,"d":"3.00E-114"},2,1,"_","Crotonyl-CoA hydratase","4.2.1.150","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",1,259,259,1,260,260]
[null,"A4YI89","IPMed?",1,1,47.88,{"v":1e-80,"d":"1.00E-80"},3,1,"_","3-hydroxypropionyl-coenzyme A dehydratase","4.2.1.116","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","18083856, 19429610","Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)","ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2",1,259,259,1,259,259]
[null,"Q52995","IPMed?",1,1.00778,47.49,{"v":5e-76,"d":"5.00E-76"},4,1,"fadB1","Probable enoyl-CoA hydratase","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","7751302, 11481430, 11474104","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",1,259,259,1,257,257]
[null,"P9WNN8","_",1,1.00778,44.4,{"v":5E-71,"d":"5.00E-71"},5,1,"echA8","Probable enoyl-CoA hydratase echA8","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",1,259,259,1,257,257]
[null,"P64017","_",1,1.00778,44.4,{"v":5E-71,"d":"5.00E-71"},5,1,"echA8","Probable enoyl-CoA hydratase echA8","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase","12788972, 28385856","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97",1,259,259,1,257,257]
[null,"P9WNN9","_",1,1.00778,44.4,{"v":5E-71,"d":"5.00E-71"},5,1,"echA8","Probable enoyl-CoA hydratase echA8","4.2.1.17","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","9634230, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",1,259,259,1,257,257]
[null,"Q8BH95","_",0.9,1.00772,45.59,{"v":3e-69,"d":"3.00E-69"},6,1,"Echs1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Phosphoprotein, Reference proteome, Transit peptide","16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / C57BL/6J",3,258,259,33,289,290]
[null,"Q1ZXF1","_",0.90614,0.96911,46.61,{"v":4e-68,"d":"4.00E-68"},7,1,"echs1","Probable enoyl-CoA hydratase, mitochondrial","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide",15875012,"Dictyostelium discoideum","AX4",9,259,259,29,277,277]
[null,"P14604","IPMed?",0.9,1.00772,44.44,{"v":4e-67,"d":"4.00E-67"},8,1,"Echs1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide","2806264, 15489334, 7883013, 8895557, 9480773, 11851409, 12445775","Rattus norvegicus","_",3,258,259,33,289,290]
[null,"Q58DM8","_",0.9069,1.01544,43.73,{"v":2E-66,"d":"2.00E-66"},9,1,"ECHS1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","Acetylation, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide",16305752,"Bos taurus","_",3,259,259,33,290,290]
[null,"O07137","_",1.01158,1.01946,43.89,{"v":6e-66,"d":"6.00E-66"},10,1,"echA8","Probable enoyl-CoA hydratase echA8","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome",11234002,"Mycobacterium leprae (strain TN)","TN",1,259,259,1,257,257]
[null,"P30084","IPMed?",0.90345,1.01158,44.27,{"v":8e-66,"d":"8.00E-66"},11,1,"ECHS1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Disease mutation, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Neurodegeneration, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","8012501, 9073515, 15164054, 15489334, 1286669, 11271497, 19608861, 21269460, 25125611, 24275569, 25393721, 25944712, 26000322, 26251176, 27221955, 26741492","Homo sapiens","_",3,259,259,33,290,290]
[null,"O34893","IPMed?",0.96923,0.97297,46.03,{"v":3E-65,"d":"3.00E-65"},12,1,"yngF","Putative enoyl-CoA hydratase/isomerase YngF","_","Complete proteome, Lyase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",10,257,259,10,258,260]
[null,"P45361","IPMed?",0.59846,1,67.74,{"v":1e-63,"d":"1.00E-63"},13,1,"crt","Short-chain-enoyl-CoA hydratase","4.2.1.150","Fatty acid metabolism, Lipid metabolism, Lyase",8001771,"Clostridioides difficile","E",94,248,259,1,154,155]
[null,"P76082","IPMed?",0.98069,0.99608,38.19,{"v":3e-58,"d":"3.00E-58"},14,1,"paaF","2,3-dehydroadipyl-CoA hydratase","4.2.1.17","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","9748275, 9097039, 9278503, 16738553, 10766858, 12846838, 20660314","Escherichia coli (strain K12)","W / ATCC 11105 / DSM 1900 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",6,259,259,4,255,255]
[null,"P94549","IPMed?",0.96911,0.97287,42.63,{"v":2e-54,"d":"2.00E-54"},15,1,"fadB","Probable enoyl-CoA hydratase","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid degradation, Lipid metabolism, Lyase, Reference proteome","8969504, 9384377, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",14,259,259,12,258,258]
[]
["CLOSTRIBL3_v1_12502","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P52042","IPMed?",0.5937,0.99472,58.36,{"v":6e-145,"d":"6.00E-145"},1,2,"bcd","Acyl-CoA dehydrogenase, short-chain specific","1.3.8.1","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,377,635,1,377,379]
[null,"P45857","IPMed?",0.58898,0.98681,55.35,{"v":3e-140,"d":"3.00E-140"},2,1,"mmgC","Acyl-CoA dehydrogenase","1.3.99.-","3D-structure, Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",6,379,635,4,377,379]
[null,"P45867","IPMed?",0.58898,0.98681,56.68,{"v":4E-136,"d":"4.00E-136"},3,2,"acdA","Acyl-CoA dehydrogenase","1.3.99.-","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid degradation, Lipid metabolism, Oxidoreductase, Reference proteome","9353933, 9384377, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",1,374,635,1,374,379]
[null,"Q06319","IPMed?",0.59213,0.98172,52.66,{"v":6e-125,"d":"6.00E-125"},4,2,"_","Acyl-CoA dehydrogenase, short-chain specific","1.3.8.1","3D-structure, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Oxidoreductase","8399220, 7857927","Megasphaera elsdenii","_",1,372,635,1,376,383]
[null,"Q3ZBF6","IPMed?",0.58583,0.90291,50.54,{"v":2e-117,"d":"2.00E-117"},5,2,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide",6712627,"Bos taurus","_",7,378,635,36,407,412]
[null,"Q5RAS0","_",0.58583,0.90291,51.08,{"v":2E-116,"d":"2.00E-116"},6,2,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","_","Pongo abelii","_",7,378,635,36,407,412]
[null,"O34421","IPMed?",0.59685,0.99737,50.92,{"v":2E-116,"d":"2.00E-116"},7,2,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,378,635,1,379,380]
[null,"P16219","IPMed?",0.58583,0.90291,50.81,{"v":1e-115,"d":"1.00E-115"},8,2,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Disease mutation, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","2565344, 9383286, 15489334, 1286669, 21269460, 21237683, 24275569, 25944712, 1692038, 9499414, 11134486","Homo sapiens","_",7,378,635,36,407,412]
[null,"Q07417","IPMed?",0.58583,0.90291,50.27,{"v":1e-115,"d":"1.00E-115"},9,2,"Acads","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","8276399, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / FVB/N",7,378,635,36,407,412]
[null,"P15651","IPMed?",0.58583,0.90291,50.27,{"v":2e-115,"d":"2.00E-115"},10,2,"Acads","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","2777793, 3968063, 11812788","Rattus norvegicus","_",7,378,635,36,407,412]
[null,"G3KIM8","IPMed?",0.59843,0.96447,50.79,{"v":4e-113,"d":"4.00E-113"},11,2,"acrC","Acryloyl-CoA reductase (NADH)","1.3.1.95","Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",1,378,635,14,392,394]
[]
["CLOSTRIBL3_v1_11587","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P52042","IPMed?",1,1,53.03,{"v":7E-139,"d":"7.00E-139"},1,3,"bcd","Acyl-CoA dehydrogenase, short-chain specific","1.3.8.1","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,379,379,1,379,379]
[null,"Q06319","IPMed?",1,1.01055,50.91,{"v":1e-124,"d":"1.00E-124"},2,3,"_","Acyl-CoA dehydrogenase, short-chain specific","1.3.8.1","3D-structure, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Oxidoreductase","8399220, 7857927","Megasphaera elsdenii","_",1,379,379,1,383,383]
[null,"P45867","IPMed?",0.98681,0.98681,49.73,{"v":4e-124,"d":"4.00E-124"},3,3,"acdA","Acyl-CoA dehydrogenase","1.3.99.-","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid degradation, Lipid metabolism, Oxidoreductase, Reference proteome","9353933, 9384377, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",1,374,379,1,374,379]
[null,"P45857","IPMed?",0.97625,0.97625,45.95,{"v":1e-113,"d":"1.00E-113"},4,3,"mmgC","Acyl-CoA dehydrogenase","1.3.99.-","3D-structure, Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",5,374,379,3,372,379]
[null,"O34421","IPMed?",1,1.00264,44.21,{"v":2e-111,"d":"2.00E-111"},5,3,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,379,379,1,380,380]
[null,"G3KIM8","IPMed?",0.96701,1.00528,45.41,{"v":6e-105,"d":"6.00E-105"},6,3,"acrC","Acryloyl-CoA reductase (NADH)","1.3.1.95","Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",1,379,379,14,393,394]
[null,"H6LGM6","IPMed?",0.98945,0.98945,43.47,{"v":2e-104,"d":"2.00E-104"},7,4,"carC","Caffeyl-CoA reductase-Etf complex subunit CarC","1.3.1.108","3D-structure, Complete proteome, Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",6,379,379,4,378,379]
[null,"P15651","IPMed?",0.91262,0.99208,42.02,{"v":4e-104,"d":"4.00E-104"},8,3,"Acads","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","2777793, 3968063, 11812788","Rattus norvegicus","_",4,379,379,33,408,412]
[null,"Q07417","IPMed?",0.91262,0.99208,42.02,{"v":4e-104,"d":"4.00E-104"},8,3,"Acads","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","8276399, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / FVB/N",4,379,379,33,408,412]
[null,"Q5RAS0","_",0.91262,0.99208,42.29,{"v":3E-103,"d":"3.00E-103"},9,3,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","_","Pongo abelii","_",4,379,379,33,408,412]
[null,"Q3ZBF6","IPMed?",0.91262,0.99208,42.55,{"v":7e-103,"d":"7.00E-103"},10,3,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide",6712627,"Bos taurus","_",4,379,379,33,408,412]
[null,"P16219","IPMed?",0.91262,0.99208,42.02,{"v":3E-102,"d":"3.00E-102"},11,3,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Disease mutation, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","2565344, 9383286, 15489334, 1286669, 21269460, 21237683, 24275569, 25944712, 1692038, 9499414, 11134486","Homo sapiens","_",4,379,379,33,408,412]
[]
["CLOSTRIBL3_v1_12012","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"H6LGM6","IPMed?",0.99211,0.99472,45.09,{"v":7e-97,"d":"7.00E-97"},1,5,"carC","Caffeyl-CoA reductase-Etf complex subunit CarC","1.3.1.108","3D-structure, Complete proteome, Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",4,375,380,1,376,379]
[null,"P45857","IPMed?",0.97895,0.98153,41.4,{"v":2e-94,"d":"2.00E-94"},2,5,"mmgC","Acyl-CoA dehydrogenase","1.3.99.-","3D-structure, Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",6,375,380,4,375,379]
[null,"P45867","IPMed?",0.99474,0.99736,42.86,{"v":2e-94,"d":"2.00E-94"},3,5,"acdA","Acyl-CoA dehydrogenase","1.3.99.-","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid degradation, Lipid metabolism, Oxidoreductase, Reference proteome","9353933, 9384377, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",1,375,380,1,377,379]
[null,"P63428","_",0.95887,0.98158,42.09,{"v":3e-93,"d":"3.00E-93"},4,3,"fadE25","Probable acyl-CoA dehydrogenase fadE25","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase","12788972, 28385856","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97",7,377,380,17,389,389]
[null,"P9WQG1","_",0.95887,0.98158,42.09,{"v":3e-93,"d":"3.00E-93"},4,3,"fadE25","Probable acyl-CoA dehydrogenase fadE25","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9634230, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",7,377,380,17,389,389]
[null,"P9WQG0","_",0.95887,0.98158,42.09,{"v":3e-93,"d":"3.00E-93"},4,3,"fadE25","Probable acyl-CoA dehydrogenase fadE25","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",7,377,380,17,389,389]
[null,"Q2LQN9","IPMed?",0.89372,0.97368,41.89,{"v":5e-93,"d":"5.00E-93"},5,2,"_","Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase","1.3.8.10","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome",23667239,"Syntrophus aciditrophicus (strain SB)","_",6,369,380,38,404,414]
[null,"Q06319","IPMed?",1.00783,1.01579,42.75,{"v":1E-91,"d":"1.00E-91"},6,4,"_","Acyl-CoA dehydrogenase, short-chain specific","1.3.8.1","3D-structure, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Oxidoreductase","8399220, 7857927","Megasphaera elsdenii","_",1,377,380,1,383,383]
[null,"P52042","IPMed?",1,1.00264,41.32,{"v":5E-91,"d":"5.00E-91"},7,5,"bcd","Acyl-CoA dehydrogenase, short-chain specific","1.3.8.1","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,377,380,1,379,379]
[null,"P45952","IPMed?",0.90024,0.99737,42.48,{"v":1e-90,"d":"1.00E-90"},8,1,"Acadm","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","7829081, 1438358, 21183079, 23806337, 23576753","Mus musculus","BALB/cJ",6,380,380,42,420,421]
[null,"P46703","_",0.95887,0.98158,41.02,{"v":1e-90,"d":"1.00E-90"},9,3,"fadE25","Probable acyl-CoA dehydrogenase fadE25","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","7489918, 11234002","Mycobacterium leprae (strain TN)","TN",7,377,380,17,389,389]
[null,"Q22347","IPMed?",0.89688,0.98421,42.25,{"v":8E-90,"d":"8.00E-90"},10,1,"acdh-10","Probable medium-chain specific acyl-CoA dehydrogenase 10, mitochondrial","1.3.8.7","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Reference proteome, Transit peptide","9851916, 18522834","Caenorhabditis elegans","Bristol N2",6,375,380,32,405,417]
[null,"G3KIM8","IPMed?",0.95178,0.98684,42.13,{"v":2e-89,"d":"2.00E-89"},11,5,"acrC","Acryloyl-CoA reductase (NADH)","1.3.1.95","Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",1,372,380,14,388,394]
[null,"P08503","IPMed?",0.90024,0.99737,41.42,{"v":4e-89,"d":"4.00E-89"},12,2,"Acadm","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","Acetylation, Complete proteome, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","3611054, 2029527","Rattus norvegicus","_",6,380,380,42,420,421]
[]
["CLOSTRIBL3_v1_12013","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P45857","IPMed?",0.95619,0.97889,32.35,{"v":8e-50,"d":"8.00E-50"},1,6,"mmgC","Acyl-CoA dehydrogenase","1.3.99.-","3D-structure, Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",14,381,388,12,376,379]
[null,"Q5RAS0","_",0.90291,0.95876,32.26,{"v":6e-48,"d":"6.00E-48"},2,6,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","_","Pongo abelii","_",13,383,388,42,409,412]
[null,"O34421","IPMed?",0.95103,0.97105,31.71,{"v":9e-48,"d":"9.00E-48"},3,6,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",14,381,388,14,379,380]
[null,"P16219","IPMed?",0.90291,0.95876,32.26,{"v":1e-47,"d":"1.00E-47"},4,6,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Disease mutation, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","2565344, 9383286, 15489334, 1286669, 21269460, 21237683, 24275569, 25944712, 1692038, 9499414, 11134486","Homo sapiens","_",13,383,388,42,409,412]
[null,"Q3ZBF6","IPMed?",0.8932,0.94845,31.79,{"v":1E-46,"d":"1.00E-46"},5,6,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide",6712627,"Bos taurus","_",17,383,388,46,409,412]
[null,"G3KIM8","IPMed?",0.9467,0.96134,29.49,{"v":2E-46,"d":"2.00E-46"},6,6,"acrC","Acryloyl-CoA reductase (NADH)","1.3.1.95","Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",14,381,388,27,392,394]
[null,"H6LGM6","IPMed?",0.9768,1,31.13,{"v":8e-46,"d":"8.00E-46"},7,6,"carC","Caffeyl-CoA reductase-Etf complex subunit CarC","1.3.1.108","3D-structure, Complete proteome, Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",9,381,388,3,377,379]
[null,"P15651","IPMed?",0.8932,0.94845,31.25,{"v":4e-45,"d":"4.00E-45"},8,6,"Acads","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","2777793, 3968063, 11812788","Rattus norvegicus","_",17,383,388,46,409,412]
[null,"P63428","_",0.94602,0.94845,31.25,{"v":2e-44,"d":"2.00E-44"},10,6,"fadE25","Probable acyl-CoA dehydrogenase fadE25","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase","12788972, 28385856","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97",16,381,388,26,388,389]
[null,"P9WQG0","_",0.94602,0.94845,31.25,{"v":2e-44,"d":"2.00E-44"},10,6,"fadE25","Probable acyl-CoA dehydrogenase fadE25","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",16,381,388,26,388,389]
[null,"P9WQG1","_",0.94602,0.94845,31.25,{"v":2e-44,"d":"2.00E-44"},10,6,"fadE25","Probable acyl-CoA dehydrogenase fadE25","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9634230, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",16,381,388,26,388,389]
[null,"P45867","IPMed?",0.97938,1.00264,32.37,{"v":2e-44,"d":"2.00E-44"},9,6,"acdA","Acyl-CoA dehydrogenase","1.3.99.-","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid degradation, Lipid metabolism, Oxidoreductase, Reference proteome","9353933, 9384377, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",4,380,388,5,377,379]
[null,"Q07417","IPMed?",0.8932,0.94845,30.98,{"v":6e-44,"d":"6.00E-44"},11,6,"Acads","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","8276399, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / FVB/N",17,383,388,46,409,412]
[null,"Q2LQN9","IPMed?",0.93478,0.99742,31.52,{"v":8e-44,"d":"8.00E-44"},12,6,"_","Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase","1.3.8.10","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome",23667239,"Syntrophus aciditrophicus (strain SB)","_",1,381,388,34,411,414]
[]
["CLOSTRIBL3_v1_20310","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P52042","IPMed?",1,1,79.42,0,1,1,"bcd","Acyl-CoA dehydrogenase, short-chain specific","1.3.8.1","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,379,379,1,379,379]
[null,"P45867","IPMed?",0.98681,0.98681,58.29,{"v":3e-154,"d":"3.00E-154"},2,1,"acdA","Acyl-CoA dehydrogenase","1.3.99.-","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid degradation, Lipid metabolism, Oxidoreductase, Reference proteome","9353933, 9384377, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",1,374,379,1,374,379]
[null,"Q06319","IPMed?",1,1.01055,59.53,{"v":4e-152,"d":"4.00E-152"},3,1,"_","Acyl-CoA dehydrogenase, short-chain specific","1.3.8.1","3D-structure, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Oxidoreductase","8399220, 7857927","Megasphaera elsdenii","_",1,379,379,1,383,383]
[null,"G3KIM8","IPMed?",0.96701,1.00528,53.81,{"v":2e-138,"d":"2.00E-138"},4,1,"acrC","Acryloyl-CoA reductase (NADH)","1.3.1.95","Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",1,379,379,14,393,394]
[null,"P45857","IPMed?",0.97625,0.97625,52.16,{"v":6e-137,"d":"6.00E-137"},5,2,"mmgC","Acyl-CoA dehydrogenase","1.3.99.-","3D-structure, Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",5,374,379,3,372,379]
[null,"O34421","IPMed?",1,1.00264,52.11,{"v":5e-131,"d":"5.00E-131"},6,1,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,379,379,1,380,380]
[null,"Q07417","IPMed?",0.91019,0.98945,48.53,{"v":3e-123,"d":"3.00E-123"},7,1,"Acads","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","8276399, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / FVB/N",5,379,379,34,408,412]
[null,"P15651","IPMed?",0.91019,0.98945,48.27,{"v":5e-123,"d":"5.00E-123"},8,1,"Acads","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","2777793, 3968063, 11812788","Rattus norvegicus","_",5,379,379,34,408,412]
[null,"Q3ZBF6","IPMed?",0.91019,0.98945,48.53,{"v":4e-122,"d":"4.00E-122"},9,1,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide",6712627,"Bos taurus","_",5,379,379,34,408,412]
[null,"H6LGM6","IPMed?",0.98945,0.98945,47.73,{"v":9e-121,"d":"9.00E-121"},10,2,"carC","Caffeyl-CoA reductase-Etf complex subunit CarC","1.3.1.108","3D-structure, Complete proteome, Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",6,379,379,4,378,379]
[]
["CLOSTRIBL3_v1_20311","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P52040","IPMed?",1,1,71.81,{"v":3E-131,"d":"3.00E-131"},1,1,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,259,259,1,259,259]
[null,"P97089","_",1,1.00386,67.31,{"v":2E-113,"d":"2.00E-113"},2,1,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",1,259,259,1,260,260]
[null,"H6LGM7","IPMed?",1,1.01158,56.87,{"v":6e-93,"d":"6.00E-93"},3,2,"carD","Caffeyl-CoA reductase-Etf complex subunit CarD","1.3.1.108","3D-structure, Complete proteome, Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",1,259,259,1,262,262]
[null,"O85691","IPMed?",0.91111,0.94981,48.78,{"v":2e-72,"d":"2.00E-72"},4,3,"etfB","Electron transfer flavoprotein subunit beta","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,238,259,1,246,270]
[null,"G3KIM7","IPMed?",1.00375,1.03475,45.9,{"v":1e-66,"d":"1.00E-66"},5,2,"acrB","Acryloyl-CoA reductase electron transfer subunit gamma","_","Cytoplasm, Electron transport, Transport","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",1,259,259,1,267,267]
[null,"P53576","_",0.9573,1.03861,42.38,{"v":5e-64,"d":"5.00E-64"},6,3,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",1,257,259,1,269,281]
[null,"P26482","IPMed?",0.86477,0.93822,44.86,{"v":8e-63,"d":"8.00E-63"},7,3,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Reference proteome, Transport","1850088, 3216855","Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)","_",1,234,259,1,243,281]
[null,"P53577","IPMed?",0.84375,0.93822,43.21,{"v":4e-58,"d":"4.00E-58"},8,3,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Reference proteome, Transport","8599534, 11157954, 12597275","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","USDA 3I1b110 / USDA 110spc4 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110",1,234,259,1,243,288]
[null,"Q53210","_",0.82105,0.90347,44.02,{"v":2e-57,"d":"2.00E-57"},9,3,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Transport","8796346, 9163424, 19376903","Sinorhizobium fredii (strain NBRC 101917 / NGR234)","NBRC 101917 / NGR234 / NBRC 101917 / NGR234",1,225,259,1,234,285]
[null,"P09818","IPMed?",0.88014,0.99228,41.25,{"v":4e-57,"d":"4.00E-57"},10,2,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104, 6317191","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",1,244,259,1,257,292]
[null,"Q05559","IPMed?",0.83871,0.90347,43.16,{"v":7e-54,"d":"7.00E-54"},11,3,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport",8369342,"Rhizobium leguminosarum bv. phaseoli","_",1,225,259,1,232,279]
[null,"P64098","IPMed?",0.91729,0.94208,36.89,{"v":8e-43,"d":"8.00E-43"},12,1,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Transport","12788972, 28385856, 16006064","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97 / BCG / Pasteur",2,238,259,3,246,266]
[null,"Q68FU3","IPMed?",0.83784,0.85098,34.56,{"v":4e-31,"d":"4.00E-31"},13,1,"Etfb","Electron transfer flavoprotein subunit beta","_","Acetylation, Complete proteome, Electron transport, Methylation, Mitochondrion, Nucleotide-binding, Phosphoprotein, Reference proteome, Transport","15489334, 7334008","Rattus norvegicus","_",1,210,259,4,217,255]
[]
["CLOSTRIBL3_v1_20312","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P52039","IPMed?",0.99107,1,69.67,{"v":5E-166,"d":"5.00E-166"},1,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,331,333,1,333,336]
[null,"P53578","IPMed?",0.99401,0.997,66.87,{"v":1e-158,"d":"1.00E-158"},2,1,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Transport",7875566,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",1,332,333,1,330,334]
[null,"P71153","_",0.98799,0.99697,61.7,{"v":8e-144,"d":"8.00E-144"},3,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",5,333,333,3,330,330]
[null,"H6LGM8","IPMed?",0.83586,0.99399,56.5,{"v":3e-130,"d":"3.00E-130"},4,2,"carE","Caffeyl-CoA reductase-Etf complex subunit CarE","1.3.1.108","3D-structure, 4Fe-4S, Complete proteome, Cytoplasm, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",2,332,333,64,394,396]
[null,"O85692","IPMed?",0.99112,1.00601,57.01,{"v":3e-125,"d":"3.00E-125"},5,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,333,333,1,335,338]
[null,"G3KIM6","IPMed?",0.97003,1.06907,51.4,{"v":2e-115,"d":"2.00E-115"},6,1,"acrA","Acryloyl-CoA reductase electron transfer subunit beta","_","Cytoplasm, Electron transport, Transport","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",2,330,333,7,362,367]
[null,"P26483","IPMed?",0.89431,0.99099,46.67,{"v":1E-91,"d":"1.00E-91"},7,2,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Reference proteome, Transport",1850088,"Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)","_",6,331,333,29,357,369]
[null,"P10449","IPMed?",0.89431,0.99099,46.06,{"v":6e-87,"d":"6.00E-87"},8,2,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Reference proteome, Transport","8599534, 11157954, 12597275, 2503674","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","USDA 3I1b110 / USDA 110spc4 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110 / USDA 110spc4",6,331,333,29,357,369]
[null,"P09819","IPMed?",0.92351,0.97898,45.09,{"v":3e-86,"d":"3.00E-86"},9,2,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",5,325,333,11,335,353]
[null,"Q53209","_",0.88076,0.97598,45.54,{"v":2E-85,"d":"2.00E-85"},10,2,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Plasmid, Transport","8796346, 9163424, 19376903","Sinorhizobium fredii (strain NBRC 101917 / NGR234)","NBRC 101917 / NGR234 / NBRC 101917 / NGR234",5,325,333,28,351,369]
[null,"Q0AZ33","IPMed?",0.96997,1.01893,43.03,{"v":3e-81,"d":"3.00E-81"},11,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Cytoplasm, Electron transport, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Reference proteome, Transport","21966920, 19648244, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",8,330,333,3,316,317]
[null,"P13803","IPMed?",0.98198,0.98198,37,{"v":5e-49,"d":"5.00E-49"},12,3,"Etfa","Electron transfer flavoprotein subunit alpha, mitochondrial","_","Acetylation, Complete proteome, Direct protein sequencing, Electron transport, FAD, Flavoprotein, Mitochondrion, Phosphoprotein, Reference proteome, Transit peptide, Transport","3415685, 15489334, 7334008, 22673903","Rattus norvegicus","_",6,330,333,19,331,333]
[]
["CLOSTRIBL3_v1_11710","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q0TMV4","IPMed?",0.99721,1.00281,52.1,{"v":1e-126,"d":"1.00E-126"},1,2,"buk","Butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Transferase","10585557, 16825665","Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)","ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 / Type A",1,355,358,1,355,356]
[null,"P0C2D8","_",0.99721,1.00281,52.38,{"v":2e-126,"d":"2.00E-126"},2,2,"buk","Butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",11792842,"Clostridium perfringens (strain 13 / Type A)","13 / Type A",1,355,358,1,355,356]
[null,"Q0SQK0","_",0.99721,1.00281,51.82,{"v":6e-126,"d":"6.00E-126"},3,2,"buk","Probable butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Transferase",16825665,"Clostridium perfringens (strain SM101 / Type A)","SM101 / Type A",1,355,358,1,355,356]
[null,"Q45829","IPMed?",0.99162,1,54.08,{"v":3e-123,"d":"3.00E-123"},4,2,"buk1","Butyrate kinase 1","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase","8244020, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",3,355,358,2,354,355]
[null,"Q890U0","_",0.99721,1.00281,52.38,{"v":9e-123,"d":"9.00E-123"},5,3,"buk","Butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",12552129,"Clostridium tetani (strain Massachusetts / E88)","Massachusetts / E88",1,355,358,1,355,356]
[null,"Q8R832","_",0.98603,0.9888,51.84,{"v":1e-122,"d":"1.00E-122"},6,3,"buk1","Probable butyrate kinase 1","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",11997336,"Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4)","DSM 15242 / JCM 11007 / NBRC 100824 / MB4",5,355,358,6,356,357]
[null,"Q97II1","IPMed?",0.99721,1.00281,50.98,{"v":7e-122,"d":"7.00E-122"},7,3,"buk2","Butyrate kinase 2","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase","11466286, 10937485","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,355,358,1,355,356]
[null,"B7IXF5","_",0.96458,0.98883,50.28,{"v":2E-119,"d":"2.00E-119"},8,3,"buk","Probable butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Transferase","_","Bacillus cereus (strain G9842)","_",4,355,358,5,356,367]
[null,"Q05619","IPMed?",0.99721,1.00563,49.58,{"v":2E-119,"d":"2.00E-119"},9,3,"buk","Butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",8396545,"Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052)","_",1,355,358,1,355,355]
[null,"B7HB35","_",0.96458,0.98883,49.72,{"v":7e-119,"d":"7.00E-119"},10,3,"buk","Probable butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Transferase","_","Bacillus cereus (strain B4264)","_",4,355,358,5,356,367]
[null,"Q9RPS7","IPMed?",0.98056,0.98603,45.33,{"v":4e-97,"d":"4.00E-97"},11,2,"buk","Probable butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase","10464218, 12663927","Enterococcus faecalis (strain ATCC 700802 / V583)","ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1 / ATCC 700802 / V583",5,355,358,4,352,360]
[null,"Q9WYB1","IPMed?",0.86104,0.96927,23.92,2e-10,12,2,"ackA","Acetate kinase","2.7.2.1","3D-structure, ATP-binding, Complete proteome, Cytoplasm, Direct protein sequencing, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","10360571, 10074080","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","ATCC 43589 / MSB8 / DSM 3109 / JCM 10099",4,311,358,2,339,403]
[null,"P74879","IPMed?",0.83168,0.93855,23.81,6E-10,13,2,"pduW","Probable propionate kinase","2.7.2.15","ATP-binding, Complete proteome, Kinase, Nucleotide-binding, Reference proteome, Transferase","10498708, 11677609","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / LT2 / SGSC1412 / ATCC 700720",1,304,358,1,331,404]
[null,"P38502","IPMed?",0.85784,0.97765,24.29,2e-09,15,4,"ackA","Acetate kinase","2.7.2.1","3D-structure, ATP-binding, Cytoplasm, Direct protein sequencing, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase","8226623, 2844814, 11562377, 15774882, 17999468, 11133963, 15647264","Methanosarcina thermophila","ATCC 43570 / DSM 1825 / OCM 12 / TM-1",4,318,358,2,343,408]
[null,"P77845","IPMed?",0.43073,0.47765,27.49,2e-09,14,3,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","10075432, 12743753, 12948626, 15090522, 16547043, 18355281","Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)","ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025",137,304,358,167,332,397]
[null,"P71104","IPMed?",0.84788,0.94972,25,2E-8,16,2,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","8702268, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",4,304,358,2,332,401]
[]
["CLOSTRIBL3_v1_11711","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P58255","_",0.98339,0.98339,42.23,{"v":2e-75,"d":"2.00E-75"},1,3,"ptb","Phosphate butyryltransferase","2.3.1.19","Acyltransferase, Complete proteome, Reference proteome, Transferase",11466286,"Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",2,297,301,1,295,301]
[null,"Q9X0L4","IPMed?",0.92359,0.94558,43.53,{"v":1e-74,"d":"1.00E-74"},2,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","10360571, 10074080","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","ATCC 43589 / MSB8 / DSM 3109 / JCM 10099",20,297,301,15,291,294]
[null,"Q05624","IPMed?",0.97351,0.97674,39.12,{"v":2E-66,"d":"2.00E-66"},3,3,"ptb","Phosphate butyryltransferase","2.3.1.19","Acyltransferase, Complete proteome, Reference proteome, Transferase",8396545,"Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052)","_",4,297,301,3,295,302]
[null,"P54530","_",0.93688,0.94314,41.49,{"v":4e-65,"d":"4.00E-65"},4,3,"yqiS","Probable phosphate butyryltransferase","2.3.1.19","Acyltransferase, Complete proteome, Reference proteome, Transferase","8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / JH642 / 168",18,299,301,14,293,299]
[null,"Q68XX7","_",0.84527,0.98007,37.97,{"v":8e-61,"d":"8.00E-61"},5,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",15317790,"Rickettsia typhi (strain ATCC VR-144 / Wilmington)","ATCC VR-144 / Wilmington",4,297,301,40,333,349]
[null,"Q9ZE39","_",0.84046,0.98007,37.97,{"v":2e-59,"d":"2.00E-59"},6,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",9823893,"Rickettsia prowazekii (strain Madrid E)","Madrid E",4,297,301,40,333,351]
[null,"Q4UNB1","_",0.84527,0.98007,37.29,{"v":3e-59,"d":"3.00E-59"},7,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",15984913,"Rickettsia felis (strain ATCC VR-1525 / URRWXCal2)","ATCC VR-1525 / URRWXCal2",4,297,301,40,333,349]
[null,"Q9X448","IPMed?",0.85127,0.89369,36.43,{"v":2e-58,"d":"2.00E-58"},8,3,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Cytoplasm, Transferase",10094701,"Rhizobium meliloti","104A14",29,297,301,34,302,316]
[null,"P57273","_",0.43785,1.0299,23.87,3e-14,9,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",10993077,"Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)","APS",17,297,301,399,704,708]
[null,"P45107","_",0.43601,1.0299,22.26,3e-12,10,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",19,297,301,403,706,711]
[null,"P71103","IPMed?",0.92492,1.02326,24.35,7e-12,11,3,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","8702268, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",17,288,301,13,317,333]
[null,"P38503","IPMed?",0.89489,0.99003,24.5,3E-10,12,3,"pta","Phosphate acetyltransferase","2.3.1.8","3D-structure, Acyltransferase, Cell membrane, Direct protein sequencing, Membrane, Transferase","8226623, 9401029, 15062079","Methanosarcina thermophila","ATCC 43570 / DSM 1825 / OCM 12 / TM-1",23,288,301,20,316,333]
[null,"P41790","IPMed?",0.89349,1.00332,22.85,7e-10,13,2,"eutD","Ethanolamine utilization protein EutD","_","Acyltransferase, Complete proteome, Reference proteome, Transferase","10464203, 11677609, 7868611","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / LT2 / SGSC1412 / ATCC 700720 / ATCC 14028s / SGSG 2262",27,298,301,22,320,338]
[null,"Q8ZND6","IPMed?",0.29832,0.70764,25.35,1e-09,14,3,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","11677609, 16272400, 17339319","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720 / LT2",89,297,301,500,706,714]
[null,"P0A9M8","IPMed?",0.29832,0.70764,24.88,6E-9,15,3,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","7883769, 7918659, 9205837, 9278503, 16738553, 2536666, 10542166, 15687190, 19852855, 20236319","Escherichia coli (strain K12)","K12 / KH131 / K12 / 1100 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12 / W3110 / ATCC 27325 / DSM 5911",89,297,301,501,707,714]
[null,"Q9I5A5","IPMed?",0.36648,0.85714,22.09,6e-08,16,3,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","10984043, 15231792","Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1",44,297,301,446,695,704]
[null,"P77844","IPMed?",0.99088,1.08306,21.78,3e-06,17,4,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","10075432, 12743753, 12948626, 15090522, 16179344, 16547043","Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)","ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025",2,297,301,5,322,329]
[]
["CLOSTRIBL3_v1_12016","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q05624","IPMed?",0.99669,1.00333,46.18,{"v":1e-82,"d":"1.00E-82"},1,2,"ptb","Phosphate butyryltransferase","2.3.1.19","Acyltransferase, Complete proteome, Reference proteome, Transferase",8396545,"Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052)","_",1,300,300,1,298,302]
[null,"P58255","_",1,1.00333,45.51,{"v":1e-82,"d":"1.00E-82"},2,2,"ptb","Phosphate butyryltransferase","2.3.1.19","Acyltransferase, Complete proteome, Reference proteome, Transferase",11466286,"Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,300,300,1,298,301]
[null,"P54530","_",0.92667,0.92977,42.09,{"v":3e-67,"d":"3.00E-67"},3,2,"yqiS","Probable phosphate butyryltransferase","2.3.1.19","Acyltransferase, Complete proteome, Reference proteome, Transferase","8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / JH642 / 168",19,296,300,14,290,299]
[null,"Q9X0L4","IPMed?",0.96667,0.98639,39.66,{"v":1e-64,"d":"1.00E-64"},4,3,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","10360571, 10074080","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","ATCC 43589 / MSB8 / DSM 3109 / JCM 10099",9,297,300,3,291,294]
[null,"Q68XX7","_",0.76791,0.89333,44.4,{"v":3e-61,"d":"3.00E-61"},5,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",15317790,"Rickettsia typhi (strain ATCC VR-144 / Wilmington)","ATCC VR-144 / Wilmington",39,299,300,73,335,349]
[null,"Q9ZE39","_",0.76353,0.89333,44.78,{"v":2e-60,"d":"2.00E-60"},6,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",9823893,"Rickettsia prowazekii (strain Madrid E)","Madrid E",39,299,300,73,335,351]
[null,"Q4UNB1","_",0.76791,0.89333,43.66,{"v":3e-60,"d":"3.00E-60"},7,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",15984913,"Rickettsia felis (strain ATCC VR-1525 / URRWXCal2)","ATCC VR-1525 / URRWXCal2",39,299,300,73,335,349]
[null,"Q9X448","IPMed?",0.9462,0.99667,40.13,{"v":4e-60,"d":"4.00E-60"},8,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Cytoplasm, Transferase",10094701,"Rhizobium meliloti","104A14",16,297,300,4,302,316]
[null,"P71103","IPMed?",0.96997,1.07667,30.03,{"v":8e-19,"d":"8.00E-19"},9,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","8702268, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",7,282,300,2,311,333]
[null,"Q59330","_",0.78963,0.86333,28.19,1E-14,10,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",27,275,300,55,304,328]
[null,"P0A9M8","IPMed?",0.36835,0.87667,23.95,3E-11,11,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","7883769, 7918659, 9205837, 9278503, 16738553, 2536666, 10542166, 15687190, 19852855, 20236319","Escherichia coli (strain K12)","K12 / KH131 / K12 / 1100 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12 / W3110 / ATCC 27325 / DSM 5911",43,297,300,450,707,714]
[null,"Q8ZND6","IPMed?",0.38235,0.91,24.18,1E-10,12,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","11677609, 16272400, 17339319","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720 / LT2",32,297,300,438,706,714]
[null,"P38503","IPMed?",0.84084,0.93333,24.64,2e-10,13,2,"pta","Phosphate acetyltransferase","2.3.1.8","3D-structure, Acyltransferase, Cell membrane, Direct protein sequencing, Membrane, Transferase","8226623, 9401029, 15062079","Methanosarcina thermophila","ATCC 43570 / DSM 1825 / OCM 12 / TM-1",9,256,300,5,283,333]
[null,"Q49112","IPMed?",1,1.07333,23.91,1E-8,14,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",8844861,"Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)","_",9,300,300,4,321,322]
[null,"P41790","IPMed?",0.6568,0.74,23.87,2E-8,15,3,"eutD","Ethanolamine utilization protein EutD","_","Acyltransferase, Complete proteome, Reference proteome, Transferase","10464203, 11677609, 7868611","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / LT2 / SGSC1412 / ATCC 700720 / ATCC 14028s / SGSG 2262",85,299,300,107,321,338]
[null,"Q9I5A5","IPMed?",0.31108,0.73,24.2,5e-08,16,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","10984043, 15231792","Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1",81,297,300,481,695,704]
[]
["CLOSTRIBL3_v1_12308","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P58255","_",0.99003,1,53.69,{"v":2E-100,"d":"2.00E-100"},1,1,"ptb","Phosphate butyryltransferase","2.3.1.19","Acyltransferase, Complete proteome, Reference proteome, Transferase",11466286,"Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,298,298,1,298,301]
[null,"Q05624","IPMed?",0.98675,1,52.01,{"v":4e-99,"d":"4.00E-99"},2,1,"ptb","Phosphate butyryltransferase","2.3.1.19","Acyltransferase, Complete proteome, Reference proteome, Transferase",8396545,"Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052)","_",1,298,298,1,298,302]
[null,"P54530","_",0.98662,0.98993,48.47,{"v":7e-84,"d":"7.00E-84"},3,1,"yqiS","Probable phosphate butyryltransferase","2.3.1.19","Acyltransferase, Complete proteome, Reference proteome, Transferase","8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / JH642 / 168",4,298,298,2,294,299]
[null,"Q9X0L4","IPMed?",0.97987,0.9932,44.18,{"v":4e-75,"d":"4.00E-75"},4,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","10360571, 10074080","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","ATCC 43589 / MSB8 / DSM 3109 / JCM 10099",5,296,298,3,292,294]
[null,"Q9X448","IPMed?",0.92722,0.98322,39.25,{"v":7e-64,"d":"7.00E-64"},5,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Cytoplasm, Transferase",10094701,"Rhizobium meliloti","104A14",4,296,298,11,303,316]
[null,"Q4UNB1","_",0.77937,0.91275,37.13,{"v":2e-54,"d":"2.00E-54"},6,3,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",15984913,"Rickettsia felis (strain ATCC VR-1525 / URRWXCal2)","ATCC VR-1525 / URRWXCal2",27,297,298,64,335,349]
[null,"Q9ZE39","_",0.77493,0.91275,37.13,{"v":1E-53,"d":"1.00E-53"},7,3,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",9823893,"Rickettsia prowazekii (strain Madrid E)","Madrid E",27,297,298,64,335,351]
[null,"Q68XX7","_",0.77937,0.91275,37.13,{"v":2e-53,"d":"2.00E-53"},8,3,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",15317790,"Rickettsia typhi (strain ATCC VR-144 / Wilmington)","ATCC VR-144 / Wilmington",27,297,298,64,335,349]
[null,"Q9ZKU4","_",0.57996,1.01007,25.91,3e-12,9,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",9923682,"Helicobacter pylori (strain J99 / ATCC 700824)","J99 / ATCC 700824",12,280,298,205,498,519]
[null,"P71103","IPMed?",0.97898,1.09396,22.7,2e-09,10,4,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","8702268, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",5,293,298,3,324,333]
[null,"P38503","IPMed?",0.98799,1.10403,24.01,3e-08,11,4,"pta","Phosphate acetyltransferase","2.3.1.8","3D-structure, Acyltransferase, Cell membrane, Direct protein sequencing, Membrane, Transferase","8226623, 9401029, 15062079","Methanosarcina thermophila","ATCC 43570 / DSM 1825 / OCM 12 / TM-1",1,296,298,1,326,333]
[null,"P77844","IPMed?",0.91185,1.00671,25,4e-07,12,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","10075432, 12743753, 12948626, 15090522, 16179344, 16547043","Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)","ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025",27,296,298,28,323,329]
[null,"Q8ZND6","IPMed?",0.45098,1.08054,22.05,6e-06,13,4,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","11677609, 16272400, 17339319","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720 / LT2",7,296,298,394,707,714]
[null,"P0A9M8","IPMed?",0.38515,0.92282,24.73,8e-06,14,4,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","7883769, 7918659, 9205837, 9278503, 16738553, 2536666, 10542166, 15687190, 19852855, 20236319","Escherichia coli (strain K12)","K12 / KH131 / K12 / 1100 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12 / W3110 / ATCC 27325 / DSM 5911",33,298,298,445,710,714]
[null,"O30807","IPMed?",0.42468,1.09732,23.85,1e-05,15,3,"dme","NAD-dependent malic enzyme","1.1.1.39","Allosteric enzyme, Complete proteome, Metal-binding, Multifunctional enzyme, NAD, Oxidoreductase, Reference proteome","9535928, 11481430, 11474104, 10407149","Rhizobium meliloti (strain 1021)","RCR2011 / SU47 / 1021 / 1021",12,298,298,450,766,770]
[null,"P41790","IPMed?",0.89645,1.01678,22.44,0.0002,16,4,"eutD","Ethanolamine utilization protein EutD","_","Acyltransferase, Complete proteome, Reference proteome, Transferase","10464203, 11677609, 7868611","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / LT2 / SGSC1412 / ATCC 700720 / ATCC 14028s / SGSG 2262",25,297,298,22,321,338]
[]
["CLOSTRIBL3_v1_20086","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q97II1","IPMed?",0.9723,0.98596,54.7,{"v":3E-132,"d":"3.00E-132"},1,1,"buk2","Butyrate kinase 2","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase","11466286, 10937485","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",5,354,361,5,355,356]
[null,"A7GSI3","_",0.96185,0.97784,55.52,{"v":5e-129,"d":"5.00E-129"},2,1,"buk","Probable butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",17434157,"Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98)","DSM 22905 / CIP 110041 / 391-98 / NVH 391-98",3,354,361,4,356,367]
[null,"Q8R828","_",0.96953,0.9887,53.43,{"v":6e-129,"d":"6.00E-129"},3,1,"buk2","Probable butyrate kinase 2","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",11997336,"Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4)","DSM 15242 / JCM 11007 / NBRC 100824 / MB4",5,354,361,4,353,354]
[null,"Q8R832","_",0.97507,0.98599,52.27,{"v":1E-127,"d":"1.00E-127"},4,2,"buk1","Probable butyrate kinase 1","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",11997336,"Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4)","DSM 15242 / JCM 11007 / NBRC 100824 / MB4",4,354,361,5,356,357]
[null,"P0C2D8","_",0.9723,0.98596,51,{"v":2e-126,"d":"2.00E-126"},6,3,"buk","Butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",11792842,"Clostridium perfringens (strain 13 / Type A)","13 / Type A",5,354,361,5,355,356]
[null,"Q0TMV4","IPMed?",0.9723,0.98596,51,{"v":2e-126,"d":"2.00E-126"},6,3,"buk","Butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Transferase","10585557, 16825665","Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)","ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 / Type A",5,354,361,5,355,356]
[null,"Q890U0","_",0.98338,0.99719,53.24,{"v":2e-126,"d":"2.00E-126"},5,2,"buk","Butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",12552129,"Clostridium tetani (strain Massachusetts / E88)","Massachusetts / E88",1,354,361,1,355,356]
[null,"Q0SQK0","_",0.9723,0.98596,50.71,{"v":1E-125,"d":"1.00E-125"},7,3,"buk","Probable butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Transferase",16825665,"Clostridium perfringens (strain SM101 / Type A)","SM101 / Type A",5,354,361,5,355,356]
[null,"B2UYH0","_",0.9723,0.98873,51,{"v":7E-125,"d":"7.00E-125"},8,2,"buk","Probable butyrate kinase","2.7.2.7","ATP-binding, Cytoplasm, Kinase, Nucleotide-binding, Transferase","_","Clostridium botulinum (strain Alaska E43 / Type E3)","_",5,354,361,5,355,355]
[null,"Q818T1","_",0.96185,0.97784,53.54,{"v":1e-124,"d":"1.00E-124"},9,1,"buk","Probable butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",12721630,"Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)","ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711",3,354,361,4,356,367]
[null,"B7IXF5","_",0.96185,0.97784,53.26,{"v":2e-124,"d":"2.00E-124"},10,1,"buk","Probable butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Transferase","_","Bacillus cereus (strain G9842)","_",3,354,361,4,356,367]
[null,"Q45829","IPMed?",0.9723,0.98873,52.42,{"v":4e-122,"d":"4.00E-122"},11,3,"buk1","Butyrate kinase 1","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase","8244020, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",5,354,361,4,354,355]
[null,"Q05619","IPMed?",0.9723,0.98873,50.14,{"v":9e-121,"d":"9.00E-121"},12,2,"buk","Butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",8396545,"Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052)","_",5,354,361,5,355,355]
[null,"Q9RPS7","IPMed?",0.97784,0.98056,45.89,{"v":2e-105,"d":"2.00E-105"},13,1,"buk","Probable butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase","10464218, 12663927","Enterococcus faecalis (strain ATCC 700802 / V583)","ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1 / ATCC 700802 / V583",5,356,361,4,354,360]
[null,"O06961","IPMed?",0.82587,0.91967,21.08,8e-11,14,3,"tdcD","Propionate kinase","2.7.2.15","3D-structure, ATP-binding, Complete proteome, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","10498722, 11677609, 16139298, 17894350","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / LT2 / SGSC1412 / ATCC 700720",4,311,361,6,333,402]
[null,"C9XHG0","IPMed?",0.82587,0.91967,21.08,8e-11,14,3,"tdcD","Propionate kinase","2.7.2.15","ATP-binding, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase",19901036,"Salmonella typhimurium (strain D23580)","D23580",4,311,361,6,333,402]
[null,"P38502","IPMed?",0.81618,0.92244,22.82,6E-10,15,3,"ackA","Acetate kinase","2.7.2.1","3D-structure, ATP-binding, Cytoplasm, Direct protein sequencing, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase","8226623, 2844814, 11562377, 15774882, 17999468, 11133963, 15647264","Methanosarcina thermophila","ATCC 43570 / DSM 1825 / OCM 12 / TM-1",5,305,361,3,332,408]
[null,"P11868","IPMed?",0.81841,0.91136,21.58,2e-09,17,3,"tdcD","Propionate kinase","2.7.2.15","ATP-binding, Complete proteome, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","9278503, 16738553, 2660107, 3053659, 8226682, 9484901","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / W3110 / ATCC 27325 / DSM 5911",4,305,361,6,327,402]
[null,"Q9WYB1","IPMed?",0.84864,0.94737,24.56,2e-09,16,3,"ackA","Acetate kinase","2.7.2.1","3D-structure, ATP-binding, Complete proteome, Cytoplasm, Direct protein sequencing, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","10360571, 10074080","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","ATCC 43589 / MSB8 / DSM 3109 / JCM 10099",5,312,361,3,339,403]
[null,"P37877","IPMed?",0.85063,0.93075,22.92,1E-8,18,3,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","8226682, 9387221, 9384377","Bacillus subtilis (strain 168)","168 / 168 / 168",5,310,361,4,335,395]
[]
["CLOSTRIBL3_v1_20087","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q890U0","_",0.99441,1,57.87,{"v":8e-145,"d":"8.00E-145"},1,1,"buk","Butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",12552129,"Clostridium tetani (strain Massachusetts / E88)","Massachusetts / E88",1,355,358,1,356,356]
[null,"Q0SQK0","_",0.99441,1,55.9,{"v":1e-138,"d":"1.00E-138"},2,1,"buk","Probable butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Transferase",16825665,"Clostridium perfringens (strain SM101 / Type A)","SM101 / Type A",1,355,358,1,356,356]
[null,"Q0TMV4","IPMed?",0.99441,1,55.62,{"v":7e-138,"d":"7.00E-138"},3,1,"buk","Butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Transferase","10585557, 16825665","Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)","ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 / Type A",1,355,358,1,356,356]
[null,"Q45829","IPMed?",0.98883,0.99718,55.65,{"v":9e-138,"d":"9.00E-138"},4,1,"buk1","Butyrate kinase 1","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase","8244020, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",3,355,358,2,355,355]
[null,"P0C2D8","_",0.99441,1,55.06,{"v":2E-136,"d":"2.00E-136"},5,1,"buk","Butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",11792842,"Clostridium perfringens (strain 13 / Type A)","13 / Type A",1,355,358,1,356,356]
[null,"Q05619","IPMed?",0.97765,0.98592,55.71,{"v":2E-136,"d":"2.00E-136"},6,1,"buk","Butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",8396545,"Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052)","_",1,350,358,1,350,355]
[null,"B2UYH0","_",0.97765,0.98592,56.29,{"v":3e-136,"d":"3.00E-136"},7,1,"buk","Probable butyrate kinase","2.7.2.7","ATP-binding, Cytoplasm, Kinase, Nucleotide-binding, Transferase","_","Clostridium botulinum (strain Alaska E43 / Type E3)","_",1,350,358,1,350,355]
[null,"B2TIN4","_",0.97765,0.98592,56,{"v":9e-136,"d":"9.00E-136"},8,1,"buk","Probable butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Transferase","_","Clostridium botulinum (strain Eklund 17B / Type B)","_",1,350,358,1,350,355]
[null,"Q8R832","_",0.96648,0.96919,53.76,{"v":2e-129,"d":"2.00E-129"},9,1,"buk1","Probable butyrate kinase 1","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",11997336,"Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4)","DSM 15242 / JCM 11007 / NBRC 100824 / MB4",5,350,358,6,351,357]
[null,"A7GSI3","_",0.96458,0.98883,54.52,{"v":2e-127,"d":"2.00E-127"},10,2,"buk","Probable butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase",17434157,"Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98)","DSM 22905 / CIP 110041 / 391-98 / NVH 391-98",4,356,358,5,358,367]
[null,"Q97II1","IPMed?",0.99441,1,52.53,{"v":1e-126,"d":"1.00E-126"},11,2,"buk2","Butyrate kinase 2","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase","11466286, 10937485","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,355,358,1,356,356]
[null,"Q9RPS7","IPMed?",0.96111,0.96648,42.2,{"v":2e-89,"d":"2.00E-89"},12,3,"buk","Probable butyrate kinase","2.7.2.7","ATP-binding, Complete proteome, Cytoplasm, Kinase, Nucleotide-binding, Reference proteome, Transferase","10464218, 12663927","Enterococcus faecalis (strain ATCC 700802 / V583)","ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1 / ATCC 700802 / V583",5,350,358,4,347,360]
[null,"O06961","IPMed?",0.4204,0.47207,26.63,2E-12,13,2,"tdcD","Propionate kinase","2.7.2.15","3D-structure, ATP-binding, Complete proteome, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","10498722, 11677609, 16139298, 17894350","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / LT2 / SGSC1412 / ATCC 700720",150,316,358,170,337,402]
[null,"C9XHG0","IPMed?",0.4204,0.47207,26.63,2E-12,13,2,"tdcD","Propionate kinase","2.7.2.15","ATP-binding, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase",19901036,"Salmonella typhimurium (strain D23580)","D23580",150,316,358,170,337,402]
[null,"P11868","IPMed?",0.4204,0.47207,25.44,1e-11,14,2,"tdcD","Propionate kinase","2.7.2.15","ATP-binding, Complete proteome, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","9278503, 16738553, 2660107, 3053659, 8226682, 9484901","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / W3110 / ATCC 27325 / DSM 5911",150,316,358,170,337,402]
[null,"P38502","IPMed?",0.41176,0.46927,27.98,2e-11,15,2,"ackA","Acetate kinase","2.7.2.1","3D-structure, ATP-binding, Cytoplasm, Direct protein sequencing, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase","8226623, 2844814, 11562377, 15774882, 17999468, 11133963, 15647264","Methanosarcina thermophila","ATCC 43570 / DSM 1825 / OCM 12 / TM-1",150,315,358,175,341,408]
[null,"P77845","IPMed?",0.42065,0.46648,26.35,3E-11,16,2,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","10075432, 12743753, 12948626, 15090522, 16547043, 18355281","Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)","ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025",150,315,358,176,341,397]
[null,"P37877","IPMed?",0.45316,0.5,29.61,4e-10,17,2,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","8226682, 9387221, 9384377","Bacillus subtilis (strain 168)","168 / 168 / 168",150,320,358,173,341,395]
[]
["CLOSTRIBL3_v1_13110","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"G2SYC0","_",0.98009,0.99327,49.89,{"v":6e-146,"d":"6.00E-146"},1,1,"_","Butyryl-CoA:acetate CoA-transferase","2.8.3.-","Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","16385128, 26543119","Roseburia hominis (strain DSM 16839 / NCIMB 14029 / A2-183)","DSM 16839 / NCIMB 14029 / A2-183 / DSM 16839 / NCIMB 14029 / A2-183",10,449,452,6,446,446]
[null,"Q0AVM5","IPMed?",0.98894,1,48.77,{"v":3e-140,"d":"3.00E-140"},2,1,"_","Probable butyrate:acetyl-CoA coenzyme A-transferase","2.8.3.-","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",6,450,452,4,446,447]
[null,"B0MC58","_",0.98009,0.99327,45.6,{"v":4e-135,"d":"4.00E-135"},3,1,"_","Butyryl-CoA:acetate CoA-transferase","2.8.3.-","Complete proteome, Fatty acid metabolism, Lipid metabolism, Transferase",16385128,"Anaerostipes caccae (strain DSM 14662 / NCIMB 13811 / L1-92)","DSM 14662 / NCIMB 13811 / L1-92",10,449,452,6,446,446]
[null,"P38942","IPMed?",0.95354,1.00466,38.28,{"v":8e-81,"d":"8.00E-81"},4,3,"cat2","4-hydroxybutyrate coenzyme A transferase","2.8.3.-","Complete proteome, Reference proteome, Transferase","18218779, 8550525","Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)","ATCC 8527 / DSM 555 / NCIMB 10680",11,440,452,7,427,429]
[null,"P38946","IPMed?",0.89963,1.0708,25.41,{"v":5e-18,"d":"5.00E-18"},5,4,"cat1","Succinyl-CoA:coenzyme A transferase","2.8.3.-","Complete proteome, Reference proteome, Transferase","8550525, 18218779","Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)","ATCC 8527 / DSM 555 / NCIMB 10680",12,439,452,52,507,538]
[null,"P83773","IPMed?",0.71183,0.82522,24.66,{"v":4e-17,"d":"4.00E-17"},6,2,"ACH1","Acetyl-CoA hydrolase","3.1.2.1","Complete proteome, Cytoplasm, Direct protein sequencing, Hydrolase, Reference proteome","15123810, 17419877, 24025428, 15378761","Candida albicans (strain SC5314 / ATCC MYA-2876)","SC5314 / ATCC MYA-2876 / SC5314 / ATCC MYA-2876 / SC5314 / ATCC MYA-2876 / SC5314 / ATCC MYA-2876",119,449,452,134,491,524]
[null,"Q6BKW1","_",0.72275,0.83628,24.34,5e-14,7,2,"ACH1","Acetyl-CoA hydrolase","3.1.2.1","Complete proteome, Cytoplasm, Hydrolase, Reference proteome",15229592,"Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968)","ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968",115,449,452,128,490,523]
[null,"B3EY95","IPMed?",0.94455,1.05531,23.27,2e-11,8,4,"_","Succinyl-CoA:acetate CoA-transferase","2.8.3.18","3D-structure, Transferase","18502856, 23030530","Acetobacter aceti","1023 / 1023 / 1023",12,434,452,11,466,505]
[null,"P52043","IPMed?",0.96748,1.0531,23.32,2e-11,9,4,"scpC","Propionyl-CoA:succinate CoA transferase","2.8.3.-","Complete proteome, Reference proteome, Transferase","9278503, 16738553, 10769117","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",16,439,452,8,463,492]
[null,"P32316","IPMed?",0.69202,0.80531,23.9,5e-11,10,3,"ACH1","Acetyl-CoA hydrolase","3.1.2.1","Acetylation, Complete proteome, Cytoplasm, Direct protein sequencing, Glycoprotein, Hydrolase, Phosphoprotein, Reference proteome","1970569, 1441754, 7813418, 24374639, 11502169, 14562106, 17761666, 22814378","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 201238 / W303-1B / ATCC 76625 / YPH499",123,440,452,140,484,526]
[null,"P15937","IPMed?",0.68,0.78982,22.13,5e-10,11,4,"acu-8","Acetyl-CoA hydrolase","3.1.2.1","Complete proteome, Cytoplasm, Hydrolase, Reference proteome","2140429, 12712197, 1357077","Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)","ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987",122,436,452,142,482,525]
[]
["CLOSTRIBL3_v1_11114","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P71153","_",0.81436,0.99697,43.47,{"v":7e-87,"d":"7.00E-87"},1,6,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",71,398,404,4,330,330]
[null,"H6LGM8","IPMed?",0.93069,0.94949,39.36,{"v":1e-86,"d":"1.00E-86"},2,5,"carE","Caffeyl-CoA reductase-Etf complex subunit CarE","1.3.1.108","3D-structure, 4Fe-4S, Complete proteome, Cytoplasm, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",23,394,404,20,391,396]
[null,"O85692","IPMed?",0.84158,1.00592,43.53,{"v":6e-85,"d":"6.00E-85"},3,5,"etfA","Electron transfer flavoprotein subunit alpha","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",66,400,404,1,337,338]
[null,"P53578","IPMed?",0.81436,0.98503,43.77,{"v":5e-82,"d":"5.00E-82"},4,6,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Transport",7875566,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",71,395,404,6,328,334]
[null,"P52039","IPMed?",0.83168,1,42.86,{"v":2e-81,"d":"2.00E-81"},5,6,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",66,396,404,1,333,336]
[null,"P26483","IPMed?",0.82178,0.89973,37.65,{"v":7e-73,"d":"7.00E-73"},6,6,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Reference proteome, Transport",1850088,"Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)","_",71,397,404,29,358,369]
[null,"P10449","IPMed?",0.81683,0.89431,37.58,{"v":1E-70,"d":"1.00E-70"},8,6,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Reference proteome, Transport","8599534, 11157954, 12597275, 2503674","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","USDA 3I1b110 / USDA 110spc4 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110 / USDA 110spc4",71,397,404,29,358,369]
[null,"P53574","_",0.82673,0.92778,38.62,{"v":1E-70,"d":"1.00E-70"},7,5,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",76,404,404,27,359,360]
[null,"Q53209","_",0.80446,0.88076,37.54,{"v":4e-69,"d":"4.00E-69"},9,6,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Plasmid, Transport","8796346, 9163424, 19376903","Sinorhizobium fredii (strain NBRC 101917 / NGR234)","NBRC 101917 / NGR234 / NBRC 101917 / NGR234",71,392,404,29,353,369]
[null,"P09819","IPMed?",0.80693,0.92351,36.81,{"v":2E-66,"d":"2.00E-66"},10,6,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",71,392,404,12,337,353]
[null,"G3KIM6","IPMed?",0.90347,0.99455,35.62,{"v":4e-66,"d":"4.00E-66"},11,5,"acrA","Acryloyl-CoA reductase electron transfer subunit beta","_","Cytoplasm, Electron transport, Transport","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",67,398,404,7,365,367]
[null,"Q0AZ33","IPMed?",0.80941,1.03155,30.58,{"v":3e-47,"d":"3.00E-47"},12,6,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Cytoplasm, Electron transport, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Reference proteome, Transport","21966920, 19648244, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",73,395,404,3,316,317]
[null,"Q9C6I6","IPMed?",0.83911,0.93388,30.38,{"v":4e-43,"d":"4.00E-43"},13,6,"ETFA","Electron transfer flavoprotein subunit alpha, mitochondrial","_","Complete proteome, Electron transport, FAD, Flavoprotein, Mitochondrion, Reference proteome, Transit peptide, Transport","11130712, 27862469, 14593172, 11910074, 14671022, 16923016, 25732537","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Landsberg erecta",76,398,404,39,363,363]
[]
["CLOSTRIBL3_v1_11115","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P52040","IPMed?",1,1.01158,46.18,{"v":1e-66,"d":"1.00E-66"},1,4,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,262,262,1,259,259]
[null,"P97089","_",0.98092,0.98846,47.08,{"v":4e-65,"d":"4.00E-65"},2,5,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",1,256,262,1,254,260]
[null,"H6LGM7","IPMed?",1.00763,1.00763,43.56,{"v":3e-60,"d":"3.00E-60"},3,5,"carD","Caffeyl-CoA reductase-Etf complex subunit CarD","1.3.1.108","3D-structure, Complete proteome, Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",1,262,262,1,262,262]
[null,"O85691","IPMed?",1.00741,1.03817,40.07,{"v":4e-58,"d":"4.00E-58"},4,5,"etfB","Electron transfer flavoprotein subunit beta","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,262,262,1,270,270]
[null,"P26482","IPMed?",0.86833,0.9313,42.21,{"v":8e-58,"d":"8.00E-58"},5,4,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Reference proteome, Transport","1850088, 3216855","Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)","_",1,238,262,1,244,281]
[null,"P53577","IPMed?",0.91319,1.00382,38.02,{"v":4e-53,"d":"4.00E-53"},6,4,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Reference proteome, Transport","8599534, 11157954, 12597275","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","USDA 3I1b110 / USDA 110spc4 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110",1,256,262,1,262,288]
[null,"Q53210","_",0.92281,1.00382,37.64,{"v":7e-52,"d":"7.00E-52"},7,5,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Transport","8796346, 9163424, 19376903","Sinorhizobium fredii (strain NBRC 101917 / NGR234)","NBRC 101917 / NGR234 / NBRC 101917 / NGR234",1,256,262,1,262,285]
[null,"P53576","_",0.94662,1.01527,36.09,{"v":5e-50,"d":"5.00E-50"},8,5,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",1,256,262,1,265,281]
[null,"G3KIM7","IPMed?",1.00749,1.02672,38.29,{"v":5e-47,"d":"5.00E-47"},9,5,"acrB","Acryloyl-CoA reductase electron transfer subunit gamma","_","Cytoplasm, Electron transport, Transport","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",1,258,262,1,263,267]
[null,"Q05559","IPMed?",0.94265,1.00382,36.5,{"v":7e-47,"d":"7.00E-47"},10,4,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport",8369342,"Rhizobium leguminosarum bv. phaseoli","_",1,256,262,1,260,279]
[null,"P09818","IPMed?",0.91096,1.01527,38.35,{"v":3e-46,"d":"3.00E-46"},11,5,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104, 6317191","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",1,252,262,1,262,292]
[null,"P64098","IPMed?",0.91729,0.9313,29.51,{"v":2e-26,"d":"2.00E-26"},12,6,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Transport","12788972, 28385856, 16006064","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97 / BCG / Pasteur",2,239,262,3,244,266]
[null,"Q0AZ34","IPMed?",0.82061,0.85317,30.7,{"v":1e-23,"d":"1.00E-23"},13,4,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Cytoplasm, Electron transport, Fatty acid metabolism, Lipid metabolism, Nucleotide-binding, Reference proteome, Transport","21966920, 19648244, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",1,212,262,3,210,252]
[]
["CLOSTRIBL3_v1_11486","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O29853","IPMed?",0.95329,1.01354,38.53,{"v":1e-102,"d":"1.00E-102"},1,1,"dld","D-lactate dehydrogenase (acceptor)","1.1.99.6","Cell membrane, Complete proteome, FAD, Flavoprotein, Membrane, Oxidoreductase, Reference proteome, Transmembrane, Transmembrane helix, Zinc","9389475, 10601217, 15803647","Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)","ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126",29,470,471,4,440,443]
[null,"P9WIT1","_",0.98301,1.00871,33.48,{"v":2e-81,"d":"2.00E-81"},2,3,"_","Uncharacterized FAD-linked oxidoreductase Rv2280","1.-.-.-","Complete proteome, FAD, Flavoprotein, Isopeptide bond, Oxidoreductase, Reference proteome, Ubl conjugation","9634230, 20066036, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",14,469,471,3,455,459]
[null,"P9WIT0","_",0.98301,1.00871,33.48,{"v":2e-81,"d":"2.00E-81"},2,3,"_","Uncharacterized FAD-linked oxidoreductase MT2338","1.-.-.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",14,469,471,3,455,459]
[null,"P94535","_",0.98089,0.98298,32.9,{"v":9e-72,"d":"9.00E-72"},3,5,"glcD","Glycolate oxidase subunit GlcD","_","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","8969504, 9384377","Bacillus subtilis (strain 168)","168 / 168",14,467,471,5,455,470]
[null,"Q94AX4","IPMed?",0.82363,0.99151,30.84,{"v":2e-58,"d":"2.00E-58"},4,4,"DLD","D-lactate dehydrogenase [cytochrome], mitochondrial","1.1.2.4","Complete proteome, FAD, Flavoprotein, Mitochondrion, Oxidoreductase, Reference proteome, Transit peptide","27862469, 14593172, 14966218, 19586914","Arabidopsis thaliana","cv. Columbia / cv. Columbia",14,470,471,109,561,567]
[null,"P0AEQ0","_",0.83768,0.88747,30.62,{"v":3E-57,"d":"3.00E-57"},5,4,"glcD","Glycolate oxidase subunit GlcD","_","Complete proteome, FAD, Flavoprotein, Oxidoreductase",12471157,"Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","CFT073 / ATCC 700928 / UPEC",56,467,471,58,469,499]
[null,"P0AEP9","IPMed?",0.83768,0.88747,30.62,{"v":3E-57,"d":"3.00E-57"},5,4,"glcD","Glycolate oxidase subunit GlcD","_","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","8606183, 9278503, 16738553","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",56,467,471,58,469,499]
[null,"Q7TNG8","IPMed?",0.96901,0.99575,27.51,{"v":3e-54,"d":"3.00E-54"},6,4,"Ldhd","Probable D-lactate dehydrogenase, mitochondrial","1.1.2.4","Acetylation, Complete proteome, FAD, Flavoprotein, Mitochondrion, Oxidoreductase, Reference proteome, Transit peptide","12127981, 15489334, 16141072, 21183079, 23806337, 23576753","Mus musculus","129/Sv / FVB/N / C57BL/6J",11,470,471,27,484,484]
[null,"P32891","IPMed?",0.81431,1.01486,30.13,{"v":6E-52,"d":"6.00E-52"},7,2,"DLD1","D-lactate dehydrogenase [cytochrome] 1, mitochondrial","1.1.2.4","Complete proteome, Direct protein sequencing, FAD, Flavoprotein, Membrane, Mitochondrion, Mitochondrion inner membrane, Oxidoreductase, Reference proteome, Transit peptide, Zinc","8492799, 9169867, 24374639, 11502169, 14562106","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 201238 / W303-1B",13,469,471,108,574,587]
[null,"P46681","IPMed?",0.83396,0.93843,31.45,{"v":5E-51,"d":"5.00E-51"},8,3,"DLD2","D-2-hydroxyglutarate--pyruvate transhydrogenase DLD2","1.1.99.40","Complete proteome, FAD, Flavoprotein, Mitochondrion, Oxidoreductase, Reference proteome, Transit peptide","9169867, 24374639, 17322287, 10509019, 14562106, 15158445, 26774271","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 201388 / BY4741",44,466,471,92,526,530]
[null,"Q12627","IPMed?",0.75694,0.92569,32.11,{"v":2E-50,"d":"2.00E-50"},9,2,"DLD1","D-lactate dehydrogenase [cytochrome], mitochondrial","1.1.2.4","Complete proteome, FAD, Flavoprotein, Mitochondrion, Oxidoreductase, Reference proteome, Transit peptide, Zinc","7969031, 15229592","Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)","ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37 / ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37",48,469,471,143,566,576]
[null,"Q86WU2","IPMed?",0.9783,1.05308,26.81,{"v":2e-49,"d":"2.00E-49"},10,4,"LDHD","Probable D-lactate dehydrogenase, mitochondrial","1.1.2.4","Acetylation, Alternative splicing, Complete proteome, Disease mutation, FAD, Flavoprotein, Mitochondrion, Oxidoreductase, Polymorphism, Reference proteome, Transit peptide","12127981, 15489334, 24275569, 30931947","Homo sapiens","_",14,470,471,30,507,507]
[null,"P39976","IPMed?",0.96573,1.01699,30.27,{"v":2e-49,"d":"2.00E-49"},11,2,"DLD3","D-2-hydroxyglutarate--pyruvate transhydrogenase DLD3","1.1.99.40","Complete proteome, Cytoplasm, FAD, Flavoprotein, Isopeptide bond, Oxidoreductase, Reference proteome, Ubl conjugation","9169868, 24374639, 10509019, 14562106, 12872131, 18407956, 22814378, 26774271","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c / SUB592 / ATCC 201388 / BY4741",11,466,471,27,492,496]
[null,"O23240","IPMed?",0.87299,1.03609,27.87,{"v":1E-46,"d":"1.00E-46"},12,4,"D2HGDH","D-2-hydroxyglutarate dehydrogenase, mitochondrial","1.1.99.39","Complete proteome, FAD, Flavoprotein, Mitochondrion, Oxidoreductase, Reference proteome, Transit peptide","9461215, 10617198, 27862469, 14593172, 19586914, 20501910, 21296880, 25732537","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia",10,470,471,94,552,559]
[]
["CLOSTRIBL3_v1_11487","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P71153","_",0.98485,0.99085,49.54,{"v":1e-94,"d":"1.00E-94"},1,5,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",4,323,328,3,327,330]
[null,"H6LGM8","IPMed?",0.81818,0.9878,47.22,{"v":2E-85,"d":"2.00E-85"},2,6,"carE","Caffeyl-CoA reductase-Etf complex subunit CarE","1.3.1.108","3D-structure, 4Fe-4S, Complete proteome, Cytoplasm, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",5,322,328,68,391,396]
[null,"P52039","IPMed?",0.97917,1.00305,44.68,{"v":1E-83,"d":"1.00E-83"},3,5,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",4,323,328,5,332,336]
[null,"P53578","IPMed?",0.97305,0.99085,44.62,{"v":2e-82,"d":"2.00E-82"},4,5,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Transport",7875566,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",4,323,328,5,328,334]
[null,"O85692","IPMed?",0.98225,1.0122,46.69,{"v":5E-80,"d":"5.00E-80"},5,6,"etfA","Electron transfer flavoprotein subunit alpha","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",4,325,328,5,334,338]
[null,"P26483","IPMed?",0.89431,1.0061,41.21,{"v":2e-75,"d":"2.00E-75"},6,4,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Reference proteome, Transport",1850088,"Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)","_",3,323,328,27,356,369]
[null,"Q53209","_",0.88618,0.99695,40.98,{"v":5E-74,"d":"5.00E-74"},7,5,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Plasmid, Transport","8796346, 9163424, 19376903","Sinorhizobium fredii (strain NBRC 101917 / NGR234)","NBRC 101917 / NGR234 / NBRC 101917 / NGR234",3,320,328,27,353,369]
[null,"P10449","IPMed?",0.88076,0.99085,40.92,{"v":7e-71,"d":"7.00E-71"},8,5,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Reference proteome, Transport","8599534, 11157954, 12597275, 2503674","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","USDA 3I1b110 / USDA 110spc4 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110 / USDA 110spc4",3,318,328,27,351,369]
[null,"P09819","IPMed?",0.92918,1,40.24,{"v":1e-69,"d":"1.00E-69"},9,5,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",3,320,328,10,337,353]
[null,"P53574","_",0.91944,1.00915,38.67,{"v":6E-65,"d":"6.00E-65"},10,6,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",4,323,328,21,350,360]
[null,"G3KIM6","IPMed?",0.97275,1.08841,38.66,{"v":6e-63,"d":"6.00E-63"},11,6,"acrA","Acryloyl-CoA reductase electron transfer subunit beta","_","Cytoplasm, Electron transport, Transport","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",5,323,328,11,362,367]
[null,"Q0AZ33","IPMed?",0.98171,1.01577,36.34,{"v":3e-62,"d":"3.00E-62"},12,4,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Cytoplasm, Electron transport, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Reference proteome, Transport","21966920, 19648244, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",7,323,328,3,316,317]
[null,"P13803","IPMed?",1.003,1.01829,35.33,{"v":2e-49,"d":"2.00E-49"},13,2,"Etfa","Electron transfer flavoprotein subunit alpha, mitochondrial","_","Acetylation, Complete proteome, Direct protein sequencing, Electron transport, FAD, Flavoprotein, Mitochondrion, Phosphoprotein, Reference proteome, Transit peptide, Transport","3415685, 15489334, 7334008, 22673903","Rattus norvegicus","_",5,325,328,19,333,333]
[]
["CLOSTRIBL3_v1_11488","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P97089","_",1,1.01923,42.64,{"v":4e-62,"d":"4.00E-62"},1,6,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",1,264,265,1,260,260]
[null,"P52040","IPMed?",1,1.02317,40,{"v":1E-56,"d":"1.00E-56"},2,6,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,264,265,1,259,259]
[null,"O85691","IPMed?",1.00741,1.02642,41.54,{"v":6e-50,"d":"6.00E-50"},3,6,"etfB","Electron transfer flavoprotein subunit beta","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,255,265,1,265,270]
[null,"H6LGM7","IPMed?",1,1.01145,35.85,{"v":3e-46,"d":"3.00E-46"},4,6,"carD","Caffeyl-CoA reductase-Etf complex subunit CarD","1.3.1.108","3D-structure, Complete proteome, Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",1,264,265,1,262,262]
[null,"G3KIM7","IPMed?",1.00749,1.01509,37.92,{"v":2e-44,"d":"2.00E-44"},5,6,"acrB","Acryloyl-CoA reductase electron transfer subunit gamma","_","Cytoplasm, Electron transport, Transport","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",1,264,265,1,267,267]
[null,"P26482","IPMed?",0.9573,1.01509,35.32,{"v":2e-44,"d":"2.00E-44"},6,6,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Reference proteome, Transport","1850088, 3216855","Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)","_",1,261,265,1,267,281]
[null,"Q53210","_",0.92281,0.99245,34.98,{"v":1e-43,"d":"1.00E-43"},7,6,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Transport","8796346, 9163424, 19376903","Sinorhizobium fredii (strain NBRC 101917 / NGR234)","NBRC 101917 / NGR234 / NBRC 101917 / NGR234",1,256,265,1,260,285]
[null,"P53576","_",0.88968,0.9434,38,{"v":4e-43,"d":"4.00E-43"},8,6,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",1,242,265,1,246,281]
[null,"P53577","IPMed?",0.90972,0.98868,35.5,{"v":6e-43,"d":"6.00E-43"},9,6,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Reference proteome, Transport","8599534, 11157954, 12597275","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","USDA 3I1b110 / USDA 110spc4 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110",1,256,265,1,260,288]
[null,"P09818","IPMed?",0.84589,0.93208,34.41,{"v":1e-37,"d":"1.00E-37"},10,6,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104, 6317191","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",1,241,265,1,246,292]
[null,"Q05559","IPMed?",0.95699,1.00755,36.7,{"v":6E-37,"d":"6.00E-37"},11,6,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport",8369342,"Rhizobium leguminosarum bv. phaseoli","_",1,260,265,1,259,279]
[null,"P64098","IPMed?",0.92481,0.9283,34.15,{"v":4e-33,"d":"4.00E-33"},12,5,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Transport","12788972, 28385856, 16006064","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97 / BCG / Pasteur",2,241,265,3,244,266]
[null,"P60566","IPMed?",0.82264,0.85156,32.57,{"v":1E-27,"d":"1.00E-27"},13,1,"fixA","Protein FixA","_","Complete proteome, Electron transport, Reference proteome, Transport","7473063, 1630901, 9278503, 16738553, 12081978","Escherichia coli (strain K12)","O44:K74 / K12 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / BW25113",1,215,265,1,217,256]
[]
["CLOSTRIBL3_v1_12010","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O85692","IPMed?",1,1.00595,50.3,{"v":2e-114,"d":"2.00E-114"},1,3,"etfA","Electron transfer flavoprotein subunit alpha","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,336,336,1,337,338]
[null,"P71153","_",0.98214,1,50.61,{"v":1e-110,"d":"1.00E-110"},2,3,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",5,334,336,3,330,330]
[null,"H6LGM8","IPMed?",0.82828,0.97619,48.48,{"v":1E-107,"d":"1.00E-107"},3,3,"carE","Caffeyl-CoA reductase-Etf complex subunit CarE","1.3.1.108","3D-structure, 4Fe-4S, Complete proteome, Cytoplasm, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",6,333,336,68,394,396]
[null,"P53578","IPMed?",0.99107,0.99701,48.65,{"v":2e-105,"d":"2.00E-105"},4,3,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Transport",7875566,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",1,333,336,1,330,334]
[null,"P52039","IPMed?",1.00298,1.00298,47.77,{"v":7e-100,"d":"7.00E-100"},5,3,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,335,336,1,336,336]
[null,"P26483","IPMed?",0.90244,0.99107,43.54,{"v":7e-90,"d":"7.00E-90"},6,3,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Reference proteome, Transport",1850088,"Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)","_",3,332,336,26,357,369]
[null,"G3KIM6","IPMed?",0.97275,1.0625,43.7,{"v":8e-89,"d":"8.00E-89"},7,3,"acrA","Acryloyl-CoA reductase electron transfer subunit beta","_","Cytoplasm, Electron transport, Transport","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",6,335,336,11,366,367]
[null,"P10449","IPMed?",0.90244,0.99107,42.34,{"v":1E-87,"d":"1.00E-87"},8,1,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Reference proteome, Transport","8599534, 11157954, 12597275, 2503674","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","USDA 3I1b110 / USDA 110spc4 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110 / USDA 110spc4",3,332,336,26,357,369]
[null,"Q53209","_",0.88618,0.97321,41.59,{"v":9e-85,"d":"9.00E-85"},9,3,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Plasmid, Transport","8796346, 9163424, 19376903","Sinorhizobium fredii (strain NBRC 101917 / NGR234)","NBRC 101917 / NGR234 / NBRC 101917 / NGR234",3,326,336,26,351,369]
[null,"P09819","IPMed?",0.92918,0.97619,42.68,{"v":2e-82,"d":"2.00E-82"},10,3,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",3,326,336,9,335,353]
[null,"Q0AZ33","IPMed?",0.95833,1.01577,38.82,{"v":5e-73,"d":"5.00E-73"},11,3,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Cytoplasm, Electron transport, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Reference proteome, Transport","21966920, 19648244, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",10,331,336,5,316,317]
[null,"P13803","IPMed?",0.87202,0.87988,37.54,{"v":2E-50,"d":"2.00E-50"},12,1,"Etfa","Electron transfer flavoprotein subunit alpha, mitochondrial","_","Acetylation, Complete proteome, Direct protein sequencing, Electron transport, FAD, Flavoprotein, Mitochondrion, Phosphoprotein, Reference proteome, Transit peptide, Transport","3415685, 15489334, 7334008, 22673903","Rattus norvegicus","_",35,326,336,44,326,333]
[]
["CLOSTRIBL3_v1_12011","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P97089","_",0.9771,0.98462,53.12,{"v":8e-86,"d":"8.00E-86"},1,3,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",1,256,262,1,254,260]
[null,"P52040","IPMed?",0.98473,0.99614,53.49,{"v":2e-83,"d":"2.00E-83"},2,3,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,258,262,1,255,259]
[null,"O85691","IPMed?",1.0037,1.03435,50.18,{"v":2e-81,"d":"2.00E-81"},3,2,"etfB","Electron transfer flavoprotein subunit beta","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,262,262,1,270,270]
[null,"H6LGM7","IPMed?",1.00382,1.00382,49.81,{"v":2e-77,"d":"2.00E-77"},4,3,"carD","Caffeyl-CoA reductase-Etf complex subunit CarD","1.3.1.108","3D-structure, Complete proteome, Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",1,262,262,1,262,262]
[null,"P53576","_",0.9573,1.02672,45.72,{"v":1e-66,"d":"1.00E-66"},5,1,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",1,256,262,1,265,281]
[null,"P26482","IPMed?",0.93594,1.00382,42.21,{"v":5e-66,"d":"5.00E-66"},6,1,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Reference proteome, Transport","1850088, 3216855","Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)","_",1,256,262,1,263,281]
[null,"Q53210","_",0.94035,1.0229,44.78,{"v":1e-65,"d":"1.00E-65"},7,1,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Transport","8796346, 9163424, 19376903","Sinorhizobium fredii (strain NBRC 101917 / NGR234)","NBRC 101917 / NGR234 / NBRC 101917 / NGR234",1,259,262,1,265,285]
[null,"P53577","IPMed?",0.90625,0.99618,42.15,{"v":3e-64,"d":"3.00E-64"},8,1,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Reference proteome, Transport","8599534, 11157954, 12597275","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","USDA 3I1b110 / USDA 110spc4 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110",1,253,262,1,259,288]
[null,"P09818","IPMed?",0.86301,0.96183,42.06,{"v":1E-59,"d":"1.00E-59"},9,1,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104, 6317191","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",1,244,262,1,252,292]
[null,"G3KIM7","IPMed?",1.00749,1.02672,42.38,{"v":3e-59,"d":"3.00E-59"},10,3,"acrB","Acryloyl-CoA reductase electron transfer subunit gamma","_","Cytoplasm, Electron transport, Transport","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",1,262,262,1,267,267]
[null,"Q05559","IPMed?",0.94982,1.01145,41.13,{"v":1e-57,"d":"1.00E-57"},11,1,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport",8369342,"Rhizobium leguminosarum bv. phaseoli","_",1,257,262,1,261,279]
[null,"P64098","IPMed?",1.00376,1.01908,29.96,{"v":6e-38,"d":"6.00E-38"},12,2,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Transport","12788972, 28385856, 16006064","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97 / BCG / Pasteur",2,262,262,3,266,266]
[null,"P53570","IPMed?",0.84848,0.85496,33.48,{"v":8e-29,"d":"8.00E-29"},13,1,"etfB","Electron transfer flavoprotein subunit beta","_","3D-structure, Direct protein sequencing, Electron transport, Nucleotide-binding, Transport","7798207, 12567183","Methylophilus methylotrophus","_",34,252,262,35,255,264]
[]
["CLOSTRIBL3_v1_20124","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P97089","_",1.00377,1.02308,43.23,{"v":3e-71,"d":"3.00E-71"},1,4,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",1,265,265,1,260,260]
[null,"P52040","IPMed?",0.98868,1.01158,43.89,{"v":2e-65,"d":"2.00E-65"},2,5,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,262,265,1,252,259]
[null,"H6LGM7","IPMed?",1.00377,1.01527,42.48,{"v":5e-65,"d":"5.00E-65"},3,4,"carD","Caffeyl-CoA reductase-Etf complex subunit CarD","1.3.1.108","3D-structure, Complete proteome, Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",1,265,265,1,262,262]
[null,"O85691","IPMed?",1.00741,1.02642,38.97,{"v":3e-59,"d":"3.00E-59"},4,4,"etfB","Electron transfer flavoprotein subunit beta","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,265,265,1,270,270]
[null,"P53576","_",0.85053,0.90189,42.26,{"v":2e-56,"d":"2.00E-56"},5,4,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",1,232,265,1,238,281]
[null,"Q53210","_",0.92281,0.99245,38.4,{"v":3E-52,"d":"3.00E-52"},6,4,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Transport","8796346, 9163424, 19376903","Sinorhizobium fredii (strain NBRC 101917 / NGR234)","NBRC 101917 / NGR234 / NBRC 101917 / NGR234",1,256,265,1,262,285]
[null,"P26482","IPMed?",0.86477,0.91698,39.51,{"v":4E-52,"d":"4.00E-52"},7,5,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Reference proteome, Transport","1850088, 3216855","Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)","_",1,236,265,1,243,281]
[null,"G3KIM7","IPMed?",0.98876,0.99623,37.5,{"v":8e-50,"d":"8.00E-50"},8,4,"acrB","Acryloyl-CoA reductase electron transfer subunit gamma","_","Cytoplasm, Electron transport, Transport","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",1,256,265,1,262,267]
[null,"P53577","IPMed?",0.90972,0.98868,36.26,{"v":1e-49,"d":"1.00E-49"},9,5,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Reference proteome, Transport","8599534, 11157954, 12597275","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","USDA 3I1b110 / USDA 110spc4 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110",1,255,265,1,262,288]
[null,"P09818","IPMed?",0.81507,0.89811,38.24,{"v":4e-47,"d":"4.00E-47"},10,4,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104, 6317191","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",1,231,265,1,238,292]
[null,"Q05559","IPMed?",0.85305,0.89811,39.5,{"v":2E-45,"d":"2.00E-45"},11,5,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport",8369342,"Rhizobium leguminosarum bv. phaseoli","_",1,231,265,1,236,279]
[null,"P64098","IPMed?",1.01504,1.01887,33.33,{"v":1e-33,"d":"1.00E-33"},12,4,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Transport","12788972, 28385856, 16006064","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97 / BCG / Pasteur",3,265,265,4,266,266]
[null,"P60566","IPMed?",0.8,0.82812,32.55,{"v":1E-27,"d":"1.00E-27"},13,2,"fixA","Protein FixA","_","Complete proteome, Electron transport, Reference proteome, Transport","7473063, 1630901, 9278503, 16738553, 12081978","Escherichia coli (strain K12)","O44:K74 / K12 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / BW25113",1,209,265,1,211,256]
[]
["CLOSTRIBL3_v1_20125","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P71153","_",0.98498,0.99394,50.3,{"v":6e-107,"d":"6.00E-107"},1,4,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",2,329,333,5,330,330]
[null,"P53578","IPMed?",0.97605,0.97898,47.85,{"v":2e-97,"d":"2.00E-97"},2,4,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Transport",7875566,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",2,327,333,7,329,334]
[null,"H6LGM8","IPMed?",0.83081,0.98799,46.2,{"v":2E-95,"d":"2.00E-95"},3,4,"carE","Caffeyl-CoA reductase-Etf complex subunit CarE","1.3.1.108","3D-structure, 4Fe-4S, Complete proteome, Cytoplasm, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",2,330,333,69,396,396]
[null,"P52039","IPMed?",0.97619,0.98498,47.26,{"v":3e-95,"d":"3.00E-95"},4,4,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",2,326,333,7,332,336]
[null,"O85692","IPMed?",0.97633,0.99099,47.88,{"v":3e-94,"d":"3.00E-94"},5,4,"etfA","Electron transfer flavoprotein subunit alpha","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",2,329,333,7,335,338]
[null,"G3KIM6","IPMed?",0.97003,1.06907,41.85,{"v":3e-75,"d":"3.00E-75"},6,4,"acrA","Acryloyl-CoA reductase electron transfer subunit beta","_","Cytoplasm, Electron transport, Transport","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",2,329,333,12,365,367]
[null,"P26483","IPMed?",0.88889,0.98498,39.94,{"v":1e-74,"d":"1.00E-74"},7,5,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Reference proteome, Transport",1850088,"Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)","_",2,326,333,30,356,369]
[null,"Q53209","_",0.87534,0.96997,40.87,{"v":3e-74,"d":"3.00E-74"},8,4,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Plasmid, Transport","8796346, 9163424, 19376903","Sinorhizobium fredii (strain NBRC 101917 / NGR234)","NBRC 101917 / NGR234 / NBRC 101917 / NGR234",2,321,333,30,351,369]
[null,"P10449","IPMed?",0.87805,0.97297,41.05,{"v":2E-73,"d":"2.00E-73"},9,4,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Reference proteome, Transport","8599534, 11157954, 12597275, 2503674","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","USDA 3I1b110 / USDA 110spc4 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110 / USDA 110spc4",2,321,333,30,351,369]
[null,"P09819","IPMed?",0.91785,0.97297,40.12,{"v":6e-73,"d":"6.00E-73"},10,4,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",2,321,333,13,335,353]
[null,"Q0AZ33","IPMed?",0.98198,1.03155,33.03,{"v":3e-56,"d":"3.00E-56"},11,5,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Cytoplasm, Electron transport, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Reference proteome, Transport","21966920, 19648244, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",1,327,333,1,317,317]
[null,"Q9C6I6","IPMed?",0.91185,0.99399,30.82,{"v":2E-45,"d":"2.00E-45"},12,3,"ETFA","Electron transfer flavoprotein subunit alpha, mitochondrial","_","Complete proteome, Electron transport, FAD, Flavoprotein, Mitochondrion, Reference proteome, Transit peptide, Transport","11130712, 27862469, 14593172, 11910074, 14671022, 16923016, 25732537","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Landsberg erecta",7,329,333,40,363,363]
[]
["CLOSTRIBL3_v1_10629","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"D8GR66","IPMed?",1,1,80.31,0,1,1,"rnfC","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit C","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Repeat, Translocase, Transport","20616070, 23269825","Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC)","ATCC 55383 / DSM 13528 / PETC / ATCC 55383 / DSM 13528 / PETC",1,457,457,1,457,457]
[null,"H6LC32","IPMed?",0.93435,0.96388,48.24,{"v":3e-143,"d":"3.00E-143"},2,1,"rnfC","Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit C","7.2.1.2","4Fe-4S, Cell membrane, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Reference proteome, Repeat, Translocase, Transport","17873051, 19222539, 20921383, 24045950","Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",4,429,457,7,432,443]
[null,"D5ARZ1","IPMed?",0.91522,1.03939,42.95,{"v":1E-117,"d":"1.00E-117"},3,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Nitrogen fixation, Reference proteome, Repeat, Translocase, Transport","20418398, 9154934","Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)","ATCC BAA-309 / NBRC 16581 / SB1003 / ATCC BAA-309 / NBRC 16581 / SB1003",4,456,457,17,488,519]
[null,"Q52716","IPMed?",0.91522,1.03939,42.95,{"v":1E-117,"d":"1.00E-117"},3,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Nitrogen fixation, Repeat, Translocase, Transport","8264535, 9492268","Rhodobacter capsulatus","B10S / ATCC 33303 / B10",4,456,457,17,488,519]
[null,"Q9HYB8","_",0.58915,0.99781,39.47,{"v":2e-101,"d":"2.00E-101"},4,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport",10984043,"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1",2,454,457,4,455,774]
[null,"A5UBJ0","_",0.71736,1.02188,38.54,{"v":5e-101,"d":"5.00E-101"},5,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",17550610,"Haemophilus influenzae (strain PittEE)","PittEE",2,454,457,13,476,651]
[null,"Q4QJQ6","_",0.70226,1.02188,38.12,{"v":3e-100,"d":"3.00E-100"},6,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",15968074,"Haemophilus influenzae (strain 86-028NP)","86-028NP",2,454,457,13,476,665]
[null,"P71397","_",0.57021,1.02188,38.12,{"v":6e-99,"d":"6.00E-99"},7,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",2,454,457,13,476,819]
[null,"Q65U33","_",0.64039,1.01313,37.8,{"v":6e-99,"d":"6.00E-99"},8,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport",15378067,"Mannheimia succiniciproducens (strain MBEL55E)","MBEL55E",2,454,457,13,472,723]
[null,"A8GE00","_",0.65861,1.01313,38.23,{"v":5e-98,"d":"5.00E-98"},9,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport","_","Serratia proteamaculans (strain 568)","_",5,457,457,16,474,703]
[null,"Q9KT88","_",0.60207,1.01969,36.48,{"v":5e-97,"d":"5.00E-97"},10,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport",10952301,"Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","ATCC 39315 / El Tor Inaba N16961",2,457,457,13,475,774]
[null,"A0A0H3AJC2","IPMed?",0.60285,1.01969,36.48,{"v":5e-97,"d":"5.00E-97"},10,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",25831459,"Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395",2,457,457,13,475,773]
[null,"P77611","IPMed?",0.62297,1.00875,36.23,{"v":1E-89,"d":"1.00E-89"},11,1,"rsxC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport","9097039, 9278503, 16738553, 12773378","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",5,457,457,16,469,740]
[null,"Q8TSY4","IPMed?",0.97374,0.99553,32.36,{"v":7e-65,"d":"7.00E-65"},12,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.2.1.-","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport","11932238, 23066798","Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)","ATCC 35395 / DSM 2834 / JCM 12185 / C2A / ATCC 35395 / DSM 2834 / JCM 12185 / C2A",28,439,457,22,447,447]
[null,"P31979","IPMed?",0.58206,0.59775,27.07,7e-08,13,3,"nuoF","NADH-quinone oxidoreductase subunit F","7.1.1.-","4Fe-4S, Complete proteome, Direct protein sequencing, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Ubiquinone","7690854, 8157582, 9205837, 9278503, 16738553, 8366049, 7607227","Escherichia coli (strain K12)","K12 / AN387 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / W3110 / ATCC 27325 / DSM 5911",119,342,457,45,309,445]
[null,"P33901","IPMed?",0.58206,0.59775,26.32,5e-07,14,3,"nuoF","NADH-quinone oxidoreductase subunit F","7.1.1.-","4Fe-4S, Complete proteome, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Ubiquinone","8234329, 11677609","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720",119,342,457,45,309,445]
[null,"Q56222","IPMed?",0.59081,0.61644,24.44,5e-06,15,6,"nqo1","NADH-quinone oxidoreductase subunit 1","7.1.1.-","3D-structure, 4Fe-4S, Cell membrane, Complete proteome, Direct protein sequencing, Flavoprotein, FMN, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Translocase","9020134, 16584177, 16469879","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","HB8 / ATCC 27634 / DSM 579 / HB8 / ATCC 27634 / DSM 579",113,342,457,42,311,438]
[null,"Q46507","IPMed?",0.63265,0.67834,22.9,0.0008,16,13,"hndC","NADP-reducing hydrogenase subunit HndC","1.12.1.3","4Fe-4S, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat","7751270, 9703971","Desulfovibrio fructosivorans","_",119,371,457,44,351,490]
[]
["CLOSTRIBL3_v1_10630","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"D8GR67","IPMed?",1,1,84.89,0,1,1,"rnfD","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit D","7.1.1.-","Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, NAD, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","20616070, 23269825","Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC)","ATCC 55383 / DSM 13528 / PETC / ATCC 55383 / DSM 13528 / PETC",1,331,331,1,331,331]
[null,"H6LC31","IPMed?",0.97885,1.01887,46.3,{"v":1E-83,"d":"1.00E-83"},2,1,"rnfD","Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit D","7.2.1.2","Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, NAD, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","17873051, 19222539, 20921383, 24045950","Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",12,331,331,7,311,318]
[null,"Q9EVN4","_",0.92938,0.99396,39.82,{"v":5e-64,"d":"5.00E-64"},3,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","_","Pseudomonas stutzeri","_",24,328,331,5,331,354]
[null,"A1WTR8","_",0.95798,1.03323,35.67,{"v":6e-61,"d":"6.00E-61"},4,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","_","Halorhodospira halophila (strain DSM 244 / SL1)","_",15,331,331,6,345,357]
[null,"A8AH11","_",1.02,1.07855,35.57,{"v":9e-59,"d":"9.00E-59"},5,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","_","Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)","_",10,330,331,2,350,350]
[null,"A6VQ43","_",0.99437,1.06647,35.41,{"v":2e-58,"d":"2.00E-58"},6,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",21118570,"Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / 130Z)","ATCC 55618 / DSM 22257 / 130Z",10,324,331,1,344,355]
[null,"B6IB68","_",1.02273,1.08761,36.94,{"v":2e-58,"d":"2.00E-58"},7,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",18931093,"Escherichia coli (strain SE11)","SE11",10,331,331,2,351,352]
[null,"B7M0I7","_",1.02273,1.08761,36.94,{"v":2e-58,"d":"2.00E-58"},7,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",19165319,"Escherichia coli O8 (strain IAI1)","IAI1",10,331,331,2,351,352]
[null,"B7L5I3","_",1.02273,1.08761,36.94,{"v":2e-58,"d":"2.00E-58"},7,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",19165319,"Escherichia coli (strain 55989 / EAEC)","55989 / EAEC",10,331,331,2,351,352]
[null,"B7NU03","_",1.02273,1.08761,36.67,{"v":3e-58,"d":"3.00E-58"},8,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",19165319,"Escherichia coli O7:K1 (strain IAI39 / ExPEC)","IAI39 / ExPEC",10,331,331,2,351,352]
[null,"B2U2C9","_",1.02273,1.08761,36.67,{"v":7e-58,"d":"7.00E-58"},9,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","_","Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)","_",10,331,331,2,351,352]
[null,"Q32FE3","_",1.02273,1.08761,36.67,{"v":7e-58,"d":"7.00E-58"},9,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",16275786,"Shigella dysenteriae serotype 1 (strain Sd197)","Sd197",10,331,331,2,351,352]
[null,"Q320Y7","_",1.02273,1.08761,36.67,{"v":7e-58,"d":"7.00E-58"},9,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",16275786,"Shigella boydii serotype 4 (strain Sb227)","Sb227",10,331,331,2,351,352]
[null,"A8A0H3","_",1.02273,1.08761,36.67,{"v":7e-58,"d":"7.00E-58"},9,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",18676672,"Escherichia coli O9:H4 (strain HS)","HS",10,331,331,2,351,352]
[null,"P76182","IPMed?",1.02273,1.08761,36.67,{"v":7e-58,"d":"7.00E-58"},9,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","9278503, 16738553, 12773378","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",10,331,331,2,351,352]
[null,"B1IQC4","_",1.02273,1.08761,36.94,{"v":1e-57,"d":"1.00E-57"},10,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","_","Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)","_",10,331,331,2,351,352]
[null,"Q52715","IPMed?",0.84916,0.91843,38.16,{"v":1E-53,"d":"1.00E-53"},11,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Electron transport, Flavoprotein, FMN, Membrane, Nitrogen fixation, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","8264535, 9492268","Rhodobacter capsulatus","B10S / ATCC 33303 / B10",15,297,331,6,309,358]
[null,"A5F2R1","IPMed?",1.00575,1.0574,35.71,{"v":3E-52,"d":"3.00E-52"},12,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","19115014, 18831535, 25831459","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",11,328,331,3,347,348]
[null,"Q8TSY3","IPMed?",0.96375,1.10764,32.29,{"v":9e-49,"d":"9.00E-49"},13,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.2.1.-","Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","11932238, 23066798","Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)","ATCC 35395 / DSM 2834 / JCM 12185 / C2A / ATCC 35395 / DSM 2834 / JCM 12185 / C2A",11,328,331,4,283,288]
[null,"Q56587","IPMed?",0.57971,0.72508,35,{"v":3E-34,"d":"3.00E-34"},14,1,"nqrB","Na(+)-translocating NADH-quinone reductase subunit B","7.2.1.1","Cell inner membrane, Cell membrane, Direct protein sequencing, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7805867, 9490015, 10838078, 10549856, 11163785, 11248187, 11248188","Vibrio alginolyticus","NCIMB 11038 / LMG 3418",85,319,331,160,397,414]
[null,"Q9RFW0","IPMed?",0.69976,0.87311,31.83,{"v":2e-33,"d":"2.00E-33"},15,1,"nqrB","Na(+)-translocating NADH-quinone reductase subunit B","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",10587447,"Vibrio campbellii (strain ATCC BAA-1116 / BB120)","_",37,319,331,113,396,413]
[null,"Q9KPS2","IPMed?",0.57831,0.72508,33.75,{"v":5e-32,"d":"5.00E-32"},16,1,"nqrB","Na(+)-translocating NADH-quinone reductase subunit B","7.2.1.1","3D-structure, Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","10077658, 10952301","Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","ATCC 39315 / El Tor Inaba N16961 / ATCC 39315 / El Tor Inaba N16961",85,319,331,160,397,415]
[null,"A5F5X0","IPMed?",0.57831,0.72508,33.75,{"v":5e-32,"d":"5.00E-32"},16,1,"nqrB","Na(+)-translocating NADH-quinone reductase subunit B","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","19115014, 11888296, 20558724, 22366169","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",85,319,331,160,397,415]
[null,"O05011","IPMed?",0.74696,0.92749,30.29,{"v":3e-30,"d":"3.00E-30"},17,1,"nqrB","Na(+)-translocating NADH-quinone reductase subunit B","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7542800, 8601449","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd / ATCC 51907 / DSM 11121 / KW20 / Rd",30,331,331,115,406,411]
[]
["CLOSTRIBL3_v1_10631","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"D8GR68","IPMed?",1,1,84.86,{"v":4E-107,"d":"4.00E-107"},1,1,"rnfG","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit G","7.1.1.-","Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, NAD, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","20616070, 23269825","Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC)","ATCC 55383 / DSM 13528 / PETC / ATCC 55383 / DSM 13528 / PETC",1,185,185,1,185,185]
[null,"H6LC30","IPMed?",0.93237,1.04324,30.57,{"v":1e-18,"d":"1.00E-18"},2,1,"rnfG","Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit G","7.2.1.2","Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, NAD, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","19222539, 20921383, 24045950","Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",6,176,185,10,200,207]
[null,"Q8TSY2","IPMed?",1.00532,1.02162,30.16,{"v":1e-18,"d":"1.00E-18"},3,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.2.1.-","Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","11932238, 23066798, 24836163","Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)","ATCC 35395 / DSM 2834 / JCM 12185 / C2A / ATCC 35395 / DSM 2834 / JCM 12185 / C2A",6,183,185,3,188,188]
[null,"A5UBI8","_",0.86957,0.97297,30.56,9e-12,4,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",17550610,"Haemophilus influenzae (strain PittEE)","PittEE",17,174,185,14,188,207]
[null,"P44291","_",0.86957,0.97297,30,2e-11,5,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",17,174,185,14,188,207]
[null,"B7VLT4","_",0.90431,1.02162,25.93,6E-11,6,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","_","Vibrio tasmaniensis (strain LGP32)","_",12,178,185,4,192,209]
[null,"Q4QJQ4","_",0.86957,0.97297,29.44,1E-10,7,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",15968074,"Haemophilus influenzae (strain 86-028NP)","86-028NP",17,174,185,14,188,207]
[null,"Q5E6C0","_",0.61429,0.6973,33.33,3E-10,8,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",15703294,"Aliivibrio fischeri (strain ATCC 700601 / ES114)","ATCC 700601 / ES114",54,175,185,65,190,210]
[null,"B6EGH3","_",0.60952,0.69189,34.38,4e-10,9,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",19099551,"Aliivibrio salmonicida (strain LFI1238)","LFI1238",54,175,185,65,190,210]
[null,"B8E552","_",0.51887,0.59459,34.55,5e-10,10,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","_","Shewanella baltica (strain OS223)","_",71,175,185,81,190,212]
[null,"A5F2S8","IPMed?",0.91866,1.03784,27.6,5e-09,11,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","19115014, 18831535, 25831459","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",12,178,185,4,192,209]
[null,"P97054","IPMed?",0.48387,0.56757,33.33,3e-08,12,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Electron transport, Flavoprotein, FMN, Membrane, Nitrogen fixation, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","8264535, 9492268","Rhodobacter capsulatus","B10S / ATCC 33303 / B10",71,171,185,91,195,217]
[null,"P77285","IPMed?",0.86893,0.96757,27.93,9e-08,13,1,"rsxG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","9097039, 9278503, 16738553, 12773378","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",17,174,185,10,187,206]
[null,"P43957","IPMed?",0.58197,0.76757,24.65,3e-05,14,1,"nqrC","Na(+)-translocating NADH-quinone reductase subunit C","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7542800, 8601449","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd / ATCC 51907 / DSM 11121 / KW20 / Rd",38,167,185,78,219,244]
[null,"A5F5Y7","IPMed?",0.41634,0.57838,28.04,1E-4,15,1,"nqrC","Na(+)-translocating NADH-quinone reductase subunit C","7.2.1.1","3D-structure, Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","10077658, 19115014, 11248234, 11888296, 20558724, 22366169","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",71,167,185,125,231,257]
[null,"Q56582","IPMed?",0.37109,0.51351,30.53,2E-3,16,1,"nqrC","Na(+)-translocating NADH-quinone reductase subunit C","7.2.1.1","Cell inner membrane, Cell membrane, Direct protein sequencing, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7805867, 7729558, 7805866, 9490015, 10838078, 10549856, 11163785, 11248187, 11248188","Vibrio alginolyticus","NCIMB 11038 / LMG 3418",83,167,185,136,230,256]
[null,"Q9RFV9","IPMed?",0.40996,0.57838,26.17,0.004,17,1,"nqrC","Na(+)-translocating NADH-quinone reductase subunit C","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Direct protein sequencing, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",10587447,"Vibrio campbellii (strain ATCC BAA-1116 / BB120)","_",71,167,185,129,235,261]
[]
["CLOSTRIBL3_v1_10632","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"D8GR69","IPMed?",0.98592,0.99057,87.14,{"v":4e-129,"d":"4.00E-129"},1,1,"rnfE","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit E","7.1.1.-","Cell membrane, Complete proteome, Electron transport, Membrane, NAD, Translocase, Transmembrane, Transmembrane helix, Transport","20616070, 23269825","Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC)","ATCC 55383 / DSM 13528 / PETC / ATCC 55383 / DSM 13528 / PETC",3,212,212,4,213,213]
[null,"H6LC29","IPMed?",0.85377,0.92347,46.41,{"v":2e-57,"d":"2.00E-57"},2,1,"rnfE","Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit E","7.2.1.2","Cell membrane, Complete proteome, Electron transport, Membrane, NAD, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","19222539, 20921383, 24045950","Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",9,189,212,9,189,196]
[null,"Q9F5Y1","_",0.85714,0.96226,43.14,{"v":5e-50,"d":"5.00E-50"},3,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",19429624,"Azotobacter vinelandii (strain DJ / ATCC BAA-1303)","DJ / ATCC BAA-1303",4,194,212,18,221,238]
[null,"Q4QJQ3","_",0.85106,0.9434,41.5,{"v":2e-48,"d":"2.00E-48"},4,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",15968074,"Haemophilus influenzae (strain 86-028NP)","86-028NP",3,188,212,27,226,235]
[null,"A5UFC5","_",0.8547,0.9434,41.5,{"v":2e-48,"d":"2.00E-48"},4,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",17550610,"Haemophilus influenzae (strain PittGG)","PittGG",3,188,212,26,225,234]
[null,"Q57020","_",0.85106,0.9434,41.5,{"v":2e-48,"d":"2.00E-48"},4,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",3,188,212,27,226,235]
[null,"A5UBI7","_",0.85106,0.9434,41,{"v":1e-47,"d":"1.00E-47"},5,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",17550610,"Haemophilus influenzae (strain PittEE)","PittEE",3,188,212,27,226,235]
[null,"A1TZ60","_",0.88655,0.99528,40.28,{"v":4e-47,"d":"4.00E-47"},6,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport","_","Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / VT8)","_",5,202,212,8,218,238]
[null,"Q87MW9","_",0.93043,1.00943,41.59,{"v":1E-46,"d":"1.00E-46"},7,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",12620739,"Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)","RIMD 2210633",6,206,212,7,219,230]
[null,"P97055","IPMed?",0.92181,1.0566,41.07,{"v":2E-46,"d":"2.00E-46"},10,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Electron transport, Membrane, Nitrogen fixation, Translocase, Transmembrane, Transmembrane helix, Transport","8264535, 9492268","Rhodobacter capsulatus","B10S / ATCC 33303 / B10",6,209,212,8,231,243]
[null,"B7VLT3","_",0.93043,1.00943,41.12,{"v":2E-46,"d":"2.00E-46"},9,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","_","Vibrio tasmaniensis (strain LGP32)","_",6,206,212,7,219,230]
[null,"Q2W403","_",0.95067,1,41.51,{"v":2E-46,"d":"2.00E-46"},8,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",16303747,"Magnetospirillum magneticum (strain AMB-1 / ATCC 700264)","AMB-1 / ATCC 700264",6,202,212,8,218,223]
[null,"Q8TSY1","IPMed?",0.90141,0.90566,43.75,{"v":9e-45,"d":"9.00E-45"},11,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.2.1.-","Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","11932238, 23066798","Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)","ATCC 35395 / DSM 2834 / JCM 12185 / C2A / ATCC 35395 / DSM 2834 / JCM 12185 / C2A",7,194,212,15,206,213]
[null,"A5F2S7","IPMed?",0.86957,0.9434,41,{"v":3e-44,"d":"3.00E-44"},12,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport","19115014, 25831459","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",10,196,212,11,210,230]
[null,"Q57095","IPMed?",0.96226,0.97143,38.73,{"v":2e-39,"d":"2.00E-39"},13,1,"nqrD","Na(+)-translocating NADH-quinone reductase subunit D","7.2.1.1","Cell inner membrane, Cell membrane, Direct protein sequencing, Ion transport, Membrane, NAD, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7805867, 7729558, 9490015, 10549856, 11248187, 11248188","Vibrio alginolyticus","NCIMB 11038 / LMG 3418",8,200,212,8,209,210]
[null,"Q9X4Q6","IPMed?",0.96226,0.97143,37.25,{"v":2e-39,"d":"2.00E-39"},14,1,"nqrD","Na(+)-translocating NADH-quinone reductase subunit D","7.2.1.1","3D-structure, Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","10077658, 10952301","Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","ATCC 39315 / El Tor Inaba N16961 / ATCC 39315 / El Tor Inaba N16961",8,200,212,8,209,210]
[null,"A5F5Y6","IPMed?",0.96226,0.97143,37.25,{"v":2e-39,"d":"2.00E-39"},14,1,"nqrD","Na(+)-translocating NADH-quinone reductase subunit D","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","19115014, 11888296, 20558724","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",8,200,212,8,209,210]
[null,"P77179","IPMed?",0.84848,0.92453,38.27,{"v":3e-39,"d":"3.00E-39"},15,1,"rsxE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","9097039, 9278503, 16738553, 10411911, 12773378, 15919996","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / JM109 / ATCC 53323 / K12 / MG1655 / ATCC 47076",5,187,212,6,201,231]
[null,"Q9RFV8","IPMed?",0.96226,0.97143,38.24,{"v":5e-39,"d":"5.00E-39"},16,1,"nqrD","Na(+)-translocating NADH-quinone reductase subunit D","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",10587447,"Vibrio campbellii (strain ATCC BAA-1116 / BB120)","_",8,200,212,8,209,210]
[null,"P43958","IPMed?",0.89151,0.90865,35.45,{"v":9e-34,"d":"9.00E-34"},17,1,"nqrD","Na(+)-translocating NADH-quinone reductase subunit D","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7542800, 8601449","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd / ATCC 51907 / DSM 11121 / KW20 / Rd",5,186,212,9,195,208]
[]
["CLOSTRIBL3_v1_10633","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"D8GR70","IPMed?",1,1,93.78,{"v":3E-124,"d":"3.00E-124"},1,1,"rnfA","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit A","7.1.1.-","Cell membrane, Complete proteome, Electron transport, Membrane, NAD, Translocase, Transmembrane, Transmembrane helix, Transport","20616070, 23269825","Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC)","ATCC 55383 / DSM 13528 / PETC / ATCC 55383 / DSM 13528 / PETC",1,193,193,1,193,193]
[null,"H6LC28","IPMed?",0.97409,0.97917,50.53,{"v":3E-65,"d":"3.00E-65"},2,1,"rnfA","Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit A","7.2.1.2","Cell membrane, Complete proteome, Electron transport, Membrane, NAD, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","19222539, 20921383, 24045950","Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",3,190,193,2,189,192]
[null,"A8GE02","_",0.98964,0.98964,48.69,{"v":6E-65,"d":"6.00E-65"},3,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport","_","Serratia proteamaculans (strain 568)","_",1,191,193,1,191,193]
[null,"Q2NSZ5","_",1,1,47.15,{"v":6E-65,"d":"6.00E-65"},4,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",16365377,"Sodalis glossinidius (strain morsitans)","morsitans",1,193,193,1,193,193]
[null,"Q7VNT6","_",1,1,50.26,{"v":1e-64,"d":"1.00E-64"},5,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","_","Haemophilus ducreyi (strain 35000HP / ATCC 700724)","_",1,193,193,1,193,193]
[null,"B5XWQ1","_",1,1,48.7,{"v":4e-64,"d":"4.00E-64"},6,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",18654632,"Klebsiella pneumoniae (strain 342)",342,1,193,193,1,193,193]
[null,"A1JM88","_",0.98964,0.98964,47.64,{"v":7e-64,"d":"7.00E-64"},7,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",17173484,"Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)","NCTC 13174 / 8081",1,191,193,1,191,193]
[null,"B2VEQ1","_",0.98964,0.98964,47.12,{"v":7e-64,"d":"7.00E-64"},8,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",18462403,"Erwinia tasmaniensis (strain DSM 17950 / CIP 109463 / Et1/99)","DSM 17950 / CIP 109463 / Et1/99",1,191,193,1,191,193]
[null,"B0BS70","_",1,1,49.74,{"v":1e-63,"d":"1.00E-63"},10,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",18197260,"Actinobacillus pleuropneumoniae serotype 3 (strain JL03)","JL03",1,193,193,1,193,193]
[null,"C4LEP7","_",0.98446,0.98446,50.53,{"v":1e-63,"d":"1.00E-63"},9,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","_","Tolumonas auensis (strain DSM 9187 / TA4)","_",4,193,193,4,193,193]
[null,"A3MYN7","_",1,1,49.74,{"v":1e-63,"d":"1.00E-63"},10,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",18065534,"Actinobacillus pleuropneumoniae serotype 5b (strain L20)","L20",1,193,193,1,193,193]
[null,"P0A766","IPMed?",1,1,47.67,{"v":3e-63,"d":"3.00E-63"},11,1,"rsxA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","9278503, 16738553, 10411911, 12773378, 15919996","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / JM109 / ATCC 53323 / K12 / MG1655 / ATCC 47076",1,193,193,1,193,193]
[null,"A0A0H3AKU6","IPMed?",0.9061,1,46.11,{"v":4e-62,"d":"4.00E-62"},12,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",25831459,"Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395",1,193,193,21,213,213]
[null,"Q8TSY0","IPMed?",0.94975,0.97927,42.33,{"v":2E-51,"d":"2.00E-51"},13,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.2.1.-","Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","11932238, 23066798","Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)","ATCC 35395 / DSM 2834 / JCM 12185 / C2A / ATCC 35395 / DSM 2834 / JCM 12185 / C2A",6,193,193,10,198,199]
[null,"P0CZ13","IPMed?",0.98964,0.98964,40.84,{"v":8e-51,"d":"8.00E-51"},14,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Electron transport, Membrane, Nitrogen fixation, Translocase, Transmembrane, Transmembrane helix, Transport","8264535, 9492268","Rhodobacter capsulatus","B10S / ATCC 33303 / B10",1,191,193,1,191,193]
[null,"D5ARY9","IPMed?",0.98964,0.98964,40.84,{"v":8e-51,"d":"8.00E-51"},14,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Complete proteome, Electron transport, Membrane, Nitrogen fixation, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","8199774, 20418398, 9154934","Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)","ATCC BAA-309 / NBRC 16581 / SB1003 / ATCC BAA-309 / NBRC 16581 / SB1003 / ATCC BAA-309 / NBRC 16581 / SB1003",1,191,193,1,191,193]
[null,"Q9X4Q7","IPMed?",0.9899,1.01554,41.84,{"v":1E-46,"d":"1.00E-46"},15,1,"nqrE","Na(+)-translocating NADH-quinone reductase subunit E","7.2.1.1","3D-structure, Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","10077658, 10952301","Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","ATCC 39315 / El Tor Inaba N16961 / ATCC 39315 / El Tor Inaba N16961",1,190,193,1,196,198]
[null,"A5F5Y5","IPMed?",0.9899,1.01554,41.84,{"v":1E-46,"d":"1.00E-46"},15,1,"nqrE","Na(+)-translocating NADH-quinone reductase subunit E","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","19115014, 11888296, 20558724","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",1,190,193,1,196,198]
[null,"P71342","IPMed?",0.9899,1.01554,41.84,{"v":4e-46,"d":"4.00E-46"},16,1,"nqrE","Na(+)-translocating NADH-quinone reductase subunit E","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7542800, 8601449","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd / ATCC 51907 / DSM 11121 / KW20 / Rd",1,190,193,1,196,198]
[null,"Q5E6X2","IPMed?",0.9899,1.01554,40.82,{"v":2E-45,"d":"2.00E-45"},17,1,"nqrE","Na(+)-translocating NADH-quinone reductase subunit E","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","15703294, 18366731","Aliivibrio fischeri (strain ATCC 700601 / ES114)","ATCC 700601 / ES114",1,190,193,1,196,198]
[null,"Q56589","IPMed?",0.9899,1.01554,39.8,{"v":6e-45,"d":"6.00E-45"},18,1,"nqrE","Na(+)-translocating NADH-quinone reductase subunit E","7.2.1.1","Cell inner membrane, Cell membrane, Direct protein sequencing, Ion transport, Membrane, NAD, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7729558, 7805867, 9490015, 10549856, 11248187, 11248188","Vibrio alginolyticus","NCIMB 11038 / LMG 3418",1,190,193,1,196,198]
[null,"Q9RFV7","IPMed?",0.9899,1.01554,39.8,{"v":6e-45,"d":"6.00E-45"},18,1,"nqrE","Na(+)-translocating NADH-quinone reductase subunit E","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",10587447,"Vibrio campbellii (strain ATCC BAA-1116 / BB120)","_",1,190,193,1,196,198]
[]
["CLOSTRIBL3_v1_10634","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"D8GR71","IPMed?",0.99303,1.00352,82.81,0,1,1,"rnfB","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit B","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Repeat, Translocase, Transport","20616070, 23269825","Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC)","ATCC 55383 / DSM 13528 / PETC / ATCC 55383 / DSM 13528 / PETC",2,286,287,1,283,284]
[null,"H6LC27","IPMed?",0.8018,0.93031,41.2,{"v":9e-66,"d":"9.00E-66"},2,1,"rnfB","Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit B","7.2.1.2","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Reference proteome, Repeat, Translocase, Transport","19222539, 20921383, 24045950","Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",1,266,287,1,261,333]
[null,"Q8TSX9","IPMed?",0.92683,1.00758,40.23,{"v":4e-65,"d":"4.00E-65"},3,1,"rnfB","Ion-translocating oxidoreductase complex subunit B","7.2.1.-","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transmembrane, Transmembrane helix, Transport","11932238, 23066798, 24836163","Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)","ATCC 35395 / DSM 2834 / JCM 12185 / C2A / ATCC 35395 / DSM 2834 / JCM 12185 / C2A",1,266,287,1,261,264]
[null,"A9N024","_",0.66202,0.98958,34.21,{"v":6e-28,"d":"6.00E-28"},4,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport","_","Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7)","_",2,191,287,1,165,192]
[null,"Q8ZPM1","_",0.66202,0.98958,34.21,{"v":6e-28,"d":"6.00E-28"},4,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport",11677609,"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720",2,191,287,1,165,192]
[null,"B5FIE6","_",0.66202,0.98958,34.21,{"v":6e-28,"d":"6.00E-28"},4,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",21602358,"Salmonella dublin (strain CT_02021853)","CT_02021853",2,191,287,1,165,192]
[null,"B4THD5","_",0.66202,0.98958,34.21,{"v":6e-28,"d":"6.00E-28"},4,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",21602358,"Salmonella heidelberg (strain SL476)","SL476",2,191,287,1,165,192]
[null,"Q8Z6R0","_",0.66202,0.98958,34.21,{"v":1E-27,"d":"1.00E-27"},5,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport","11677608, 12644504","Salmonella typhi","CT18 / ATCC 700931 / Ty2",2,191,287,1,165,192]
[null,"B4TV18","_",0.66202,0.98958,34.21,{"v":1E-27,"d":"1.00E-27"},5,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",21602358,"Salmonella schwarzengrund (strain CVM19633)","CVM19633",2,191,287,1,165,192]
[null,"B5F6I9","_",0.66202,0.98958,34.21,{"v":1E-27,"d":"1.00E-27"},5,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",21602358,"Salmonella agona (strain SL483)","SL483",2,191,287,1,165,192]
[null,"B5BKB1","_",0.66202,0.98958,34.21,{"v":1E-27,"d":"1.00E-27"},5,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",19159446,"Salmonella paratyphi A (strain AKU_12601)","AKU_12601",2,191,287,1,165,192]
[null,"C0Q507","_",0.66202,0.98958,34.21,{"v":1E-27,"d":"1.00E-27"},5,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",19229335,"Salmonella paratyphi C (strain RKS4594)","RKS4594",2,191,287,1,165,192]
[null,"B8CM57","_",0.63763,0.96825,32.24,{"v":1E-27,"d":"1.00E-27"},6,1,"rnfB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",18398463,"Shewanella piezotolerans (strain WP3 / JCM 13877)","WP3 / JCM 13877",6,188,287,5,159,189]
[null,"A8H537","_",0.65157,0.98942,32.09,{"v":1E-27,"d":"1.00E-27"},7,1,"rnfB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport","_","Shewanella pealeana (strain ATCC 700345 / ANG-SQ1)","_",2,188,287,1,159,189]
[null,"B4T595","_",0.66202,0.98958,33.68,{"v":3e-27,"d":"3.00E-27"},8,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",21602358,"Salmonella newport (strain SL254)","SL254",2,191,287,1,165,192]
[null,"A7MMM3","_",0.64808,0.96875,32.26,{"v":4e-27,"d":"4.00E-27"},9,1,"rnfB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",20221447,"Cronobacter sakazakii (strain ATCC BAA-894)","ATCC BAA-894",6,191,287,5,165,192]
[null,"A8AH09","_",0.66202,0.98958,31.58,{"v":1E-26,"d":"1.00E-26"},10,1,"rnfB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport","_","Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)","_",2,191,287,1,165,192]
[null,"P77223","IPMed?",0.66551,0.99479,30.89,{"v":3e-25,"d":"3.00E-25"},11,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport","9097039, 9278503, 16738553, 12773378","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",2,191,287,1,165,192]
[null,"A5F2R3","IPMed?",0.65157,0.95897,30.48,{"v":1e-24,"d":"1.00E-24"},12,1,"rnfB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transmembrane, Transmembrane helix, Transport","19115014, 25831459","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",2,188,287,1,159,195]
[null,"P0CZ14","IPMed?",0.65505,1.00535,28.19,{"v":4e-18,"d":"4.00E-18"},13,1,"rnfB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Nitrogen fixation, Repeat, Translocase, Transport","8264535, 9492268","Rhodobacter capsulatus","B10S / ATCC 33303 / B10",12,192,287,8,161,187]
[null,"D5ARZ0","IPMed?",0.65505,1.00535,28.19,{"v":4e-18,"d":"4.00E-18"},13,1,"rnfB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Nitrogen fixation, Reference proteome, Repeat, Translocase, Transport","8199774, 20418398, 9154934","Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)","ATCC BAA-309 / NBRC 16581 / SB1003 / ATCC BAA-309 / NBRC 16581 / SB1003 / ATCC BAA-309 / NBRC 16581 / SB1003",12,192,287,8,161,187]
[null,"Q50784","IPMed?",0.42233,0.60627,25.86,5e-09,14,4,"mvhB","Polyferredoxin protein MvhB","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","2654933, 9371463","Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)","ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H / ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H",143,281,287,37,205,412]
[null,"P00202","IPMed?",0.16376,0.79661,46.81,3e-08,15,4,"_","Ferredoxin","_","4Fe-4S, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",6754724,"Methanosarcina barkeri","ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474",143,188,287,9,55,59]
[null,"Q49180","IPMed?",0.32767,0.47038,29.63,1e-07,17,5,"mvhB","Polyferredoxin protein MvhB","_","4Fe-4S, Iron, Iron-sulfur, Metal-binding, Repeat",2115877,"Methanothermus fervidus","_",143,269,287,216,342,412]
[null,"P60232","IPMed?",0.33495,0.48084,30.43,1e-07,16,5,"mvhB","Polyferredoxin protein MvhB","_","4Fe-4S, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport","20802048, 1312016","Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)","ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg / ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg",143,266,287,285,409,412]
[]
["CLOSTRIBL3_v1_10096","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P0AAK4","IPMed?",0.86702,0.93143,46.63,{"v":8e-48,"d":"8.00E-48"},1,1,"hydN","Electron transport protein HydN","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","9278503, 16738553, 8661925","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",3,165,188,2,152,175]
[null,"P0AAK5","_",0.86702,0.93143,46.63,{"v":8e-48,"d":"8.00E-48"},1,1,"hydN","Electron transport protein HydN","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",12471157,"Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","CFT073 / ATCC 700928 / UPEC",3,165,188,2,152,175]
[null,"P0AAK6","_",0.86702,0.93143,46.63,{"v":8e-48,"d":"8.00E-48"},1,1,"hydN","Electron transport protein HydN","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",3,165,188,2,152,175]
[null,"P56256","_",0.87234,1.04459,46.34,{"v":2E-45,"d":"2.00E-45"},2,1,"ysaA","Putative electron transport protein YsaA","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","8041620, 9278503, 16738553","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",3,166,188,2,140,157]
[null,"P37127","IPMed?",0.25341,0.8883,43.11,{"v":8E-41,"d":"8.00E-41"},3,5,"aegA","Protein AegA","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat","8955321, 9205837, 9278503, 16738553","Escherichia coli (strain K12)","K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",3,169,188,2,146,659]
[null,"Q46819","_",0.87234,1.01235,41.46,{"v":4e-39,"d":"4.00E-39"},4,1,"ygfS","Putative electron transport protein YgfS","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","9278503, 16738553","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",6,169,188,5,142,162]
[null,"P0AAK2","_",0.91626,0.98936,39.78,{"v":1e-38,"d":"1.00E-38"},5,1,"hycB","Formate hydrogenlyase subunit 2","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",12471157,"Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","CFT073 / ATCC 700928 / UPEC",3,180,188,2,179,203]
[null,"P0AAK1","IPMed?",0.91626,0.98936,39.78,{"v":1e-38,"d":"1.00E-38"},5,1,"hycB","Formate hydrogenlyase subunit 2","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","2187144, 9278503, 16738553","Escherichia coli (strain K12)","K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",3,180,188,2,179,203]
[null,"P0AAK3","_",0.91626,0.98936,39.78,{"v":1e-38,"d":"1.00E-38"},5,1,"hycB","Formate hydrogenlyase subunit 2","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","12384590, 12704152","Shigella flexneri","301 / Serotype 2a / ATCC 700930 / 2457T / Serotype 2a",3,180,188,2,179,203]
[null,"P23481","IPMed?",0.94634,1.03191,36.6,{"v":2e-38,"d":"2.00E-38"},6,1,"hyfA","Hydrogenase-4 component A","1.-.-.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","2016588, 9205837, 9278503, 16738553, 9387241, 12426353, 14702328","Escherichia coli (strain K12)","K12 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12",3,180,188,2,182,205]
[null,"P20925","IPMed?",0.76596,0.9172,43.75,{"v":7e-37,"d":"7.00E-37"},7,1,"_","Frd operon probable iron-sulfur subunit A","_","4Fe-4S, Iron, Iron-sulfur, Metal-binding, Repeat",3308458,"Proteus vulgaris","_",37,180,188,11,143,157]
[null,"Q46820","_",0.27074,0.92021,39.31,{"v":5e-35,"d":"5.00E-35"},8,5,"ygfT","Uncharacterized protein YgfT","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat","9278503, 16738553","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",3,174,188,2,141,639]
[null,"P31894","IPMed?",0.99474,1.00532,34.39,{"v":1e-34,"d":"1.00E-34"},9,1,"cooF","Iron-sulfur protein","_","4Fe-4S, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",1644755,"Rhodospirillum rubrum","UR1",2,184,188,6,178,190]
[null,"O30080","IPMed?",0.87923,0.96809,34.62,{"v":7e-23,"d":"7.00E-23"},10,3,"ttrB","Tetrathionate reductase subunit B","_","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Signal, Transport","9389475, 22289056","Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)","ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126 / ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126",7,182,188,37,185,207]
[null,"P0A1I1","IPMed?",0.9375,0.95745,31.11,{"v":7e-20,"d":"7.00E-20"},11,3,"phsB","Thiosulfate reductase electron transfer subunit PhsB","_","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Transport","7751291, 7737516, 11677609, 3108233, 22081391","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / LT2 / LT2 / SGSC1412 / ATCC 700720 / LT2 / LT2",1,173,188,4,156,192]
[null,"P31076","IPMed?",1.01047,1.0266,30.05,{"v":8e-19,"d":"8.00E-19"},12,3,"psrB","Polysulfide reductase chain B","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","1597189, 14500908","Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W)","ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W",9,184,188,10,164,191]
[null,"Q9HR73","IPMed?",0.74046,1.03191,28.87,{"v":2e-18,"d":"2.00E-18"},13,4,"dmsB","Putative dimethyl sulfoxide reductase iron-sulfur subunit B","_","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Transport","11016950, 15716436","Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)","ATCC 700922 / JCM 11081 / NRC-1 / ATCC 700922 / JCM 11081 / NRC-1",1,179,188,1,185,262]
[]
["CLOSTRIBL3_v1_10095","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q46508","IPMed?",0.74872,0.94805,46.35,{"v":2e-115,"d":"2.00E-115"},1,1,"hndD","NADP-reducing hydrogenase subunit HndD","1.12.1.3","2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat","7751270, 9703971","Desulfovibrio fructosivorans","_",43,460,462,151,584,585]
[null,"P29166","IPMed?",0.76481,0.95022,42.37,{"v":2e-112,"d":"2.00E-112"},2,1,"_","Iron hydrogenase 1","1.12.7.2","3D-structure, 4Fe-4S, Direct protein sequencing, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Repeat","1911757, 9836629, 10529166","Clostridium pasteurianum","ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5",33,456,462,135,573,574]
[null,"P07598","IPMed?",0.84632,0.92874,47.83,{"v":9e-112,"d":"9.00E-112"},3,1,"hydA","Periplasmic [Fe] hydrogenase large subunit","1.12.7.2","3D-structure, 4Fe-4S, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Periplasm, Reference proteome, Repeat, Transport","3888621, 15077118, 3322275, 11456963, 10368269, 11456758","Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)","Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303",8,394,462,28,389,421]
[null,"P13629","IPMed?",0.84632,0.92874,46.04,{"v":2E-109,"d":"2.00E-109"},4,1,"hydA","Periplasmic [Fe] hydrogenase large subunit","1.12.7.2","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Periplasm, Repeat, Transport",2661538,"Desulfovibrio oxamicus (strain Monticello)","_",8,394,462,28,389,421]
[null,"A8WH18","_",0.80462,0.829,28.46,{"v":4e-49,"d":"4.00E-49"},5,1,"narfl","Cytosolic Fe-S cluster assembly factor narfl","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome","_","Xenopus tropicalis","_",90,462,462,95,469,476]
[null,"Q5BK18","_",0.76261,0.78571,30.03,{"v":1e-47,"d":"1.00E-47"},6,1,"Ciao3","Cytosolic iron-sulfur assembly component 3","_","4Fe-4S, Acetylation, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome",15489334,"Rattus norvegicus","_",110,462,462,113,469,476]
[null,"Q7TMW6","_",0.75,0.77273,29.97,{"v":3e-46,"d":"3.00E-46"},7,1,"Ciao3","Cytosolic iron-sulfur assembly component 3","_","4Fe-4S, Acetylation, Alternative splicing, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome","16141072, 15489334, 21183079","Mus musculus","C57BL/6J / C57BL/6NCr",110,455,462,113,462,476]
[null,"A2RRV9","_",0.80519,0.90511,27.42,{"v":3e-44,"d":"3.00E-44"},8,1,"narfl","Cytosolic Fe-S cluster assembly factor narfl","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome","_","Danio rerio","_",99,455,462,36,397,411]
[null,"Q94CL6","IPMed?",0.79958,0.82035,31.13,{"v":1e-43,"d":"1.00E-43"},9,1,"NAR1","Protein NAR1","_","4Fe-4S, Complete proteome, Cytoplasm, Iron, Iron-sulfur, Metal-binding, Nucleus, Reference proteome","9461215, 10617198, 27862469, 11910074, 14593172, 18493040, 18329103, 23104832, 23734982, 23639116","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia",103,455,462,90,460,474]
[null,"A4FV58","_",0.7479,0.77056,28.93,{"v":3E-43,"d":"3.00E-43"},10,1,"CIAO3","Cytosolic iron-sulfur assembly component 3","_","4Fe-4S, Acetylation, Alternative splicing, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome",19390049,"Bos taurus","Hereford",110,455,462,113,462,476]
[null,"Q9H6Q4","IPMed?",0.83193,0.85714,27.27,{"v":6e-42,"d":"6.00E-42"},11,1,"CIAO3","Cytosolic iron-sulfur assembly component 3","_","4Fe-4S, Acetylation, Alternative splicing, Complete proteome, Iron, Iron-sulfur, Metal-binding, Polymorphism, Reference proteome","14702039, 11157797, 15616553, 15489334, 16956324, 18270200, 20068231, 21269460, 22678362, 22678361, 23585563","Homo sapiens","_",77,455,462,76,462,476]
[null,"Q9UHQ1","IPMed?",0.84416,0.85526,26.15,{"v":4e-38,"d":"4.00E-38"},12,1,"NARF","Nuclear prelamin A recognition factor","_","Alternative splicing, Complete proteome, Nucleus, Phosphoprotein, Reference proteome","10514485, 14702039, 16625196, 15489334, 23186163","Homo sapiens","_",91,460,462,72,447,456]
[null,"Q9N392","IPMed?",0.64935,0.65646,28.67,{"v":4e-25,"d":"4.00E-25"},13,1,"oxy-4","Probable cytosolic Fe-S cluster assembly factor oxy-4","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome","9851916, 19335616","Caenorhabditis elegans","Bristol N2",137,414,462,131,410,457]
[null,"P23503","IPMed?",0.78004,0.829,22.19,{"v":9e-16,"d":"9.00E-16"},14,1,"NAR1","Cytosolic Fe-S cluster assembly factor NAR1","_","4Fe-4S, Complete proteome, Cytoplasm, Iron, Iron-sulfur, Metal-binding, Nucleus, Reference proteome","8896273, 9169873, 24374639, 17322287, 2269430, 15103330, 15667273, 16314508, 19385603","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 204508 / S288c",63,392,462,50,421,491]
[null,"P07603","IPMed?",0.11255,0.42276,44.23,1e-07,15,1,"hydB","Periplasmic [Fe] hydrogenase small subunit","1.12.7.2","3D-structure, Complete proteome, Direct protein sequencing, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Periplasm, Reference proteome, Signal","3888621, 15077118, 3322275, 3525521, 10368269","Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)","Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303",409,460,462,46,97,123]
[]
[]
["CLOSTRIBL3_v1_10094","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P0AAK5","_",0.85946,0.90857,40.25,{"v":6e-36,"d":"6.00E-36"},1,2,"hydN","Electron transport protein HydN","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",12471157,"Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","CFT073 / ATCC 700928 / UPEC",5,162,185,1,156,175]
[null,"P0AAK6","_",0.85946,0.90857,40.25,{"v":6e-36,"d":"6.00E-36"},1,2,"hydN","Electron transport protein HydN","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",5,162,185,1,156,175]
[null,"P0AAK4","IPMed?",0.85946,0.90857,40.25,{"v":6e-36,"d":"6.00E-36"},1,2,"hydN","Electron transport protein HydN","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","9278503, 16738553, 8661925","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",5,162,185,1,156,175]
[null,"P56256","_",0.8973,1.05732,39.16,{"v":6e-35,"d":"6.00E-35"},2,2,"ysaA","Putative electron transport protein YsaA","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","8041620, 9278503, 16738553","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",5,170,185,1,151,157]
[null,"P37127","IPMed?",0.23824,0.84865,39.49,{"v":1e-33,"d":"1.00E-33"},3,6,"aegA","Protein AegA","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat","8955321, 9205837, 9278503, 16738553","Escherichia coli (strain K12)","K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",5,161,185,1,145,659]
[null,"P31894","IPMed?",0.85263,0.87568,37.65,{"v":3E-32,"d":"3.00E-32"},4,2,"cooF","Iron-sulfur protein","_","4Fe-4S, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",1644755,"Rhodospirillum rubrum","UR1",6,162,185,7,163,190]
[null,"P0AAK3","_",0.94581,1.03784,35.42,{"v":2e-30,"d":"2.00E-30"},5,2,"hycB","Formate hydrogenlyase subunit 2","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","12384590, 12704152","Shigella flexneri","301 / Serotype 2a / ATCC 700930 / 2457T / Serotype 2a",5,172,185,1,182,203]
[null,"P0AAK1","IPMed?",0.94581,1.03784,35.42,{"v":2e-30,"d":"2.00E-30"},5,2,"hycB","Formate hydrogenlyase subunit 2","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","2187144, 9278503, 16738553","Escherichia coli (strain K12)","K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",5,172,185,1,182,203]
[null,"P0AAK2","_",0.94581,1.03784,35.42,{"v":2e-30,"d":"2.00E-30"},5,2,"hycB","Formate hydrogenlyase subunit 2","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",12471157,"Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","CFT073 / ATCC 700928 / UPEC",5,172,185,1,182,203]
[null,"Q46819","_",0.9027,1.03086,34.73,{"v":2e-30,"d":"2.00E-30"},6,2,"ygfS","Putative electron transport protein YgfS","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","9278503, 16738553","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",5,170,185,1,150,162]
[null,"Q46820","_",0.25196,0.87027,35.4,{"v":3e-29,"d":"3.00E-29"},7,6,"ygfT","Uncharacterized protein YgfT","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat","9278503, 16738553","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",5,164,185,1,140,639]
[null,"P23481","IPMed?",0.87805,0.97297,32.78,{"v":2e-27,"d":"2.00E-27"},8,2,"hyfA","Hydrogenase-4 component A","1.-.-.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","2016588, 9205837, 9278503, 16738553, 9387241, 12426353, 14702328","Escherichia coli (strain K12)","K12 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12",5,161,185,1,170,205]
[null,"P20925","IPMed?",0.71892,0.84713,39.85,{"v":1e-24,"d":"1.00E-24"},9,2,"_","Frd operon probable iron-sulfur subunit A","_","4Fe-4S, Iron, Iron-sulfur, Metal-binding, Repeat",3308458,"Proteus vulgaris","_",49,177,185,18,150,157]
[null,"Q57713","_",0.9027,1.00602,36.53,{"v":1e-24,"d":"1.00E-24"},10,1,"_","Uncharacterized ferredoxin MJ0265","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport",8688087,"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440",9,172,185,6,137,166]
[null,"Q9HR73","IPMed?",0.64122,0.90811,30.95,{"v":2E-19,"d":"2.00E-19"},11,3,"dmsB","Putative dimethyl sulfoxide reductase iron-sulfur subunit B","_","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Transport","11016950, 15716436","Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)","ATCC 700922 / JCM 11081 / NRC-1 / ATCC 700922 / JCM 11081 / NRC-1",6,157,185,3,170,262]
[null,"P0A1I1","IPMed?",0.90104,0.93514,32.37,{"v":2E-19,"d":"2.00E-19"},12,4,"phsB","Thiosulfate reductase electron transfer subunit PhsB","_","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Transport","7751291, 7737516, 11677609, 3108233, 22081391","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / LT2 / LT2 / SGSC1412 / ATCC 700720 / LT2 / LT2",6,172,185,6,162,192]
[null,"P0AAJ5","IPMed?",0.63333,1.02703,31.05,{"v":3e-18,"d":"3.00E-18"},13,3,"fdoH","Formate dehydrogenase-O iron-sulfur subunit","_","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Transmembrane, Transmembrane helix, Transport","8346018, 9278503, 16738553, 8522521, 9852007","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",10,178,185,33,203,300]
[null,"O30080","IPMed?",0.72947,0.81622,31.79,{"v":4e-18,"d":"4.00E-18"},14,4,"ttrB","Tetrathionate reductase subunit B","_","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Signal, Transport","9389475, 22289056","Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)","ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126 / ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126",10,157,185,37,165,207]
[]
["CLOSTRIBL3_v1_10091","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q46505","IPMed?",0.81871,0.8589,40,{"v":1e-34,"d":"1.00E-34"},1,1,"hndA","NADP-reducing hydrogenase subunit HndA","1.12.1.3","2Fe-2S, 3D-structure, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase","7751270, 9703971, 16731971","Desulfovibrio fructosivorans","_",20,159,163,32,171,171]
[null,"Q1RJJ1","_",0.88623,0.90798,40.54,{"v":4e-30,"d":"4.00E-30"},2,1,"nuoE","NADH-quinone oxidoreductase subunit E","7.1.1.-","2Fe-2S, Complete proteome, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Translocase",16703114,"Rickettsia bellii (strain RML369-C)","RML369-C",16,160,163,18,165,167]
[null,"P19234","IPMed?",0.59274,0.90184,37.41,{"v":2e-28,"d":"2.00E-28"},3,1,"Ndufv2","NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial","1.6.99.3, 7.1.1.2","2Fe-2S, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Phosphoprotein, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","15489334, 2974699","Rattus norvegicus","_",19,163,163,65,211,248]
[null,"O66842","_",0.8589,0.875,40.71,{"v":2e-28,"d":"2.00E-28"},4,1,"nuoE","NADH-quinone oxidoreductase subunit E","7.1.1.-","2Fe-2S, 3D-structure, Complete proteome, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Reference proteome, Translocase",9537320,"Aquifex aeolicus (strain VF5)","VF5",20,159,163,20,159,160]
[null,"P04394","IPMed?",0.59036,0.90184,36.05,{"v":5e-28,"d":"5.00E-28"},5,1,"NDUFV2","NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial","1.6.99.3, 7.1.1.2","2Fe-2S, 3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Phosphoprotein, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","2500970, 2598272, 6861757, 10852722, 18721790","Bos taurus","_",19,163,163,66,212,249]
[null,"Q20719","_",0.77824,1.1411,32.8,{"v":8e-28,"d":"8.00E-28"},6,1,"_","Probable NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial","1.6.99.3, 7.1.1.2","2Fe-2S, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone",9851916,"Caenorhabditis elegans","Bristol N2",2,163,163,16,201,239]
[null,"Q9D6J6","_",0.59274,0.90184,36.05,{"v":9e-28,"d":"9.00E-28"},7,1,"Ndufv2","NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial","1.6.99.3, 7.1.1.2","2Fe-2S, 3D-structure, Acetylation, Alternative splicing, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Phosphoprotein, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","16141072, 15489334, 21183079, 23576753","Mus musculus","C57BL/6J / FVB/N-3",19,163,163,65,211,248]
[null,"Q4UM09","_",0.88024,0.90184,38.78,{"v":1E-27,"d":"1.00E-27"},8,1,"nuoE","NADH-quinone oxidoreductase subunit E","7.1.1.-","2Fe-2S, Complete proteome, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Translocase",15984913,"Rickettsia felis (strain ATCC VR-1525 / URRWXCal2)","ATCC VR-1525 / URRWXCal2",16,159,163,15,161,167]
[null,"P19404","IPMed?",0.59036,0.90184,35.37,{"v":7e-27,"d":"7.00E-27"},9,1,"NDUFV2","NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial","1.6.99.3, 7.1.1.2","2Fe-2S, 3D-structure, Acetylation, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Phosphoprotein, Polymorphism, Primary mitochondrial disease, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","2500970, 15489334, 12611891, 21269460, 22823520, 24275569, 25944712, 12754703, 26008862","Homo sapiens","_",19,163,163,66,212,249]
[null,"Q0MQI7","_",0.59036,0.90184,35.37,{"v":7e-27,"d":"7.00E-27"},9,1,"NDUFV2","NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial","1.6.99.3, 7.1.1.2","2Fe-2S, Acetylation, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Phosphoprotein, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone",16828987,"Pongo pygmaeus","_",19,163,163,66,212,249]
[null,"Q0MQI9","_",0.59036,0.90184,35.37,{"v":7e-27,"d":"7.00E-27"},9,1,"NDUFV2","NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial","1.6.99.3, 7.1.1.2","2Fe-2S, Acetylation, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Phosphoprotein, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone",16828987,"Pan troglodytes","_",19,163,163,66,212,249]
[null,"Q0MQI8","_",0.59036,0.90184,35.37,{"v":7e-27,"d":"7.00E-27"},9,1,"NDUFV2","NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial","1.6.99.3, 7.1.1.2","2Fe-2S, Acetylation, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Phosphoprotein, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone",16828987,"Gorilla gorilla gorilla","_",19,163,163,66,212,249]
[null,"Q9ZDH5","_",0.83051,0.90184,37.41,{"v":9e-26,"d":"9.00E-26"},10,1,"nuoE","NADH-quinone oxidoreductase subunit E","7.1.1.-","2Fe-2S, Complete proteome, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Reference proteome, Translocase",9823893,"Rickettsia prowazekii (strain Madrid E)","Madrid E",16,159,163,20,166,177]
[null,"P0AFD1","IPMed?",0.92771,0.94479,35.06,{"v":8e-25,"d":"8.00E-25"},11,1,"nuoE","NADH-quinone oxidoreductase subunit E","7.1.1.-","2Fe-2S, Complete proteome, Direct protein sequencing, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Ubiquinone","7690854, 8157582, 9205837, 9278503, 16738553, 7607227","Escherichia coli (strain K12)","K12 / AN387 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",13,160,163,13,166,166]
[null,"P0A1Y8","IPMed?",0.92771,0.94479,35.06,{"v":1e-24,"d":"1.00E-24"},12,1,"nuoE","NADH-quinone oxidoreductase subunit E","7.1.1.-","2Fe-2S, Complete proteome, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Ubiquinone","8234329, 11677609","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720",13,160,163,13,166,166]
[null,"P40915","IPMed?",0.54753,0.88344,32.64,{"v":5e-22,"d":"5.00E-22"},13,1,"nuo-24","NADH-ubiquinone oxidoreductase 24 kDa subunit, mitochondrial","1.6.99.3, 7.1.1.2","2Fe-2S, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","7947902, 12655011, 12712197","Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)","ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987 / ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987",18,157,163,73,216,263]
[null,"Q56221","IPMed?",0.8232,0.91411,32.89,{"v":6e-20,"d":"6.00E-20"},14,1,"nqo2","NADH-quinone oxidoreductase subunit 2","7.1.1.-","2Fe-2S, 3D-structure, Cell membrane, Complete proteome, Direct protein sequencing, Disulfide bond, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Translocase","9020134, 16584177, 16469879","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","HB8 / ATCC 27634 / DSM 579 / HB8 / ATCC 27634 / DSM 579",18,163,163,13,161,181]
[null,"P29914","IPMed?",0.6318,0.92638,28.48,3e-14,15,1,"nqo2","NADH-quinone oxidoreductase chain 2","7.1.1.-","2Fe-2S, Cell inner membrane, Cell membrane, Direct protein sequencing, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Translocase, Ubiquinone","1909571, 7957917","Paracoccus denitrificans","ATCC 13543 / NRRL B-3784 / NRC 449",16,163,163,23,173,239]
[null,"P22317","IPMed?",0.24086,0.88957,26.9,5e-13,16,2,"hoxF","NAD-reducing hydrogenase HoxS subunit alpha","1.12.1.2","4Fe-4S, Complete proteome, Cytoplasm, Direct protein sequencing, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Oxidoreductase, Plasmid, Reference proteome","2188945, 12948488, 2496982","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337",19,163,163,8,152,602]
[]
["CLOSTRIBL3_v1_10092","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q46507","IPMed?",0.80634,0.98571,51.97,0,1,1,"hndC","NADP-reducing hydrogenase subunit HndC","1.12.1.3","4Fe-4S, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat","7751270, 9703971","Desulfovibrio fructosivorans","_",114,596,599,8,487,490]
[null,"P56913","_",0.69282,0.98575,45.54,{"v":1e-122,"d":"1.00E-122"},2,1,"nuoF2","NADH-quinone oxidoreductase subunit F 2","7.1.1.-","4Fe-4S, Complete proteome, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Plasmid, Quinone, Reference proteome, Translocase, Ubiquinone","11481432, 11474104","Rhizobium meliloti (strain 1021)","1021 / 1021",119,533,599,5,418,421]
[null,"Q56222","IPMed?",0.68948,0.94292,44.55,{"v":3e-116,"d":"3.00E-116"},3,1,"nqo1","NADH-quinone oxidoreductase subunit 1","7.1.1.-","3D-structure, 4Fe-4S, Cell membrane, Complete proteome, Direct protein sequencing, Flavoprotein, FMN, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Translocase","9020134, 16584177, 16469879","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","HB8 / ATCC 27634 / DSM 579 / HB8 / ATCC 27634 / DSM 579",123,532,599,20,429,438]
[null,"O66841","_",0.66277,0.93192,43.32,{"v":5e-106,"d":"5.00E-106"},4,1,"nuoF","NADH-quinone oxidoreductase subunit F","7.1.1.-","3D-structure, 4Fe-4S, Complete proteome, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Reference proteome, Translocase",9537320,"Aquifex aeolicus (strain VF5)","VF5",131,527,599,30,417,426]
[null,"Q9XAQ9","_",0.68114,0.90869,39.46,{"v":4e-102,"d":"4.00E-102"},5,1,"nuoF","NADH-quinone oxidoreductase subunit F","7.1.1.-","4Fe-4S, Complete proteome, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Reference proteome, Translocase",12000953,"Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)","ATCC BAA-471 / A3(2) / M145",126,533,599,27,431,449]
[null,"P31979","IPMed?",0.67279,0.90562,39.45,{"v":3e-100,"d":"3.00E-100"},6,1,"nuoF","NADH-quinone oxidoreductase subunit F","7.1.1.-","4Fe-4S, Complete proteome, Direct protein sequencing, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Ubiquinone","7690854, 8157582, 9205837, 9278503, 16738553, 8366049, 7607227","Escherichia coli (strain K12)","K12 / AN387 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / W3110 / ATCC 27325 / DSM 5911",129,529,599,23,424,445]
[null,"P33901","IPMed?",0.67279,0.90562,39.21,{"v":7e-100,"d":"7.00E-100"},7,1,"nuoF","NADH-quinone oxidoreductase subunit F","7.1.1.-","4Fe-4S, Complete proteome, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Ubiquinone","8234329, 11677609","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720",129,529,599,23,424,445]
[null,"P9WIV7","_",0.66444,0.89438,41.96,{"v":4e-98,"d":"4.00E-98"},8,1,"nuoF","NADH-quinone oxidoreductase subunit F","7.1.1.-","4Fe-4S, Complete proteome, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Reference proteome, Translocase","9634230, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",140,533,599,35,429,445]
[null,"P9WIV6","_",0.66444,0.89438,41.96,{"v":4e-98,"d":"4.00E-98"},8,1,"nuoF","NADH-quinone oxidoreductase subunit F","7.1.1.-","4Fe-4S, Complete proteome, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Translocase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",140,533,599,35,429,445]
[null,"P65568","_",0.66444,0.89438,41.96,{"v":4e-98,"d":"4.00E-98"},8,1,"nuoF","NADH-quinone oxidoreductase subunit F","7.1.1.-","4Fe-4S, Complete proteome, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Translocase","12788972, 28385856","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97",140,533,599,35,429,445]
[null,"Q8K9Y3","_",0.67613,0.90604,39.51,{"v":5e-96,"d":"5.00E-96"},9,1,"nuoF","NADH-quinone oxidoreductase subunit F","7.1.1.-","4Fe-4S, Complete proteome, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Translocase",12089438,"Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)","Sg",132,534,599,26,430,447]
[null,"Q9I0J7","_",0.6778,0.90625,39.16,{"v":8e-96,"d":"8.00E-96"},10,1,"nuoF","NADH-quinone oxidoreductase subunit F","7.1.1.-","4Fe-4S, Complete proteome, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Ubiquinone",10984043,"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1",126,528,599,28,433,448]
[null,"A8GQT6","IPMed?",0.64441,0.91686,40.16,{"v":3e-89,"d":"3.00E-89"},11,1,"nuoF","NADH-quinone oxidoreductase subunit F","7.1.1.-","4Fe-4S, Complete proteome, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Translocase",12867468,"Rickettsia rickettsii (strain Sheila Smith)","_",146,530,599,33,417,421]
[null,"Q91YT0","IPMed?",0.64608,0.83405,41.09,{"v":8e-88,"d":"8.00E-88"},12,1,"Ndufv1","NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial","1.6.99.3, 7.1.1.2","3D-structure, 4Fe-4S, Acetylation, Complete proteome, Direct protein sequencing, Electron transport, Flavoprotein, FMN, Iron, Iron-sulfur, Membrane, Metal-binding, Methylation, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","16141072, 15489334, 10870971, 21183079, 23806337, 23576753, 24129315","Mus musculus","C57BL/6J / FVB/N / C57BL/6J",146,529,599,66,451,464]
[null,"P25708","IPMed?",0.64608,0.83405,41.09,{"v":8e-88,"d":"8.00E-88"},12,1,"NDUFV1","NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial","1.6.99.3, 7.1.1.2","3D-structure, 4Fe-4S, Acetylation, Complete proteome, Direct protein sequencing, Electron transport, Flavoprotein, FMN, Iron, Iron-sulfur, Membrane, Metal-binding, Methylation, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","2034666, 1900194, 10852722, 18721790","Bos taurus","_",146,529,599,66,451,464]
[null,"P49821","IPMed?",0.64608,0.83405,41.09,{"v":6e-87,"d":"6.00E-87"},13,1,"NDUFV1","NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial","1.6.99.3, 7.1.1.2","3D-structure, 4Fe-4S, Acetylation, Alternative splicing, Complete proteome, Disease mutation, Electron transport, Flavoprotein, FMN, Iron, Iron-sulfur, Leigh syndrome, Membrane, Metal-binding, Methylation, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Polymorphism, Primary mitochondrial disease, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","9892733, 9571201, 10931946, 15489334, 1478657, 8288251, 12611891, 21269460, 24275569, 25944712, 10080174, 11349233","Homo sapiens","_",146,529,599,66,451,464]
[null,"Q54I90","IPMed?",0.70117,0.87683,39.29,{"v":5e-86,"d":"5.00E-86"},14,1,"ndufv1","NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial","1.6.99.3, 7.1.1.2","4Fe-4S, Complete proteome, Electron transport, Flavoprotein, FMN, Iron, Iron-sulfur, Membrane, Metal-binding, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","8643615, 15875012","Dictyostelium discoideum","AX4 / AX4",114,529,599,52,468,479]
[null,"O07948","IPMed?",0.63439,0.88167,38.42,{"v":1E-84,"d":"1.00E-84"},15,1,"nuoF","NADH-quinone oxidoreductase subunit F","7.1.1.-","4Fe-4S, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Translocase, Ubiquinone",9108316,"Rhodobacter capsulatus","ATCC 33303 / B10",156,532,599,43,421,431]
[null,"P22317","IPMed?",0.66113,0.66444,36.93,{"v":6e-84,"d":"6.00E-84"},16,1,"hoxF","NAD-reducing hydrogenase HoxS subunit alpha","1.12.1.2","4Fe-4S, Complete proteome, Cytoplasm, Direct protein sequencing, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Oxidoreductase, Plasmid, Reference proteome","2188945, 12948488, 2496982","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337",138,534,599,190,572,602]
[]
["CLOSTRIBL3_v1_10093","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P56914","_",0.26964,0.91633,29.57,{"v":5e-19,"d":"5.00E-19"},1,3,"nuoG2","NADH-quinone oxidoreductase subunit G 2","7.1.1.-","2Fe-2S, 4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, NAD, Plasmid, Quinone, Reference proteome, Repeat, Translocase, Ubiquinone","11481432, 11474104","Rhizobium meliloti (strain 1021)","1021 / 1021",1,206,251,2,228,853]
[null,"Q46508","IPMed?",0.35897,0.83665,30.95,{"v":9e-19,"d":"9.00E-19"},2,4,"hndD","NADP-reducing hydrogenase subunit HndD","1.12.1.3","2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat","7751270, 9703971","Desulfovibrio fructosivorans","_",1,181,251,4,211,585]
[null,"Q74FU6","IPMed?",0.27962,0.94024,26.69,{"v":7e-17,"d":"7.00E-17"},3,4,"sfrA","NADPH-Fe(3+) oxidoreductase subunit alpha","1.-.-.-","2Fe-2S, 4Fe-4S, Cell membrane, Complete proteome, Cytoplasm, Direct protein sequencing, Iron, Iron-sulfur, Membrane, Metal-binding, Oxidoreductase, Reference proteome, Repeat","14671304, 11443080, 17906154","Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)","ATCC 51573 / DSM 12127 / PCA / ATCC 51573 / DSM 12127 / PCA / DL-1 / KN400",1,214,251,2,234,844]
[null,"D7AF63","IPMed?",0.27962,0.94024,26.69,{"v":7e-17,"d":"7.00E-17"},3,4,"sfrA","NADPH-Fe(3+) oxidoreductase subunit alpha","1.-.-.-","2Fe-2S, 4Fe-4S, Cell membrane, Iron, Iron-sulfur, Membrane, Metal-binding, Oxidoreductase, Repeat","20544019, 17906154","Geobacter sulfurreducens (strain DL-1 / KN400)","DL-1 / KN400 / DL-1 / KN400",1,214,251,2,234,844]
[null,"Q4L8G8","_",0.21646,0.84861,24.41,8e-15,4,6,"_","Putative formate dehydrogenase SH0748","1.17.1.9","2Fe-2S, 4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD, Oxidoreductase, Repeat",16237012,"Staphylococcus haemolyticus (strain JCSC1435)","JCSC1435",3,188,251,7,212,984]
[null,"Q49ZN0","_",0.21748,0.85259,25.23,1E-14,5,5,"_","Putative formate dehydrogenase SSP0601","1.17.1.9","2Fe-2S, 4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD, Oxidoreductase, Reference proteome, Repeat",16135568,"Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41)","ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41",3,188,251,7,212,984]
[null,"Q7A057","_",0.21748,0.85259,24.77,3e-14,6,6,"_","Putative formate dehydrogenase MW2229","1.17.1.9","2Fe-2S, 4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD, Oxidoreductase, Repeat",12044378,"Staphylococcus aureus (strain MW2)","MW2",3,188,251,7,212,984]
[null,"Q6G711","_",0.21748,0.85259,24.77,3e-14,6,6,"_","Putative formate dehydrogenase SAS2201","1.17.1.9","2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD, Oxidoreductase, Repeat",15213324,"Staphylococcus aureus (strain MSSA476)","MSSA476",3,188,251,7,212,984]
[null,"Q99RW4","_",0.21748,0.85259,24.77,3e-14,6,6,"_","Putative formate dehydrogenase SA2102","1.17.1.9","2Fe-2S, 4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD, Oxidoreductase, Repeat",11418146,"Staphylococcus aureus (strain N315)","N315",3,188,251,7,212,984]
[null,"Q931G2","_",0.21748,0.85259,24.77,3e-14,6,6,"_","Putative formate dehydrogenase SAV2309","1.17.1.9","2Fe-2S, 4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD, Oxidoreductase, Repeat",11418146,"Staphylococcus aureus (strain Mu50 / ATCC 700699)","Mu50 / ATCC 700699",3,188,251,7,212,984]
[null,"Q5HDP9","_",0.21748,0.85259,24.77,3e-14,6,6,"_","Putative formate dehydrogenase SACOL2301","1.17.1.9","2Fe-2S, 4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD, Oxidoreductase, Repeat",15774886,"Staphylococcus aureus (strain COL)","COL",3,188,251,7,212,984]
[null,"Q6GEC4","_",0.21748,0.85259,24.77,4E-14,7,6,"_","Putative formate dehydrogenase SAR2393","1.17.1.9","2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD, Oxidoreductase, Repeat",15213324,"Staphylococcus aureus (strain MRSA252)","MRSA252",3,188,251,7,212,984]
[null,"P22318","IPMed?",0.65339,0.70085,31.1,4e-13,8,1,"hoxU","NAD-reducing hydrogenase HoxS subunit gamma","1.12.1.2","2Fe-2S, 4Fe-4S, Complete proteome, Cytoplasm, Direct protein sequencing, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Oxidoreductase, Plasmid, Reference proteome","2188945, 12948488, 2496982","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337",1,142,251,3,161,234]
[null,"P15690","IPMed?",0.24622,0.71315,25.7,1e-12,9,1,"NDUFS1","NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial","1.6.99.3, 7.1.1.2","2Fe-2S, 3D-structure, 4Fe-4S, Acetylation, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","2514801, 10852722, 18721790","Bos taurus","_",1,157,251,32,208,727]
[null,"P28331","IPMed?",0.24622,0.71315,25.14,3e-12,10,1,"NDUFS1","NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial","1.6.99.3, 7.1.1.2","2Fe-2S, 3D-structure, 4Fe-4S, Acetylation, Alternative splicing, Complete proteome, Direct protein sequencing, Disease mutation, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Polymorphism, Primary mitochondrial disease, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","1935949, 14702039, 15815621, 15489334, 12611891, 21269460, 24275569, 25944712, 11349233, 22499341","Homo sapiens","_",1,157,251,32,208,727]
[null,"P24918","IPMed?",0.2957,0.87649,23.18,2e-10,11,1,"nuo78","NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial","1.6.99.3, 7.1.1.2","2Fe-2S, 4Fe-4S, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","1832016, 12655011, 12712197","Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)","74-ORS-6a / FGSC 4200 / ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987 / ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987",1,196,251,36,252,744]
[null,"Q94511","IPMed?",0.25034,0.72908,24.59,3e-08,12,1,"ND-75","NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial","1.6.99.3, 7.1.1.2","2Fe-2S, 4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","10731132, 12537572, 10071211","Drosophila melanogaster","Berkeley / Berkeley",1,157,251,42,222,731]
[null,"P29915","IPMed?",0.31204,0.83665,23.81,1e-07,13,1,"nqo3","NADH-quinone oxidoreductase chain 3","7.1.1.-","2Fe-2S, 4Fe-4S, Cell inner membrane, Cell membrane, Direct protein sequencing, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Translocase, Ubiquinone","1605643, 8422400, 7629145, 12600982","Paracoccus denitrificans","ATCC 13543 / NRRL B-3784 / NRC 449",2,181,251,6,213,673]
[null,"Q00388","IPMed?",0.41206,0.65339,28.05,5e-06,14,10,"vhuB","Polyferredoxin protein VhuB","_","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",1603063,"Methanococcus voltae","ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS",56,207,251,191,353,398]
[null,"P9WIV9","IPMed?",0.2531,0.81275,24.51,1e-05,15,2,"nuoG","NADH-quinone oxidoreductase subunit G","7.1.1.-","2Fe-2S, 4Fe-4S, Acetylation, Complete proteome, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Virulence","9634230, 17658950, 20421951, 21969609, 22264515","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv / ATCC 25618 / H37Rv / ATCC 25618 / H37Rv / H37Rv",3,181,251,19,219,806]
[]
["CLOSTRIBL3_v1_13020","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P29166","IPMed?",0.74564,0.95323,28.27,{"v":4e-31,"d":"4.00E-31"},1,3,"_","Iron hydrogenase 1","1.12.7.2","3D-structure, 4Fe-4S, Direct protein sequencing, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Repeat","1911757, 9836629, 10529166","Clostridium pasteurianum","ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5",35,404,449,102,524,574]
[null,"P07598","IPMed?",0.85078,0.90736,27.75,{"v":3E-24,"d":"3.00E-24"},2,2,"hydA","Periplasmic [Fe] hydrogenase large subunit","1.12.7.2","3D-structure, 4Fe-4S, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Periplasm, Reference proteome, Repeat, Transport","3888621, 15077118, 3322275, 11456963, 10368269, 11456758","Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)","Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303",68,394,449,14,392,421]
[null,"Q46508","IPMed?",0.55214,0.71938,26.32,{"v":9e-22,"d":"9.00E-22"},3,3,"hndD","NADP-reducing hydrogenase subunit HndD","1.12.1.3","2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat","7751270, 9703971","Desulfovibrio fructosivorans","_",119,388,449,196,517,585]
[null,"P13629","IPMed?",0.85078,0.90736,27.75,{"v":7e-21,"d":"7.00E-21"},4,3,"hydA","Periplasmic [Fe] hydrogenase large subunit","1.12.7.2","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Periplasm, Repeat, Transport",2661538,"Desulfovibrio oxamicus (strain Monticello)","_",66,394,449,12,392,421]
[null,"Q94CL6","IPMed?",0.79958,0.8441,20.84,3e-08,5,3,"NAR1","Protein NAR1","_","4Fe-4S, Complete proteome, Cytoplasm, Iron, Iron-sulfur, Metal-binding, Nucleus, Reference proteome","9461215, 10617198, 27862469, 11910074, 14593172, 18493040, 18329103, 23104832, 23734982, 23639116","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia",88,395,449,29,404,474]
[null,"Q9H6Q4","IPMed?",0.71639,0.75947,23.17,6e-08,6,2,"CIAO3","Cytosolic iron-sulfur assembly component 3","_","4Fe-4S, Acetylation, Alternative splicing, Complete proteome, Iron, Iron-sulfur, Metal-binding, Polymorphism, Reference proteome","14702039, 11157797, 15616553, 15489334, 16956324, 18270200, 20068231, 21269460, 22678362, 22678361, 23585563","Homo sapiens","_",114,388,449,66,402,476]
[null,"Q9UHQ1","IPMed?",0.83991,0.85301,22.72,5e-07,7,2,"NARF","Nuclear prelamin A recognition factor","_","Alternative splicing, Complete proteome, Nucleus, Phosphoprotein, Reference proteome","10514485, 14702039, 16625196, 15489334, 23186163","Homo sapiens","_",77,388,449,2,381,456]
[null,"B6K2N0","_",0.20971,0.24053,30.56,2e-06,8,2,"_","Cytosolic Fe-S cluster assembly factor NAR1 homolog","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome",21511999,"Schizosaccharomyces japonicus (strain yFS275 / FY16936)","yFS275 / FY16936",212,307,449,183,290,515]
[null,"Q9Y7N7","_",0.20074,0.24053,32.41,5e-06,9,2,"_","Cytosolic Fe-S cluster assembly factor NAR1 homolog","_","4Fe-4S, Complete proteome, Cytoplasm, Iron, Iron-sulfur, Metal-binding, Nucleus, Reference proteome","11859360, 16823372","Schizosaccharomyces pombe (strain 972 / ATCC 24843)","972 / ATCC 24843",216,311,449,213,320,538]
[null,"H6LGM8","IPMed?",0.1069,0.12121,45.83,1e-05,10,11,"carE","Caffeyl-CoA reductase-Etf complex subunit CarE","1.3.1.108","3D-structure, 4Fe-4S, Complete proteome, Cytoplasm, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",90,137,449,12,56,396]
[null,"Q9N392","IPMed?",0.73523,0.74833,21.13,6e-05,11,3,"oxy-4","Probable cytosolic Fe-S cluster assembly factor oxy-4","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome","9851916, 19335616","Caenorhabditis elegans","Bristol N2",109,388,449,61,387,457]
[null,"P0A1I1","IPMed?",0.3029,0.70833,23.53,8e-05,12,5,"phsB","Thiosulfate reductase electron transfer subunit PhsB","_","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Transport","7751291, 7737516, 11677609, 3108233, 22081391","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / LT2 / LT2 / SGSC1412 / ATCC 700720 / LT2 / LT2",40,167,449,20,152,192]
[]
["CLOSTRIBL3_v1_20317","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P29166","IPMed?",0.68118,0.78831,26.6,{"v":2e-31,"d":"2.00E-31"},1,2,"_","Iron hydrogenase 1","1.12.7.2","3D-structure, 4Fe-4S, Direct protein sequencing, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Repeat","1911757, 9836629, 10529166","Clostridium pasteurianum","ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5",124,456,496,126,508,574]
[null,"Q46508","IPMed?",0.70769,0.83468,28.5,{"v":8e-27,"d":"8.00E-27"},2,2,"hndD","NADP-reducing hydrogenase subunit HndD","1.12.1.3","2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat","7751270, 9703971","Desulfovibrio fructosivorans","_",138,485,496,149,552,585]
[null,"P13629","IPMed?",0.72782,0.85748,26.04,{"v":3E-23,"d":"3.00E-23"},3,2,"hydA","Periplasmic [Fe] hydrogenase large subunit","1.12.7.2","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Periplasm, Repeat, Transport",2661538,"Desulfovibrio oxamicus (strain Monticello)","_",164,464,496,41,397,421]
[null,"P07598","IPMed?",0.73185,0.86223,28.1,{"v":8e-23,"d":"8.00E-23"},4,3,"hydA","Periplasmic [Fe] hydrogenase large subunit","1.12.7.2","3D-structure, 4Fe-4S, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Periplasm, Reference proteome, Repeat, Transport","3888621, 15077118, 3322275, 11456963, 10368269, 11456758","Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)","Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303",164,464,496,41,397,421]
[null,"Q94CL6","IPMed?",0.69556,0.72785,25.22,9E-13,5,2,"NAR1","Protein NAR1","_","4Fe-4S, Complete proteome, Cytoplasm, Iron, Iron-sulfur, Metal-binding, Nucleus, Reference proteome","9461215, 10617198, 27862469, 11910074, 14593172, 18493040, 18329103, 23104832, 23734982, 23639116","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia",184,456,496,56,399,474]
[null,"P81292","_",0.21774,0.66258,35.19,1e-11,6,1,"_","Uncharacterized polyferredoxin-like protein MJ0514.1","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport",8688087,"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440",109,206,496,37,133,163]
[null,"P0AAK4","IPMed?",0.2379,0.67429,33.9,2e-10,7,5,"hydN","Electron transport protein HydN","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","9278503, 16738553, 8661925","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",106,215,496,53,165,175]
[null,"P0AAK5","_",0.2379,0.67429,33.9,2e-10,7,5,"hydN","Electron transport protein HydN","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",12471157,"Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","CFT073 / ATCC 700928 / UPEC",106,215,496,53,165,175]
[null,"P0AAK6","_",0.2379,0.67429,33.9,2e-10,7,5,"hydN","Electron transport protein HydN","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",106,215,496,53,165,175]
[null,"P60232","IPMed?",0.22581,0.27184,33.93,6E-10,8,1,"mvhB","Polyferredoxin protein MvhB","_","4Fe-4S, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport","20802048, 1312016","Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)","ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg / ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg",111,218,496,146,246,412]
[null,"Q00388","IPMed?",0.375,0.46734,29.03,1e-09,9,4,"vhuB","Polyferredoxin protein VhuB","_","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",1603063,"Methanococcus voltae","ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS",137,307,496,6,188,398]
[null,"Q58593","_",0.35685,0.44924,27.68,2e-09,10,2,"vhuB","Polyferredoxin protein VhuB","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport",8688087,"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440",72,204,496,153,321,394]
[null,"Q49180","IPMed?",0.22177,0.26699,30,5e-09,11,2,"mvhB","Polyferredoxin protein MvhB","_","4Fe-4S, Iron, Iron-sulfur, Metal-binding, Repeat",2115877,"Methanothermus fervidus","_",111,218,496,146,245,412]
[null,"P0AAL6","IPMed?",0.19758,0.47115,32.65,7e-09,12,5,"ydhY","Uncharacterized ferredoxin-like protein YdhY","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat","9097039, 9023191, 9278503, 16738553, 18227264","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",109,204,496,121,198,208]
[]
["CLOSTRIBL3_v1_12009","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P38135","IPMed?",0.96113,0.97143,44.49,{"v":3e-167,"d":"3.00E-167"},1,1,"fadK","Medium-chain fatty-acid--CoA ligase","6.2.1.-","ATP-binding, Cell membrane, Complete proteome, Fatty acid metabolism, Ligase, Lipid metabolism, Magnesium, Membrane, Nucleotide-binding, Reference proteome","9097039, 9278503, 16738553, 7984428, 12535077, 15213221, 19477415","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / MC1061 / ATCC 53338 / DSM 7140",5,548,560,23,563,566]
[null,"O31826","IPMed?",0.92857,0.94718,32.12,{"v":1e-68,"d":"1.00E-68"},2,2,"yngI","Putative acyl-CoA synthetase YngI","6.2.1.-","ATP-binding, Complete proteome, Ligase, Nucleotide-binding, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",37,534,560,20,537,549]
[null,"P40871","IPMed?",0.94464,0.98145,26.47,{"v":9e-58,"d":"9.00E-58"},3,1,"dhbE","2,3-dihydroxybenzoate-AMP ligase","6.3.2.-","3D-structure, ATP-binding, Complete proteome, Cytoplasm, Ligase, Nucleotide-binding, Reference proteome","8921902, 9384377, 8224884, 12221282","Bacillus subtilis (strain 168)","168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501 / 168 / 168",15,540,560,16,533,539]
[null,"Q8VCW8","_",0.87805,0.96429,28.89,{"v":4e-56,"d":"4.00E-56"},4,2,"Acsf2","Medium-chain acyl-CoA ligase ACSF2, mitochondrial","6.2.1.2","Acetylation, ATP-binding, Complete proteome, Fatty acid metabolism, Ligase, Lipid metabolism, Mitochondrion, Nucleotide-binding, Reference proteome, Transit peptide","16141072, 19468303, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / C57BL/6J / FVB/N",31,537,560,79,610,615]
[null,"Q4WR83","IPMed?",0.90847,0.95714,28.54,{"v":9e-55,"d":"9.00E-55"},5,2,"sidI","Acyl-CoA ligase sidI","6.2.1.-","ATP-binding, Complete proteome, Ligase, Nucleotide-binding, Peroxisome, Reference proteome","16372009, 15504822, 16113265, 17845073, 18721228, 21622789, 22106303, 23617799","Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)","ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100",23,534,560,36,571,590]
[null,"Q96CM8","IPMed?",0.88618,0.97321,28.26,{"v":6e-54,"d":"6.00E-54"},6,2,"ACSF2","Medium-chain acyl-CoA ligase ACSF2, mitochondrial","6.2.1.2","Acetylation, Alternative splicing, ATP-binding, Complete proteome, Fatty acid metabolism, Ligase, Lipid metabolism, Mitochondrion, Nucleotide-binding, Polymorphism, Reference proteome, Transit peptide","12975309, 14702039, 16625196, 15489334, 16380219, 17762044, 24275569, 25944712","Homo sapiens","_",24,541,560,72,614,615]
[null,"Q17QJ1","_",0.89756,0.98571,27.17,{"v":8e-54,"d":"8.00E-54"},7,2,"ACSF2","Medium-chain acyl-CoA ligase ACSF2, mitochondrial","6.2.1.2","Acetylation, ATP-binding, Complete proteome, Fatty acid metabolism, Ligase, Lipid metabolism, Mitochondrion, Nucleotide-binding, Reference proteome, Transit peptide","_","Bos taurus","_",23,541,560,71,614,615]
[null,"Q4R4Z9","_",0.85761,0.94643,28.68,{"v":9e-54,"d":"9.00E-54"},8,2,"ACSF2","Medium-chain acyl-CoA ligase ACSF2, mitochondrial","6.2.1.2","Acetylation, ATP-binding, Complete proteome, Fatty acid metabolism, Ligase, Lipid metabolism, Mitochondrion, Nucleotide-binding, Reference proteome, Transit peptide","_","Macaca fascicularis","_",39,541,560,90,617,618]
[null,"Q0S7V5","IPMed?",0.925,1.00583,28.76,{"v":2e-53,"d":"2.00E-53"},9,2,"fadD3","3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoyl:CoA ligase","6.2.1.41","ATP-binding, Cholesterol metabolism, Complete proteome, Ligase, Lipid metabolism, Nucleotide-binding, Steroid metabolism, Sterol metabolism","17030794, 23146019","Rhodococcus jostii (strain RHA1)","RHA1 / RHA1",38,537,560,15,515,515]
[null,"O07899","IPMed?",0.94286,0.97238,27.08,{"v":1E-52,"d":"1.00E-52"},10,1,"vibE","Vibriobactin-specific 2,3-dihydroxybenzoate-AMP ligase","6.3.2.-","Cell inner membrane, Cell membrane, Complete proteome, Ligase, Membrane, Reference proteome, Transmembrane, Transmembrane helix","9371453, 10952301","Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","El Tor Lou15 / ATCC 39315 / El Tor Inaba N16961",15,533,560,16,531,543]
[null,"P96843","IPMed?",0.89286,0.98619,28.4,{"v":2E-51,"d":"2.00E-51"},11,2,"fadD3","3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoyl:CoA ligase","6.2.1.41","ATP-binding, Cholesterol metabolism, Complete proteome, Ligase, Lipid metabolism, Nucleotide-binding, Reference proteome, Steroid metabolism, Sterol metabolism","9634230, 12368430, 21969609, 23146019","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",43,534,560,26,505,507]
[null,"O07610","IPMed?",0.9,0.98246,28.57,{"v":4E-51,"d":"4.00E-51"},12,3,"lcfB","Long-chain-fatty-acid--CoA ligase","6.2.1.3","ATP-binding, Complete proteome, Fatty acid metabolism, Ligase, Lipid degradation, Lipid metabolism, Nucleotide-binding, Reference proteome","9579061, 9384377, 19383706, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",47,536,560,23,511,513]
[null,"A4YDR9","IPMed?",0.95893,0.97814,30.54,{"v":1e-49,"d":"1.00E-49"},13,1,"_","4-hydroxybutyrate--CoA ligase 2","6.2.1.40","ATP-binding, Complete proteome, Fatty acid metabolism, Ligase, Lipid metabolism, Magnesium, Nucleotide-binding, Reference proteome","18083856, 23258541","Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)","ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2 / ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2",35,544,560,33,548,549]
[]
["CLOSTRIBL3_v1_10745","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P71103","IPMed?",0.99099,0.99698,69.7,{"v":1e-163,"d":"1.00E-163"},1,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","8702268, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,330,331,1,330,333]
[null,"Q59330","_",0.99698,1.0061,63.94,{"v":1e-143,"d":"1.00E-143"},2,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",1,330,331,1,328,328]
[null,"O52593","_",0.99398,0.99698,55.45,{"v":7e-122,"d":"7.00E-122"},3,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","_","Hungateiclostridium thermocellum (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)","_",1,330,331,1,328,332]
[null,"P38503","IPMed?",0.97898,0.98489,57.06,{"v":1e-118,"d":"1.00E-118"},4,1,"pta","Phosphate acetyltransferase","2.3.1.8","3D-structure, Acyltransferase, Cell membrane, Direct protein sequencing, Membrane, Transferase","8226623, 9401029, 15062079","Methanosarcina thermophila","ATCC 43570 / DSM 1825 / OCM 12 / TM-1",4,329,331,5,328,333]
[null,"Q726S7","_",0.45455,0.96677,51.25,{"v":4e-100,"d":"4.00E-100"},5,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",15077118,"Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)","Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303",11,330,331,386,698,704]
[null,"P77844","IPMed?",0.96979,0.97568,47.66,{"v":6e-95,"d":"6.00E-95"},6,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","10075432, 12743753, 12948626, 15090522, 16179344, 16547043","Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)","ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025",11,331,331,14,327,329]
[null,"Q9ZKU4","_",0.61657,0.96677,49.69,{"v":1e-94,"d":"1.00E-94"},7,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",9923682,"Helicobacter pylori (strain J99 / ATCC 700824)","J99 / ATCC 700824",11,330,331,205,517,519]
[null,"P39646","_",0.94562,0.96904,49.84,{"v":4e-94,"d":"4.00E-94"},8,1,"pta","Phosphate acetyltransferase","2.3.1.8","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","7934828, 9384377, 9298659","Bacillus subtilis (strain 168)","168 / 168 / 168 / IS58",17,329,331,18,322,323]
[null,"Q8CJR5","_",0.47202,0.99396,47.42,{"v":5E-91,"d":"5.00E-91"},9,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",12000953,"Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)","ATCC BAA-471 / A3(2) / M145",2,330,331,370,687,697]
[null,"P9WHP0","_",0.47246,0.98489,47.55,{"v":6e-91,"d":"6.00E-91"},10,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",6,331,331,369,687,690]
[null,"P9WHP1","_",0.47246,0.98489,47.55,{"v":6e-91,"d":"6.00E-91"},10,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","9634230, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",6,331,331,369,687,690]
[null,"P0A9M8","IPMed?",0.45378,0.97885,48.15,{"v":1e-85,"d":"1.00E-85"},11,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","7883769, 7918659, 9205837, 9278503, 16738553, 2536666, 10542166, 15687190, 19852855, 20236319","Escherichia coli (strain K12)","K12 / KH131 / K12 / 1100 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12 / W3110 / ATCC 27325 / DSM 5911",6,329,331,395,710,714]
[null,"Q8ZND6","IPMed?",0.45378,0.97885,48.15,{"v":3e-85,"d":"3.00E-85"},12,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","11677609, 16272400, 17339319","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720 / LT2",6,329,331,394,709,714]
[null,"Q9I5A5","IPMed?",0.46165,0.98187,46.15,{"v":7e-81,"d":"7.00E-81"},13,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","10984043, 15231792","Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1",6,329,331,383,698,704]
[null,"P39197","IPMed?",1.00302,1.04403,41.27,{"v":3E-79,"d":"3.00E-79"},14,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Cytoplasm, Transferase",7480167,"Paracoccus denitrificans","_",1,330,331,1,318,318]
[null,"P41790","IPMed?",0.97041,0.99094,37.5,{"v":6E-68,"d":"6.00E-68"},15,1,"eutD","Ethanolamine utilization protein EutD","_","Acyltransferase, Complete proteome, Reference proteome, Transferase","10464203, 11677609, 7868611","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / LT2 / SGSC1412 / ATCC 700720 / ATCC 14028s / SGSG 2262",3,330,331,2,324,338]
[null,"Q49112","IPMed?",0.99094,1.01863,35.06,{"v":2E-51,"d":"2.00E-51"},16,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",8844861,"Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)","_",1,325,331,1,317,322]
[null,"P76558","IPMed?",0.43742,1.00302,33.43,{"v":3e-50,"d":"3.00E-50"},17,1,"maeB","NADP-dependent malic enzyme","1.1.1.40","Acetylation, Complete proteome, Metal-binding, Multifunctional enzyme, NADP, Oxidoreductase, Reference proteome","9205837, 9278503, 16738553, 36376, 17557829, 18723842","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / W / ATCC 11105 / DSM 1900 / K12 / K12 / JW1106",4,330,331,431,755,759]
[]
["CLOSTRIBL3_v1_10746","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"A5N802","_",0.98025,0.99499,76.57,0,1,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase",18218779,"Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)","ATCC 8527 / DSM 555 / NCIMB 10680",1,396,399,1,397,405]
[null,"C1FSN0","_",0.98747,0.99244,75.89,0,2,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase","_","Clostridium botulinum (strain Kyoto / Type A2)","_",1,394,399,1,394,397]
[null,"B1KWP9","_",0.98747,0.99244,75.89,0,3,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase",18060065,"Clostridium botulinum (strain Loch Maree / Type A3)","Loch Maree / Type A3",1,394,399,1,394,397]
[null,"C3L0F7","_",0.98747,0.99244,75.63,0,4,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase","_","Clostridium botulinum (strain 657 / Type Ba4)","_",1,394,399,1,394,397]
[null,"A7FW24","_",0.98747,0.99244,75.63,0,4,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase",18060065,"Clostridium botulinum (strain ATCC 19397 / Type A)","ATCC 19397 / Type A",1,394,399,1,394,397]
[null,"A5I4N7","_",0.98747,0.99244,75.63,0,4,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","17519437, 18060065","Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)","Hall / ATCC 3502 / NCTC 13319 / Type A / Hall / ATCC 3502 / NCTC 13319 / Type A",1,394,399,1,394,397]
[null,"B1II90","_",0.98747,0.99244,75.38,0,5,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase",18060065,"Clostridium botulinum (strain Okra / Type B1)","Okra / Type B1",1,394,399,1,394,397]
[null,"A7GG48","_",0.98747,0.99244,75.13,0,6,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase","_","Clostridium botulinum (strain Langeland / NCTC 10281 / Type F)","_",1,394,399,1,394,397]
[null,"Q895N2","_",1,1.00251,72.25,0,7,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase",12552129,"Clostridium tetani (strain Massachusetts / E88)","Massachusetts / E88",1,399,399,1,400,400]
[null,"A0Q0Z5","_",0.98753,0.99248,67.93,0,8,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase",17115055,"Clostridium novyi (strain NT)","NT",1,396,399,1,396,401]
[null,"P71104","IPMed?",1,1.00501,64.34,0,9,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","8702268, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,399,399,1,401,401]
[null,"Q59331","_",1,1.00251,66,0,10,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",1,399,399,1,400,400]
[null,"P38502","IPMed?",0.97304,0.99499,64.48,0,11,1,"ackA","Acetate kinase","2.7.2.1","3D-structure, ATP-binding, Cytoplasm, Direct protein sequencing, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase","8226623, 2844814, 11562377, 15774882, 17999468, 11133963, 15647264","Methanosarcina thermophila","ATCC 43570 / DSM 1825 / OCM 12 / TM-1",1,396,399,1,397,408]
[null,"Q9WYB1","IPMed?",0.99504,1.00501,60.6,{"v":3e-174,"d":"3.00E-174"},12,1,"ackA","Acetate kinase","2.7.2.1","3D-structure, ATP-binding, Complete proteome, Cytoplasm, Direct protein sequencing, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","10360571, 10074080","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","ATCC 43589 / MSB8 / DSM 3109 / JCM 10099",1,398,399,1,401,403]
[null,"P37877","IPMed?",0.98997,1,55.7,{"v":6E-158,"d":"6.00E-158"},13,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","8226682, 9387221, 9384377","Bacillus subtilis (strain 168)","168 / 168 / 168",2,396,399,3,395,395]
[null,"P74879","IPMed?",0.97277,0.98496,49.36,{"v":3e-133,"d":"3.00E-133"},14,1,"pduW","Probable propionate kinase","2.7.2.15","ATP-binding, Complete proteome, Kinase, Nucleotide-binding, Reference proteome, Transferase","10498708, 11677609","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / LT2 / SGSC1412 / ATCC 700720",2,394,399,4,392,404]
[null,"Q9X4M1","IPMed?",0.97744,0.98985,45.38,{"v":8e-117,"d":"8.00E-117"},15,1,"ackA1","Acetate kinase 1","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","10941799, 16273110","Lactobacillus sakei subsp. sakei (strain 23K)","23K",2,390,399,3,389,394]
[null,"P77845","IPMed?",0.97744,0.98237,45.38,{"v":2E-113,"d":"2.00E-113"},16,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","10075432, 12743753, 12948626, 15090522, 16547043, 18355281","Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)","ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025",4,389,399,5,391,397]
[null,"Q49113","IPMed?",0.99248,1.00763,45.71,{"v":1e-111,"d":"1.00E-111"},17,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase",8844861,"Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)","_",3,396,399,2,393,393]
[null,"P0A6A3","IPMed?",0.9875,0.98997,45.32,{"v":4e-108,"d":"4.00E-108"},18,1,"ackA","Acetate kinase","2.7.2.1","3D-structure, ATP-binding, Complete proteome, Cytoplasm, Direct protein sequencing, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","2536666, 7883769, 9205837, 9278503, 16738553, 9298644","Escherichia coli (strain K12)","K12 / K12 / KH131 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",3,390,399,6,394,400]
[null,"P63411","IPMed?",0.9875,0.98997,45.06,{"v":5E-108,"d":"5.00E-108"},19,1,"ackA","Acetate kinase","2.7.2.1","3D-structure, ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","11677609, 23031654","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720",3,390,399,6,394,400]
[]
["CLOSTRIBL3_v1_11881","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"A4IP64","IPMed?",0.93924,0.95866,37.74,{"v":4e-74,"d":"4.00E-74"},1,1,"adh1","Long-chain-alcohol dehydrogenase 1","1.1.1.192","Complete proteome, NAD, Oxidoreductase","17372208, 19383697, 24826896","Geobacillus thermodenitrificans (strain NG80-2)","NG80-2 / NG80-2",16,382,387,15,381,395]
[null,"F8DVL8","IPMed?",0.9509,0.96084,37.23,{"v":2e-71,"d":"2.00E-71"},2,1,"adhB","Alcohol dehydrogenase 2","1.1.1.1","Complete proteome, Iron, NAD, Oxidoreductase","2308827, 21725006","Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1)","ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1 / ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1",16,382,387,15,379,383]
[null,"P0DJA2","IPMed?",0.9509,0.96084,37.23,{"v":2e-71,"d":"2.00E-71"},2,1,"adhB","Alcohol dehydrogenase 2","1.1.1.1","3D-structure, Complete proteome, Direct protein sequencing, Iron, NAD, Oxidoreductase, Reference proteome","3584063, 15592456, 2935393","Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)","ATCC 31821 / ZM4 / CP4 / ATCC 31821 / ZM4 / CP4 / ATCC 31821 / ZM4 / CP4",16,382,387,15,379,383]
[null,"A6ZTT5","_",0.8708,0.8822,39.17,{"v":6e-70,"d":"6.00E-70"},3,2,"ADH4","Alcohol dehydrogenase 4","1.1.1.1","Complete proteome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Zinc",17652520,"Saccharomyces cerevisiae (strain YJM789)","YJM789",23,356,387,20,351,382]
[null,"P10127","IPMed?",0.8708,0.8822,38.87,{"v":6e-69,"d":"6.00E-69"},4,2,"ADH4","Alcohol dehydrogenase 4","1.1.1.1","Complete proteome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Zinc","2823079, 8972578, 9169869, 24374639, 3282541, 10978274, 10884426, 14562095, 14562106, 17139254, 16503288, 17933919, 17938904","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 96604 / S288c / FY1679 / ATCC 204508 / S288c / ATCC 204508 / S288c",23,356,387,20,351,382]
[null,"P31005","IPMed?",0.96641,0.98163,34.22,{"v":9e-69,"d":"9.00E-69"},5,1,"mdh","NAD-dependent methanol dehydrogenase","1.1.1.244","Cytoplasm, Direct protein sequencing, Magnesium, Methanol utilization, NAD, Oxidoreductase, Zinc","1644761, 1995642, 2673121, 1995643, 12089158, 12351635","Bacillus methanolicus","C1 / C1 / C1 / C1 / C1 / C1",14,386,387,11,381,381]
[null,"P45513","IPMed?",0.95607,0.95607,37.03,{"v":4e-68,"d":"4.00E-68"},6,1,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","Iron, NAD, Oxidoreductase",7721705,"Citrobacter freundii","ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK",16,382,387,17,383,387]
[null,"Q59477","_",0.95607,0.95607,36.49,{"v":4e-68,"d":"4.00E-68"},7,1,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","3D-structure, Iron, NAD, Oxidoreductase","_","Klebsiella pneumoniae","_",16,382,387,17,383,387]
[null,"P37686","IPMed?",0.83979,0.84856,37.23,{"v":4e-63,"d":"4.00E-63"},8,3,"yiaY","Probable alcohol dehydrogenase","1.1.1.1","Complete proteome, Iron, NAD, Oxidoreductase, Reference proteome","8041620, 9278503, 16397293, 16738553, 7768815","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",38,361,387,35,359,383]
[null,"Q09669","IPMed?",0.82464,0.89922,36.21,{"v":5e-63,"d":"5.00E-63"},9,1,"adh4","Alcohol dehydrogenase 4","1.1.1.1","Complete proteome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide, Zinc","11859360, 15040954, 16823372, 16999687, 18203864","Schizosaccharomyces pombe (strain 972 / ATCC 24843)","972 / ATCC 24843",16,361,387,58,398,422]
[null,"P0A9S1","IPMed?",0.95607,0.96859,31.35,{"v":1E-59,"d":"1.00E-59"},10,4,"fucO","Lactaldehyde reductase","1.1.1.77","3D-structure, Carbohydrate metabolism, Complete proteome, Fucose metabolism, Iron, Metal-binding, NAD, Oxidoreductase, Reference proteome","2553671, 2664711, 2661535, 9278503, 16738553, 8385012, 15995211","Escherichia coli (strain K12)","K12 / K12 / K12 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12 / ECL1",16,382,387,14,378,382]
[null,"P0A9S2","_",0.95607,0.96859,31.35,{"v":1E-59,"d":"1.00E-59"},10,4,"fucO","Lactaldehyde reductase","1.1.1.77","Carbohydrate metabolism, Complete proteome, Fucose metabolism, Iron, Metal-binding, NAD, Oxidoreductase, Reference proteome","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",16,382,387,14,378,382]
[null,"P71017","IPMed?",0.96517,1.00258,31.44,{"v":2e-54,"d":"2.00E-54"},11,1,"gbsB","Choline dehydrogenase","1.1.1.-","Alternative initiation, Complete proteome, Direct protein sequencing, NAD, Oxidoreductase, Reference proteome","8752328, 9384377, 19383706, 22408163","Bacillus subtilis (strain 168)","168 / JH642 / 168 / 168 / JH642",1,384,387,10,393,402]
[null,"P13604","IPMed?",1,1.00258,29.38,{"v":1e-49,"d":"1.00E-49"},12,4,"adh1","NADPH-dependent butanol dehydrogenase","1.1.1.-","NADP, Oxidoreductase",2673928,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",6,382,387,3,377,388]
[]
["CLOSTRIBL3_v1_20137","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P13604","IPMed?",1.00515,1.02094,39.49,{"v":8e-89,"d":"8.00E-89"},1,3,"adh1","NADPH-dependent butanol dehydrogenase","1.1.1.-","NADP, Oxidoreductase",2673928,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",4,381,382,4,381,388]
[null,"Q24803","IPMed?",0.46437,1.05759,40.35,{"v":5e-83,"d":"5.00E-83"},2,4,"ADH2","Alcohol dehydrogenase / Acetaldehyde dehydrogenase","1.1.1.1, 1.2.1.10","Direct protein sequencing, Iron, Multifunctional enzyme, NAD, Oxidoreductase","7935603, 7980441","Entamoeba histolytica","ATCC 30459 / HM-1:IMSS / ATCC 30459 / HM-1:IMSS",4,381,382,465,866,870]
[null,"P0A9Q7","IPMed?",0.43322,1.01047,37.05,{"v":3e-69,"d":"3.00E-69"},3,5,"adhE","Alcohol dehydrogenase / Acetaldehyde dehydrogenase [acetylating] / Pyruvate-formate-lyase deactivase","1.1.1.1, 1.2.1.10","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Iron, Multifunctional enzyme, NAD, Oxidoreductase, Reference proteome","2695398, 2015910, 8905232, 9278503, 16738553, 7773397, 7521508, 9298644, 12783863, 18723842","Escherichia coli (strain K12)","K12 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / JW1106",25,381,382,479,862,891]
[null,"P0A9Q8","_",0.43322,1.01047,37.05,{"v":3e-69,"d":"3.00E-69"},3,5,"adhE","Alcohol dehydrogenase / Acetaldehyde dehydrogenase [acetylating] / Pyruvate-formate-lyase deactivase","1.1.1.1, 1.2.1.10","Acetylation, Complete proteome, Iron, Multifunctional enzyme, NAD, Oxidoreductase, Reference proteome","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",25,381,382,479,862,891]
[null,"P31005","IPMed?",0.9712,0.97375,35.58,{"v":7e-65,"d":"7.00E-65"},4,3,"mdh","NAD-dependent methanol dehydrogenase","1.1.1.244","Cytoplasm, Direct protein sequencing, Magnesium, Methanol utilization, NAD, Oxidoreductase, Zinc","1644761, 1995642, 2673121, 1995643, 12089158, 12351635","Bacillus methanolicus","C1 / C1 / C1 / C1 / C1 / C1",19,379,382,23,379,381]
[null,"F8DVL8","IPMed?",0.98956,0.99215,35.88,{"v":8e-63,"d":"8.00E-63"},5,4,"adhB","Alcohol dehydrogenase 2","1.1.1.1","Complete proteome, Iron, NAD, Oxidoreductase","2308827, 21725006","Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1)","ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1 / ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1",13,377,382,15,379,383]
[null,"P0DJA2","IPMed?",0.98695,0.98953,35.19,{"v":2e-62,"d":"2.00E-62"},6,4,"adhB","Alcohol dehydrogenase 2","1.1.1.1","3D-structure, Complete proteome, Direct protein sequencing, Iron, NAD, Oxidoreductase, Reference proteome","3584063, 15592456, 2935393","Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)","ATCC 31821 / ZM4 / CP4 / ATCC 31821 / ZM4 / CP4 / ATCC 31821 / ZM4 / CP4",13,377,382,15,379,383]
[null,"P10127","IPMed?",1.00524,1.00524,34.9,{"v":7e-61,"d":"7.00E-61"},7,4,"ADH4","Alcohol dehydrogenase 4","1.1.1.1","Complete proteome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Zinc","2823079, 8972578, 9169869, 24374639, 3282541, 10978274, 10884426, 14562095, 14562106, 17139254, 16503288, 17933919, 17938904","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 96604 / S288c / FY1679 / ATCC 204508 / S288c / ATCC 204508 / S288c",12,382,382,15,381,382]
[null,"A4IP64","IPMed?",0.94177,0.97382,34.95,{"v":9E-61,"d":"9.00E-61"},8,2,"adh1","Long-chain-alcohol dehydrogenase 1","1.1.1.192","Complete proteome, NAD, Oxidoreductase","17372208, 19383697, 24826896","Geobacillus thermodenitrificans (strain NG80-2)","NG80-2 / NG80-2",14,372,382,20,375,395]
[null,"P33744","IPMed?",0.46752,1.05497,33.25,{"v":1e-60,"d":"1.00E-60"},9,5,"adhE","Alcohol dehydrogenase / Aldehyde dehydrogenase","1.1.1.1, 1.2.1.3","Complete proteome, Multifunctional enzyme, NAD, Oxidoreductase, Plasmid, Reference proteome","8226639, 8300540, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",4,377,382,452,854,862]
[null,"A6ZTT5","_",1.00524,1.00524,34.9,{"v":1e-60,"d":"1.00E-60"},10,4,"ADH4","Alcohol dehydrogenase 4","1.1.1.1","Complete proteome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Zinc",17652520,"Saccharomyces cerevisiae (strain YJM789)","YJM789",12,382,382,15,381,382]
[null,"P45513","IPMed?",1.02584,1.03927,34.26,{"v":1e-60,"d":"1.00E-60"},11,4,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","Iron, NAD, Oxidoreductase",7721705,"Citrobacter freundii","ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK",1,381,382,5,387,387]
[]
["CLOSTRIBL3_v1_12484","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P0A9Q7","IPMed?",0.50281,0.84528,48.21,{"v":3e-130,"d":"3.00E-130"},1,1,"adhE","Alcohol dehydrogenase / Acetaldehyde dehydrogenase [acetylating] / Pyruvate-formate-lyase deactivase","1.1.1.1, 1.2.1.10","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Iron, Multifunctional enzyme, NAD, Oxidoreductase, Reference proteome","2695398, 2015910, 8905232, 9278503, 16738553, 7773397, 7521508, 9298644, 12783863, 18723842","Escherichia coli (strain K12)","K12 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / JW1106",10,450,530,5,450,891]
[null,"P0A9Q8","_",0.50281,0.84528,48.21,{"v":3e-130,"d":"3.00E-130"},1,1,"adhE","Alcohol dehydrogenase / Acetaldehyde dehydrogenase [acetylating] / Pyruvate-formate-lyase deactivase","1.1.1.1, 1.2.1.10","Acetylation, Complete proteome, Iron, Multifunctional enzyme, NAD, Oxidoreductase, Reference proteome","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",10,450,530,5,450,891]
[null,"P33744","IPMed?",0.51392,0.83585,45.15,{"v":3e-114,"d":"3.00E-114"},2,1,"adhE","Alcohol dehydrogenase / Aldehyde dehydrogenase","1.1.1.1, 1.2.1.3","Complete proteome, Multifunctional enzyme, NAD, Oxidoreductase, Plasmid, Reference proteome","8226639, 8300540, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",10,445,530,5,443,862]
[null,"Q24803","IPMed?",0.51264,0.84151,45.29,{"v":2E-109,"d":"2.00E-109"},3,1,"ADH2","Alcohol dehydrogenase / Acetaldehyde dehydrogenase","1.1.1.1, 1.2.1.10","Direct protein sequencing, Iron, Multifunctional enzyme, NAD, Oxidoreductase","7935603, 7980441","Entamoeba histolytica","ATCC 30459 / HM-1:IMSS / ATCC 30459 / HM-1:IMSS",12,445,530,11,456,870]
[null,"P38947","IPMed?",0.82075,0.96026,40.69,{"v":7E-105,"d":"7.00E-105"},4,1,"sucD","Succinate-semialdehyde dehydrogenase (acetylating)","1.2.1.76","Complete proteome, Direct protein sequencing, NADP, Oxidoreductase, Reference proteome","8550525, 18218779","Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)","ATCC 8527 / DSM 555 / NCIMB 10680",15,446,530,8,438,453]
[null,"Q0K845","IPMed?",0.7566,0.81339,33.67,{"v":6e-64,"d":"6.00E-64"},5,1,"sauS","Sulfoacetaldehyde dehydrogenase (acylating)","1.2.1.81","Complete proteome, Cytoplasm, Direct protein sequencing, NADP, Oxidoreductase, Reference proteome","16964242, 20693281","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337",54,448,530,77,473,493]
[null,"P41793","IPMed?",0.69811,0.79229,30.27,{"v":3e-46,"d":"3.00E-46"},6,2,"eutE","Ethanolamine utilization protein EutE","_","Complete proteome, Oxidoreductase, Reference proteome","7868611, 10464203, 11677609","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","ATCC 14028s / SGSG 2262 / LT2 / LT2 / SGSC1412 / ATCC 700720",45,408,530,65,427,467]
[null,"P77445","_",0.69811,0.79229,30,{"v":6e-46,"d":"6.00E-46"},7,2,"eutE","Ethanolamine utilization protein EutE","_","Complete proteome, Oxidoreductase, Reference proteome","9205837, 9278503, 16738553","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",45,408,530,65,427,467]
[null,"P71016","IPMed?",0.46038,0.49796,27.46,8e-13,8,1,"gbsA","Betaine aldehyde dehydrogenase","1.2.1.8","Complete proteome, Direct protein sequencing, NAD, Oxidoreductase, Reference proteome","8752328, 9384377, 9297465, 22408163, 26658822","Bacillus subtilis (strain 168)","168 / JH642 / 168 / 168 / JH642 / 168 / 3NA",38,274,530,68,306,490]
[null,"Q9HK01","IPMed?",0.60189,0.64706,21,4e-09,9,2,"_","D-glyceraldehyde dehydrogenase (NADP(+))","1.2.1.89","3D-structure, Coiled coil, Complete proteome, NADP, Oxidoreductase, Reference proteome","11029001, 16566751, 16458304","Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)","ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165 / ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165",38,348,530,66,368,493]
[null,"Q6L285","IPMed?",0.4717,0.5071,22,5e-09,10,3,"_","D-glyceraldehyde dehydrogenase (NADP(+))","1.2.1.89","Complete proteome, NADP, Oxidoreductase, Reference proteome","15184674, 16458304","Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)","ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828",29,271,530,55,299,493]
[null,"P96489","IPMed?",0.51698,0.65865,24.82,5e-08,11,2,"proA","Gamma-glutamyl phosphate reductase","1.2.1.41","Amino-acid biosynthesis, Cytoplasm, NADP, Oxidoreductase, Proline biosynthesis",8969524,"Streptococcus thermophilus","ATCC 19258 / DSM 20617 / LMG 6896 / NCDO 573 / NCIMB 8510",17,271,530,7,271,416]
[]
["CLOSTRIBL3_v1_12496","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P0A9Q7","IPMed?",0.48934,0.87903,39.45,{"v":2E-91,"d":"2.00E-91"},1,4,"adhE","Alcohol dehydrogenase / Acetaldehyde dehydrogenase [acetylating] / Pyruvate-formate-lyase deactivase","1.1.1.1, 1.2.1.10","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Iron, Multifunctional enzyme, NAD, Oxidoreductase, Reference proteome","2695398, 2015910, 8905232, 9278503, 16738553, 7773397, 7521508, 9298644, 12783863, 18723842","Escherichia coli (strain K12)","K12 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / JW1106",10,440,496,5,439,891]
[null,"P0A9Q8","_",0.48934,0.87903,39.45,{"v":2E-91,"d":"2.00E-91"},1,4,"adhE","Alcohol dehydrogenase / Acetaldehyde dehydrogenase [acetylating] / Pyruvate-formate-lyase deactivase","1.1.1.1, 1.2.1.10","Acetylation, Complete proteome, Iron, Multifunctional enzyme, NAD, Oxidoreductase, Reference proteome","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",10,440,496,5,439,891]
[null,"P33744","IPMed?",0.49768,0.86492,37.3,{"v":1e-77,"d":"1.00E-77"},2,4,"adhE","Alcohol dehydrogenase / Aldehyde dehydrogenase","1.1.1.1, 1.2.1.3","Complete proteome, Multifunctional enzyme, NAD, Oxidoreductase, Plasmid, Reference proteome","8226639, 8300540, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",22,445,496,17,442,862]
[null,"P38947","IPMed?",0.8871,0.9713,34.32,{"v":3e-77,"d":"3.00E-77"},3,2,"sucD","Succinate-semialdehyde dehydrogenase (acetylating)","1.2.1.76","Complete proteome, Direct protein sequencing, NADP, Oxidoreductase, Reference proteome","8550525, 18218779","Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)","ATCC 8527 / DSM 555 / NCIMB 10680",9,447,496,5,438,453]
[null,"Q24803","IPMed?",0.50575,0.8871,35.91,{"v":5e-77,"d":"5.00E-77"},4,5,"ADH2","Alcohol dehydrogenase / Acetaldehyde dehydrogenase","1.1.1.1, 1.2.1.10","Direct protein sequencing, Iron, Multifunctional enzyme, NAD, Oxidoreductase","7935603, 7980441","Entamoeba histolytica","ATCC 30459 / HM-1:IMSS / ATCC 30459 / HM-1:IMSS",17,445,496,16,455,870]
[null,"Q0K845","IPMed?",0.87702,0.88235,29.89,{"v":2e-48,"d":"2.00E-48"},5,2,"sauS","Sulfoacetaldehyde dehydrogenase (acylating)","1.2.1.81","Complete proteome, Cytoplasm, Direct protein sequencing, NADP, Oxidoreductase, Reference proteome","16964242, 20693281","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337",17,445,496,38,469,493]
[null,"P41793","IPMed?",0.85887,0.91221,27,{"v":4e-36,"d":"4.00E-36"},6,3,"eutE","Ethanolamine utilization protein EutE","_","Complete proteome, Oxidoreductase, Reference proteome","7868611, 10464203, 11677609","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","ATCC 14028s / SGSG 2262 / LT2 / LT2 / SGSC1412 / ATCC 700720",18,431,496,40,448,467]
[null,"P77445","_",0.85484,0.90792,27.12,{"v":5E-36,"d":"5.00E-36"},7,3,"eutE","Ethanolamine utilization protein EutE","_","Complete proteome, Oxidoreductase, Reference proteome","9205837, 9278503, 16738553","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",18,431,496,40,448,467]
[null,"Q6L285","IPMed?",0.91532,0.92089,22.25,1e-09,8,2,"_","D-glyceraldehyde dehydrogenase (NADP(+))","1.2.1.89","Complete proteome, NADP, Oxidoreductase, Reference proteome","15184674, 16458304","Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)","ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828",6,424,496,55,458,493]
[null,"B0TBV8","_",0.61089,0.72662,23.1,3E-9,9,2,"proA","Gamma-glutamyl phosphate reductase","1.2.1.41","Amino-acid biosynthesis, Complete proteome, Cytoplasm, NADP, Oxidoreductase, Proline biosynthesis, Reference proteome",18441057,"Heliobacterium modesticaldum (strain ATCC 51547 / Ice1)","ATCC 51547 / Ice1",105,405,496,113,373,417]
[null,"Q0SPX8","_",0.31048,0.37108,30.52,6E-9,10,2,"proA","Gamma-glutamyl phosphate reductase","1.2.1.41","Amino-acid biosynthesis, Complete proteome, Cytoplasm, NADP, Oxidoreductase, Proline biosynthesis",16825665,"Clostridium perfringens (strain SM101 / Type A)","SM101 / Type A",107,258,496,113,264,415]
[null,"P96489","IPMed?",0.46371,0.55288,26.52,6e-08,11,3,"proA","Gamma-glutamyl phosphate reductase","1.2.1.41","Amino-acid biosynthesis, Cytoplasm, NADP, Oxidoreductase, Proline biosynthesis",8969524,"Streptococcus thermophilus","ATCC 19258 / DSM 20617 / LMG 6896 / NCDO 573 / NCIMB 8510",101,328,496,106,311,416]
[null,"P42236","IPMed?",0.48387,0.4918,26.25,3e-07,12,2,"gucD","Alpha-ketoglutaric semialdehyde dehydrogenase","1.2.1.26","Complete proteome, NAD, NADP, Oxidoreductase, Reference proteome","7704254, 9384377, 17202142, 26658822","Bacillus subtilis (strain 168)","168 / 168 / 168 / 3NA",33,263,496,84,301,488]
[null,"Q58806","IPMed?",0.54839,0.58747,23.16,6e-07,13,3,"_","Lactaldehyde dehydrogenase","1.2.1.22","3D-structure, Complete proteome, NAD, Oxidoreductase, Reference proteome","8688087, 16585745","Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440",9,273,496,30,296,463]
[]
["CLOSTRIBL3_v1_12732","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q2RHL2","_",0.99313,0.99655,79.93,{"v":5E-166,"d":"5.00E-166"},1,1,"_","Acetaldehyde dehydrogenase","1.2.1.10","Aromatic hydrocarbons catabolism, Complete proteome, NAD, Oxidoreductase, Reference proteome",18631365,"Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320",1,289,290,1,289,291]
[null,"A5D522","_",0.95973,0.98621,69.23,{"v":3e-138,"d":"3.00E-138"},2,1,"mhpF","Acetaldehyde dehydrogenase","1.2.1.10","Aromatic hydrocarbons catabolism, Complete proteome, NAD, Oxidoreductase, Reference proteome",18218977,"Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)","DSM 13744 / JCM 10971 / SI",1,285,290,1,286,298]
[null,"Q3ACM1","_",0.95987,0.98966,65.16,{"v":8e-132,"d":"8.00E-132"},3,1,"mhpF","Acetaldehyde dehydrogenase","1.2.1.10","Aromatic hydrocarbons catabolism, Complete proteome, NAD, Oxidoreductase, Reference proteome",16311624,"Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)","ATCC BAA-161 / DSM 6008 / Z-2901",3,288,290,4,290,299]
[null,"B8G186","_",0.97643,1,60,{"v":1E-119,"d":"1.00E-119"},4,1,"_","Acetaldehyde dehydrogenase","1.2.1.10","Aromatic hydrocarbons catabolism, Complete proteome, NAD, Oxidoreductase",22316246,"Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)","DCB-2 / DSM 10664",2,286,290,4,293,297]
[null,"B0VXM6","_",0.9932,1.0069,59.25,{"v":6e-115,"d":"6.00E-115"},5,1,"pheF","Acetaldehyde dehydrogenase","1.2.1.10","Aromatic hydrocarbons catabolism, NAD, Oxidoreductase, Plasmid","_","Geobacillus stearothermophilus","_",1,288,290,1,292,294]
[null,"A4IT43","_",0.97288,0.98966,59.58,{"v":3e-112,"d":"3.00E-112"},6,1,"nbaJ","Acetaldehyde dehydrogenase","1.2.1.10","Aromatic hydrocarbons catabolism, Complete proteome, NAD, Oxidoreductase",17372208,"Geobacillus thermodenitrificans (strain NG80-2)","NG80-2",1,282,290,1,287,295]
[null,"B9L2J1","_",0.95455,1.01379,58.16,{"v":1e-110,"d":"1.00E-110"},7,1,"_","Acetaldehyde dehydrogenase","1.2.1.10","Aromatic hydrocarbons catabolism, Complete proteome, NAD, Oxidoreductase",19148287,"Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2)","ATCC 27502 / DSM 5159 / P-2",4,285,290,7,300,308]
[null,"Q764S1","IPMed?",0.97351,1.01379,56.46,{"v":5E-110,"d":"5.00E-110"},8,1,"nahO","Acetaldehyde dehydrogenase","1.2.1.10","Aromatic hydrocarbons catabolism, NAD, Oxidoreductase",15073308,"Bacillus sp. (strain JF8)","_",2,285,290,3,296,302]
[null,"B8GBV4","_",0.9769,1.02069,57.43,{"v":4e-108,"d":"4.00E-108"},9,1,"_","Acetaldehyde dehydrogenase","1.2.1.10","Aromatic hydrocarbons catabolism, Complete proteome, NAD, Oxidoreductase","_","Chloroflexus aggregans (strain MD-66 / DSM 9485)","_",3,287,290,5,300,303]
[null,"Q53WH9","IPMed?",0.97068,1.02759,55.37,{"v":5e-107,"d":"5.00E-107"},10,1,"_","Acetaldehyde dehydrogenase","1.2.1.10","Aromatic hydrocarbons catabolism, Complete proteome, NAD, Oxidoreductase, Plasmid, Reference proteome",22316175,"Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","HB8 / ATCC 27634 / DSM 579",2,287,290,3,300,307]
[null,"Q9ZI57","IPMed?",0.94463,1,54.48,{"v":6e-105,"d":"6.00E-105"},11,1,"nahO","Acetaldehyde dehydrogenase","1.2.1.10","Aromatic hydrocarbons catabolism, NAD, Oxidoreductase",10713446,"Pseudomonas stutzeri","AN10",2,284,290,3,292,307]
[null,"Q52039","IPMed?",0.96053,1.0069,54.45,{"v":4e-104,"d":"4.00E-104"},12,1,"bphX2","Acetaldehyde dehydrogenase 2","1.2.1.10","Aromatic hydrocarbons catabolism, NAD, Oxidoreductase",9190809,"Pseudomonas furukawaii","DSM 10086 / NBRC 110670 / KF707",2,286,290,3,294,304]
[null,"Q79AF6","IPMed?",0.96053,1.0069,54.45,{"v":4e-104,"d":"4.00E-104"},12,1,"bphJ","Acetaldehyde dehydrogenase 4","1.2.1.10","Allosteric enzyme, Aromatic hydrocarbons catabolism, Complete proteome, NAD, NADP, Oxidoreductase, Reference proteome","8026764, 17030797, 19476337, 20364820, 21838275, 22574886","Paraburkholderia xenovorans (strain LB400)","LB400 / LB400 / LB400",2,286,290,3,294,304]
[null,"Q9RHN2","IPMed?",0.95114,1.0069,52.4,{"v":2e-101,"d":"2.00E-101"},13,1,"aphF","Acetaldehyde dehydrogenase 2","1.2.1.10","Aromatic hydrocarbons catabolism, NAD, Oxidoreductase",10878134,"Comamonas testosteroni","TA441",2,286,290,3,294,307]
[null,"Q52060","IPMed?",0.98718,1.06207,51.62,{"v":1e-96,"d":"1.00E-96"},14,1,"dmpF","Acetaldehyde dehydrogenase","1.2.1.10","3D-structure, Aromatic hydrocarbons catabolism, Direct protein sequencing, NAD, Oxidoreductase, Plasmid","1732207, 8419288, 12764229","Pseudomonas sp. (strain CF600)","CF600 / CF600 / CF600",2,285,290,3,310,312]
[null,"P77580","IPMed?",0.99367,1.08276,50.96,{"v":5e-95,"d":"5.00E-95"},15,1,"mhpF","Acetaldehyde dehydrogenase","1.2.1.10","Aromatic hydrocarbons catabolism, Complete proteome, NAD, Oxidoreductase, Reference proteome","9098055, 9278503, 16738553, 16782065","Escherichia coli (strain K12)","K12 / CS520 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",1,290,290,1,314,316]
[null,"Q9KWS1","IPMed?",0.9557,1.04138,51.66,{"v":2e-93,"d":"2.00E-93"},16,1,"amnH","Acetaldehyde dehydrogenase","1.2.1.10","Aromatic hydrocarbons catabolism, NAD, Oxidoreductase","9169437, 11081795","Pseudomonas sp","AP-3 / AP-3",3,281,290,5,306,316]
[null,"Q0RXC4","IPMed?",0.97659,1.0069,48.63,{"v":4E-92,"d":"4.00E-92"},17,1,"hpdG","Acetaldehyde dehydrogenase 6","1.2.1.10","Aromatic hydrocarbons catabolism, Complete proteome, NAD, Oxidoreductase, Plasmid","12514024, 17030794","Rhodococcus jostii (strain RHA1)","RHA1",1,282,290,1,292,299]
[null,"Q9S153","IPMed?",0.97468,1.06207,49.35,{"v":1e-90,"d":"1.00E-90"},18,1,"mhpF","Acetaldehyde dehydrogenase 3","1.2.1.10","Aromatic hydrocarbons catabolism, NAD, Oxidoreductase",10537203,"Comamonas testosteroni","TA441",2,286,290,3,310,316]

{"sheet":"UniFIRE ","index":6,"n_rows":524,"n_cols":8,"rows_kept":524}
["CLOSTRIBL3_v1_10012","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000103159","catalytic activity","(S)-lactate + NAD(+) = pyruvate + NADH","_","_","MF_00488","HAMAP"]
[null,"UR000103159","gene name","ldh","_","_","MF_00488","HAMAP"]
[null,"UR000103159","GO","GO:0005737","_","_","MF_00488","HAMAP"]
[null,"UR000103159","GO","GO:0006096","_","_","MF_00488","HAMAP"]
[null,"UR000103159","GO","GO:0004459","_","_","MF_00488","HAMAP"]
[null,"UR000103159","keyword","Cytoplasm","_","_","MF_00488","HAMAP"]
[null,"UR000103159","keyword","Oxidoreductase","_","_","MF_00488","HAMAP"]
[null,"UR000103159","keyword","NAD","_","_","MF_00488","HAMAP"]
[null,"UR000000418","keyword","Oxidoreductase","_","_","RU003369","RuleBase"]
[null,"UR000103159","nucleotide binding","NAD",14,42,"MF_00488","HAMAP"]
[null,"UR000103159","pathway","Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1","_","_","MF_00488","HAMAP"]
[null,"UR000103159","product - EC number","1.1.1.27","_","_","MF_00488","HAMAP"]
[null,"UR000103159","product name","L-lactate dehydrogenase","_","_","MF_00488","HAMAP"]
[null,"UR000103159","product name","L-LDH","_","_","MF_00488","HAMAP"]
[null,"UR000000418","similarity","Belongs to the LDH/MDH superfamily","_","_","RU003369","RuleBase"]
[null,"UR000103159","similarity","Belongs to the LDH/MDH superfamily. LDH family","_","_","MF_00488","HAMAP"]
[null,"UR000103159","site actif","Proton acceptor",181,181,"MF_00488","HAMAP"]
[null,"UR000103159","site binding","Substrate",94,94,"MF_00488","HAMAP"]
[null,"UR000103159","site binding","NAD or substrate",126,126,"MF_00488","HAMAP"]
[null,"UR000103159","site binding","Substrate",157,157,"MF_00488","HAMAP"]
[null,"UR000103159","site binding","Substrate",235,235,"MF_00488","HAMAP"]
[null,"UR000103159","subcellular location","Cytoplasm","_","_","MF_00488","HAMAP"]
[null,"UR000103159","subunit","Homotetramer","_","_","MF_00488","HAMAP"]
[]
["CLOSTRIBL3_v1_12309","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000416792","cofactor","Name=FMN; Xref=ChEBI:CHEBI:58210","_","_","PRU00683","ProRule"]
[null,"UR000416792","keyword","FMN","_","_","PRU00683","ProRule"]
[null,"UR000416792","keyword","Flavoprotein","_","_","PRU00683","ProRule"]
[null,"UR000416792","nucleotide binding","FMN",284,308,"PRU00683","ProRule"]
[null,"UR000416792","similarity","Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family","_","_","PRU00683","ProRule"]
[null,"UR000416792","site actif","Proton acceptor",253,253,"PRU00683","ProRule"]
[null,"UR000416792","site binding","FMN",229,229,"PRU00683","ProRule"]
[null,"UR000416792","site binding","Substrate",256,256,"PRU00683","ProRule"]
[]
["CLOSTRIBL3_v1_12417","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000001527","catalytic activity","Pyruvate + CoA + oxidized flavodoxin = acetyl-CoA + CO(2) + reduced flavodoxin","_","_","PIRNR000159","PIR"]
[null,"UR000001527","function","Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Electron transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Oxidoreductase","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","product - EC number","1.2.7.-","_","_","PIRNR000159","PIR"]
[null,"UR000001527","product name","Pyruvate-flavodoxin oxidoreductase","_","_","PIRNR000159","PIR"]
[null,"UR000001527","similarity","Belongs to the nifJ family","_","_","PIRNR000159","PIR"]
[]
["CLOSTRIBL3_v1_10343","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000001527","catalytic activity","Pyruvate + CoA + oxidized flavodoxin = acetyl-CoA + CO(2) + reduced flavodoxin","_","_","PIRNR000159","PIR"]
[null,"UR000001527","function","Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Electron transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Oxidoreductase","_","_","PIRNR000159","PIR"]
[null,"UR000001527","product - EC number","1.2.7.-","_","_","PIRNR000159","PIR"]
[null,"UR000001527","product name","Pyruvate-flavodoxin oxidoreductase","_","_","PIRNR000159","PIR"]
[null,"UR000001527","similarity","Belongs to the nifJ family","_","_","PIRNR000159","PIR"]
[]
["CLOSTRIBL3_v1_20129","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000001527","catalytic activity","Pyruvate + CoA + oxidized flavodoxin = acetyl-CoA + CO(2) + reduced flavodoxin","_","_","PIRNR000159","PIR"]
[null,"UR000001527","function","Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Electron transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Oxidoreductase","_","_","PIRNR000159","PIR"]
[null,"UR000001527","product - EC number","1.2.7.-","_","_","PIRNR000159","PIR"]
[null,"UR000001527","product name","Pyruvate-flavodoxin oxidoreductase","_","_","PIRNR000159","PIR"]
[null,"UR000001527","similarity","Belongs to the nifJ family","_","_","PIRNR000159","PIR"]
[]
["CLOSTRIBL3_v1_12838","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000000536","keyword","Acyltransferase","_","_","RU003557","RuleBase"]
[null,"UR000000536","keyword","Transferase","_","_","RU003557","RuleBase"]
[null,"UR000000536","similarity","Belongs to the thiolase family","_","_","RU003557","RuleBase"]
[]
["CLOSTRIBL3_v1_13111","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000000536","keyword","Transferase","_","_","RU003557","RuleBase"]
[null,"UR000000536","keyword","Acyltransferase","_","_","RU003557","RuleBase"]
[null,"UR000000536","similarity","Belongs to the thiolase family","_","_","RU003557","RuleBase"]
[]
["CLOSTRIBL3_v1_11283","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000000536","keyword","Acyltransferase","_","_","RU003557","RuleBase"]
[null,"UR000000536","keyword","Transferase","_","_","RU003557","RuleBase"]
[null,"UR000000536","similarity","Belongs to the thiolase family","_","_","RU003557","RuleBase"]
[]
["CLOSTRIBL3_v1_11276","UniRule","Annotation type","Annotation value"]
[null,"SAAS00649305","keyword","Oxidoreductase"]
[]
["CLOSTRIBL3_v1_13113","UniRule","Annotation type","Annotation value"]
[null,"SAAS00649305","keyword","Oxidoreductase"]
[]
["CLOSTRIBL3_v1_20313","UniRule","Annotation type","Annotation value"]
[null,"SAAS00649305","keyword","Oxidoreductase"]
[]
["CLOSTRIBL3_v1_13112","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000000628","similarity","Belongs to the enoyl-CoA hydratase/isomerase family","_","_","RU003707","RuleBase"]
[]
["CLOSTRIBL3_v1_20308","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000000628","similarity","Belongs to the enoyl-CoA hydratase/isomerase family","_","_","RU003707","RuleBase"]
[]
["CLOSTRIBL3_v1_12502","UniRule","Annotation type","Annotation value"]
[null,"SAAS00804701","keyword","Electron transport"]
[null,"SAAS00804703","keyword","Iron"]
[null,"SAAS00804711","keyword","Metal-binding"]
[null,"SAAS00804702","keyword","Transport"]
[]
["CLOSTRIBL3_v1_12502","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000170765","cofactor","Name=FAD; Xref=ChEBI:CHEBI:57692","_","_","RU362125","RuleBase"]
[null,"UR000170765","GO","GO:0050660","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","FAD","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Oxidoreductase","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Flavoprotein","_","_","RU362125","RuleBase"]
[null,"UR000170765","similarity","Belongs to the acyl-CoA dehydrogenase family","_","_","RU362125","RuleBase"]
[]
["CLOSTRIBL3_v1_11587","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000170765","cofactor","Name=FAD; Xref=ChEBI:CHEBI:57692","_","_","RU362125","RuleBase"]
[null,"UR000170765","GO","GO:0050660","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Oxidoreductase","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Flavoprotein","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","FAD","_","_","RU362125","RuleBase"]
[null,"UR000170765","similarity","Belongs to the acyl-CoA dehydrogenase family","_","_","RU362125","RuleBase"]
[]
["CLOSTRIBL3_v1_12012","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000170765","cofactor","Name=FAD; Xref=ChEBI:CHEBI:57692","_","_","RU362125","RuleBase"]
[null,"UR000170765","GO","GO:0050660","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Oxidoreductase","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Flavoprotein","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","FAD","_","_","RU362125","RuleBase"]
[null,"UR000170765","similarity","Belongs to the acyl-CoA dehydrogenase family","_","_","RU362125","RuleBase"]
[]
["CLOSTRIBL3_v1_12013","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000170765","cofactor","Name=FAD; Xref=ChEBI:CHEBI:57692","_","_","RU362125","RuleBase"]
[null,"UR000170765","GO","GO:0050660","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Flavoprotein","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Oxidoreductase","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","FAD","_","_","RU362125","RuleBase"]
[null,"UR000170765","similarity","Belongs to the acyl-CoA dehydrogenase family","_","_","RU362125","RuleBase"]
[]
["CLOSTRIBL3_v1_20310","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000170765","cofactor","Name=FAD; Xref=ChEBI:CHEBI:57692","_","_","RU362125","RuleBase"]
[null,"UR000170765","GO","GO:0050660","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Oxidoreductase","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Flavoprotein","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","FAD","_","_","RU362125","RuleBase"]
[null,"UR000170765","similarity","Belongs to the acyl-CoA dehydrogenase family","_","_","RU362125","RuleBase"]
[]
["CLOSTRIBL3_v1_11710","UniRule","Annotation type","Annotation value"]
[null,"SAAS00483886","keyword","ATP-binding"]
[null,"SAAS00483909","keyword","Kinase"]
[null,"SAAS00483892","keyword","Nucleotide-binding"]
[null,"SAAS00483925","keyword","Transferase"]
[null,"SAAS00688878","similarity","Belongs to the acetokinase family"]
[]
["CLOSTRIBL3_v1_11710","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000162883","catalytic activity","ATP + butanoate = ADP + butanoyl phosphate","_","_","MF_00542","HAMAP"]
[null,"UR000162883","gene name","buk","_","_","MF_00542","HAMAP"]
[null,"UR000162883","GO","GO:0005737","_","_","MF_00542","HAMAP"]
[null,"UR000162883","GO","GO:0016310","_","_","MF_00542","HAMAP"]
[null,"UR000162883","GO","GO:0047761","_","_","MF_00542","HAMAP"]
[null,"UR000162883","keyword","Transferase","_","_","MF_00542","HAMAP"]
[null,"UR000162883","keyword","ATP-binding","_","_","MF_00542","HAMAP"]
[null,"UR000000717","keyword","Transferase","_","_","RU003835","RuleBase"]
[null,"UR000162883","keyword","Kinase","_","_","MF_00542","HAMAP"]
[null,"UR000162883","keyword","Cytoplasm","_","_","MF_00542","HAMAP"]
[null,"UR000162883","keyword","Nucleotide-binding","_","_","MF_00542","HAMAP"]
[null,"UR000000717","keyword","Kinase","_","_","RU003835","RuleBase"]
[null,"UR000162883","product  name (synonym)","Branched-chain carboxylic acid kinase","_","_","MF_00542","HAMAP"]
[null,"UR000162883","product - EC number","2.7.2.7","_","_","MF_00542","HAMAP"]
[null,"UR000162883","product name","Probable butyrate kinase","_","_","MF_00542","HAMAP"]
[null,"UR000162883","product name","BK","_","_","MF_00542","HAMAP"]
[null,"UR000000717","similarity","Belongs to the acetokinase family","_","_","RU003835","RuleBase"]
[null,"UR000162883","similarity","Belongs to the acetokinase family","_","_","MF_00542","HAMAP"]
[null,"UR000162883","subcellular location","Cytoplasm","_","_","MF_00542","HAMAP"]
[]
["CLOSTRIBL3_v1_20086","UniRule","Annotation type","Annotation value"]
[null,"SAAS00483886","keyword","ATP-binding"]
[null,"SAAS00483909","keyword","Kinase"]
[null,"SAAS00483892","keyword","Nucleotide-binding"]
[null,"SAAS00483925","keyword","Transferase"]
[null,"SAAS00688878","similarity","Belongs to the acetokinase family"]
[]
["CLOSTRIBL3_v1_20086","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000162883","catalytic activity","ATP + butanoate = ADP + butanoyl phosphate","_","_","MF_00542","HAMAP"]
[null,"UR000162883","gene name","buk","_","_","MF_00542","HAMAP"]
[null,"UR000162883","GO","GO:0005737","_","_","MF_00542","HAMAP"]
[null,"UR000162883","GO","GO:0047761","_","_","MF_00542","HAMAP"]
[null,"UR000162883","GO","GO:0016310","_","_","MF_00542","HAMAP"]
[null,"UR000162883","keyword","Kinase","_","_","MF_00542","HAMAP"]
[null,"UR000162883","keyword","ATP-binding","_","_","MF_00542","HAMAP"]
[null,"UR000000717","keyword","Kinase","_","_","RU003835","RuleBase"]
[null,"UR000162883","keyword","Transferase","_","_","MF_00542","HAMAP"]
[null,"UR000162883","keyword","Cytoplasm","_","_","MF_00542","HAMAP"]
[null,"UR000162883","keyword","Nucleotide-binding","_","_","MF_00542","HAMAP"]
[null,"UR000000717","keyword","Transferase","_","_","RU003835","RuleBase"]
[null,"UR000162883","product  name (synonym)","Branched-chain carboxylic acid kinase","_","_","MF_00542","HAMAP"]
[null,"UR000162883","product - EC number","2.7.2.7","_","_","MF_00542","HAMAP"]
[null,"UR000162883","product name","Probable butyrate kinase","_","_","MF_00542","HAMAP"]
[null,"UR000162883","product name","BK","_","_","MF_00542","HAMAP"]
[null,"UR000162883","similarity","Belongs to the acetokinase family","_","_","MF_00542","HAMAP"]
[null,"UR000000717","similarity","Belongs to the acetokinase family","_","_","RU003835","RuleBase"]
[null,"UR000162883","subcellular location","Cytoplasm","_","_","MF_00542","HAMAP"]
[]
["CLOSTRIBL3_v1_20087","UniRule","Annotation type","Annotation value"]
[null,"SAAS00483886","keyword","ATP-binding"]
[null,"SAAS00483909","keyword","Kinase"]
[null,"SAAS00483892","keyword","Nucleotide-binding"]
[null,"SAAS00483925","keyword","Transferase"]
[null,"SAAS00688878","similarity","Belongs to the acetokinase family"]
[]
["CLOSTRIBL3_v1_20087","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000162883","catalytic activity","ATP + butanoate = ADP + butanoyl phosphate","_","_","MF_00542","HAMAP"]
[null,"UR000162883","gene name","buk","_","_","MF_00542","HAMAP"]
[null,"UR000162883","GO","GO:0016310","_","_","MF_00542","HAMAP"]
[null,"UR000162883","GO","GO:0047761","_","_","MF_00542","HAMAP"]
[null,"UR000162883","GO","GO:0005737","_","_","MF_00542","HAMAP"]
[null,"UR000162883","keyword","Nucleotide-binding","_","_","MF_00542","HAMAP"]
[null,"UR000000717","keyword","Transferase","_","_","RU003835","RuleBase"]
[null,"UR000162883","keyword","Kinase","_","_","MF_00542","HAMAP"]
[null,"UR000000717","keyword","Kinase","_","_","RU003835","RuleBase"]
[null,"UR000162883","keyword","ATP-binding","_","_","MF_00542","HAMAP"]
[null,"UR000162883","keyword","Transferase","_","_","MF_00542","HAMAP"]
[null,"UR000162883","keyword","Cytoplasm","_","_","MF_00542","HAMAP"]
[null,"UR000162883","product  name (synonym)","Branched-chain carboxylic acid kinase","_","_","MF_00542","HAMAP"]
[null,"UR000162883","product - EC number","2.7.2.7","_","_","MF_00542","HAMAP"]
[null,"UR000162883","product name","Probable butyrate kinase","_","_","MF_00542","HAMAP"]
[null,"UR000162883","product name","BK","_","_","MF_00542","HAMAP"]
[null,"UR000000717","similarity","Belongs to the acetokinase family","_","_","RU003835","RuleBase"]
[null,"UR000162883","similarity","Belongs to the acetokinase family","_","_","MF_00542","HAMAP"]
[null,"UR000162883","subcellular location","Cytoplasm","_","_","MF_00542","HAMAP"]
[]
["CLOSTRIBL3_v1_11486","UniRule","Annotation type","Annotation value"]
[null,"SAAS00990849","keyword","FAD"]
[null,"SAAS00990758","keyword","Flavoprotein"]
[]
["CLOSTRIBL3_v1_10629","UniRule","Annotation type","Annotation value"]
[null,"SAAS00608488, SAAS01039547","cofactor","Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883"]
[null,"SAAS01036652, SAAS01039352, SAAS01039535","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane"]
[null,"SAAS00028344, SAAS00943857, SAAS01039527","keyword","4Fe-4S"]
[null,"SAAS01036632, SAAS01039362, SAAS01039544","keyword","Electron transport"]
[null,"SAAS00429791, SAAS00943838, SAAS01039522","keyword","Iron"]
[null,"SAAS00028405, SAAS00943845, SAAS01039532","keyword","Iron-sulfur"]
[null,"SAAS01036650, SAAS01039354, SAAS01039538","keyword","Membrane"]
[null,"SAAS00028366, SAAS00943864, SAAS01039539","keyword","Metal-binding"]
[null,"SAAS01033193, SAAS01034144, SAAS01039525","keyword","Oxidoreductase"]
[null,"SAAS01033200, SAAS01034695, SAAS01039528","keyword","Repeat"]
[null,"SAAS01036643, SAAS01039349, SAAS01039533","keyword","Transport"]
[null,"SAAS01036653, SAAS01039348, SAAS01039530","similarity","Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC subfamily"]
[]
["CLOSTRIBL3_v1_10629","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000090104","cofactor","Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 2 [4Fe-4S] clusters per subunit","_","_","MF_00461","HAMAP"]
[null,"UR000090104","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane","_","_","MF_00461","HAMAP"]
[null,"UR000090104","gene name","rnfC","_","_","MF_00461","HAMAP"]
[null,"UR000090104","GO","GO:0022900","_","_","MF_00461","HAMAP"]
[null,"UR000090104","GO","GO:0055114","_","_","MF_00461","HAMAP"]
[null,"UR000090104","GO","GO:0005886","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Membrane","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Metal-binding","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Iron-sulfur","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Electron transport","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Iron","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Transport","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Repeat","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Cell membrane","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","4Fe-4S","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Oxidoreductase","_","_","MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 1 (4Fe-4S)",365,365,"MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 1 (4Fe-4S)",368,368,"MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 1 (4Fe-4S)",371,371,"MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 2 (4Fe-4S)",375,375,"MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 2 (4Fe-4S)",405,405,"MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 2 (4Fe-4S)",408,408,"MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 2 (4Fe-4S)",411,411,"MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 1 (4Fe-4S)",415,415,"MF_00461","HAMAP"]
[null,"UR000090104","product  name (synonym)","Rnf electron transport complex subunit C","_","_","MF_00461","HAMAP"]
[null,"UR000090104","product - EC number","1.18.1.-","_","_","MF_00461","HAMAP"]
[null,"UR000090104","product name","Ion-translocating oxidoreductase complex subunit C","_","_","MF_00461","HAMAP"]
[null,"UR000090104","similarity","Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC subfamily","_","_","MF_00461","HAMAP"]
[null,"UR000090104","subunit","The complex is composed of six subunits: RnfA, RnfB, RnfC, RnfD, RnfE and RnfG","_","_","MF_00461","HAMAP"]
[]
["CLOSTRIBL3_v1_10630","UniRule","Annotation type","Annotation value"]
[null,"SAAS01034734, SAAS01035299","cofactor","Name=FMN; Xref=ChEBI:CHEBI:58210"]
[null,"SAAS01034728","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane"]
[null,"SAAS01034737","keyword","Cell membrane"]
[null,"SAAS01034732","keyword","Electron transport"]
[null,"SAAS01034738, SAAS01035302","keyword","Flavoprotein"]
[null,"SAAS01034739, SAAS01035309","keyword","FMN"]
[null,"SAAS00951777, SAAS01034741","keyword","Membrane"]
[null,"SAAS01034735, SAAS01035300","keyword","Oxidoreductase"]
[null,"SAAS00951796, SAAS01034736","keyword","Transmembrane"]
[null,"SAAS00951768, SAAS01034724","keyword","Transmembrane helix"]
[null,"SAAS00951776, SAAS01034740","keyword","Transport"]
[null,"SAAS00951779, SAAS01034714","similarity","Belongs to the NqrB/RnfD family"]
[]
["CLOSTRIBL3_v1_10630","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000062690","cofactor","Name=FMN; Xref=ChEBI:CHEBI:58210","_","_","MF_00462","HAMAP"]
[null,"UR000062690","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane","_","_","MF_00462","HAMAP"]
[null,"UR000062690","gene name","rnfD","_","_","MF_00462","HAMAP"]
[null,"UR000062690","GO","GO:0022900","_","_","MF_00462","HAMAP"]
[null,"UR000062690","GO","GO:0005886","_","_","MF_00462","HAMAP"]
[null,"UR000062690","GO","GO:0055114","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Transport","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Transmembrane helix","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Electron transport","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Flavoprotein","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Transmembrane","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Cell membrane","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Oxidoreductase","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Membrane","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Phosphoprotein","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","FMN","_","_","MF_00462","HAMAP"]
[null,"UR000062690","modified residue","FMN phosphoryl threonine",163,163,"MF_00462","HAMAP"]
[null,"UR000062690","product  name (synonym)","Rnf electron transport complex subunit D","_","_","MF_00462","HAMAP"]
[null,"UR000062690","product - EC number","1.18.1.-","_","_","MF_00462","HAMAP"]
[null,"UR000062690","product name","Ion-translocating oxidoreductase complex subunit D","_","_","MF_00462","HAMAP"]
[null,"UR000062690","similarity","Belongs to the NqrB/RnfD family","_","_","MF_00462","HAMAP"]
[null,"UR000062690","subunit","The complex is composed of six subunits: RnfA, RnfB, RnfC, RnfD, RnfE and RnfG","_","_","MF_00462","HAMAP"]
[]
["CLOSTRIBL3_v1_10631","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000064652","cofactor","Name=FMN; Xref=ChEBI:CHEBI:58210","_","_","MF_00479","HAMAP"]
[null,"UR000064652","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane","_","_","MF_00479","HAMAP"]
[null,"UR000064652","gene name","rnfG","_","_","MF_00479","HAMAP"]
[null,"UR000064652","GO","GO:0055114","_","_","MF_00479","HAMAP"]
[null,"UR000064652","GO","GO:0005886","_","_","MF_00479","HAMAP"]
[null,"UR000064652","GO","GO:0022900","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Transport","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Cell membrane","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Membrane","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Phosphoprotein","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","FMN","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Flavoprotein","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Transmembrane helix","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Oxidoreductase","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Electron transport","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Transmembrane","_","_","MF_00479","HAMAP"]
[null,"UR000064652","modified residue","FMN phosphoryl threonine",161,161,"MF_00479","HAMAP"]
[null,"UR000064652","product  name (synonym)","Rnf electron transport complex subunit G","_","_","MF_00479","HAMAP"]
[null,"UR000064652","product - EC number","1.18.1.-","_","_","MF_00479","HAMAP"]
[null,"UR000064652","product name","Ion-translocating oxidoreductase complex subunit G","_","_","MF_00479","HAMAP"]
[null,"UR000064652","similarity","Belongs to the RnfG family","_","_","MF_00479","HAMAP"]
[null,"UR000064652","subunit","The complex is composed of six subunits: RnfA, RnfB, RnfC, RnfD, RnfE and RnfG","_","_","MF_00479","HAMAP"]
[]
["CLOSTRIBL3_v1_10632","UniRule","Annotation type","Annotation value"]
[null,"SAAS01034762","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane"]
[null,"SAAS01034760","keyword","Cell membrane"]
[null,"SAAS01034757","keyword","Electron transport"]
[null,"SAAS00095226","keyword","Membrane"]
[null,"SAAS01035351","keyword","Oxidoreductase"]
[null,"SAAS00095471","keyword","Transmembrane"]
[null,"SAAS00465084","keyword","Transmembrane helix"]
[null,"SAAS00095348","keyword","Transport"]
[null,"SAAS00573673","similarity","Belongs to the NqrDE/RnfAE family"]
[]
["CLOSTRIBL3_v1_10632","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000063677","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane","_","_","MF_00478","HAMAP"]
[null,"UR000063677","gene name","rnfE","_","_","MF_00478","HAMAP"]
[null,"UR000063677","GO","GO:0005886","_","_","MF_00478","HAMAP"]
[null,"UR000063677","GO","GO:0055114","_","_","MF_00478","HAMAP"]
[null,"UR000063677","GO","GO:0022900","_","_","MF_00478","HAMAP"]
[null,"UR000063677","keyword","Cell membrane","_","_","MF_00478","HAMAP"]
[null,"UR000063677","keyword","Oxidoreductase","_","_","MF_00478","HAMAP"]
[null,"UR000063677","keyword","Membrane","_","_","MF_00478","HAMAP"]
[null,"UR000063677","keyword","Transport","_","_","MF_00478","HAMAP"]
[null,"UR000063677","keyword","Transmembrane helix","_","_","MF_00478","HAMAP"]
[null,"UR000063677","keyword","Transmembrane","_","_","MF_00478","HAMAP"]
[null,"UR000063677","keyword","Electron transport","_","_","MF_00478","HAMAP"]
[null,"UR000063677","product  name (synonym)","Rnf electron transport complex subunit E","_","_","MF_00478","HAMAP"]
[null,"UR000063677","product - EC number","1.18.1.-","_","_","MF_00478","HAMAP"]
[null,"UR000063677","product name","Ion-translocating oxidoreductase complex subunit E","_","_","MF_00478","HAMAP"]
[null,"UR000063677","similarity","Belongs to the NqrDE/RnfAE family","_","_","MF_00478","HAMAP"]
[null,"UR000063677","subunit","The complex is composed of six subunits: RnfA, RnfB, RnfC, RnfD, RnfE and RnfG","_","_","MF_00478","HAMAP"]
[]
["CLOSTRIBL3_v1_10633","UniRule","Annotation type","Annotation value"]
[null,"SAAS01034726","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane"]
[null,"SAAS01034715","keyword","Electron transport"]
[null,"SAAS00095226","keyword","Membrane"]
[null,"SAAS01035351","keyword","Oxidoreductase"]
[null,"SAAS00095471","keyword","Transmembrane"]
[null,"SAAS00465084","keyword","Transmembrane helix"]
[null,"SAAS00095348","keyword","Transport"]
[null,"SAAS01034710","product - EC number","1.18.1.-"]
[null,"SAAS00573673","similarity","Belongs to the NqrDE/RnfAE family"]
[]
["CLOSTRIBL3_v1_10633","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000062678","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane","_","_","MF_00459","HAMAP"]
[null,"UR000062678","gene name","rnfA","_","_","MF_00459","HAMAP"]
[null,"UR000062678","GO","GO:0005886","_","_","MF_00459","HAMAP"]
[null,"UR000062678","GO","GO:0022900","_","_","MF_00459","HAMAP"]
[null,"UR000062678","GO","GO:0055114","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Transmembrane helix","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Oxidoreductase","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Membrane","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Transport","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Transmembrane","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Cell membrane","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Electron transport","_","_","MF_00459","HAMAP"]
[null,"UR000062678","product  name (synonym)","Rnf electron transport complex subunit A","_","_","MF_00459","HAMAP"]
[null,"UR000062678","product - EC number","1.18.1.-","_","_","MF_00459","HAMAP"]
[null,"UR000062678","product name","Ion-translocating oxidoreductase complex subunit A","_","_","MF_00459","HAMAP"]
[null,"UR000062678","similarity","Belongs to the NqrDE/RnfAE family","_","_","MF_00459","HAMAP"]
[null,"UR000062678","subunit","The complex is composed of six subunits: RnfA, RnfB, RnfC, RnfD, RnfE and RnfG","_","_","MF_00459","HAMAP"]
[]
["CLOSTRIBL3_v1_10634","UniRule","Annotation type","Annotation value"]
[null,"SAAS00617120, SAAS01039554","cofactor","Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883"]
[null,"SAAS01039548","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane"]
[null,"SAAS00617118, SAAS01039526","keyword","4Fe-4S"]
[null,"SAAS01039523","keyword","Electron transport"]
[null,"SAAS00617117, SAAS01039549","keyword","Iron"]
[null,"SAAS00617121, SAAS01039553","keyword","Iron-sulfur"]
[null,"SAAS01039536","keyword","Membrane"]
[null,"SAAS00617119, SAAS01039542","keyword","Metal-binding"]
[null,"SAAS01039529","keyword","Oxidoreductase"]
[null,"SAAS01039551","keyword","Repeat"]
[null,"SAAS01039534","keyword","Transport"]
[null,"SAAS01039531","similarity","Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily"]
[]
["CLOSTRIBL3_v1_10634","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000090116","cofactor","Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883","_","_","MF_00463","HAMAP"]
[null,"UR000090116","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane","_","_","MF_00463","HAMAP"]
[null,"UR000090116","gene name","rnfB","_","_","MF_00463","HAMAP"]
[null,"UR000090116","GO","GO:0051539","_","_","MF_00463","HAMAP"]
[null,"UR000090116","GO","GO:0055114","_","_","MF_00463","HAMAP"]
[null,"UR000090116","GO","GO:0005886","_","_","MF_00463","HAMAP"]
[null,"UR000090116","GO","GO:0022900","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Oxidoreductase","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Transport","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Repeat","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","4Fe-4S","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Metal-binding","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Electron transport","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Iron","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Membrane","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Iron-sulfur","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Cell membrane","_","_","MF_00463","HAMAP"]
[null,"UR000090116","metal binding","Iron-sulfur 2 (4Fe-4S)",139,139,"MF_00463","HAMAP"]
[null,"UR000090116","metal binding","Iron-sulfur 2 (4Fe-4S)",143,143,"MF_00463","HAMAP"]
[null,"UR000090116","metal binding","Iron-sulfur 2 (4Fe-4S)",149,149,"MF_00463","HAMAP"]
[null,"UR000090116","metal binding","Iron-sulfur 2 (4Fe-4S)",183,183,"MF_00463","HAMAP"]
[null,"UR000090116","product  name (synonym)","Rnf electron transport complex subunit B","_","_","MF_00463","HAMAP"]
[null,"UR000090116","product - EC number","1.18.1.-","_","_","MF_00463","HAMAP"]
[null,"UR000090116","product name","Ion-translocating oxidoreductase complex subunit B","_","_","MF_00463","HAMAP"]
[null,"UR000090116","similarity","Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily","_","_","MF_00463","HAMAP"]
[null,"UR000090116","subunit","The complex is composed of six subunits: RnfA, RnfB, RnfC, RnfD, RnfE and RnfG","_","_","MF_00463","HAMAP"]
[]
["CLOSTRIBL3_v1_10092","UniRule","Annotation type","Annotation value"]
[null,"SAAS00608488","cofactor","Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883"]
[null,"SAAS00028344, SAAS00943857","keyword","4Fe-4S"]
[null,"SAAS00429791, SAAS00943838","keyword","Iron"]
[null,"SAAS00028405, SAAS00943845","keyword","Iron-sulfur"]
[null,"SAAS00028366, SAAS00943864","keyword","Metal-binding"]
[null,"SAAS01033193, SAAS01034144","keyword","Oxidoreductase"]
[null,"SAAS01033200, SAAS01034695","keyword","Repeat"]
[]
["CLOSTRIBL3_v1_10745","UniRule","Annotation type","Annotation value"]
[null,"SAAS00923789","keyword","Acyltransferase"]
[null,"SAAS00923780","keyword","Transferase"]
[]
["CLOSTRIBL3_v1_10746","UniRule","Annotation type","Annotation value"]
[null,"SAAS00672006","cofactor","Name=Mg(2+); Xref=ChEBI:CHEBI:18420"]
[null,"SAAS00483886","keyword","ATP-binding"]
[null,"SAAS00483909","keyword","Kinase"]
[null,"SAAS00011608, SAAS00091199","keyword","Magnesium"]
[null,"SAAS00011656, SAAS00091203","keyword","Metal-binding"]
[null,"SAAS00483892","keyword","Nucleotide-binding"]
[null,"SAAS00483925","keyword","Transferase"]
[null,"SAAS00688878","similarity","Belongs to the acetokinase family"]
[null,"SAAS00011637, SAAS00011667, SAAS00130554, SAAS00130644","subcellular location,keyword","Cytoplasm"]
[]
["CLOSTRIBL3_v1_10746","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000037499","catalytic activity","ATP + acetate = ADP + acetyl phosphate","_","_","MF_00020","HAMAP"]
[null,"UR000037499","cofactor","Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Mg(2+). Can also accept Mn(2+)","_","_","MF_00020","HAMAP"]
[null,"UR000037499","function","Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction","_","_","MF_00020","HAMAP"]
[null,"UR000037499","gene name","ackA","_","_","MF_00020","HAMAP"]
[null,"UR000037499","GO","GO:0005737","_","_","MF_00020","HAMAP"]
[null,"UR000037499","GO","GO:0000287","_","_","MF_00020","HAMAP"]
[null,"UR000037499","GO","GO:0016310","_","_","MF_00020","HAMAP"]
[null,"UR000037499","GO","GO:0008776","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Metal-binding","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Nucleotide-binding","_","_","MF_00020","HAMAP"]
[null,"UR000000717","keyword","Kinase","_","_","RU003835","RuleBase"]
[null,"UR000037499","keyword","Kinase","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Magnesium","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","ATP-binding","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Cytoplasm","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Transferase","_","_","MF_00020","HAMAP"]
[null,"UR000000717","keyword","Transferase","_","_","RU003835","RuleBase"]
[null,"UR000037499","metal binding","Magnesium",7,7,"MF_00020","HAMAP"]
[null,"UR000037499","metal binding","Magnesium",383,383,"MF_00020","HAMAP"]
[null,"UR000037499","nucleotide binding","ATP",207,211,"MF_00020","HAMAP"]
[null,"UR000037499","nucleotide binding","ATP",282,284,"MF_00020","HAMAP"]
[null,"UR000037499","nucleotide binding","ATP",330,334,"MF_00020","HAMAP"]
[null,"UR000037499","pathway","Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2","_","_","MF_00020","HAMAP"]
[null,"UR000037499","product  name (synonym)","Acetokinase","_","_","MF_00020","HAMAP"]
[null,"UR000037499","product - EC number","2.7.2.1","_","_","MF_00020","HAMAP"]
[null,"UR000037499","product name","Acetate kinase","_","_","MF_00020","HAMAP"]
[null,"UR000000717","similarity","Belongs to the acetokinase family","_","_","RU003835","RuleBase"]
[null,"UR000037499","similarity","Belongs to the acetokinase family","_","_","MF_00020","HAMAP"]
[null,"UR000037499","site","Transition state stabilizer",179,179,"MF_00020","HAMAP"]
[null,"UR000037499","site","Transition state stabilizer",240,240,"MF_00020","HAMAP"]
[null,"UR000037499","site actif","Proton donor/acceptor",147,147,"MF_00020","HAMAP"]
[null,"UR000037499","site binding","ATP",14,14,"MF_00020","HAMAP"]
[null,"UR000037499","site binding","Substrate",90,90,"MF_00020","HAMAP"]
[null,"UR000037499","subcellular location","Cytoplasm","_","_","MF_00020","HAMAP"]
[null,"UR000037499","subunit","Homodimer","_","_","MF_00020","HAMAP"]
[]
["CLOSTRIBL3_v1_12732","UniRule","Annotation type","Annotation value"]
[null,"SAAS00334059, SAAS00359424","catalytic activity","Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH"]
[null,"SAAS00436908","keyword","Aromatic hydrocarbons catabolism"]
[null,"SAAS00436899","keyword","NAD"]
[null,"SAAS00436905","keyword","Oxidoreductase"]
[null,"SAAS00327777","product - EC number","1.2.1.10"]
[null,"SAAS00334124, SAAS00359423","product name","Acetaldehyde dehydrogenase"]
[null,"SAAS00551863","similarity","Belongs to the acetaldehyde dehydrogenase family"]
[]
["CLOSTRIBL3_v1_12732","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000083169","catalytic activity","Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH","_","_","MF_01657","HAMAP"]
[null,"UR000083169","function","Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds","_","_","MF_01657","HAMAP"]
[null,"UR000083169","GO","GO:0019439","_","_","MF_01657","HAMAP"]
[null,"UR000083169","GO","GO:0008774","_","_","MF_01657","HAMAP"]
[null,"UR000083169","GO","GO:0051287","_","_","MF_01657","HAMAP"]
[null,"UR000083169","keyword","Aromatic hydrocarbons catabolism","_","_","MF_01657","HAMAP"]
[null,"UR000083169","keyword","Oxidoreductase","_","_","MF_01657","HAMAP"]
[null,"UR000083169","keyword","NAD","_","_","MF_01657","HAMAP"]
[null,"UR000083169","nucleotide binding","NAD",155,163,"MF_01657","HAMAP"]
[null,"UR000083169","product  name (synonym)","Acetaldehyde dehydrogenase [acetylating]","_","_","MF_01657","HAMAP"]
[null,"UR000083169","product - EC number","1.2.1.10","_","_","MF_01657","HAMAP"]
[null,"UR000083169","product name","Acetaldehyde dehydrogenase","_","_","MF_01657","HAMAP"]
[null,"UR000083169","similarity","Belongs to the acetaldehyde dehydrogenase family","_","_","MF_01657","HAMAP"]
[null,"UR000083169","site actif","Acyl-thioester intermediate",124,124,"MF_01657","HAMAP"]
[null,"UR000083169","site binding","NAD",265,265,"MF_01657","HAMAP"]

{"sheet":"PRIAM EC number","index":7,"n_rows":285,"n_cols":15,"rows_kept":285}
["CLOSTRIBL3_v1_10010","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.1.27","high",1,321,8e-11,23,125,389,265,"L-lactate dehydrogenase","L-lactic acid dehydrogenase. L-lactic dehydrogenase","(S)-lactate + NAD(+) = pyruvate + NADH","_","-!- Also oxidizes other (S)-2-hydroxymonocarboxylic acids. -!- NADP(+) acts, more slowly, with the animal, but not the bacterial, enzyme"]
[]
["CLOSTRIBL3_v1_10012","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.1.27","high",1,321,{"v":3e-95,"d":"3.00E-95"},41,1,309,309,"L-lactate dehydrogenase","L-lactic acid dehydrogenase. L-lactic dehydrogenase","(S)-lactate + NAD(+) = pyruvate + NADH","_","-!- Also oxidizes other (S)-2-hydroxymonocarboxylic acids. -!- NADP(+) acts, more slowly, with the animal, but not the bacterial, enzyme"]
[null,"1.1.1.37","no",1,302,{"v":2e-38,"d":"2.00E-38"},30,34,315,282,"Malate dehydrogenase","Malic dehydrogenase","(S)-malate + NAD(+) = oxaloacetate + NADH","_","-!- Also oxidizes some other 2-hydroxydicarboxylic acids"]
[null,"1.1.1.82","no",1,322,1e-11,21,116,314,199,"Malate dehydrogenase (NADP(+))","NADP-linked malate dehydrogenase","(S)-malate + NADP(+) = oxaloacetate + NADPH","_","-!- Activated by light"]
[]
["CLOSTRIBL3_v1_12309","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.3.15","medium",1,363,{"v":2e-40,"d":"2.00E-40"},50,222,356,135,"(S)-2-hydroxy-acid oxidase","Glycolate oxidase. Hydroxy-acid oxidase A. Hydroxy-acid oxidase B","(S)-2-hydroxy acid + O(2) = 2-oxo acid + H(2)O(2)","FMN","-!- Exists as two major isoenzymes; the A form preferentially oxidizes short-chain aliphatic hydroxy acids; the B form preferentially oxidizes long-chain and aromatic hydroxy acids. -!- The rat isoenzyme B also acts as EC 1.4.3.2. -!- Formerly EC 1.1.3.1"]
[null,"1.13.12.4","no",1,383,{"v":3e-25,"d":"3.00E-25"},36,213,346,134,"Lactate 2-monooxygenase","Lactate oxidase. Lactate oxidative decarboxylase. Lactate oxygenase","(S)-lactate + O(2) = acetate + CO(2) + H(2)O","FMN","-!- Formerly EC 1.1.3.2"]
[null,"5.3.3.2","no",1,362,{"v":6e-19,"d":"6.00E-19"},33,212,346,135,"Isopentenyl-diphosphate Delta-isomerase","IPP isomerase. Isopentenylpyrophosphate Delta-isomerase. Isopentenylpyrophosphate isomerase. Methylbutenylpyrophosphate isomerase","Isopentenyl diphosphate = dimethylallyl diphosphate","FAD or FMN; Mg(2+) or Ca(2+) or Mn(2+)","_"]
[null,"1.1.99.31","no",1,393,9e-15,35,227,345,119,"(S)-mandelate dehydrogenase","L(+)-mandelate dehydrogenase. MDH","(S)-2-hydroxy-2-phenylacetate + acceptor = 2-oxo-2-phenylacetate + reduced acceptor","_","-!- While all enzymes of this family oxidize the (S)-enantiomer of an alpha-hydroxy acid to an alpha-oxo acid, the ultimate oxidant (oxygen, intramolecular heme or some other acceptor) depends on the particular enzyme. -!- Transfers the electron pair from FMNH(2) to a component of the electron transport chain, most probably ubiquinone. -!- It is part of a metabolic pathway in Pseudomonads that allows these organisms to utilize mandelic acid, derivatized from the common soil metabolite amygdalin, as the sole source of carbon and energy. -!- Has a large active-site pocket and preferentially binds substrates with longer sidechains, e.g. 2-hydroxyoctanoate rather than 2-hydroxybutyrate. -!- It also prefers substrates that, like (S)-mandelate, have beta unsaturation, e.g. (indol-3-yl)glycolate compared with (indol-3- yl)lactate. -!- Esters of mandelate, such as methyl (S)-mandelate, are also substrates"]
[]
["CLOSTRIBL3_v1_12417","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.2.1.51","high",1,1928,0,47,8,1171,1164,"Pyruvate dehydrogenase (NADP(+))","Pyruvate:NADP(+) oxidoreductase","Pyruvate + CoA + NADP(+) = acetyl-CoA + CO(2) + NADPH","_","-!- The Euglena enzyme can also use FAD or methylviologen as acceptor, more slowly. -!- Inhibited by oxygen"]
[null,"1.16.1.5","no",1,1803,0,50,6,1169,1164,"Aquacobalamin reductase (NADPH)","Aquacobalamin (reduced nicotinamide adenine dinucleotide phosphate) reductase. NADPH-linked aquacobalamin reductase. NADPH:aquacob(III)alamin oxidoreductase","2 cob(II)alamin + NADP(+) + 2 H(2)O = 2 aquacob(III)alamin + NADPH","Flavoprotein","-!- Acts on aquacob(III)alamin and hydroxycobalamin, but not on cyanocobalamin. -!- Formerly EC 1.6.99.11"]
[null,"1.2.7.1","no",3,395,{"v":5e-60,"d":"5.00E-60"},34,5,385,381,"Pyruvate synthase","2-oxobutyrate synthase. 2-oxobutyrate-ferredoxin oxidoreductase. Alpha-ketobutyrate synthase. Alpha-ketobutyrate-ferredoxin oxidoreductase. Pyruvate oxidoreductase. Pyruvate synthetase. Pyruvic-ferredoxin oxidoreductase","Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Thiamine diphosphate","-!- The enzyme also decarboxylates 2-oxobutanoate with lower efficiency, but shows no activity with 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.3 and EC 1.2.7.7"]
[null,"1.2.7.7","no",4,328,{"v":3E-32,"d":"3.00E-32"},25,6,329,324,"3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)","2-ketoisovalerate ferredoxin reductase. 2-oxoisovalerate ferredoxin reductase. 3-methyl-2-oxobutanoate synthase (ferredoxin). Branched-chain ketoacid ferredoxin reductase. Branched-chain oxo acid ferredoxin reductase. Keto-valine-ferredoxin oxidoreductase. Ketoisovalerate ferredoxin reductase. Ketoisovalerate oxidoreductase. VOR","3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO(2) + 2 reduced ferredoxin + H(+)","Iron-sulfur; Tungstopterin","-!- The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. -!- Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo- pentanoate, and 2-oxobutanoate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that reversibly catalyze the oxidative decarboxylation of different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.1 and EC 1.2.7.3"]
[null,"1.2.7.1","no",1,184,6e-15,25,417,611,195,"Pyruvate synthase","2-oxobutyrate synthase. 2-oxobutyrate-ferredoxin oxidoreductase. Alpha-ketobutyrate synthase. Alpha-ketobutyrate-ferredoxin oxidoreductase. Pyruvate oxidoreductase. Pyruvate synthetase. Pyruvic-ferredoxin oxidoreductase","Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Thiamine diphosphate","-!- The enzyme also decarboxylates 2-oxobutanoate with lower efficiency, but shows no activity with 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.3 and EC 1.2.7.7"]
[]
["CLOSTRIBL3_v1_12774","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.2.7.7","high",3,210,{"v":6E-37,"d":"6.00E-37"},34,22,226,205,"3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)","2-ketoisovalerate ferredoxin reductase. 2-oxoisovalerate ferredoxin reductase. 3-methyl-2-oxobutanoate synthase (ferredoxin). Branched-chain ketoacid ferredoxin reductase. Branched-chain oxo acid ferredoxin reductase. Keto-valine-ferredoxin oxidoreductase. Ketoisovalerate ferredoxin reductase. Ketoisovalerate oxidoreductase. VOR","3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO(2) + 2 reduced ferredoxin + H(+)","Iron-sulfur; Tungstopterin","-!- The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. -!- Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo- pentanoate, and 2-oxobutanoate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that reversibly catalyze the oxidative decarboxylation of different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.1 and EC 1.2.7.3"]
[null,"1.2.1.51","no",1,1928,3e-14,26,107,301,195,"Pyruvate dehydrogenase (NADP(+))","Pyruvate:NADP(+) oxidoreductase","Pyruvate + CoA + NADP(+) = acetyl-CoA + CO(2) + NADPH","_","-!- The Euglena enzyme can also use FAD or methylviologen as acceptor, more slowly. -!- Inhibited by oxygen"]
[null,"1.2.7.3","no",2,265,2e-11,27,19,221,203,"2-oxoglutarate synthase","2-ketoglutarate ferredoxin oxidoreductase. 2-oxoglutarate ferredoxin oxidoreductase. Alpha-ketoglutarate synthase. Alpha-ketoglutarate-ferredoxin oxidoreductase. KGOR","2-oxoglutarate + CoA + 2 oxidized ferredoxin = succinyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Thiamine diphosphate","-!- Highly specific for 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.1 and EC 1.2.7.7. -!- Formerly EC 1.2.7.9"]
[]
["CLOSTRIBL3_v1_12775","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.2.7.1","high",3,395,{"v":1e-137,"d":"1.00E-137"},50,7,391,385,"Pyruvate synthase","2-oxobutyrate synthase. 2-oxobutyrate-ferredoxin oxidoreductase. Alpha-ketobutyrate synthase. Alpha-ketobutyrate-ferredoxin oxidoreductase. Pyruvate oxidoreductase. Pyruvate synthetase. Pyruvic-ferredoxin oxidoreductase","Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Thiamine diphosphate","-!- The enzyme also decarboxylates 2-oxobutanoate with lower efficiency, but shows no activity with 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.3 and EC 1.2.7.7"]
[null,"1.2.7.7","no",4,328,{"v":8E-70,"d":"8.00E-70"},38,7,324,318,"3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)","2-ketoisovalerate ferredoxin reductase. 2-oxoisovalerate ferredoxin reductase. 3-methyl-2-oxobutanoate synthase (ferredoxin). Branched-chain ketoacid ferredoxin reductase. Branched-chain oxo acid ferredoxin reductase. Keto-valine-ferredoxin oxidoreductase. Ketoisovalerate ferredoxin reductase. Ketoisovalerate oxidoreductase. VOR","3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO(2) + 2 reduced ferredoxin + H(+)","Iron-sulfur; Tungstopterin","-!- The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. -!- Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo- pentanoate, and 2-oxobutanoate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that reversibly catalyze the oxidative decarboxylation of different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.1 and EC 1.2.7.3"]
[null,"1.2.1.51","no",1,1928,{"v":3e-35,"d":"3.00E-35"},27,23,372,350,"Pyruvate dehydrogenase (NADP(+))","Pyruvate:NADP(+) oxidoreductase","Pyruvate + CoA + NADP(+) = acetyl-CoA + CO(2) + NADPH","_","-!- The Euglena enzyme can also use FAD or methylviologen as acceptor, more slowly. -!- Inhibited by oxygen"]
[null,"1.16.1.5","no",1,1803,{"v":2e-34,"d":"2.00E-34"},30,6,372,367,"Aquacobalamin reductase (NADPH)","Aquacobalamin (reduced nicotinamide adenine dinucleotide phosphate) reductase. NADPH-linked aquacobalamin reductase. NADPH:aquacob(III)alamin oxidoreductase","2 cob(II)alamin + NADP(+) + 2 H(2)O = 2 aquacob(III)alamin + NADPH","Flavoprotein","-!- Acts on aquacob(III)alamin and hydroxycobalamin, but not on cyanocobalamin. -!- Formerly EC 1.6.99.11"]
[null,"1.2.7.3","no",3,344,{"v":5e-27,"d":"5.00E-27"},27,7,335,329,"2-oxoglutarate synthase","2-ketoglutarate ferredoxin oxidoreductase. 2-oxoglutarate ferredoxin oxidoreductase. Alpha-ketoglutarate synthase. Alpha-ketoglutarate-ferredoxin oxidoreductase. KGOR","2-oxoglutarate + CoA + 2 oxidized ferredoxin = succinyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Thiamine diphosphate","-!- Highly specific for 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.1 and EC 1.2.7.7. -!- Formerly EC 1.2.7.9"]
[]
["CLOSTRIBL3_v1_12777","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.2.7.1","high",1,184,{"v":8e-49,"d":"8.00E-49"},45,5,190,186,"Pyruvate synthase","2-oxobutyrate synthase. 2-oxobutyrate-ferredoxin oxidoreductase. Alpha-ketobutyrate synthase. Alpha-ketobutyrate-ferredoxin oxidoreductase. Pyruvate oxidoreductase. Pyruvate synthetase. Pyruvic-ferredoxin oxidoreductase","Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Thiamine diphosphate","-!- The enzyme also decarboxylates 2-oxobutanoate with lower efficiency, but shows no activity with 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.3 and EC 1.2.7.7"]
[null,"1.2.7.7","no",1,187,{"v":3E-37,"d":"3.00E-37"},42,5,172,168,"3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)","2-ketoisovalerate ferredoxin reductase. 2-oxoisovalerate ferredoxin reductase. 3-methyl-2-oxobutanoate synthase (ferredoxin). Branched-chain ketoacid ferredoxin reductase. Branched-chain oxo acid ferredoxin reductase. Keto-valine-ferredoxin oxidoreductase. Ketoisovalerate ferredoxin reductase. Ketoisovalerate oxidoreductase. VOR","3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO(2) + 2 reduced ferredoxin + H(+)","Iron-sulfur; Tungstopterin","-!- The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. -!- Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo- pentanoate, and 2-oxobutanoate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that reversibly catalyze the oxidative decarboxylation of different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.1 and EC 1.2.7.3"]
[]
["CLOSTRIBL3_v1_10343","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.2.1.51","high",1,1928,0,47,7,1164,1158,"Pyruvate dehydrogenase (NADP(+))","Pyruvate:NADP(+) oxidoreductase","Pyruvate + CoA + NADP(+) = acetyl-CoA + CO(2) + NADPH","_","-!- The Euglena enzyme can also use FAD or methylviologen as acceptor, more slowly. -!- Inhibited by oxygen"]
[null,"1.16.1.5","no",1,1803,0,50,5,1164,1160,"Aquacobalamin reductase (NADPH)","Aquacobalamin (reduced nicotinamide adenine dinucleotide phosphate) reductase. NADPH-linked aquacobalamin reductase. NADPH:aquacob(III)alamin oxidoreductase","2 cob(II)alamin + NADP(+) + 2 H(2)O = 2 aquacob(III)alamin + NADPH","Flavoprotein","-!- Acts on aquacob(III)alamin and hydroxycobalamin, but not on cyanocobalamin. -!- Formerly EC 1.6.99.11"]
[null,"1.2.7.1","no",3,395,{"v":4e-62,"d":"4.00E-62"},34,4,391,388,"Pyruvate synthase","2-oxobutyrate synthase. 2-oxobutyrate-ferredoxin oxidoreductase. Alpha-ketobutyrate synthase. Alpha-ketobutyrate-ferredoxin oxidoreductase. Pyruvate oxidoreductase. Pyruvate synthetase. Pyruvic-ferredoxin oxidoreductase","Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Thiamine diphosphate","-!- The enzyme also decarboxylates 2-oxobutanoate with lower efficiency, but shows no activity with 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.3 and EC 1.2.7.7"]
[null,"1.2.7.7","no",4,328,{"v":3E-32,"d":"3.00E-32"},23,5,328,324,"3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)","2-ketoisovalerate ferredoxin reductase. 2-oxoisovalerate ferredoxin reductase. 3-methyl-2-oxobutanoate synthase (ferredoxin). Branched-chain ketoacid ferredoxin reductase. Branched-chain oxo acid ferredoxin reductase. Keto-valine-ferredoxin oxidoreductase. Ketoisovalerate ferredoxin reductase. Ketoisovalerate oxidoreductase. VOR","3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO(2) + 2 reduced ferredoxin + H(+)","Iron-sulfur; Tungstopterin","-!- The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. -!- Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo- pentanoate, and 2-oxobutanoate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that reversibly catalyze the oxidative decarboxylation of different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.1 and EC 1.2.7.3"]
[null,"1.2.7.1","no",1,184,2e-11,24,446,610,165,"Pyruvate synthase","2-oxobutyrate synthase. 2-oxobutyrate-ferredoxin oxidoreductase. Alpha-ketobutyrate synthase. Alpha-ketobutyrate-ferredoxin oxidoreductase. Pyruvate oxidoreductase. Pyruvate synthetase. Pyruvic-ferredoxin oxidoreductase","Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Thiamine diphosphate","-!- The enzyme also decarboxylates 2-oxobutanoate with lower efficiency, but shows no activity with 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.3 and EC 1.2.7.7"]
[]
["CLOSTRIBL3_v1_20129","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.2.1.51","high",1,1928,0,47,11,1168,1158,"Pyruvate dehydrogenase (NADP(+))","Pyruvate:NADP(+) oxidoreductase","Pyruvate + CoA + NADP(+) = acetyl-CoA + CO(2) + NADPH","_","-!- The Euglena enzyme can also use FAD or methylviologen as acceptor, more slowly. -!- Inhibited by oxygen"]
[null,"1.16.1.5","no",1,1803,0,49,8,1168,1161,"Aquacobalamin reductase (NADPH)","Aquacobalamin (reduced nicotinamide adenine dinucleotide phosphate) reductase. NADPH-linked aquacobalamin reductase. NADPH:aquacob(III)alamin oxidoreductase","2 cob(II)alamin + NADP(+) + 2 H(2)O = 2 aquacob(III)alamin + NADPH","Flavoprotein","-!- Acts on aquacob(III)alamin and hydroxycobalamin, but not on cyanocobalamin. -!- Formerly EC 1.6.99.11"]
[null,"1.2.7.1","no",3,395,{"v":4e-49,"d":"4.00E-49"},31,9,386,378,"Pyruvate synthase","2-oxobutyrate synthase. 2-oxobutyrate-ferredoxin oxidoreductase. Alpha-ketobutyrate synthase. Alpha-ketobutyrate-ferredoxin oxidoreductase. Pyruvate oxidoreductase. Pyruvate synthetase. Pyruvic-ferredoxin oxidoreductase","Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Thiamine diphosphate","-!- The enzyme also decarboxylates 2-oxobutanoate with lower efficiency, but shows no activity with 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.3 and EC 1.2.7.7"]
[null,"1.2.7.7","no",4,328,{"v":3e-26,"d":"3.00E-26"},23,9,337,329,"3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)","2-ketoisovalerate ferredoxin reductase. 2-oxoisovalerate ferredoxin reductase. 3-methyl-2-oxobutanoate synthase (ferredoxin). Branched-chain ketoacid ferredoxin reductase. Branched-chain oxo acid ferredoxin reductase. Keto-valine-ferredoxin oxidoreductase. Ketoisovalerate ferredoxin reductase. Ketoisovalerate oxidoreductase. VOR","3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO(2) + 2 reduced ferredoxin + H(+)","Iron-sulfur; Tungstopterin","-!- The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. -!- Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo- pentanoate, and 2-oxobutanoate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that reversibly catalyze the oxidative decarboxylation of different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.1 and EC 1.2.7.3"]
[null,"1.2.7.1","no",1,184,2e-13,27,420,612,193,"Pyruvate synthase","2-oxobutyrate synthase. 2-oxobutyrate-ferredoxin oxidoreductase. Alpha-ketobutyrate synthase. Alpha-ketobutyrate-ferredoxin oxidoreductase. Pyruvate oxidoreductase. Pyruvate synthetase. Pyruvic-ferredoxin oxidoreductase","Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Thiamine diphosphate","-!- The enzyme also decarboxylates 2-oxobutanoate with lower efficiency, but shows no activity with 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. -!- For examples of other members of this family, see EC 1.2.7.3 and EC 1.2.7.7"]
[]
["CLOSTRIBL3_v1_12838","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.3.1.9","high",1,391,{"v":1e-171,"d":"1.00E-171"},68,5,392,388,"Acetyl-CoA C-acetyltransferase","Acetoacetyl-CoA thiolase","2 acetyl-CoA = CoA + acetoacetyl-CoA","_","-!- The enzyme, found in both eukaryotes and prokaryotes, catalyzes the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. -!- The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA. -!- In the second step the acyl group is transferred to an acetyl-CoA molecule. -!- Cf. EC 2.3.1.16"]
[null,"2.3.1.16","no",1,420,{"v":1e-118,"d":"1.00E-118"},45,1,392,392,"Acetyl-CoA C-acyltransferase","3-ketoacyl-CoA thiolase. Beta-ketothiolase","Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA","_","-!- The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation. -!- The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl- CoA shortened by two carbon atoms. -!- The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA. -!- In the second step the acyl group is transferred to CoA. -!- Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. -!- cf. EC 2.3.1.9"]
[null,"2.3.1.174","no",1,401,{"v":8e-95,"d":"8.00E-95"},43,1,392,392,"3-oxoadipyl-CoA thiolase","Beta-ketoadipyl-CoA thiolase","Succinyl-CoA + acetyl-CoA = CoA + 3-oxoadipyl-CoA","_","-!- The enzyme from the bacterium Escherichia coli also has the activity of EC 2.3.1.223"]
[]
["CLOSTRIBL3_v1_13111","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.3.1.9","high",1,391,{"v":1E-127,"d":"1.00E-127"},51,5,390,386,"Acetyl-CoA C-acetyltransferase","Acetoacetyl-CoA thiolase","2 acetyl-CoA = CoA + acetoacetyl-CoA","_","-!- The enzyme, found in both eukaryotes and prokaryotes, catalyzes the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. -!- The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA. -!- In the second step the acyl group is transferred to an acetyl-CoA molecule. -!- Cf. EC 2.3.1.16"]
[null,"2.3.1.16","no",1,420,{"v":1e-116,"d":"1.00E-116"},42,1,390,390,"Acetyl-CoA C-acyltransferase","3-ketoacyl-CoA thiolase. Beta-ketothiolase","Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA","_","-!- The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation. -!- The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl- CoA shortened by two carbon atoms. -!- The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA. -!- In the second step the acyl group is transferred to CoA. -!- Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. -!- cf. EC 2.3.1.9"]
[null,"2.3.1.174","no",1,401,{"v":1e-101,"d":"1.00E-101"},45,1,390,390,"3-oxoadipyl-CoA thiolase","Beta-ketoadipyl-CoA thiolase","Succinyl-CoA + acetyl-CoA = CoA + 3-oxoadipyl-CoA","_","-!- The enzyme from the bacterium Escherichia coli also has the activity of EC 2.3.1.223"]
[null,"2.3.1.176","no",1,547,3E-11,22,80,391,312,"Propanoyl-CoA C-acyltransferase","3-oxopristanoyl-CoA hydrolase. 3-oxopristanoyl-CoA thiolase. Peroxisomal thiolase 2. Propionyl-CoA C(2)-trimethyltridecanoyltransferase. PTE-2. SCP(chi). SCP-X. Sterol carrier protein-chi. Sterol carrier protein-X","3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3-alpha,7-alpha,12-alpha-trihydroxy-24-oxo-5-beta-cholestanoyl- CoA","_","-!- Also acts on dihydroxy-5-beta-cholestanoyl-CoA and other branched chain acyl-CoA derivatives. -!- Catalyzes the penultimate step in the formation of bile acids. -!- The bile acid moiety is transferred from the acyl-CoA thioester (RCO- SCoA) to either glycine or taurine (NH(2)R') by EC 2.3.1.65. -!- Formerly EC 2.3.1.154"]
[]
["CLOSTRIBL3_v1_11283","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.3.1.176","high",1,547,{"v":8E-41,"d":"8.00E-41"},31,1,393,393,"Propanoyl-CoA C-acyltransferase","3-oxopristanoyl-CoA hydrolase. 3-oxopristanoyl-CoA thiolase. Peroxisomal thiolase 2. Propionyl-CoA C(2)-trimethyltridecanoyltransferase. PTE-2. SCP(chi). SCP-X. Sterol carrier protein-chi. Sterol carrier protein-X","3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3-alpha,7-alpha,12-alpha-trihydroxy-24-oxo-5-beta-cholestanoyl- CoA","_","-!- Also acts on dihydroxy-5-beta-cholestanoyl-CoA and other branched chain acyl-CoA derivatives. -!- Catalyzes the penultimate step in the formation of bile acids. -!- The bile acid moiety is transferred from the acyl-CoA thioester (RCO- SCoA) to either glycine or taurine (NH(2)R') by EC 2.3.1.65. -!- Formerly EC 2.3.1.154"]
[null,"2.3.1.16","no",1,420,3e-12,21,1,379,379,"Acetyl-CoA C-acyltransferase","3-ketoacyl-CoA thiolase. Beta-ketothiolase","Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA","_","-!- The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation. -!- The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl- CoA shortened by two carbon atoms. -!- The reaction starts with the acylation of a nucleophilic cysteine at the active site by a 3-oxoacyl-CoA, with the concomitant release of acetyl-CoA. -!- In the second step the acyl group is transferred to CoA. -!- Most enzymes have a broad substrate range for the 3-oxoacyl-CoA. -!- cf. EC 2.3.1.9"]
[]
["CLOSTRIBL3_v1_11276","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.1.157","high",1,280,{"v":1E-53,"d":"1.00E-53"},37,7,288,282,"3-hydroxybutyryl-CoA dehydrogenase","Beta-hydroxybutyryl-CoA dehydrogenase. BHBD","(S)-3-hydroxybutanoyl-CoA + NADP(+) = 3-acetoacetyl-CoA + NADPH","_","_"]
[null,"1.1.1.35","no",1,301,{"v":8e-51,"d":"8.00E-51"},34,4,286,283,"3-hydroxyacyl-CoA dehydrogenase","Beta-hydroxyacyl dehydrogenase. Beta-keto-reductase","(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH","_","-!- Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3- hydroxyacylhydrolipoate. -!- Some enzymes act, more slowly, with NADP(+). -!- Broad specificity to acyl chain-length (cf. EC 1.1.1.211)"]
[null,"5.1.2.3","no",1,707,{"v":5e-41,"d":"5.00E-41"},27,5,286,282,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"1.1.1.211","no",1,763,{"v":4e-27,"d":"4.00E-27"},28,4,305,302,"Long-chain-3-hydroxyacyl-CoA dehydrogenase","Beta-hydroxyacyl-CoA dehydrogenase","A long-chain (S)-3-hydroxyacyl-CoA + NAD(+) = a long-chain 3-oxoacyl-CoA + NADH","_","-!- This enzyme was purified from the mitochondrial inner membrane. -!- The enzyme has a preference for long-chain substrates, and activity with C(16) substrates was 6- to 15-fold higher than with C(4) substrates (cf. EC 1.1.1.35)"]
[]
["CLOSTRIBL3_v1_13113","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.1.157","high",1,280,{"v":7e-61,"d":"7.00E-61"},39,5,287,283,"3-hydroxybutyryl-CoA dehydrogenase","Beta-hydroxybutyryl-CoA dehydrogenase. BHBD","(S)-3-hydroxybutanoyl-CoA + NADP(+) = 3-acetoacetyl-CoA + NADPH","_","_"]
[null,"1.1.1.35","no",1,301,{"v":2e-54,"d":"2.00E-54"},34,2,288,287,"3-hydroxyacyl-CoA dehydrogenase","Beta-hydroxyacyl dehydrogenase. Beta-keto-reductase","(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH","_","-!- Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3- hydroxyacylhydrolipoate. -!- Some enzymes act, more slowly, with NADP(+). -!- Broad specificity to acyl chain-length (cf. EC 1.1.1.211)"]
[null,"5.1.2.3","no",1,707,{"v":5e-47,"d":"5.00E-47"},34,3,288,286,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"1.1.1.211","no",1,763,{"v":2e-28,"d":"2.00E-28"},29,2,288,287,"Long-chain-3-hydroxyacyl-CoA dehydrogenase","Beta-hydroxyacyl-CoA dehydrogenase","A long-chain (S)-3-hydroxyacyl-CoA + NAD(+) = a long-chain 3-oxoacyl-CoA + NADH","_","-!- This enzyme was purified from the mitochondrial inner membrane. -!- The enzyme has a preference for long-chain substrates, and activity with C(16) substrates was 6- to 15-fold higher than with C(4) substrates (cf. EC 1.1.1.35)"]
[]
["CLOSTRIBL3_v1_20313","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.1.157","high",1,280,{"v":1E-119,"d":"1.00E-119"},61,3,280,278,"3-hydroxybutyryl-CoA dehydrogenase","Beta-hydroxybutyryl-CoA dehydrogenase. BHBD","(S)-3-hydroxybutanoyl-CoA + NADP(+) = 3-acetoacetyl-CoA + NADPH","_","_"]
[null,"1.1.1.35","no",1,301,{"v":6e-84,"d":"6.00E-84"},40,1,282,282,"3-hydroxyacyl-CoA dehydrogenase","Beta-hydroxyacyl dehydrogenase. Beta-keto-reductase","(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH","_","-!- Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3- hydroxyacylhydrolipoate. -!- Some enzymes act, more slowly, with NADP(+). -!- Broad specificity to acyl chain-length (cf. EC 1.1.1.211)"]
[null,"5.1.2.3","no",1,707,{"v":5e-70,"d":"5.00E-70"},39,1,281,281,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"1.1.1.211","no",1,763,{"v":1e-49,"d":"1.00E-49"},36,1,282,282,"Long-chain-3-hydroxyacyl-CoA dehydrogenase","Beta-hydroxyacyl-CoA dehydrogenase","A long-chain (S)-3-hydroxyacyl-CoA + NAD(+) = a long-chain 3-oxoacyl-CoA + NADH","_","-!- This enzyme was purified from the mitochondrial inner membrane. -!- The enzyme has a preference for long-chain substrates, and activity with C(16) substrates was 6- to 15-fold higher than with C(4) substrates (cf. EC 1.1.1.35)"]
[]
["CLOSTRIBL3_v1_13112","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"4.2.1.17","high",1,264,{"v":3e-60,"d":"3.00E-60"},40,12,254,243,"Enoyl-CoA hydratase","Enoyl hydrase. Unsaturated acyl-CoA hydratase","(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O","_","-!- Acts in the reverse direction. -!- With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74)"]
[null,"4.2.1.55","no",1,261,{"v":1E-58,"d":"1.00E-58"},45,1,249,249,"3-hydroxybutyryl-CoA dehydratase","Crotonase","(3R)-3-hydroxybutanoyl-CoA = crotonoyl-CoA + H(2)O","_","-!- Also acts on crotonoyl thioesters of pantetheine and acyl-carrier protein"]
[null,"4.2.1.18","no",1,276,{"v":2E-50,"d":"2.00E-50"},38,12,255,244,"Methylglutaconyl-CoA hydratase","_","(S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA + H(2)O","_","_"]
[null,"5.1.2.3","no",1,707,{"v":3E-43,"d":"3.00E-43"},42,12,192,181,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"5.3.3.8","no",1,265,{"v":5e-43,"d":"5.00E-43"},37,2,188,187,"Delta(3)-Delta(2)-enoyl-CoA isomerase","3,2-trans-enoyl-CoA isomerase. Acetylene-allene isomerase. Delta(3),Delta(2)-enoyl-CoA isomerase. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase. Dodecenoyl-CoA Delta-isomerase. Dodecenoyl-CoA isomerase","(1) A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA. (2) A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA","_","-!- The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position. -!- Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C(3), which cannot be processed further by the regular enzymes of the beta- oxidation system. -!- This enzyme isomerizes the bond to a trans bond at position C(2), which can be processed further. -!- The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers. -!- The enzyme can also catalyze the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters"]
[null,"1.1.1.211","no",1,763,{"v":1e-32,"d":"1.00E-32"},35,3,225,223,"Long-chain-3-hydroxyacyl-CoA dehydrogenase","Beta-hydroxyacyl-CoA dehydrogenase","A long-chain (S)-3-hydroxyacyl-CoA + NAD(+) = a long-chain 3-oxoacyl-CoA + NADH","_","-!- This enzyme was purified from the mitochondrial inner membrane. -!- The enzyme has a preference for long-chain substrates, and activity with C(16) substrates was 6- to 15-fold higher than with C(4) substrates (cf. EC 1.1.1.35)"]
[null,"4.1.3.36","no",1,263,{"v":4e-27,"d":"4.00E-27"},28,12,250,239,"1,4-dihydroxy-2-naphthoyl-CoA synthase","DHNA synthetase. Dihydroxynaphthoic acid synthetase. Naphthoate synthase. o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing)","4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H(2)O","_","-!- This enzyme is involved in the synthesis of 1,4-dihydroxy-2- naphthoate, a branch point metabolite leading to the biosynthesis of menaquinone (vitamin K(2), in bacteria), phylloquinone (vitamin K(1) in plants), and many plant pigments. -!- The coenzyme A group is subsequently removed from the product by EC 3.1.2.28"]
[null,"4.1.1.41","no",1,261,{"v":4e-23,"d":"4.00E-23"},27,9,254,246,"Transferred entry: 7.2.4.3","_","_","_","_"]
[null,"3.1.2.4","no",1,408,{"v":3e-21,"d":"3.00E-21"},30,6,182,177,"3-hydroxyisobutyryl-CoA hydrolase","_","3-hydroxy-2-methylpropanoyl-CoA + H(2)O = CoA + 3-hydroxy-2- methylpropanoate","_","-!- Also hydrolyzes 3-hydroxypropanoyl-CoA"]
[null,"4.2.1.100","no",1,258,7e-15,25,7,255,249,"Cyclohexa-1,5-dienecarbonyl-CoA hydratase","Cyclohexa-1,5-diene-1-carbonyl-CoA hydratase. Cyclohexa-1,5-diene-1-carboxyl-CoA hydratase. Dienoyl-CoA hydratase","6-hydroxycyclohex-1-enecarbonyl-CoA = cyclohexa-1,5-dienecarbonyl-CoA + H(2)O","_","-!- Forms part of the anaerobic benzoate degradation pathway, which also includes EC 1.3.8.6, EC 1.3.7.8 and EC 4.2.1.55. -!- Formerly EC 4.2.1.102"]
[]
["CLOSTRIBL3_v1_11087","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"4.2.1.17","high",1,264,{"v":7e-29,"d":"7.00E-29"},26,4,251,248,"Enoyl-CoA hydratase","Enoyl hydrase. Unsaturated acyl-CoA hydratase","(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O","_","-!- Acts in the reverse direction. -!- With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74)"]
[null,"4.2.1.55","no",1,261,{"v":4e-25,"d":"4.00E-25"},31,1,247,247,"3-hydroxybutyryl-CoA dehydratase","Crotonase","(3R)-3-hydroxybutanoyl-CoA = crotonoyl-CoA + H(2)O","_","-!- Also acts on crotonoyl thioesters of pantetheine and acyl-carrier protein"]
[null,"5.3.3.8","no",1,265,{"v":1e-24,"d":"1.00E-24"},26,12,205,194,"Delta(3)-Delta(2)-enoyl-CoA isomerase","3,2-trans-enoyl-CoA isomerase. Acetylene-allene isomerase. Delta(3),Delta(2)-enoyl-CoA isomerase. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase. Dodecenoyl-CoA Delta-isomerase. Dodecenoyl-CoA isomerase","(1) A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA. (2) A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA","_","-!- The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position. -!- Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C(3), which cannot be processed further by the regular enzymes of the beta- oxidation system. -!- This enzyme isomerizes the bond to a trans bond at position C(2), which can be processed further. -!- The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers. -!- The enzyme can also catalyze the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters"]
[null,"4.1.3.36","no",1,263,{"v":1E-22,"d":"1.00E-22"},32,12,251,240,"1,4-dihydroxy-2-naphthoyl-CoA synthase","DHNA synthetase. Dihydroxynaphthoic acid synthetase. Naphthoate synthase. o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing)","4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H(2)O","_","-!- This enzyme is involved in the synthesis of 1,4-dihydroxy-2- naphthoate, a branch point metabolite leading to the biosynthesis of menaquinone (vitamin K(2), in bacteria), phylloquinone (vitamin K(1) in plants), and many plant pigments. -!- The coenzyme A group is subsequently removed from the product by EC 3.1.2.28"]
[null,"5.1.2.3","no",1,707,7e-15,24,12,206,195,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"4.1.1.41","no",1,261,5e-14,24,3,251,249,"Transferred entry: 7.2.4.3","_","_","_","_"]
[null,"4.2.1.18","no",1,276,9E-13,25,23,251,229,"Methylglutaconyl-CoA hydratase","_","(S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA + H(2)O","_","_"]
[null,"3.1.2.4","no",1,408,5e-11,24,6,182,177,"3-hydroxyisobutyryl-CoA hydrolase","_","3-hydroxy-2-methylpropanoyl-CoA + H(2)O = CoA + 3-hydroxy-2- methylpropanoate","_","-!- Also hydrolyzes 3-hydroxypropanoyl-CoA"]
[]
["CLOSTRIBL3_v1_20308","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"4.2.1.55","high",1,261,{"v":3e-99,"d":"3.00E-99"},75,1,259,259,"3-hydroxybutyryl-CoA dehydratase","Crotonase","(3R)-3-hydroxybutanoyl-CoA = crotonoyl-CoA + H(2)O","_","-!- Also acts on crotonoyl thioesters of pantetheine and acyl-carrier protein"]
[null,"4.2.1.17","no",1,264,{"v":3e-64,"d":"3.00E-64"},45,15,257,243,"Enoyl-CoA hydratase","Enoyl hydrase. Unsaturated acyl-CoA hydratase","(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O","_","-!- Acts in the reverse direction. -!- With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74)"]
[null,"4.2.1.18","no",1,276,{"v":4e-49,"d":"4.00E-49"},38,8,257,250,"Methylglutaconyl-CoA hydratase","_","(S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA + H(2)O","_","_"]
[null,"5.3.3.8","no",1,265,{"v":2E-46,"d":"2.00E-46"},41,11,210,200,"Delta(3)-Delta(2)-enoyl-CoA isomerase","3,2-trans-enoyl-CoA isomerase. Acetylene-allene isomerase. Delta(3),Delta(2)-enoyl-CoA isomerase. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase. Dodecenoyl-CoA Delta-isomerase. Dodecenoyl-CoA isomerase","(1) A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA. (2) A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA","_","-!- The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position. -!- Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C(3), which cannot be processed further by the regular enzymes of the beta- oxidation system. -!- This enzyme isomerizes the bond to a trans bond at position C(2), which can be processed further. -!- The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers. -!- The enzyme can also catalyze the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters"]
[null,"5.1.2.3","no",1,707,{"v":8e-44,"d":"8.00E-44"},44,11,200,190,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"4.1.3.36","no",1,263,{"v":2e-36,"d":"2.00E-36"},33,2,256,255,"1,4-dihydroxy-2-naphthoyl-CoA synthase","DHNA synthetase. Dihydroxynaphthoic acid synthetase. Naphthoate synthase. o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing)","4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H(2)O","_","-!- This enzyme is involved in the synthesis of 1,4-dihydroxy-2- naphthoate, a branch point metabolite leading to the biosynthesis of menaquinone (vitamin K(2), in bacteria), phylloquinone (vitamin K(1) in plants), and many plant pigments. -!- The coenzyme A group is subsequently removed from the product by EC 3.1.2.28"]
[null,"1.1.1.211","no",1,763,{"v":8e-33,"d":"8.00E-33"},39,11,199,189,"Long-chain-3-hydroxyacyl-CoA dehydrogenase","Beta-hydroxyacyl-CoA dehydrogenase","A long-chain (S)-3-hydroxyacyl-CoA + NAD(+) = a long-chain 3-oxoacyl-CoA + NADH","_","-!- This enzyme was purified from the mitochondrial inner membrane. -!- The enzyme has a preference for long-chain substrates, and activity with C(16) substrates was 6- to 15-fold higher than with C(4) substrates (cf. EC 1.1.1.35)"]
[null,"3.1.2.4","no",1,408,{"v":5e-27,"d":"5.00E-27"},30,6,239,234,"3-hydroxyisobutyryl-CoA hydrolase","_","3-hydroxy-2-methylpropanoyl-CoA + H(2)O = CoA + 3-hydroxy-2- methylpropanoate","_","-!- Also hydrolyzes 3-hydroxypropanoyl-CoA"]
[null,"4.1.1.41","no",1,261,{"v":1E-25,"d":"1.00E-25"},28,1,256,256,"Transferred entry: 7.2.4.3","_","_","_","_"]
[null,"4.2.1.100","no",1,258,{"v":2e-21,"d":"2.00E-21"},30,6,259,254,"Cyclohexa-1,5-dienecarbonyl-CoA hydratase","Cyclohexa-1,5-diene-1-carbonyl-CoA hydratase. Cyclohexa-1,5-diene-1-carboxyl-CoA hydratase. Dienoyl-CoA hydratase","6-hydroxycyclohex-1-enecarbonyl-CoA = cyclohexa-1,5-dienecarbonyl-CoA + H(2)O","_","-!- Forms part of the anaerobic benzoate degradation pathway, which also includes EC 1.3.8.6, EC 1.3.7.8 and EC 4.2.1.55. -!- Formerly EC 4.2.1.102"]
[null,"2.3.1.48","no",43,544,{"v":2e-20,"d":"2.00E-20"},25,3,256,254,"Histone acetyltransferase","Lysine acetyltransferase. Protein lysine acetyltransferase","Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine","_","-!- A group of enzymes acetylating histones. -!- Several of the enzymes can also acetylate lysines in other proteins"]
[]
["CLOSTRIBL3_v1_12502","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.3.99.2","high",1,383,{"v":1e-145,"d":"1.00E-145"},56,1,377,377,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":2e-86,"d":"2.00E-86"},37,7,373,367,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":2e-81,"d":"2.00E-81"},39,3,380,378,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":2e-65,"d":"2.00E-65"},35,6,379,374,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":6e-61,"d":"6.00E-61"},36,6,378,373,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":1e-34,"d":"1.00E-34"},28,1,378,378,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":1e-31,"d":"1.00E-31"},22,10,368,359,"Acyl-CoA oxidase","_","Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + H(2)O(2)","FAD","-!- Acts on CoA derivatives of fatty acids with chain length from C(8) to C(18)"]
[]
["CLOSTRIBL3_v1_11587","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.3.99.2","high",1,383,{"v":1e-126,"d":"1.00E-126"},48,1,379,379,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":1e-88,"d":"1.00E-88"},40,3,374,372,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":4e-87,"d":"4.00E-87"},34,5,379,375,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":7e-70,"d":"7.00E-70"},35,4,377,374,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":8e-59,"d":"8.00E-59"},35,14,377,364,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":5e-40,"d":"5.00E-40"},30,1,374,374,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":3E-32,"d":"3.00E-32"},24,26,379,354,"Acyl-CoA oxidase","_","Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + H(2)O(2)","FAD","-!- Acts on CoA derivatives of fatty acids with chain length from C(8) to C(18)"]
[]
["CLOSTRIBL3_v1_12012","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.3.99.2","high",1,383,{"v":6e-97,"d":"6.00E-97"},42,1,377,377,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":3e-90,"d":"3.00E-90"},42,2,372,371,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":2E-78,"d":"2.00E-78"},34,2,371,370,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":3E-52,"d":"3.00E-52"},33,16,372,357,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":2e-39,"d":"2.00E-39"},27,1,366,366,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":3e-33,"d":"3.00E-33"},28,1,372,372,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":7e-28,"d":"7.00E-28"},22,1,375,375,"Acyl-CoA oxidase","_","Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + H(2)O(2)","FAD","-!- Acts on CoA derivatives of fatty acids with chain length from C(8) to C(18)"]
[]
["CLOSTRIBL3_v1_12013","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.3.99.2","high",1,383,{"v":2E-55,"d":"2.00E-55"},32,13,381,369,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":3e-45,"d":"3.00E-45"},30,30,380,351,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":1e-44,"d":"1.00E-44"},28,4,381,378,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":2e-34,"d":"2.00E-34"},31,57,384,328,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":3E-23,"d":"3.00E-23"},23,1,381,381,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.7","no",1,405,3e-15,26,59,292,234,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.3.6","no",1,494,1e-12,21,82,381,300,"Acyl-CoA oxidase","_","Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + H(2)O(2)","FAD","-!- Acts on CoA derivatives of fatty acids with chain length from C(8) to C(18)"]
[]
["CLOSTRIBL3_v1_20310","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.3.99.2","high",1,383,{"v":1E-169,"d":"1.00E-169"},63,1,379,379,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":4E-95,"d":"4.00E-95"},40,5,379,375,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":2e-84,"d":"2.00E-84"},38,3,374,372,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":9e-59,"d":"9.00E-59"},32,5,373,369,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":7e-58,"d":"7.00E-58"},34,8,374,367,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":1e-40,"d":"1.00E-40"},30,1,377,377,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":2e-21,"d":"2.00E-21"},20,1,379,379,"Acyl-CoA oxidase","_","Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + H(2)O(2)","FAD","-!- Acts on CoA derivatives of fatty acids with chain length from C(8) to C(18)"]
[]
["CLOSTRIBL3_v1_11710","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.7.2.7","high",1,355,{"v":1E-127,"d":"1.00E-127"},55,4,355,352,"Butyrate kinase","_","ATP + butanoate = ADP + butanoyl phosphate","_","-!- The enzyme from Clostridium sp. also acts, more slowly on pentanoate and propanoate, and on some branched-chain fatty acids (cf. EC 2.7.1.14)"]
[null,"2.7.2.1","no",1,410,1e-15,25,1,304,304,"Acetate kinase","Acetate kinase (phosphorylating). Acetic kinase. Acetokinase. AK","ATP + acetate = ADP + acetyl phosphate","Mg(2+)","-!- While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly. -!- Acetate can be converted into the key metabolic intermediate acetyl- CoA by coupling acetate kinase with EC 2.3.1.8. -!- Both this enzyme and EC 2.7.2.15 play important roles in the production of propanoate"]
[]
["CLOSTRIBL3_v1_11711","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.3.1.19","high",1,288,{"v":5e-63,"d":"5.00E-63"},44,18,296,279,"Phosphate butyryltransferase","Phosphotransbutyrylase","Butanoyl-CoA + phosphate = CoA + butanoylphosphate","_","_"]
[null,"2.3.1.8","no",1,331,{"v":1E-46,"d":"1.00E-46"},24,19,298,280,"Phosphate acetyltransferase","Phosphoacylase. Phosphotransacetylase","Acetyl-CoA + phosphate = CoA + acetyl phosphate","_","-!- Also acts with other short-chain acyl-CoAs"]
[]
["CLOSTRIBL3_v1_12016","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.3.1.19","high",1,288,{"v":1e-68,"d":"1.00E-68"},46,7,296,290,"Phosphate butyryltransferase","Phosphotransbutyrylase","Butanoyl-CoA + phosphate = CoA + butanoylphosphate","_","_"]
[null,"2.3.1.8","no",1,331,{"v":8e-42,"d":"8.00E-42"},25,9,297,289,"Phosphate acetyltransferase","Phosphoacylase. Phosphotransacetylase","Acetyl-CoA + phosphate = CoA + acetyl phosphate","_","-!- Also acts with other short-chain acyl-CoAs"]
[]
["CLOSTRIBL3_v1_12308","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.3.1.19","high",1,288,{"v":7e-82,"d":"7.00E-82"},54,7,293,287,"Phosphate butyryltransferase","Phosphotransbutyrylase","Butanoyl-CoA + phosphate = CoA + butanoylphosphate","_","_"]
[null,"2.3.1.8","no",1,331,{"v":2e-38,"d":"2.00E-38"},24,8,296,289,"Phosphate acetyltransferase","Phosphoacylase. Phosphotransacetylase","Acetyl-CoA + phosphate = CoA + acetyl phosphate","_","-!- Also acts with other short-chain acyl-CoAs"]
[]
["CLOSTRIBL3_v1_20086","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.7.2.7","high",1,355,{"v":1e-133,"d":"1.00E-133"},58,5,354,350,"Butyrate kinase","_","ATP + butanoate = ADP + butanoyl phosphate","_","-!- The enzyme from Clostridium sp. also acts, more slowly on pentanoate and propanoate, and on some branched-chain fatty acids (cf. EC 2.7.1.14)"]
[null,"2.7.2.1","no",1,410,{"v":9e-18,"d":"9.00E-18"},22,1,305,305,"Acetate kinase","Acetate kinase (phosphorylating). Acetic kinase. Acetokinase. AK","ATP + acetate = ADP + acetyl phosphate","Mg(2+)","-!- While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly. -!- Acetate can be converted into the key metabolic intermediate acetyl- CoA by coupling acetate kinase with EC 2.3.1.8. -!- Both this enzyme and EC 2.7.2.15 play important roles in the production of propanoate"]
[]
["CLOSTRIBL3_v1_20087","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.7.2.7","high",1,355,{"v":1e-128,"d":"1.00E-128"},59,4,355,352,"Butyrate kinase","_","ATP + butanoate = ADP + butanoyl phosphate","_","-!- The enzyme from Clostridium sp. also acts, more slowly on pentanoate and propanoate, and on some branched-chain fatty acids (cf. EC 2.7.1.14)"]
[null,"2.7.2.1","no",1,410,{"v":6e-17,"d":"6.00E-17"},29,150,306,157,"Acetate kinase","Acetate kinase (phosphorylating). Acetic kinase. Acetokinase. AK","ATP + acetate = ADP + acetyl phosphate","Mg(2+)","-!- While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly. -!- Acetate can be converted into the key metabolic intermediate acetyl- CoA by coupling acetate kinase with EC 2.3.1.8. -!- Both this enzyme and EC 2.7.2.15 play important roles in the production of propanoate"]
[null,"2.7.2.15","no",1,408,2e-15,24,150,316,167,"Propionate kinase","Propionate/acetate kinase","ATP + propanoate = ADP + propanoyl phosphate","Mg(2+)","-!- Both propanoate and acetate can act as a substrate. -!- Involved in the anaerobic degradation of L-threonine in bacteria. -!- Both this enzyme and EC 2.7.2.1 play important roles in the production of propanoate"]
[]
["CLOSTRIBL3_v1_13110","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"3.1.2.1","high",1,525,{"v":2e-17,"d":"2.00E-17"},24,123,440,318,"Acetyl-CoA hydrolase","Acetyl-CoA acylase. Acetyl-CoA deacylase","Acetyl-CoA + H(2)O = CoA + acetate","_","_"]
[]
["CLOSTRIBL3_v1_11486","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.2.4","high",1,541,{"v":8e-76,"d":"8.00E-76"},29,11,467,457,"D-lactate dehydrogenase (cytochrome)","D-lactate ferricytochrome c oxidoreductase. Lactic acid dehydrogenase","(R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H(+)","FAD","_"]
[null,"2.5.1.26","no",1,594,{"v":5e-29,"d":"5.00E-29"},24,56,470,415,"Alkylglycerone-phosphate synthase","Alkyl-DHAP synthase. Alkyldihydroxyacetonephosphate synthase","1-acyl-glycerone 3-phosphate + a long-chain alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid anion","_","-!- The ester-linked fatty acid of the substrate is cleaved and replaced by a long-chain alcohol in an ether linkage"]
[null,"1.1.3.37","no",1,526,8e-12,25,48,225,178,"D-arabinono-1,4-lactone oxidase","D-arabinono-gamma-lactone oxidase","D-arabinono-1,4-lactone + O(2) = dehydro-D-arabinono-1,4-lactone + H(2)O(2)","FAD","_"]
[]
["CLOSTRIBL3_v1_10095","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.12.7.2","high",2,435,{"v":1e-114,"d":"1.00E-114"},44,8,396,389,"Ferredoxin hydrogenase","Bidirectional hydrogenase. H(2) oxidizing hydrogenase. H(2) producing hydrogenase. Hydrogen-lyase. Hydrogenase. Hydrogenase (ferredoxin). Hydrogenase I. Hydrogenase II. Hydrogenlyase. Uptake hydrogenase","H(2) + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Ni(2+)","-!- Can use molecular hydrogen for the reduction of a variety of substances. -!- Formerly EC 1.12.1.1, EC 1.12.7.1, EC 1.18.3.1, EC 1.18.99.1 and EC 1.98.1.1"]
[null,"1.12.7.2","medium",1,124,4e-11,36,409,460,52,"Ferredoxin hydrogenase","Bidirectional hydrogenase. H(2) oxidizing hydrogenase. H(2) producing hydrogenase. Hydrogen-lyase. Hydrogenase. Hydrogenase (ferredoxin). Hydrogenase I. Hydrogenase II. Hydrogenlyase. Uptake hydrogenase","H(2) + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Ni(2+)","-!- Can use molecular hydrogen for the reduction of a variety of substances. -!- Formerly EC 1.12.1.1, EC 1.12.7.1, EC 1.18.3.1, EC 1.18.99.1 and EC 1.98.1.1"]
[]
["CLOSTRIBL3_v1_10091","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.6.99.5","high",16,161,{"v":8e-38,"d":"8.00E-38"},44,16,159,144,"Transferred entry: 1.6.5.11","_","_","_","_"]
[null,"1.6.5.3","no",72,166,{"v":9e-26,"d":"9.00E-26"},34,16,163,148,"Transferred entry: 7.1.1.2","_","_","_","_"]
[null,"1.6.99.3","no",4,166,{"v":9e-26,"d":"9.00E-26"},34,16,163,148,"NADH dehydrogenase","Beta-NADH dehydrogenase dinucleotide. Cytochrome c reductase. Diaphorase. Dihydrocodehydrogenase I dehydrogenase. Dihydronicotinamide adenine dinucleotide dehydrogenase. Diphosphopyrinase. DPNH diaphorase. NADH diaphorase. NADH hydrogenase. NADH oxidoreductase. NADH-menadione oxidoreductase. NADH:cytochrome c oxidoreductase. Reduced diphosphopyridine nucleotide diaphorase. Type 1 dehydrogenase. Type I dehydrogenase","NADH + acceptor = NAD(+) + reduced acceptor","Flavoprotein; Iron-sulfur","-!- After preparations have been subjected to certain treatments cytochrome c may act as acceptor. -!- Under normal conditions, two protons are extruded from the cytoplasm or the intramitochondrial or stromal compartment. -!- Present in a mitochondrial co"]
[null,"1.12.1.2","no",4,602,2E-14,26,19,163,145,"Hydrogen dehydrogenase","Bidirectional hydrogenase. H(2):NAD(+) oxidoreductase. Hydrogenase. NAD-linked hydrogenase","H(2) + NAD(+) = H(+) + NADH","FAD or FMN; Iron-sulfur; Ni(2+)","_"]
[]
["CLOSTRIBL3_v1_10092","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.6.99.5","high",10,423,{"v":1e-124,"d":"1.00E-124"},45,114,529,416,"Transferred entry: 1.6.5.11","_","_","_","_"]
[null,"1.6.5.3","no",74,438,{"v":2E-91,"d":"2.00E-91"},37,114,529,416,"Transferred entry: 7.1.1.2","_","_","_","_"]
[null,"1.6.99.3","no",7,438,{"v":2E-91,"d":"2.00E-91"},37,114,529,416,"NADH dehydrogenase","Beta-NADH dehydrogenase dinucleotide. Cytochrome c reductase. Diaphorase. Dihydrocodehydrogenase I dehydrogenase. Dihydronicotinamide adenine dinucleotide dehydrogenase. Diphosphopyrinase. DPNH diaphorase. NADH diaphorase. NADH hydrogenase. NADH oxidoreductase. NADH-menadione oxidoreductase. NADH:cytochrome c oxidoreductase. Reduced diphosphopyridine nucleotide diaphorase. Type 1 dehydrogenase. Type I dehydrogenase","NADH + acceptor = NAD(+) + reduced acceptor","Flavoprotein; Iron-sulfur","-!- After preparations have been subjected to certain treatments cytochrome c may act as acceptor. -!- Under normal conditions, two protons are extruded from the cytoplasm or the intramitochondrial or stromal compartment. -!- Present in a mitochondrial co"]
[null,"1.12.1.2","no",4,602,{"v":2E-78,"d":"2.00E-78"},36,138,534,397,"Hydrogen dehydrogenase","Bidirectional hydrogenase. H(2):NAD(+) oxidoreductase. Hydrogenase. NAD-linked hydrogenase","H(2) + NAD(+) = H(+) + NADH","FAD or FMN; Iron-sulfur; Ni(2+)","_"]
[]
["CLOSTRIBL3_v1_10093","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.12.1.2","high",2,234,3e-12,31,1,142,142,"Hydrogen dehydrogenase","Bidirectional hydrogenase. H(2):NAD(+) oxidoreductase. Hydrogenase. NAD-linked hydrogenase","H(2) + NAD(+) = H(+) + NADH","FAD or FMN; Iron-sulfur; Ni(2+)","_"]
[]
["CLOSTRIBL3_v1_13020","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.12.7.2","high",2,435,{"v":5e-32,"d":"5.00E-32"},27,62,395,334,"Ferredoxin hydrogenase","Bidirectional hydrogenase. H(2) oxidizing hydrogenase. H(2) producing hydrogenase. Hydrogen-lyase. Hydrogenase. Hydrogenase (ferredoxin). Hydrogenase I. Hydrogenase II. Hydrogenlyase. Uptake hydrogenase","H(2) + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Ni(2+)","-!- Can use molecular hydrogen for the reduction of a variety of substances. -!- Formerly EC 1.12.1.1, EC 1.12.7.1, EC 1.18.3.1, EC 1.18.99.1 and EC 1.98.1.1"]
[]
["CLOSTRIBL3_v1_20317","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.12.7.2","high",2,435,{"v":9e-33,"d":"9.00E-33"},25,137,463,327,"Ferredoxin hydrogenase","Bidirectional hydrogenase. H(2) oxidizing hydrogenase. H(2) producing hydrogenase. Hydrogen-lyase. Hydrogenase. Hydrogenase (ferredoxin). Hydrogenase I. Hydrogenase II. Hydrogenlyase. Uptake hydrogenase","H(2) + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Ni(2+)","-!- Can use molecular hydrogen for the reduction of a variety of substances. -!- Formerly EC 1.12.1.1, EC 1.12.7.1, EC 1.18.3.1, EC 1.18.99.1 and EC 1.98.1.1"]
[]
["CLOSTRIBL3_v1_12009","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"6.2.1.26","high",1,484,{"v":2e-57,"d":"2.00E-57"},24,51,534,484,"o-succinylbenzoate--CoA ligase","o-succinylbenzoyl-CoA synthetase. OSB-CoA synthetase","ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 2-succinylbenzoyl- CoA","_","_"]
[null,"1.13.12.7","no",1,547,{"v":1E-46,"d":"1.00E-46"},26,48,537,490,"Firefly luciferase","Luciferase. Photinus pyralis luciferase. Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing)","D-firefly luciferin + O(2) + ATP = firefly oxyluciferin + CO(2) + AMP + diphosphate + light","_","-!- The enzyme, which is found in fireflies (Lampyridae), is responsible for their biolouminescence. -!- The reaction begins with the formation of an acid anhydride between the carboxylic group of D-firefly luciferin and AMP, with the release of diphospha"]
[null,"6.2.1.3","no",1,578,{"v":1e-45,"d":"1.00E-45"},22,52,486,435,"Long-chain-fatty-acid--CoA ligase","Acyl-activating enzyme. Acyl-CoA synthetase. Fatty acid thiokinase (long chain). Lignoceroyl-CoA synthase","ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA","_","-!- Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. -!- The liver enzyme acts on acids from C(6) to C(20); that from brain shows high activity up to C(24)"]
[null,"2.7.7.58","no",1,536,{"v":1e-40,"d":"1.00E-40"},25,15,539,525,"(2,3-dihydroxybenzoyl)adenylate synthase","2,3-dihydroxybenzoate-AMP ligase","ATP + 2,3-dihydroxybenzoate = diphosphate + (2,3- dihydroxybenzoyl)adenylate","_","_"]
[null,"5.1.1.11","no",1,1084,{"v":1e-36,"d":"1.00E-36"},24,50,534,485,"Phenylalanine racemase (ATP-hydrolyzing)","_","ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine","_","_"]
[null,"6.2.1.20","no",1,505,{"v":2e-32,"d":"2.00E-32"},24,151,526,376,"Long-chain-fatty-acid--[acyl-carrier-protein] ligase","Acyl-[acyl-carrier-protein] synthetase","ATP + a long-chain fatty acid + an [acyl-carrier-protein] = AMP + diphosphate + a long-chain acyl-[acyl-carrier-protein]","_","-!- The enzyme ligates long chain fatty acids (with aliphatic chain of 13-22 carbons) to an acyl-carrier protein. -!- Not identical with EC 6.2.1.3"]
[null,"5.1.1.13","no",2,6359,{"v":5e-28,"d":"5.00E-28"},24,50,534,485,"Aspartate racemase","_","L-aspartate = D-aspartate","_","-!- Also acts, at half the rate, on L-alanine"]
[null,"6.2.1.2","no",1,438,{"v":6e-26,"d":"6.00E-26"},24,50,442,393,"Medium-chain acyl-CoA ligase","Acyl-activating enzyme. Butyryl-CoA synthetase. Fatty acid thiokinase (medium chain)","ATP + a medium-chain fatty acid + CoA = AMP + diphosphate + a medium- chain acyl-CoA","_","-!- Acts on fatty acids from C(4) to C(11) and on the corresponding 3-hydroxy and 2,3- or 3,4-unsaturated acids. -!- The enzyme from the bacterium Pseudomonas putida also acts on 4-oxo and 4-hydroxy derivatives"]
[null,"5.1.1.3","no",39,5255,{"v":3e-25,"d":"3.00E-25"},23,52,534,483,"Glutamate racemase","_","L-glutamate = D-glutamate","Pyridoxal 5'-phosphate","_"]
[null,"5.1.1.12","no",1,2607,{"v":7e-23,"d":"7.00E-23"},22,52,534,483,"Ornithine racemase","_","L-ornithine = D-ornithine","_","_"]
[null,"6.2.1.1","no",1,612,{"v":4e-22,"d":"4.00E-22"},28,356,533,178,"Acetate--CoA ligase","Acetate thiokinase. Acetyl-activating enzyme. Acetyl-CoA synthase. Acetyl-CoA synthetase. Acyl-activating enzyme","ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA","_","-!- Also acts on propanoate and propenoate"]
[null,"2.3.1.40","no",1,623,{"v":5e-19,"d":"5.00E-19"},25,139,443,305,"Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase","_","Acyl-[acyl-carrier-protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine = [acyl-carrier-protein] + O-(1-beta-acyl-2-acyl-sn-glycero-3- phospho)ethanolamine","_","_"]
[null,"6.1.1.13","no",2,510,{"v":3e-17,"d":"3.00E-17"},20,33,534,502,"D-alanine--poly(phosphoribitol) ligase","D-alanine-activating enzyme. D-alanine-D-alanyl carrier protein ligase. D-alanine-membrane acceptor ligase. D-alanine: membrane acceptor ligase. D-alanyl-poly(phosphoribitol) synthetase","ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate + O-D- alanyl-poly(ribitol phosphate)","_","-!- A thioester bond is formed transiently between D-alanine and the sulfhydryl group of the 4'-phosphopantetheine prosthetic group of D-alanyl carrier protein during the activation of the alanine. -!- Involved in the synthesis of teichoic acids"]
[null,"6.3.2.26","no",1,3762,{"v":7e-16,"d":"7.00E-16"},22,38,532,495,"N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase","ACV synthetase. L-alpha-aminoadipyl-cysteinyl-valine synthetase. L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase","L-2-aminohexanedioate + L-cysteine + L-valine + 3 ATP + H(2)O = N-(L-5- amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + 3 AMP + 3 diphosphate","Mg(2+)","-!- The enzyme contains 4'-phosphopantetheine, which may be involved in the mechanism of the reaction. -!- Forms part of the penicillin biosynthesis pathway"]
[null,"1.2.1.31","no",1,403,7e-15,21,37,382,346,"L-aminoadipate-semialdehyde dehydrogenase","2-aminoadipate semialdehyde dehydrogenase. 2-aminoadipic semialdehyde dehydrogenase. Alpha-aminoadipate reductase. Alpha-aminoadipate-semialdehyde dehydrogenase. Aminoadipate semialdehyde dehydrogenase. L-alpha-aminoadipate delta-semialdehyde oxidoreductase","(S)-2-amino-6-oxohexanoate + NAD(P)(+) + H(2)O = L-2-aminoadipate + NAD(P)H","_","-!- (S)-2-amino-6-oxohexanoate undergoes a spontaneous dehydration forming the cyclic (S)-2,3,4,5-tetrahydropyridine-2-carboxylate, which serves as a substrate for the hydrogenation reaction"]
[null,"6.2.1.12","no",1,405,4e-12,21,286,528,243,"4-coumarate--CoA ligase","4-coumaroyl-CoA synthase. 4-coumaryl-CoA synthetase","ATP + 4-coumarate + CoA = AMP + diphosphate + 4-coumaroyl-CoA","_","_"]
[]
["CLOSTRIBL3_v1_10745","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.3.1.8","high",1,331,{"v":1e-120,"d":"1.00E-120"},60,5,329,325,"Phosphate acetyltransferase","Phosphoacylase. Phosphotransacetylase","Acetyl-CoA + phosphate = CoA + acetyl phosphate","_","-!- Also acts with other short-chain acyl-CoAs"]
[null,"2.3.1.19","no",1,288,2e-15,27,16,324,309,"Phosphate butyryltransferase","Phosphotransbutyrylase","Butanoyl-CoA + phosphate = CoA + butanoylphosphate","_","_"]
[]
["CLOSTRIBL3_v1_10746","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.7.2.1","high",1,410,0,65,2,397,396,"Acetate kinase","Acetate kinase (phosphorylating). Acetic kinase. Acetokinase. AK","ATP + acetate = ADP + acetyl phosphate","Mg(2+)","-!- While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly. -!- Acetate can be converted into the key metabolic intermediate acetyl- CoA by coupling ac"]
[null,"2.7.2.15","no",1,408,{"v":1e-122,"d":"1.00E-122"},46,3,390,388,"Propionate kinase","Propionate/acetate kinase","ATP + propanoate = ADP + propanoyl phosphate","Mg(2+)","-!- Both propanoate and acetate can act as a substrate. -!- Involved in the anaerobic degradation of L-threonine in bacteria. -!- Both this enzyme and EC 2.7.2.1 play important roles in the production of propanoate"]
[null,"2.7.2.7","no",1,355,{"v":2e-18,"d":"2.00E-18"},27,1,331,331,"Butyrate kinase","_","ATP + butanoate = ADP + butanoyl phosphate","_","-!- The enzyme from Clostridium sp. also acts, more slowly on pentanoate and propanoate, and on some branched-chain fatty acids (cf. EC 2.7.1.14)"]
[]
["CLOSTRIBL3_v1_11881","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.1.1","high",9,419,{"v":8e-71,"d":"8.00E-71"},35,1,387,387,"Alcohol dehydrogenase","Aldehyde reductase","(1) A primary alcohol + NAD(+) = an aldehyde + NADH. (2) A secondary alcohol + NAD(+) = a ketone + NADH","Zn(2+) or Fe cation","-!- Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. -!- The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols"]
[null,"1.1.1.202","no",1,387,{"v":3e-61,"d":"3.00E-61"},36,16,382,367,"1,3-propanediol dehydrogenase","1,3-propanediol oxidoreductase. 3-hydroxypropionaldehyde reductase","Propane-1,3-diol + NAD(+) = 3-hydroxypropanal + NADH","_","_"]
[null,"1.1.1.244","no",1,381,{"v":7e-61,"d":"7.00E-61"},34,14,386,373,"Methanol dehydrogenase","_","Methanol + NAD(+) = formaldehyde + NADH","_","_"]
[null,"1.1.1.77","no",1,383,{"v":6e-54,"d":"6.00E-54"},31,16,382,367,"Lactaldehyde reductase","Propanediol oxidoreductase","(1) (R)-propane-1,2-diol + NAD(+) = (R)-lactaldehyde + NADH. (2) (S)-propane-1,2-diol + NAD(+) = (S)-lactaldehyde + NADH","_","_"]
[null,"1.2.1.10","no",2,875,{"v":2E-51,"d":"2.00E-51"},31,28,382,355,"Acetaldehyde dehydrogenase (acetylating)","Acylating acetaldehyde dehydrogenase. Aldehyde dehydrogenase (acylating)","Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH","_","-!- Also acts, more slowly, on glycolaldehyde, propanal and butanal. -!- In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39. -!- The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perfor"]
[null,"1.1.99.24","no",1,479,{"v":8e-45,"d":"8.00E-45"},27,5,387,383,"Hydroxyacid-oxoacid transhydrogenase","_","(1) (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2- hydroxyglutarate. (2) 4-hydroxybutanoate + 2-oxoglutarate = succinic semialdehyde + (R)-2- hydroxyglutarate","_","_"]
[null,"1.1.1.61","no",1,371,{"v":4e-40,"d":"4.00E-40"},32,74,385,312,"4-hydroxybutyrate dehydrogenase","_","4-hydroxybutanoate + NAD(+) = succinate semialdehyde + NADH","_","_"]
[null,"1.3.1.32","no",1,356,{"v":3e-33,"d":"3.00E-33"},25,13,381,369,"Maleylacetate reductase","Maleolylacetate reductase","3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H","_","_"]
[]
["CLOSTRIBL3_v1_20137","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.1.1","high",9,419,{"v":9e-94,"d":"9.00E-94"},38,4,381,378,"Alcohol dehydrogenase","Aldehyde reductase","(1) A primary alcohol + NAD(+) = an aldehyde + NADH. (2) A secondary alcohol + NAD(+) = a ketone + NADH","Zn(2+) or Fe cation","-!- Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. -!- The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols"]
[null,"1.2.1.10","no",2,875,{"v":5e-89,"d":"5.00E-89"},38,4,381,378,"Acetaldehyde dehydrogenase (acetylating)","Acylating acetaldehyde dehydrogenase. Aldehyde dehydrogenase (acylating)","Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH","_","-!- Also acts, more slowly, on glycolaldehyde, propanal and butanal. -!- In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39. -!- The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perfor"]
[null,"1.1.1.244","no",1,381,{"v":9e-58,"d":"9.00E-58"},35,19,379,361,"Methanol dehydrogenase","_","Methanol + NAD(+) = formaldehyde + NADH","_","_"]
[null,"1.1.1.202","no",1,387,{"v":6e-54,"d":"6.00E-54"},33,1,381,381,"1,3-propanediol dehydrogenase","1,3-propanediol oxidoreductase. 3-hydroxypropionaldehyde reductase","Propane-1,3-diol + NAD(+) = 3-hydroxypropanal + NADH","_","_"]
[null,"1.1.1.77","no",1,383,{"v":2e-53,"d":"2.00E-53"},34,26,377,352,"Lactaldehyde reductase","Propanediol oxidoreductase","(1) (R)-propane-1,2-diol + NAD(+) = (R)-lactaldehyde + NADH. (2) (S)-propane-1,2-diol + NAD(+) = (S)-lactaldehyde + NADH","_","_"]
[null,"1.1.99.24","no",1,479,{"v":1e-36,"d":"1.00E-36"},27,49,379,331,"Hydroxyacid-oxoacid transhydrogenase","_","(1) (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2- hydroxyglutarate. (2) 4-hydroxybutanoate + 2-oxoglutarate = succinic semialdehyde + (R)-2- hydroxyglutarate","_","_"]
[null,"1.3.1.32","no",1,356,{"v":1e-33,"d":"1.00E-33"},27,86,382,297,"Maleylacetate reductase","Maleolylacetate reductase","3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H","_","_"]
[null,"1.1.1.61","no",1,371,{"v":4e-32,"d":"4.00E-32"},29,5,350,346,"4-hydroxybutyrate dehydrogenase","_","4-hydroxybutanoate + NAD(+) = succinate semialdehyde + NADH","_","_"]
[]
["CLOSTRIBL3_v1_12484","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.2.1.10","medium",2,875,{"v":1E-135,"d":"1.00E-135"},48,11,445,435,"Acetaldehyde dehydrogenase (acetylating)","Acylating acetaldehyde dehydrogenase. Aldehyde dehydrogenase (acylating)","Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH","_","-!- Also acts, more slowly, on glycolaldehyde, propanal and butanal. -!- In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39. -!- The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perfor"]
[null,"1.2.1.16","no",1,421,{"v":1E-35,"d":"1.00E-35"},19,10,401,392,"Succinate-semialdehyde dehydrogenase (NAD(P)(+))","_","Succinate semialdehyde + NAD(P)(+) + H(2)O = succinate + NAD(P)H","_","_"]
[null,"1.2.1.22","no",1,475,{"v":4e-16,"d":"4.00E-16"},20,1,391,391,"Lactaldehyde dehydrogenase","_","(S)-lactaldehyde + NAD(+) + H(2)O = (S)-lactate + NADH","_","_"]
[null,"1.2.1.41","no",1,427,7e-12,22,15,412,398,"Glutamate-5-semialdehyde dehydrogenase","Beta-glutamylphosphate reductase. Gamma-glutamylphosphate reductase. Glutamyl-gamma-semialdehyde dehydrogenase","L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH","_","_"]
[null,"1.2.1.3","no",1,462,1e-11,22,38,274,237,"Aldehyde dehydrogenase (NAD(+))","_","An aldehyde + NAD(+) + H(2)O = a carboxylate + NADH","_","-!- Wide specificity, including oxidation of D-glucuronolactone to D-glucarate. -!- Formerly EC 1.1.1.70"]
[]
["CLOSTRIBL3_v1_12496","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.2.1.10","medium",2,875,{"v":9e-99,"d":"9.00E-99"},38,17,445,429,"Acetaldehyde dehydrogenase (acetylating)","Acylating acetaldehyde dehydrogenase. Aldehyde dehydrogenase (acylating)","Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH","_","-!- Also acts, more slowly, on glycolaldehyde, propanal and butanal. -!- In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39. -!- The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perfor"]
[null,"1.2.1.16","no",1,421,{"v":3e-30,"d":"3.00E-30"},18,10,403,394,"Succinate-semialdehyde dehydrogenase (NAD(P)(+))","_","Succinate semialdehyde + NAD(P)(+) + H(2)O = succinate + NAD(P)H","_","_"]
[null,"1.2.1.41","no",1,427,2e-13,23,1,266,266,"Glutamate-5-semialdehyde dehydrogenase","Beta-glutamylphosphate reductase. Gamma-glutamylphosphate reductase. Glutamyl-gamma-semialdehyde dehydrogenase","L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH","_","_"]
[null,"1.2.1.5","no",1,407,2E-12,19,107,429,323,"Aldehyde dehydrogenase (NAD(P)(+))","_","An aldehyde + NAD(P)(+) + H(2)O = a carboxylate + NAD(P)H","_","_"]
[null,"1.2.1.22","no",1,475,5e-12,19,9,405,397,"Lactaldehyde dehydrogenase","_","(S)-lactaldehyde + NAD(+) + H(2)O = (S)-lactate + NADH","_","_"]
[]
["CLOSTRIBL3_v1_12732","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.2.1.10","high",1,313,{"v":5e-82,"d":"5.00E-82"},51,2,285,284,"Acetaldehyde dehydrogenase (acetylating)","Acylating acetaldehyde dehydrogenase. Aldehyde dehydrogenase (acylating)","Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH","_","-!- Also acts, more slowly, on glycolaldehyde, propanal and butanal. -!- In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39. -!- The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perfor"]

{"sheet":"COG","index":8,"n_rows":85,"n_cols":7,"rows_kept":85}
["CDS","COG id","Score","Begin","End","Classes","Function"]
["CLOSTRIBL3_v1_11086","COG3875",254,36,289,"S","Uncharacterized conserved protein"]
["CLOSTRIBL3_v1_11116","COG3875",387,37,423,"S","Uncharacterized conserved protein"]
["CLOSTRIBL3_v1_11117","COG1620",503,2,504,"C","L-lactate permease"]
["CLOSTRIBL3_v1_30024","COG3875",293,37,329,"S","Uncharacterized conserved protein"]
["CLOSTRIBL3_v1_10010","COG0039",259,124,382,"C","Malate/lactate dehydrogenases"]
["CLOSTRIBL3_v1_10012","COG0039",320,1,320,"C","Malate/lactate dehydrogenases"]
["CLOSTRIBL3_v1_12309","COG1304",305,52,356,"C","L-lactate dehydrogenase (FMN-dependent) and related alpha-hydroxy acid dehydrogenases"]
["CLOSTRIBL3_v1_12417","COG0674",410,1,410,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
[null,"COG1014",382,414,795,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
[null,"COG1013",378,796,1173,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
["CLOSTRIBL3_v1_12774","COG1013",309,1,309,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
["CLOSTRIBL3_v1_12775","COG0674",391,1,391,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
["CLOSTRIBL3_v1_12776","COG1144",86,13,98,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, delta subunit"]
["CLOSTRIBL3_v1_12777","COG1014",192,2,193,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
["CLOSTRIBL3_v1_10343","COG0674",410,1,410,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
[null,"COG1014",378,414,791,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
[null,"COG1013",377,792,1168,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
["CLOSTRIBL3_v1_20129","COG0674",414,1,414,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
[null,"COG1014",379,417,795,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
[null,"COG1013",375,796,1170,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
["CLOSTRIBL3_v1_12838","COG0183",392,1,392,"I","Acetyl-CoA acetyltransferase"]
["CLOSTRIBL3_v1_13111","COG0183",391,1,391,"I","Acetyl-CoA acetyltransferase"]
["CLOSTRIBL3_v1_11283","COG0183",398,1,398,"I","Acetyl-CoA acetyltransferase"]
["CLOSTRIBL3_v1_11276","COG1250",303,1,303,"I","3-hydroxyacyl-CoA dehydrogenase"]
["CLOSTRIBL3_v1_13113","COG1250",288,1,288,"I","3-hydroxyacyl-CoA dehydrogenase"]
["CLOSTRIBL3_v1_20313","COG1250",282,1,282,"I","3-hydroxyacyl-CoA dehydrogenase"]
["CLOSTRIBL3_v1_13112","COG1024",255,1,255,"I","Enoyl-CoA hydratase/carnithine racemase"]
["CLOSTRIBL3_v1_11087","COG1024",254,1,254,"I","Enoyl-CoA hydratase/carnithine racemase"]
["CLOSTRIBL3_v1_20109","COG2030",138,1,138,"I","Acyl dehydratase"]
["CLOSTRIBL3_v1_20308","COG1024",259,1,259,"I","Enoyl-CoA hydratase/carnithine racemase"]
["CLOSTRIBL3_v1_12502","COG1960",389,1,389,"I","Acyl-CoA dehydrogenases"]
[null,"COG2025",173,390,562,"C","Electron transfer flavoprotein, alpha subunit"]
[null,"COG1773",52,583,634,"C","Rubredoxin"]
["CLOSTRIBL3_v1_11587","COG1960",379,1,379,"I","Acyl-CoA dehydrogenases"]
["CLOSTRIBL3_v1_12012","COG1960",380,1,380,"I","Acyl-CoA dehydrogenases"]
["CLOSTRIBL3_v1_12013","COG1960",386,3,388,"I","Acyl-CoA dehydrogenases"]
["CLOSTRIBL3_v1_20310","COG1960",379,1,379,"I","Acyl-CoA dehydrogenases"]
["CLOSTRIBL3_v1_20311","COG2086",259,1,259,"C","Electron transfer flavoprotein, beta subunit"]
["CLOSTRIBL3_v1_20312","COG2025",333,1,333,"C","Electron transfer flavoprotein, alpha subunit"]
["CLOSTRIBL3_v1_11710","COG3426",356,3,358,"C","Butyrate kinase"]
["CLOSTRIBL3_v1_11711","COG0280",300,2,301,"C","Phosphotransacetylase"]
["CLOSTRIBL3_v1_12016","COG0280",297,3,299,"C","Phosphotransacetylase"]
["CLOSTRIBL3_v1_12308","COG0280",297,2,298,"C","Phosphotransacetylase"]
["CLOSTRIBL3_v1_20086","COG3426",350,5,354,"C","Butyrate kinase"]
["CLOSTRIBL3_v1_20087","COG3426",353,2,354,"C","Butyrate kinase"]
["CLOSTRIBL3_v1_13110","COG0427",447,4,450,"C","Acetyl-CoA hydrolase"]
["CLOSTRIBL3_v1_11114","COG2025",337,66,402,"C","Electron transfer flavoprotein, alpha subunit"]
[null,"COG1145",39,20,58,"C","Ferredoxin"]
["CLOSTRIBL3_v1_11115","COG2086",262,1,262,"C","Electron transfer flavoprotein, beta subunit"]
["CLOSTRIBL3_v1_11486","COG0277",462,10,471,"C","FAD/FMN-containing dehydrogenases"]
["CLOSTRIBL3_v1_11487","COG2025",327,2,328,"C","Electron transfer flavoprotein, alpha subunit"]
["CLOSTRIBL3_v1_11488","COG2086",264,1,264,"C","Electron transfer flavoprotein, beta subunit"]
["CLOSTRIBL3_v1_12010","COG2025",334,3,336,"C","Electron transfer flavoprotein, alpha subunit"]
["CLOSTRIBL3_v1_12011","COG2086",262,1,262,"C","Electron transfer flavoprotein, beta subunit"]
["CLOSTRIBL3_v1_20124","COG2086",265,1,265,"C","Electron transfer flavoprotein, beta subunit"]
["CLOSTRIBL3_v1_20125","COG2025",331,2,332,"C","Electron transfer flavoprotein, alpha subunit"]
["CLOSTRIBL3_v1_10629","COG4656",453,2,454,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfC"]
["CLOSTRIBL3_v1_10630","COG4658",322,10,331,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfD"]
["CLOSTRIBL3_v1_10631","COG4659",162,17,178,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfG"]
["CLOSTRIBL3_v1_10632","COG4660",192,3,194,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfE"]
["CLOSTRIBL3_v1_10633","COG4657",193,1,193,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfA"]
["CLOSTRIBL3_v1_10634","COG2878",265,2,266,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfB"]
["CLOSTRIBL3_v1_10096","COG1142",183,2,184,"C","Fe-S-cluster-containing hydrogenase components 2"]
["CLOSTRIBL3_v1_10095","COG4624",400,63,462,"R","Iron only hydrogenase large subunit, C-terminal domain"]
[null,"COG1145",62,1,62,"C","Ferredoxin"]
["CLOSTRIBL3_v1_10094","COG1142",174,4,177,"C","Fe-S-cluster-containing hydrogenase components 2"]
["CLOSTRIBL3_v1_10091","COG1905",148,13,160,"C","NADH:ubiquinone oxidoreductase 24 kD subunit"]
["CLOSTRIBL3_v1_10092","COG1894",529,7,535,"C","NADH:ubiquinone oxidoreductase, NADH-binding (51 kD) subunit"]
[null,"COG1145",64,536,599,"C","Ferredoxin"]
["CLOSTRIBL3_v1_10093","COG1034",183,1,183,"C","NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G)"]
[null,"COG1145",42,206,247,"C","Ferredoxin"]
["CLOSTRIBL3_v1_13020","COG1145",114,22,135,"C","Ferredoxin"]
[null,"COG4624",96,216,311,"R","Iron only hydrogenase large subunit, C-terminal domain"]
[null,"COG0437",31,136,166,"C","Fe-S-cluster-containing hydrogenase components 1"]
["CLOSTRIBL3_v1_20317","COG4624",318,171,488,"R","Iron only hydrogenase large subunit, C-terminal domain"]
[null,"COG1145",99,72,170,"C","Ferredoxin"]
["CLOSTRIBL3_v1_12009","COG0318",542,4,545,"IQ","Acyl-CoA synthetases (AMP-forming)/AMP-acid ligases II"]
["CLOSTRIBL3_v1_10745","COG0280",331,1,331,"C","Phosphotransacetylase"]
["CLOSTRIBL3_v1_10746","COG0282",399,1,399,"C","Acetate kinase"]
["CLOSTRIBL3_v1_11881","COG1454",387,1,387,"C","Alcohol dehydrogenase, class IV"]
["CLOSTRIBL3_v1_20137","COG1454",382,1,382,"C","Alcohol dehydrogenase, class IV"]
["CLOSTRIBL3_v1_12484","COG1012",449,2,450,"C","NAD-dependent aldehyde dehydrogenases"]
["CLOSTRIBL3_v1_12496","COG1012",493,4,496,"C","NAD-dependent aldehyde dehydrogenases"]
["CLOSTRIBL3_v1_12732","COG4569",284,3,286,"Q","Acetaldehyde dehydrogenase (acetylating)"]

{"sheet":"EGGNOG","index":9,"n_rows":70,"n_cols":7,"rows_kept":70}
["CDS","OG ID","Score","Eval","Class ID","OG function","KEGG map"]
["CLOSTRIBL3_v1_11086","05QUH",513.5,{"v":3.6e-143,"d":"3.60E-143"},"S","Domain of unknown function (DUF2088)","-"]
["CLOSTRIBL3_v1_11116","05QUH",687.6,{"v":1.4E-195,"d":"1.40E-195"},"S","Domain of unknown function (DUF2088)","-"]
["CLOSTRIBL3_v1_11117","05DAA",823.2,{"v":2.6E-236,"d":"2.60E-236"},"C","L-lactate","-"]
["CLOSTRIBL3_v1_30024","05QUH",652.9,{"v":3.8e-185,"d":"3.80E-185"},"S","Domain of unknown function (DUF2088)","-"]
["CLOSTRIBL3_v1_10010","07WFN",458.4,{"v":1.4E-126,"d":"1.40E-126"},"S","Malate lactate","-"]
["CLOSTRIBL3_v1_10012","05C80",391,{"v":2e-106,"d":"2.00E-106"},"C","Catalyzes the reversible oxidation of malate to oxaloacetate (By similarity)","00010, 00020, 00270, 00620, 00630, 00640, 00680, 00710, 00720, 01100, 01110, 01120"]
["CLOSTRIBL3_v1_12309","05DMF",620.9,{"v":1.4E-175,"d":"1.40E-175"},"C","Dehydrogenase","00620, 00630, 01100, 01110, 01120"]
["CLOSTRIBL3_v1_12417","05D95",2016.9,0,"C","Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (By similarity)","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 00910, 01100, 01120"]
["CLOSTRIBL3_v1_12774","05DDK",465.3,{"v":8.2e-129,"d":"8.20E-129"},"C","oxidoreductase, beta subunit","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 01100, 01120"]
["CLOSTRIBL3_v1_12775","05D95",542.3,{"v":6.7e-152,"d":"6.70E-152"},"C","Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (By similarity)","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 00910, 01100, 01120"]
["CLOSTRIBL3_v1_12776","05WGB",148.3,{"v":7.1e-34,"d":"7.10E-34"},"C","oxidoreductase, delta subunit","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 01100, 01120"]
["CLOSTRIBL3_v1_12777","05EJ5",290.4,{"v":2.3e-76,"d":"2.30E-76"},"C","oxidoreductase gamma subunit","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 01100, 01120"]
["CLOSTRIBL3_v1_10343","05D95",2122.1,0,"C","Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (By similarity)","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 00910, 01100, 01120"]
["CLOSTRIBL3_v1_20129","05D95",1660.2,0,"C","Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (By similarity)","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 00910, 01100, 01120"]
["CLOSTRIBL3_v1_12838","05CHU",651,{"v":1.3e-184,"d":"1.30E-184"},"I","acetyl-coa acetyltransferase","00071, 00072, 00280, 00281, 00310, 00362, 00380, 00592, 00620, 00630, 00640, 00642, 00650, 00720, 00900, 01100, 01110, 01120, 02020"]
["CLOSTRIBL3_v1_13111","05CHU",634.8,{"v":9.9e-180,"d":"9.90E-180"},"I","acetyl-coa acetyltransferase","00071, 00072, 00280, 00281, 00310, 00362, 00380, 00592, 00620, 00630, 00640, 00642, 00650, 00720, 00900, 01100, 01110, 01120, 02020"]
["CLOSTRIBL3_v1_11283","05MX0",718.8,{"v":5.3e-205,"d":"5.30E-205"},"I","acetyl-coa acetyltransferase","00071, 00072, 00280, 00310, 00362, 00380, 00620, 00630, 00640, 00650, 00720, 00900, 01100, 01110, 01120, 02020"]
["CLOSTRIBL3_v1_11276","05DYT",458.8,{"v":7.8e-127,"d":"7.80E-127"},"I","3-hydroxyacyl-CoA dehydrogenase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00640, 00650, 00720, 00903, 00930, 01040, 01100, 01110, 01120"]
["CLOSTRIBL3_v1_13113","05DYT",324.3,{"v":2.1E-86,"d":"2.10E-86"},"I","3-hydroxyacyl-CoA dehydrogenase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00640, 00650, 00720, 00903, 00930, 01040, 01100, 01110, 01120"]
["CLOSTRIBL3_v1_20313","05DYT",465.7,{"v":5.8e-129,"d":"5.80E-129"},"I","3-hydroxyacyl-CoA dehydrogenase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00640, 00650, 00720, 00903, 00930, 01040, 01100, 01110, 01120"]
["CLOSTRIBL3_v1_13112","05E39",238,{"v":1.8E-60,"d":"1.80E-60"},"I","Enoyl-CoA hydratase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00627, 00630, 00640, 00650, 00720, 00903, 00930, 01100, 01110, 01120"]
["CLOSTRIBL3_v1_11087","01W90",157.9,{"v":2.3E-36,"d":"2.30E-36"},"I","Enoyl-CoA hydratase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00627, 00640, 00650, 00903, 00930, 01100, 01110, 01120"]
["CLOSTRIBL3_v1_20109","08Z7G",221.9,{"v":7.1e-56,"d":"7.10E-56"},"I","MaoC domain protein dehydratase","-"]
["CLOSTRIBL3_v1_20308","05E39",399.1,{"v":6.1e-109,"d":"6.10E-109"},"I","Enoyl-CoA hydratase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00627, 00630, 00640, 00650, 00720, 00903, 00930, 01100, 01110, 01120"]
["CLOSTRIBL3_v1_12502","05C1G",1117.8,0,"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["CLOSTRIBL3_v1_11587","05C1G",544.7,{"v":1.3e-152,"d":"1.30E-152"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["CLOSTRIBL3_v1_12012","05C1G",686.4,{"v":2.8E-195,"d":"2.80E-195"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["CLOSTRIBL3_v1_12013","05C1G",714.1,{"v":1.3e-203,"d":"1.30E-203"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["CLOSTRIBL3_v1_20310","05C1G",623.6,{"v":2.2e-176,"d":"2.20E-176"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["CLOSTRIBL3_v1_20311","05BZJ",425.6,{"v":6.1E-117,"d":"6.10E-117"},"C","Electron transfer flavoprotein",910]
["CLOSTRIBL3_v1_20312","05C10",533.9,{"v":2E-149,"d":"2.00E-149"},"C","Electron transfer flavoprotein",910]
["CLOSTRIBL3_v1_11710","05CKM",595.1,{"v":8e-168,"d":"8.00E-168"},"C","Branched-chain carboxylic acid kinase","00650, 01100"]
["CLOSTRIBL3_v1_11711","07RE7",467.2,{"v":2.1e-129,"d":"2.10E-129"},"C","phosphate butyryltransferase","00650, 01100"]
["CLOSTRIBL3_v1_12016","07RE7",304.7,{"v":1.8e-80,"d":"1.80E-80"},"C","phosphate butyryltransferase","00650, 01100"]
["CLOSTRIBL3_v1_12308","COG0280",391.7,{"v":1.1E-106,"d":"1.10E-106"},"C","phosphate acetyltransferase","00430, 00620, 00640, 00650, 00680, 00710, 00720, 01100, 01120"]
["CLOSTRIBL3_v1_20086","05CKM",473.8,{"v":2.7e-131,"d":"2.70E-131"},"C","Branched-chain carboxylic acid kinase","00650, 01100"]
["CLOSTRIBL3_v1_20087","05CKM",443.7,{"v":3E-122,"d":"3.00E-122"},"C","Branched-chain carboxylic acid kinase","00650, 01100"]
["CLOSTRIBL3_v1_13110","05CYC",499.6,{"v":5.8e-139,"d":"5.80E-139"},"C","Transferase",620]
["CLOSTRIBL3_v1_11114","05C10",675.6,{"v":5.3e-192,"d":"5.30E-192"},"C","Electron transfer flavoprotein",910]
["CLOSTRIBL3_v1_11115","05BZJ",457.2,{"v":1.9e-126,"d":"1.90E-126"},"C","Electron transfer flavoprotein",910]
["CLOSTRIBL3_v1_11486","05CQB",777.7,{"v":1.1E-222,"d":"1.10E-222"},"C","FAD linked oxidase domain protein","00620, 00630, 01100, 01110, 01120"]
["CLOSTRIBL3_v1_11487","05C10",542.7,{"v":4.3e-152,"d":"4.30E-152"},"C","Electron transfer flavoprotein",910]
["CLOSTRIBL3_v1_11488","05BZJ",400.2,{"v":2.8e-109,"d":"2.80E-109"},"C","Electron transfer flavoprotein",910]
["CLOSTRIBL3_v1_12010","05C10",573.2,{"v":3.1e-161,"d":"3.10E-161"},"C","Electron transfer flavoprotein",910]
["CLOSTRIBL3_v1_12011","05BZJ",453.4,{"v":2.7e-125,"d":"2.70E-125"},"C","Electron transfer flavoprotein",910]
["CLOSTRIBL3_v1_20124","05BZJ",372.1,{"v":8.1e-101,"d":"8.10E-101"},"C","Electron transfer flavoprotein",910]
["CLOSTRIBL3_v1_20125","05C10",499.2,{"v":5.6e-139,"d":"5.60E-139"},"C","Electron transfer flavoprotein",910]
["CLOSTRIBL3_v1_10629","07QTR",773.9,{"v":1.6e-221,"d":"1.60E-221"},"C","Required for nitrogen fixation. May be part of a membrane complex functioning as an intermediate in the electron transport to nitrogenase (By similarity)","-"]
["CLOSTRIBL3_v1_10630","05D6A",580.1,{"v":2.5e-163,"d":"2.50E-163"},"C","Electron transport complex","-"]
["CLOSTRIBL3_v1_10631","080WF",301.6,{"v":9.4e-80,"d":"9.40E-80"},"C","Electron transport complex, RnfABCDGE type, G subunit","-"]
["CLOSTRIBL3_v1_10632","05DZB",349,{"v":5.9e-94,"d":"5.90E-94"},"C","Electron transport complex","-"]
["CLOSTRIBL3_v1_10633","05DGN",335.5,{"v":6.2e-90,"d":"6.20E-90"},"C","Electron transport complex","-"]
["CLOSTRIBL3_v1_10634","07SVV",499.2,{"v":4.8e-139,"d":"4.80E-139"},"C","electron transport complex, RnfABCDGE type, B subunit","-"]
["CLOSTRIBL3_v1_10096","081SR",273.9,{"v":2.1e-71,"d":"2.10E-71"},"C","4fe-4s ferredoxin, iron-sulfur binding","00633, 00680, 00720, 01120"]
["CLOSTRIBL3_v1_10095","07QHI",783.9,{"v":1.6e-224,"d":"1.60E-224"},"C","hydrogenase","00190, 00910, 01100"]
["CLOSTRIBL3_v1_10094","081SR",307.8,{"v":1.3e-81,"d":"1.30E-81"},"C","4fe-4s ferredoxin, iron-sulfur binding","00633, 00680, 00720, 01120"]
["CLOSTRIBL3_v1_10091","0902H",282.7,{"v":4e-74,"d":"4.00E-74"},"C","NADH dehydrogenase (Ubiquinone), 24 kDa subunit","00190, 00630, 00680, 00910, 01100, 01120"]
["CLOSTRIBL3_v1_10092","07QIZ",1132.1,0,"C","NADH dehydrogenase","00190, 00630, 00680, 00910, 01100, 01120"]
["CLOSTRIBL3_v1_10093","08Z71",441.4,{"v":1e-121,"d":"1.00E-121"},"C","Ferredoxin","-"]
["CLOSTRIBL3_v1_13020","07QHI",689.5,{"v":3.9e-196,"d":"3.90E-196"},"C","hydrogenase","00190, 00910, 01100"]
["CLOSTRIBL3_v1_20317","07QHI",775.4,{"v":6e-222,"d":"6.00E-222"},"C","hydrogenase","00190, 00910, 01100"]
["CLOSTRIBL3_v1_12009","05CEY",821.2,{"v":1.1e-235,"d":"1.10E-235"},"I","Amp-dependent synthetase and ligase","00071, 01100, 03320, 04146, 04920, 00071, 01100, 03320, 04146, 04920"]
["CLOSTRIBL3_v1_10745","08IJ2",540.8,{"v":1.7e-151,"d":"1.70E-151"},"C","phosphate acetyltransferase","00430, 00620, 00640, 00680, 00720, 01100, 01120"]
["CLOSTRIBL3_v1_10746","05C6H",644.4,{"v":1.3E-182,"d":"1.30E-182"},"C","Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction (By similarity)","00430, 00620, 00640, 00680, 00720, 01100, 01120"]
["CLOSTRIBL3_v1_11881","05C0A",476.9,{"v":3.4e-132,"d":"3.40E-132"},"C","alcohol dehydrogenase","00010, 00071, 00350, 00362, 00620, 00621, 00622, 00625, 00626, 00650, 01100, 01110, 01120"]
["CLOSTRIBL3_v1_20137","05C0A",428.3,{"v":1.4e-117,"d":"1.40E-117"},"C","alcohol dehydrogenase","00010, 00071, 00350, 00362, 00620, 00621, 00622, 00625, 00626, 00650, 01100, 01110, 01120"]
["CLOSTRIBL3_v1_12484","COG1012",845.1,{"v":6.6e-243,"d":"6.60E-243"},"C","Dehydrogenase","00010, 00040, 00053, 00071, 00250, 00280, 00310, 00330, 00340, 00350, 00380, 00410, 00561, 00620, 00625, 00640, 00650, 00903, 01100, 01110, 01120"]
["CLOSTRIBL3_v1_12496","07QIG",822,{"v":5.6e-236,"d":"5.60E-236"},"C","Dehydrogenase","00010, 00071, 00350, 00362, 00620, 00621, 00622, 00625, 00626, 00650, 01100, 01110, 01120"]
["CLOSTRIBL3_v1_12732","05DIV",469.9,{"v":3.1e-130,"d":"3.10E-130"},"Q","Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD( ) and coenzyme A. Is the final enzyme in the meta- cleavage pathway for the degradation of aromatic compounds (By similarity)","00362, 00620, 00621, 00622, 00650, 01100, 01120"]

{"sheet":"FIGfam","index":10,"n_rows":51,"n_cols":4,"rows_kept":51}
["CDS","FIGFAM id","FIGFAM Description","EC number"]
["CLOSTRIBL3_v1_10012","FIG000812","L-lactate dehydrogenase","1.1.1.27"]
["CLOSTRIBL3_v1_12417","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["CLOSTRIBL3_v1_12774","FIG003175","Pyruvate:ferredoxin oxidoreductase, beta subunit","1.2.7.1"]
["CLOSTRIBL3_v1_12775","FIG002975","Pyruvate:ferredoxin oxidoreductase, alpha subunit","1.2.7.1"]
["CLOSTRIBL3_v1_12776","FIG135572","Pyruvate:ferredoxin oxidoreductase, gamma subunit","1.2.7.1"]
["CLOSTRIBL3_v1_12777","FIG003176","Pyruvate:ferredoxin oxidoreductase, gamma subunit","1.2.7.1"]
["CLOSTRIBL3_v1_10343","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["CLOSTRIBL3_v1_20129","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["CLOSTRIBL3_v1_12838","FIG002604","Acetyl-CoA acetyltransferase","2.3.1.9"]
["CLOSTRIBL3_v1_13111","FIG002604","Acetyl-CoA acetyltransferase","2.3.1.9"]
["CLOSTRIBL3_v1_13113","FIG000819","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157, 1.1.1.35"]
["CLOSTRIBL3_v1_20313","FIG133011","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157"]
["CLOSTRIBL3_v1_13112","FIG002255","3-hydroxybutyryl-CoA dehydratase","4.2.1.55"]
["CLOSTRIBL3_v1_20109","FIG012843","3-hydroxybutyryl-CoA dehydratase","4.2.1.55"]
["CLOSTRIBL3_v1_20308","FIG002255","3-hydroxybutyryl-CoA dehydratase","4.2.1.55"]
["CLOSTRIBL3_v1_12502","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["CLOSTRIBL3_v1_11587","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["CLOSTRIBL3_v1_12012","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["CLOSTRIBL3_v1_20310","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["CLOSTRIBL3_v1_20311","FIG136866","Electron transfer flavoprotein, beta subunit","_"]
["CLOSTRIBL3_v1_20312","FIG000366","Electron transfer flavoprotein, alpha subunit","_"]
["CLOSTRIBL3_v1_11710","FIG007694","Butyrate kinase","2.7.2.7"]
["CLOSTRIBL3_v1_11711","FIG133520","Phosphate butyryltransferase","2.3.1.19"]
["CLOSTRIBL3_v1_12308","FIG133520","Phosphate butyryltransferase","2.3.1.19"]
["CLOSTRIBL3_v1_20086","FIG007694","Butyrate kinase","2.7.2.7"]
["CLOSTRIBL3_v1_20087","FIG007694","Butyrate kinase","2.7.2.7"]
["CLOSTRIBL3_v1_11114","FIG000366","Electron transfer flavoprotein, alpha subunit","_"]
["CLOSTRIBL3_v1_11487","FIG000366","Electron transfer flavoprotein, alpha subunit","_"]
["CLOSTRIBL3_v1_12010","FIG000366","Electron transfer flavoprotein, alpha subunit","_"]
["CLOSTRIBL3_v1_12011","FIG136866","Electron transfer flavoprotein, beta subunit","_"]
["CLOSTRIBL3_v1_20124","FIG136866","Electron transfer flavoprotein, beta subunit","_"]
["CLOSTRIBL3_v1_20125","FIG000366","Electron transfer flavoprotein, alpha subunit","_"]
["CLOSTRIBL3_v1_10629","FIG018536","Electron transport complex protein RnfC","_"]
["CLOSTRIBL3_v1_10630","FIG022976","Electron transport complex protein RnfD","_"]
["CLOSTRIBL3_v1_10631","FIG002689","Electron transport complex protein RnfG","_"]
["CLOSTRIBL3_v1_10632","FIG134060","Electron transport complex protein RnfE","_"]
["CLOSTRIBL3_v1_10633","FIG001505","Electron transport complex protein RnfA","_"]
["CLOSTRIBL3_v1_10634","FIG133292","Electron transport complex protein RnfB","_"]
["CLOSTRIBL3_v1_10096","FIG005118","Electron transport protein HydN","_"]
["CLOSTRIBL3_v1_10095","FIG138133","Periplasmic (Fe) hydrogenase large subunit","1.12.7.2"]
["CLOSTRIBL3_v1_10094","FIG133154","Fe-S-cluster-containing hydrogenase components 2","_"]
["CLOSTRIBL3_v1_13020","FIG133264","Periplasmic (Fe) hydrogenase","1.12.7.2"]
["CLOSTRIBL3_v1_20317","FIG133264","Periplasmic (Fe) hydrogenase","1.12.7.2"]
["CLOSTRIBL3_v1_10745","FIG000522","Phosphate acetyltransferase","2.3.1.8"]
["CLOSTRIBL3_v1_10746","FIG134300","Acetate kinase","2.7.2.1"]
["CLOSTRIBL3_v1_11881","FIG037315","Alcohol dehydrogenase","1.1.1.1"]
["CLOSTRIBL3_v1_20137","FIG138701","Alcohol dehydrogenase","1.1.1.1, 1.2.1.10"]
["CLOSTRIBL3_v1_12484","FIG004876","Acetaldehyde dehydrogenase, ethanolamine utilization cluster","_"]
["CLOSTRIBL3_v1_12496","FIG004876","Acetaldehyde dehydrogenase, ethanolamine utilization cluster","_"]
["CLOSTRIBL3_v1_12732","FIG002495","Acetaldehyde dehydrogenase, acetylating, in gene cluster for degradation of phenols, cresols, catechol","1.2.1.10"]

{"sheet":"InterProScan","index":11,"n_rows":891,"n_cols":13,"rows_kept":891}
["CLOSTRIBL3_v1_11086","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR018657","PFAM","PF09861","Lar_N",8,205,0.465721,{"v":7e-67,"d":"7.00E-67"},"LarA-like_N","Domain","LarA-like, N-terminal","Molecular Function: lactate racemase activity (GO:0050043)"]
[null,"_","_","PTHR33171","_",4,423,0.990544,{"v":5e-113,"d":"5.00E-113"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.11440","_",29,273,0.576832,{"v":2.8e-130,"d":"2.80E-130"},"_","_","_","-"]
[null,"_","_","G3DSA:3.90.226.30","_",7,417,0.969267,{"v":2.8e-130,"d":"2.80E-130"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_11116","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR018657","PFAM","PF09861","Lar_N",8,213,0.483491,{"v":1.6e-76,"d":"1.60E-76"},"LarA-like_N","Domain","LarA-like, N-terminal","Molecular Function: lactate racemase activity (GO:0050043)"]
[null,"_","_","PTHR33171","_",1,422,0.992925,{"v":1.5e-128,"d":"1.50E-128"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.11440","_",34,269,0.554245,{"v":4.3e-166,"d":"4.30E-166"},"_","_","_","-"]
[null,"_","_","G3DSA:3.90.226.30","_",6,418,0.971698,{"v":4.3e-166,"d":"4.30E-166"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_11117","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR003804","PANTHER","PTHR30003","PTHR30003",2,501,0.982283,{"v":6.5e-157,"d":"6.50E-157"},"Lactate_perm","Family","L-lactate permease","Cellular Component: integral component of plasma membrane (GO:0005887); Molecular Function: lactate transmembrane transporter activity (GO:0015129); Biological Process: lactate transport (GO:0015727)"]
[null,"IPR003804","PFAM","PF02652","Lactate_perm",7,500,0.970472,{"v":1.3e-141,"d":"1.30E-141"},"Lactate_perm","Family","L-lactate permease","Cellular Component: integral component of plasma membrane (GO:0005887); Molecular Function: lactate transmembrane transporter activity (GO:0015129); Biological Process: lactate transport (GO:0015727)"]
[null,"IPR003804","TIGRFAMs","TIGR00795","lctP",5,501,0.976378,{"v":4.1E-138,"d":"4.10E-138"},"Lactate_perm","Family","L-lactate permease","Cellular Component: integral component of plasma membrane (GO:0005887); Molecular Function: lactate transmembrane transporter activity (GO:0015129); Biological Process: lactate transport (GO:0015727)"]
[null,"_","_","PTHR30003:SF0","_",2,501,0.982283,{"v":6.5e-157,"d":"6.50E-157"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_30024","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR018657","PFAM","PF09861","Lar_N",8,213,0.483491,{"v":1.4E-71,"d":"1.40E-71"},"LarA-like_N","Domain","LarA-like, N-terminal","Molecular Function: lactate racemase activity (GO:0050043)"]
[null,"_","_","PTHR33171","_",1,422,0.992925,{"v":6.4e-127,"d":"6.40E-127"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.11440","_",34,269,0.554245,{"v":1.7e-161,"d":"1.70E-161"},"_","_","_","-"]
[null,"_","_","G3DSA:3.90.226.30","_",6,418,0.971698,{"v":1.7e-161,"d":"1.70E-161"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_10010","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036291","SSF","SSF51735","SSF51735",124,267,0.345411,2.1e-12,"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR001236","PFAM","PF00056","Ldh_1_N",124,263,0.335749,1.1e-07,"Lactate/malate_DH_N","Domain","Lactate/malate dehydrogenase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","G3DSA:3.40.50.720","_",113,272,0.384058,{"v":3.1e-22,"d":"3.10E-22"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_10012","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036291","SSF","SSF51735","SSF51735",4,150,0.45625,{"v":4.7e-36,"d":"4.70E-36"},"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR022383","PFAM","PF02866","Ldh_1_C",151,314,0.509375,{"v":1.2E-23,"d":"1.20E-23"},"Lactate/malate_DH_C","Domain","Lactate/malate dehydrogenase, C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR018177","PROSITE","PS00064","L_LDH",178,184,0.01875,"_","L-lactate_DH_AS","Active_site","L-lactate dehydrogenase, active site","Molecular Function: L-lactate dehydrogenase activity (GO:0004459); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR015955","CATHGENE3D","G3DSA:3.90.110.10","G3DSA:3.90.110.10",151,318,0.521875,{"v":1.4E-56,"d":"1.40E-56"},"Lactate_DH/Glyco_Ohase_4_C","Homologous_superfamily","Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal","Molecular Function: catalytic activity (GO:0003824); Biological Process: carbohydrate metabolic process (GO:0005975); Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR015955","SSF","SSF56327","SSF56327",149,315,0.51875,{"v":6.49e-52,"d":"6.49E-52"},"Lactate_DH/Glyco_Ohase_4_C","Homologous_superfamily","Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal","Molecular Function: catalytic activity (GO:0003824); Biological Process: carbohydrate metabolic process (GO:0005975); Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011304","HAMAP","MF_00488","Lactate_dehydrog",5,317,0.975,35.115,"L-lactate_DH","Family","L-lactate dehydrogenase","Molecular Function: L-lactate dehydrogenase activity (GO:0004459); Cellular Component: cytoplasm (GO:0005737); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011304","TIGRFAMs","TIGR01771","L-LDH-NAD",10,309,0.934375,{"v":1.3e-98,"d":"1.30E-98"},"L-lactate_DH","Family","L-lactate dehydrogenase","Molecular Function: L-lactate dehydrogenase activity (GO:0004459); Cellular Component: cytoplasm (GO:0005737); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001557","PIRSF","PIRSF000102","Lac_mal_DH",2,320,0.99375,{"v":5.5e-100,"d":"5.50E-100"},"L-lactate/malate_DH","Family","L-lactate/malate dehydrogenase","Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: carboxylic acid metabolic process (GO:0019752); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001557","PRINTS","PR00086","LLDHDRGNASE",176,189,0.040625,{"v":5.5e-32,"d":"5.50E-32"},"L-lactate/malate_DH","Family","L-lactate/malate dehydrogenase","Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: carboxylic acid metabolic process (GO:0019752); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001557","PRINTS","PR00086","LLDHDRGNASE",122,142,0.0625,{"v":5.5e-32,"d":"5.50E-32"},"L-lactate/malate_DH","Family","L-lactate/malate dehydrogenase","Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: carboxylic acid metabolic process (GO:0019752); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001557","PRINTS","PR00086","LLDHDRGNASE",146,164,0.05625,{"v":5.5e-32,"d":"5.50E-32"},"L-lactate/malate_DH","Family","L-lactate/malate dehydrogenase","Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: carboxylic acid metabolic process (GO:0019752); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001557","PRINTS","PR00086","LLDHDRGNASE",32,56,0.075,{"v":5.5e-32,"d":"5.50E-32"},"L-lactate/malate_DH","Family","L-lactate/malate dehydrogenase","Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: carboxylic acid metabolic process (GO:0019752); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001557","PRINTS","PR00086","LLDHDRGNASE",7,31,0.075,{"v":5.5e-32,"d":"5.50E-32"},"L-lactate/malate_DH","Family","L-lactate/malate dehydrogenase","Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: carboxylic acid metabolic process (GO:0019752); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001236","PFAM","PF00056","Ldh_1_N",7,148,0.440625,{"v":2.6E-25,"d":"2.60E-25"},"Lactate/malate_DH_N","Domain","Lactate/malate dehydrogenase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","G3DSA:3.40.50.720","_",1,150,0.465625,{"v":3.1e-42,"d":"3.10E-42"},"_","_","_","-"]
[null,"_","_","PTHR43128","_",4,315,0.971875,{"v":5.5e-89,"d":"5.50E-89"},"_","_","_","-"]
[null,"_","_","PTHR43128:SF4","_",4,315,0.971875,{"v":5.5e-89,"d":"5.50E-89"},"_","_","_","-"]
[null,"_","_","cd05290","_",7,314,0.959375,{"v":5.06984E-163,"d":"5.07E-163"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12309","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037396","PROFILE","PS51349","FMN_HYDROXY_ACID_DH_2",54,356,0.848315,42.627,"FMN_HAD","Domain","FMN hydroxy acid dehydrogenase domain","-"]
[null,"IPR013785","CATHGENE3D","G3DSA:3.20.20.70","G3DSA:3.20.20.70",53,355,0.848315,{"v":1e-75,"d":"1.00E-75"},"Aldolase_TIM","Homologous_superfamily","Aldolase-type TIM barrel","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR012133","CDD","cd02809","alpha_hydroxyacid_oxid_FMN",34,349,0.884831,{"v":1.92767e-97,"d":"1.93E-97"},"Alpha-hydoxy_acid_DH_FMN","Family","Alpha-hydroxy acid dehydrogenase, FMN-dependent","Molecular Function: FMN binding (GO:0010181); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR012133","PIRSF","PIRSF000138","Al-hdrx_acd_dh",14,210,0.550562,{"v":8.3e-20,"d":"8.30E-20"},"Alpha-hydoxy_acid_DH_FMN","Family","Alpha-hydroxy acid dehydrogenase, FMN-dependent","Molecular Function: FMN binding (GO:0010181); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR012133","PIRSF","PIRSF000138","Al-hdrx_acd_dh",202,356,0.432584,{"v":3.2e-60,"d":"3.20E-60"},"Alpha-hydoxy_acid_DH_FMN","Family","Alpha-hydroxy acid dehydrogenase, FMN-dependent","Molecular Function: FMN binding (GO:0010181); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR000262","PFAM","PF01070","FMN_dh",54,196,0.398876,2.3e-11,"FMN-dep_DH","Domain","FMN-dependent dehydrogenase","Molecular Function: oxidoreductase activity (GO:0016491)"]
[null,"IPR000262","PFAM","PF01070","FMN_dh",211,353,0.398876,{"v":6.6e-57,"d":"6.60E-57"},"FMN-dep_DH","Domain","FMN-dependent dehydrogenase","Molecular Function: oxidoreductase activity (GO:0016491)"]
[null,"_","_","SM01240","_",81,356,0.772472,3.3E-3,"_","_","_","-"]
[null,"_","_","SSF51395","_",55,352,0.83427,{"v":3.15e-59,"d":"3.15E-59"},"_","_","_","-"]
[null,"_","_","PTHR10578","_",7,353,0.97191,{"v":1.5E-103,"d":"1.50E-103"},"_","_","_","-"]
[null,"_","_","PTHR10578:SF109","_",7,353,0.97191,{"v":1.5E-103,"d":"1.50E-103"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12417","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037112","CATHGENE3D","G3DSA:4.10.780.10","G3DSA:4.10.780.10",631,668,0.0315431,4.8e-06,"Pyrv-flavodox_OxR_EKR_sf","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, EKR domain superfamily","-"]
[null,"IPR033412","PFAM","PF17147","PFOR_II",269,374,0.0895141,5.2e-14,"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",4,258,0.216539,{"v":1e-80,"d":"1.00E-80"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",787,1171,0.327366,{"v":8.46e-129,"d":"8.46E-129"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",425,609,0.156863,{"v":3.4e-32,"d":"3.40E-32"},"Pyrv/ketoisovalerate_OxRed_cat","Domain","Pyruvate/ketoisovalerate oxidoreductase, catalytic domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR019456","PFAM","PF10371","EKR",627,678,0.0434783,{"v":1.3E-22,"d":"1.30E-22"},"Pyrv-flavodox_OxRtase_EKR","Domain","Pyruvate-flavodoxin oxidoreductase, EKR domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR019456","SMART","SM00890","EKR",621,679,0.0494459,{"v":8.4e-28,"d":"8.40E-28"},"Pyrv-flavodox_OxRtase_EKR","Domain","Pyruvate-flavodoxin oxidoreductase, EKR domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",745,756,0.00937766,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",736,767,0.026428,9.684,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",680,710,0.0255754,8.466,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011895","PIRSF","PIRSF000159","NifJ",1,1173,0.999147,0,"Pyrv_flavodox_OxRed","Family","Pyruvate-flavodoxin oxidoreductase","Molecular Function: iron ion binding (GO:0005506); Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: electron transport chain (GO:0022900); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011895","TIGRFAMs","TIGR02176","pyruv_ox_red",5,1170,0.99318,0,"Pyrv_flavodox_OxRed","Family","Pyruvate-flavodoxin oxidoreductase","Molecular Function: iron ion binding (GO:0005506); Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: electron transport chain (GO:0022900); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011766","PFAM","PF02775","TPP_enzyme_C",959,1069,0.0937766,4.2e-08,"TPP_enzyme-bd_C","Domain","Thiamine pyrophosphate enzyme, C-terminal TPP-binding","Molecular Function: catalytic activity (GO:0003824); Molecular Function: thiamine pyrophosphate binding (GO:0030976)"]
[null,"IPR009014","CATHGENE3D","G3DSA:3.40.50.920","G3DSA:3.40.50.920",259,412,0.130435,{"v":2.5e-59,"d":"2.50E-59"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR009014","SSF","SSF52922","SSF52922",260,413,0.130435,{"v":2E-46,"d":"2.00E-46"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002880","PFAM","PF01855","POR_N",18,247,0.195226,{"v":6.3e-81,"d":"6.30E-81"},"Pyrv_Fd/Flavodoxin_OxRdtase_N","Domain","Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","CATHGENE3D","G3DSA:3.40.920.10","G3DSA:3.40.920.10",415,624,0.178176,{"v":7e-95,"d":"7.00E-95"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","SSF","SSF53323","SSF53323",415,667,0.214834,{"v":6.93e-90,"d":"6.93E-90"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PF13484","_",688,757,0.0588235,7.7e-11,"_","_","_","-"]
[null,"_","_","SSF54862","_",665,831,0.141517,{"v":1.81e-21,"d":"1.81E-21"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",669,785,0.0988917,{"v":3.8e-46,"d":"3.80E-46"},"_","_","_","-"]
[null,"_","_","cd07034","_",10,173,0.13896,{"v":9.86571e-55,"d":"9.87E-55"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",2,258,0.218244,{"v":4.2e-112,"d":"4.20E-112"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",786,1173,0.329923,{"v":2.3E-166,"d":"2.30E-166"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",1,1169,0.995737,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",1,1169,0.995737,0,"_","_","_","-"]
[null,"_","_","cd03377","_",804,1171,0.312873,0,"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12774","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR029061","SSF","SSF52518","SSF52518",10,306,0.957929,{"v":6.24e-73,"d":"6.24E-73"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR011766","PFAM","PF02775","TPP_enzyme_C",50,217,0.540453,{"v":2.7e-23,"d":"2.70E-23"},"TPP_enzyme-bd_C","Domain","Thiamine pyrophosphate enzyme, C-terminal TPP-binding","Molecular Function: catalytic activity (GO:0003824); Molecular Function: thiamine pyrophosphate binding (GO:0030976)"]
[null,"_","_","G3DSA:3.40.50.970","_",84,308,0.724919,{"v":5.2E-64,"d":"5.20E-64"},"_","_","_","-"]
[null,"_","_","PTHR42897","_",2,307,0.987055,{"v":3.6e-125,"d":"3.60E-125"},"_","_","_","-"]
[null,"_","_","PTHR42897:SF2","_",2,307,0.987055,{"v":3.6e-125,"d":"3.60E-125"},"_","_","_","-"]
[null,"_","_","cd03376","_",15,255,0.776699,{"v":1.02252E-128,"d":"1.02E-128"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12775","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033412","PFAM","PF17147","PFOR_II",261,365,0.265985,{"v":2e-30,"d":"2.00E-30"},"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",3,250,0.631714,{"v":1.86e-70,"d":"1.86E-70"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR009014","CATHGENE3D","G3DSA:3.40.50.920","G3DSA:3.40.50.920",252,389,0.350384,{"v":3.8e-47,"d":"3.80E-47"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR009014","SSF","SSF52922","SSF52922",252,376,0.317136,{"v":3.85e-38,"d":"3.85E-38"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002880","PFAM","PF01855","POR_N",16,238,0.567775,{"v":7.5e-70,"d":"7.50E-70"},"Pyrv_Fd/Flavodoxin_OxRdtase_N","Domain","Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","cd07034","_",9,169,0.409207,{"v":2.39065e-66,"d":"2.39E-66"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",1,251,0.639386,{"v":2.3E-95,"d":"2.30E-95"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",1,378,0.964194,{"v":3.1e-118,"d":"3.10E-118"},"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",1,378,0.964194,{"v":3.1e-118,"d":"3.10E-118"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12776","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR017896","PFAM","PF00037","Fer4",73,94,0.214286,7.6e-07,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",68,98,0.306122,10.23,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",39,67,0.285714,7.92,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011898","PANTHER","PTHR43724","PTHR43724",9,98,0.908163,{"v":7.5e-26,"d":"7.50E-26"},"PorD_KorD","Family","2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor (GO:0016625); Molecular Function: 4 iron, 4 sulfur cluster binding (GO:0051539)"]
[null,"IPR011898","TIGRFAMs","TIGR02179","PorD_KorD",25,98,0.744898,{"v":1.3e-30,"d":"1.30E-30"},"PorD_KorD","Family","2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor (GO:0016625); Molecular Function: 4 iron, 4 sulfur cluster binding (GO:0051539)"]
[null,"_","_","G3DSA:3.30.70.20","_",26,67,0.418367,1.2E-5,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",68,98,0.306122,1.8e-06,"_","_","_","-"]
[null,"_","_","SSF54862","_",25,98,0.744898,{"v":2.1E-18,"d":"2.10E-18"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12777","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR019752","PFAM","PF01558","POR",14,185,0.88601,{"v":1e-37,"d":"1.00E-37"},"Pyrv/ketoisovalerate_OxRed_cat","Domain","Pyruvate/ketoisovalerate oxidoreductase, catalytic domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011894","TIGRFAMs","TIGR02175","PorC_KorC",5,191,0.963731,{"v":3.2e-66,"d":"3.20E-66"},"PorC_KorC","Domain","2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor (GO:0016625); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","CATHGENE3D","G3DSA:3.40.920.10","G3DSA:3.40.920.10",3,192,0.979275,{"v":8.4e-66,"d":"8.40E-66"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","SSF","SSF53323","SSF53323",5,192,0.968912,{"v":7.98e-52,"d":"7.98E-52"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PTHR43366","_",4,192,0.974093,{"v":1.7e-62,"d":"1.70E-62"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_10343","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037112","CATHGENE3D","G3DSA:4.10.780.10","G3DSA:4.10.780.10",625,667,0.0359589,2e-05,"Pyrv-flavodox_OxR_EKR_sf","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, EKR domain superfamily","-"]
[null,"IPR033412","PFAM","PF17147","PFOR_II",268,373,0.0898973,{"v":2.3e-17,"d":"2.30E-17"},"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",3,257,0.217466,{"v":7.65e-78,"d":"7.65E-78"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",783,1166,0.327911,{"v":3.93e-135,"d":"3.93E-135"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",424,607,0.156678,{"v":9.1e-32,"d":"9.10E-32"},"Pyrv/ketoisovalerate_OxRed_cat","Domain","Pyruvate/ketoisovalerate oxidoreductase, catalytic domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR019456","PFAM","PF10371","EKR",624,677,0.0453767,{"v":6.9e-25,"d":"6.90E-25"},"Pyrv-flavodox_OxRtase_EKR","Domain","Pyruvate-flavodoxin oxidoreductase, EKR domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR019456","SMART","SM00890","EKR",620,678,0.0496575,{"v":1.2E-29,"d":"1.20E-29"},"Pyrv-flavodox_OxRtase_EKR","Domain","Pyruvate-flavodoxin oxidoreductase, EKR domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",742,753,0.00941781,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",688,699,0.00941781,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",679,708,0.0248288,9.088,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",733,764,0.0265411,8.894,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011895","PIRSF","PIRSF000159","NifJ",1,1168,0.999144,0,"Pyrv_flavodox_OxRed","Family","Pyruvate-flavodoxin oxidoreductase","Molecular Function: iron ion binding (GO:0005506); Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: electron transport chain (GO:0022900); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011895","TIGRFAMs","TIGR02176","pyruv_ox_red",4,1166,0.994863,0,"Pyrv_flavodox_OxRed","Family","Pyruvate-flavodoxin oxidoreductase","Molecular Function: iron ion binding (GO:0005506); Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: electron transport chain (GO:0022900); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011766","PFAM","PF02775","TPP_enzyme_C",953,1064,0.0950342,2.7E-10,"TPP_enzyme-bd_C","Domain","Thiamine pyrophosphate enzyme, C-terminal TPP-binding","Molecular Function: catalytic activity (GO:0003824); Molecular Function: thiamine pyrophosphate binding (GO:0030976)"]
[null,"IPR009014","CATHGENE3D","G3DSA:3.40.50.920","G3DSA:3.40.50.920",258,413,0.132705,{"v":9.7e-60,"d":"9.70E-60"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR009014","SSF","SSF52922","SSF52922",258,412,0.131849,{"v":4.71e-50,"d":"4.71E-50"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002880","PFAM","PF01855","POR_N",19,246,0.194349,{"v":5.8E-80,"d":"5.80E-80"},"Pyrv_Fd/Flavodoxin_OxRdtase_N","Domain","Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","CATHGENE3D","G3DSA:3.40.920.10","G3DSA:3.40.920.10",414,624,0.179795,{"v":3.2E-91,"d":"3.20E-91"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","SSF","SSF53323","SSF53323",415,667,0.215753,{"v":7.59e-89,"d":"7.59E-89"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PF13484","_",687,754,0.057363,8.1e-10,"_","_","_","-"]
[null,"_","_","SSF54862","_",664,828,0.140411,{"v":3.03e-20,"d":"3.03E-20"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",668,781,0.0967466,{"v":1.8E-41,"d":"1.80E-41"},"_","_","_","-"]
[null,"_","_","cd07034","_",9,172,0.139555,{"v":3.64469e-49,"d":"3.64E-49"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",2,257,0.218322,{"v":7.8E-110,"d":"7.80E-110"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",782,1168,0.330479,{"v":1.5E-176,"d":"1.50E-176"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",1,1165,0.996575,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",1,1165,0.996575,0,"_","_","_","-"]
[null,"_","_","cd03377","_",800,1166,0.313356,0,"_","_","_","-"]
[]
["CLOSTRIBL3_v1_20129","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033412","PFAM","PF17147","PFOR_II",272,375,0.0880342,{"v":2.6e-16,"d":"2.60E-16"},"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",7,261,0.217094,{"v":9.42e-74,"d":"9.42E-74"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",789,1169,0.324786,{"v":4.77e-127,"d":"4.77E-127"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",428,612,0.157265,{"v":1.4e-32,"d":"1.40E-32"},"Pyrv/ketoisovalerate_OxRed_cat","Domain","Pyruvate/ketoisovalerate oxidoreductase, catalytic domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR019456","PFAM","PF10371","EKR",627,681,0.0461538,{"v":8.2e-23,"d":"8.20E-23"},"Pyrv-flavodox_OxRtase_EKR","Domain","Pyruvate-flavodoxin oxidoreductase, EKR domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR019456","SMART","SM00890","EKR",624,682,0.0495727,{"v":7.8e-26,"d":"7.80E-26"},"Pyrv-flavodox_OxRtase_EKR","Domain","Pyruvate-flavodoxin oxidoreductase, EKR domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",749,760,0.00940171,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF13187","Fer4_9",691,763,0.0615385,4.4e-08,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",740,769,0.0247863,10.003,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",683,712,0.0247863,8.39,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011895","PIRSF","PIRSF000159","NifJ",3,1170,0.997436,0,"Pyrv_flavodox_OxRed","Family","Pyruvate-flavodoxin oxidoreductase","Molecular Function: iron ion binding (GO:0005506); Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: electron transport chain (GO:0022900); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011895","TIGRFAMs","TIGR02176","pyruv_ox_red",9,1169,0.991453,0,"Pyrv_flavodox_OxRed","Family","Pyruvate-flavodoxin oxidoreductase","Molecular Function: iron ion binding (GO:0005506); Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: electron transport chain (GO:0022900); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011766","PFAM","PF02775","TPP_enzyme_C",959,1068,0.0931624,3.9e-08,"TPP_enzyme-bd_C","Domain","Thiamine pyrophosphate enzyme, C-terminal TPP-binding","Molecular Function: catalytic activity (GO:0003824); Molecular Function: thiamine pyrophosphate binding (GO:0030976)"]
[null,"IPR009014","CATHGENE3D","G3DSA:3.40.50.920","G3DSA:3.40.50.920",262,416,0.131624,{"v":3.2e-57,"d":"3.20E-57"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR009014","SSF","SSF52922","SSF52922",262,414,0.129915,{"v":8.32e-46,"d":"8.32E-46"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002880","PFAM","PF01855","POR_N",20,250,0.196581,{"v":4.2e-76,"d":"4.20E-76"},"Pyrv_Fd/Flavodoxin_OxRdtase_N","Domain","Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","CATHGENE3D","G3DSA:3.40.920.10","G3DSA:3.40.920.10",418,628,0.179487,{"v":2.9e-90,"d":"2.90E-90"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","SSF","SSF53323","SSF53323",418,669,0.21453,{"v":1.22e-87,"d":"1.22E-87"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","SSF54862","_",675,769,0.0803419,{"v":6.84e-19,"d":"6.84E-19"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",672,786,0.0974359,{"v":5.9e-39,"d":"5.90E-39"},"_","_","_","-"]
[null,"_","_","cd07034","_",28,176,0.126496,{"v":1.24891E-44,"d":"1.25E-44"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",6,261,0.217949,{"v":7.5e-102,"d":"7.50E-102"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",788,1170,0.326496,{"v":5.7e-172,"d":"5.70E-172"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",7,1168,0.992308,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",7,1168,0.992308,0,"_","_","_","-"]
[null,"_","_","cd03377","_",804,1169,0.311966,0,"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12838","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR020617","PFAM","PF02803","Thiolase_C",271,392,0.308673,{"v":4.3e-52,"d":"4.30E-52"},"Thiolase_C","Domain","Thiolase, C-terminal","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020616","PFAM","PF00108","Thiolase_N",4,262,0.658163,{"v":2.8e-108,"d":"2.80E-108"},"Thiolase_N","Domain","Thiolase, N-terminal","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020615","PROSITE","PS00098","THIOLASE_1",84,102,0.0459184,"_","Thiolase_acyl_enz_int_AS","Active_site","Thiolase, acyl-enzyme intermediate active site","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020613","PROSITE","PS00737","THIOLASE_2",339,355,0.0408163,"_","Thiolase_CS","Conserved_site","Thiolase, conserved site","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020610","PROSITE","PS00099","THIOLASE_3",374,387,0.0331633,"_","Thiolase_AS","Active_site","Thiolase, active site","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR016039","CATHGENE3D","G3DSA:3.40.47.10","G3DSA:3.40.47.10",126,390,0.673469,{"v":1.7e-163,"d":"1.70E-163"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","CATHGENE3D","G3DSA:3.40.47.10","G3DSA:3.40.47.10",6,276,0.688776,{"v":1.7e-163,"d":"1.70E-163"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",271,392,0.308673,{"v":2.42e-44,"d":"2.42E-44"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",3,270,0.681122,2.05E-94,"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002155","CDD","cd00751","thiolase",5,392,0.987245,0,"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR002155","PIRSF","PIRSF000429","Ac-CoA_Ac_transf",1,392,0.997449,{"v":3.2e-139,"d":"3.20E-139"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR002155","TIGRFAMs","TIGR01930","AcCoA-C-Actrans",6,391,0.982143,{"v":9.9e-157,"d":"9.90E-157"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"_","_","PTHR18919","_",1,392,0.997449,{"v":1.3E-181,"d":"1.30E-181"},"_","_","_","-"]
[null,"_","_","PTHR18919:SF132","_",1,392,0.997449,{"v":1.3E-181,"d":"1.30E-181"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_13111","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR020617","PFAM","PF02803","Thiolase_C",270,390,0.306905,{"v":2.6e-48,"d":"2.60E-48"},"Thiolase_C","Domain","Thiolase, C-terminal","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020616","PFAM","PF00108","Thiolase_N",4,262,0.659847,{"v":6.8e-84,"d":"6.80E-84"},"Thiolase_N","Domain","Thiolase, N-terminal","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020613","PROSITE","PS00737","THIOLASE_2",338,354,0.0409207,"_","Thiolase_CS","Conserved_site","Thiolase, conserved site","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020610","PROSITE","PS00099","THIOLASE_3",373,386,0.0332481,"_","Thiolase_AS","Active_site","Thiolase, active site","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR016039","CATHGENE3D","G3DSA:3.40.47.10","G3DSA:3.40.47.10",127,389,0.670077,{"v":6.7e-154,"d":"6.70E-154"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","CATHGENE3D","G3DSA:3.40.47.10","G3DSA:3.40.47.10",6,275,0.68798,{"v":6.7e-154,"d":"6.70E-154"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",271,390,0.304348,{"v":4.68e-43,"d":"4.68E-43"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",3,268,0.677749,{"v":6.73e-82,"d":"6.73E-82"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002155","CDD","cd00751","thiolase",5,390,0.984655,0,"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR002155","PIRSF","PIRSF000429","Ac-CoA_Ac_transf",1,391,0.997442,{"v":5.8e-134,"d":"5.80E-134"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR002155","TIGRFAMs","TIGR01930","AcCoA-C-Actrans",6,390,0.982097,{"v":1.2E-144,"d":"1.20E-144"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"_","_","PTHR18919","_",2,390,0.992327,{"v":1.3e-152,"d":"1.30E-152"},"_","_","_","-"]
[null,"_","_","PTHR18919:SF107","_",2,390,0.992327,{"v":1.3e-152,"d":"1.30E-152"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_11283","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR020617","PFAM","PF02803","Thiolase_C",272,368,0.240602,3.8e-10,"Thiolase_C","Domain","Thiolase, C-terminal","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020616","PFAM","PF00108","Thiolase_N",4,233,0.573935,{"v":1.2E-23,"d":"1.20E-23"},"Thiolase_N","Domain","Thiolase, N-terminal","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR016039","CATHGENE3D","G3DSA:3.40.47.10","G3DSA:3.40.47.10",1,396,0.989975,{"v":1.8e-113,"d":"1.80E-113"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",6,384,0.947368,{"v":4.54e-34,"d":"4.54E-34"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002155","PIRSF","PIRSF000429","Ac-CoA_Ac_transf",1,395,0.987469,{"v":2.2e-50,"d":"2.20E-50"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"_","_","PTHR42870","_",1,394,0.984962,{"v":5.5e-120,"d":"5.50E-120"},"_","_","_","-"]
[null,"_","_","PTHR42870:SF6","_",1,394,0.984962,{"v":5.5e-120,"d":"5.50E-120"},"_","_","_","-"]
[null,"_","_","cd00829","_",7,393,0.967419,{"v":1.1105E-133,"d":"1.11E-133"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_11276","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036291","SSF","SSF51735","SSF51735",3,185,0.585209,{"v":9.51e-47,"d":"9.51E-47"},"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR022694","PIRSF","PIRSF000105","HCDH",1,309,0.990354,{"v":2.1e-83,"d":"2.10E-83"},"3-OHacyl-CoA_DH","Family","3-hydroxyacyl-CoA dehydrogenase","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Biological Process: oxidation-reduction process (GO:0055114); Molecular Function: NAD+ binding (GO:0070403)"]
[null,"IPR013328","CATHGENE3D","G3DSA:1.10.1040.10","G3DSA:1.10.1040.10",193,310,0.376206,{"v":2.8E-35,"d":"2.80E-35"},"6PGD_dom2","Homologous_superfamily","6-phosphogluconate dehydrogenase, domain 2","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR008927","SSF","SSF48179","SSF48179",190,288,0.315113,{"v":7.65e-22,"d":"7.65E-22"},"6-PGluconate_DH-like_C_sf","Homologous_superfamily","6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily","Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006180","PROSITE","PS00067","3HCDH",187,211,0.0771704,"_","3-OHacyl-CoA_DH_CS","Conserved_site","3-hydroxyacyl-CoA dehydrogenase, conserved site","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006176","PFAM","PF02737","3HCDH_N",7,187,0.578778,{"v":4.5e-54,"d":"4.50E-54"},"3-OHacyl-CoA_DH_NAD-bd","Domain","3-hydroxyacyl-CoA dehydrogenase, NAD binding","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006108","PFAM","PF00725","3HCDH",190,288,0.315113,{"v":3.5e-22,"d":"3.50E-22"},"3HC_DH_C","Domain","3-hydroxyacyl-CoA dehydrogenase, C-terminal","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","G3DSA:3.40.50.720","_",1,192,0.614148,{"v":4.9e-54,"d":"4.90E-54"},"_","_","_","-"]
[null,"_","_","PTHR43145","_",2,291,0.92926,{"v":3.1e-83,"d":"3.10E-83"},"_","_","_","-"]
[null,"_","_","PTHR43145:SF4","_",2,291,0.92926,{"v":3.1e-83,"d":"3.10E-83"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_13113","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036291","SSF","SSF51735","SSF51735",1,188,0.649306,1.93E-51,"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR022694","PIRSF","PIRSF000105","HCDH",1,288,0.996528,{"v":8.4e-85,"d":"8.40E-85"},"3-OHacyl-CoA_DH","Family","3-hydroxyacyl-CoA dehydrogenase","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Biological Process: oxidation-reduction process (GO:0055114); Molecular Function: NAD+ binding (GO:0070403)"]
[null,"IPR013328","CATHGENE3D","G3DSA:1.10.1040.10","G3DSA:1.10.1040.10",194,288,0.326389,{"v":1.2E-29,"d":"1.20E-29"},"6PGD_dom2","Homologous_superfamily","6-phosphogluconate dehydrogenase, domain 2","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR008927","SSF","SSF48179","SSF48179",191,287,0.333333,4.85E-26,"6-PGluconate_DH-like_C_sf","Homologous_superfamily","6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily","Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006180","PROSITE","PS00067","3HCDH",188,212,0.0833333,"_","3-OHacyl-CoA_DH_CS","Conserved_site","3-hydroxyacyl-CoA dehydrogenase, conserved site","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006176","PFAM","PF02737","3HCDH_N",5,187,0.631944,{"v":1.5e-53,"d":"1.50E-53"},"3-OHacyl-CoA_DH_NAD-bd","Domain","3-hydroxyacyl-CoA dehydrogenase, NAD binding","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006108","PFAM","PF00725","3HCDH",191,287,0.333333,{"v":7.9e-27,"d":"7.90E-27"},"3HC_DH_C","Domain","3-hydroxyacyl-CoA dehydrogenase, C-terminal","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","G3DSA:3.40.50.720","_",1,193,0.666667,{"v":2.2e-60,"d":"2.20E-60"},"_","_","_","-"]
[null,"_","_","PTHR43145","_",2,288,0.993056,{"v":6.4E-89,"d":"6.40E-89"},"_","_","_","-"]
[null,"_","_","PTHR43145:SF4","_",2,288,0.993056,{"v":6.4E-89,"d":"6.40E-89"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_20313","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036291","SSF","SSF51735","SSF51735",1,181,0.638298,1.47E-59,"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR022694","PIRSF","PIRSF000105","HCDH",1,282,0.996454,{"v":2.9E-94,"d":"2.90E-94"},"3-OHacyl-CoA_DH","Family","3-hydroxyacyl-CoA dehydrogenase","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Biological Process: oxidation-reduction process (GO:0055114); Molecular Function: NAD+ binding (GO:0070403)"]
[null,"IPR013328","CATHGENE3D","G3DSA:1.10.1040.10","G3DSA:1.10.1040.10",191,276,0.301418,{"v":1.8E-37,"d":"1.80E-37"},"6PGD_dom2","Homologous_superfamily","6-phosphogluconate dehydrogenase, domain 2","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR008927","SSF","SSF48179","SSF48179",183,281,0.347518,{"v":7.48e-35,"d":"7.48E-35"},"6-PGluconate_DH-like_C_sf","Homologous_superfamily","6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily","Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006180","PROSITE","PS00067","3HCDH",181,205,0.0851064,"_","3-OHacyl-CoA_DH_CS","Conserved_site","3-hydroxyacyl-CoA dehydrogenase, conserved site","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006176","PFAM","PF02737","3HCDH_N",3,181,0.631206,{"v":1.9e-67,"d":"1.90E-67"},"3-OHacyl-CoA_DH_NAD-bd","Domain","3-hydroxyacyl-CoA dehydrogenase, NAD binding","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006108","PFAM","PF00725","3HCDH",184,280,0.340426,{"v":9.4e-37,"d":"9.40E-37"},"3HC_DH_C","Domain","3-hydroxyacyl-CoA dehydrogenase, C-terminal","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","G3DSA:3.40.50.720","_",1,187,0.659574,{"v":3.5E-72,"d":"3.50E-72"},"_","_","_","-"]
[null,"_","_","PTHR43145","_",2,281,0.989362,{"v":1.7E-121,"d":"1.70E-121"},"_","_","_","-"]
[null,"_","_","PTHR43145:SF10","_",2,281,0.989362,{"v":1.7E-121,"d":"1.70E-121"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_13112","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR029045","SSF","SSF52096","SSF52096",2,254,0.988235,{"v":6.88e-80,"d":"6.88E-80"},"ClpP/crotonase-like_dom_sf","Homologous_superfamily","ClpP/crotonase-like domain superfamily","-"]
[null,"IPR018376","PROSITE","PS00166","ENOYL_COA_HYDRATASE",95,115,0.0784314,"_","Enoyl-CoA_hyd/isom_CS","Conserved_site","Enoyl-CoA hydratase/isomerase, conserved site","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR014748","CATHGENE3D","G3DSA:1.10.12.10","G3DSA:1.10.12.10",196,255,0.231373,{"v":2.7e-18,"d":"2.70E-18"},"Enoyl-CoA_hydra_C","Homologous_superfamily","Enoyl-CoA hydratase, C-terminal","-"]
[null,"IPR001753","PFAM","PF00378","ECH_1",12,254,0.94902,{"v":2.9E-68,"d":"2.90E-68"},"Enoyl-CoA_hydra/iso","Family","Enoyl-CoA hydratase/isomerase","Molecular Function: catalytic activity (GO:0003824)"]
[null,"_","_","G3DSA:3.90.226.10","_",1,195,0.760784,{"v":1.4E-66,"d":"1.40E-66"},"_","_","_","-"]
[null,"_","_","cd06558","_",4,193,0.741176,{"v":2.12066e-75,"d":"2.12E-75"},"_","_","_","-"]
[null,"_","_","PTHR11941","_",12,254,0.94902,{"v":5.3E-76,"d":"5.30E-76"},"_","_","_","-"]
[null,"_","_","PTHR11941:SF140","_",12,254,0.94902,{"v":5.3E-76,"d":"5.30E-76"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_11087","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR029045","SSF","SSF52096","SSF52096",1,253,0.992126,{"v":1.71e-63,"d":"1.71E-63"},"ClpP/crotonase-like_dom_sf","Homologous_superfamily","ClpP/crotonase-like domain superfamily","-"]
[null,"IPR001753","PFAM","PF00378","ECH_1",8,253,0.964567,{"v":2.1e-50,"d":"2.10E-50"},"Enoyl-CoA_hydra/iso","Family","Enoyl-CoA hydratase/isomerase","Molecular Function: catalytic activity (GO:0003824)"]
[null,"_","_","PTHR11941","_",4,253,0.980315,{"v":2e-48,"d":"2.00E-48"},"_","_","_","-"]
[null,"_","_","PTHR11941:SF101","_",4,253,0.980315,{"v":2e-48,"d":"2.00E-48"},"_","_","_","-"]
[null,"_","_","cd06558","_",4,193,0.744094,{"v":5.25443E-51,"d":"5.25E-51"},"_","_","_","-"]
[null,"_","_","G3DSA:3.90.226.10","_",1,254,0.996063,{"v":4.9e-62,"d":"4.90E-62"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_20109","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR029069","SSF","SSF54637","SSF54637",2,137,0.978261,{"v":3.07e-34,"d":"3.07E-34"},"HotDog_dom_sf","Homologous_superfamily","HotDog domain superfamily","-"]
[null,"IPR002539","PFAM","PF01575","MaoC_dehydratas",19,114,0.688406,{"v":5.4E-16,"d":"5.40E-16"},"MaoC-like_dom","Domain","MaoC-like dehydratase domain","-"]
[null,"_","_","PTHR43437","_",4,138,0.971014,{"v":7.5e-31,"d":"7.50E-31"},"_","_","_","-"]
[null,"_","_","G3DSA:3.10.129.10","_",1,138,0.992754,{"v":8.5e-37,"d":"8.50E-37"},"_","_","_","-"]
[null,"_","_","cd03449","_",9,135,0.913043,{"v":4.46665e-56,"d":"4.47E-56"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_20308","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR029045","SSF","SSF52096","SSF52096",1,258,0.992278,{"v":2.99e-95,"d":"2.99E-95"},"ClpP/crotonase-like_dom_sf","Homologous_superfamily","ClpP/crotonase-like domain superfamily","-"]
[null,"IPR018376","PROSITE","PS00166","ENOYL_COA_HYDRATASE",100,120,0.0772201,"_","Enoyl-CoA_hyd/isom_CS","Conserved_site","Enoyl-CoA hydratase/isomerase, conserved site","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR014748","CATHGENE3D","G3DSA:1.10.12.10","G3DSA:1.10.12.10",201,259,0.223938,{"v":2.2e-23,"d":"2.20E-23"},"Enoyl-CoA_hydra_C","Homologous_superfamily","Enoyl-CoA hydratase, C-terminal","-"]
[null,"IPR001753","PFAM","PF00378","ECH_1",10,258,0.957529,{"v":1.1E-69,"d":"1.10E-69"},"Enoyl-CoA_hydra/iso","Family","Enoyl-CoA hydratase/isomerase","Molecular Function: catalytic activity (GO:0003824)"]
[null,"_","_","G3DSA:3.90.226.10","_",1,200,0.76834,{"v":1.7E-76,"d":"1.70E-76"},"_","_","_","-"]
[null,"_","_","cd06558","_",6,198,0.741313,{"v":1.67152E-84,"d":"1.67E-84"},"_","_","_","-"]
[null,"_","_","PTHR11941","_",7,259,0.972973,{"v":6.7e-90,"d":"6.70E-90"},"_","_","_","-"]
[null,"_","_","PTHR11941:SF140","_",7,259,0.972973,{"v":6.7e-90,"d":"6.70E-90"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12502","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037069","CATHGENE3D","G3DSA:1.10.540.10","G3DSA:1.10.540.10",1,120,0.187402,{"v":6.3e-43,"d":"6.30E-43"},"AcylCoA_DH/ox_N_sf","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR036250","SSF","SSF47203","SSF47203",227,380,0.240945,{"v":4.67e-57,"d":"4.67E-57"},"AcylCo_DH-like_C","Homologous_superfamily","Acyl-CoA dehydrogenase-like, C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR029035","SSF","SSF52467","SSF52467",436,556,0.188976,1.47E-36,"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR024935","CDD","cd00730","rubredoxin",587,634,0.0740158,{"v":6.21921e-19,"d":"6.22E-19"},"Rubredoxin_dom","Domain","Rubredoxin domain","Molecular Function: iron ion binding (GO:0005506)"]
[null,"IPR024935","PFAM","PF00301","Rubredoxin",587,632,0.0708661,{"v":1.1e-18,"d":"1.10E-18"},"Rubredoxin_dom","Domain","Rubredoxin domain","Molecular Function: iron ion binding (GO:0005506)"]
[null,"IPR024935","PRINTS","PR00163","RUBREDOXIN",616,632,0.0251969,3.3e-08,"Rubredoxin_dom","Domain","Rubredoxin domain","Molecular Function: iron ion binding (GO:0005506)"]
[null,"IPR024935","PRINTS","PR00163","RUBREDOXIN",586,602,0.0251969,3.3e-08,"Rubredoxin_dom","Domain","Rubredoxin domain","Molecular Function: iron ion binding (GO:0005506)"]
[null,"IPR024934","PROFILE","PS50903","RUBREDOXIN_LIKE",584,635,0.080315,12.559,"Rubredoxin-like_dom","Domain","Rubredoxin-like domain","Molecular Function: iron ion binding (GO:0005506)"]
[null,"IPR018527","PROSITE","PS00202","RUBREDOXIN",616,626,0.015748,"_","Rubredoxin_Fe_BS","Binding_site","Rubredoxin, iron-binding site","Molecular Function: metal ion binding (GO:0046872)"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",438,519,0.127559,{"v":1.2e-24,"d":"1.20E-24"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR013786","PFAM","PF02771","Acyl-CoA_dh_N",6,118,0.176378,{"v":2.9e-38,"d":"2.90E-38"},"AcylCoA_DH/ox_N","Domain","Acyl-CoA dehydrogenase/oxidase, N-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR009100","SSF","SSF56645","SSF56645",3,242,0.376378,{"v":3.01e-88,"d":"3.01E-88"},"AcylCoA_DH/oxidase_NM_dom","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR009075","PFAM","PF00441","Acyl-CoA_dh_1",229,377,0.233071,{"v":8.7E-49,"d":"8.70E-49"},"AcylCo_DH/oxidase_C","Domain","Acyl-CoA dehydrogenase/oxidase C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006091","PFAM","PF02770","Acyl-CoA_dh_M",122,217,0.149606,{"v":1.8e-27,"d":"1.80E-27"},"Acyl-CoA_Oxase/DH_cen-dom","Domain","Acyl-CoA oxidase/dehydrogenase, central domain","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00072","ACYL_COA_DH_1",124,136,0.0188976,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","SSF57802","_",583,634,0.080315,{"v":3.87e-17,"d":"3.87E-17"},"_","_","_","-"]
[null,"_","_","G3DSA:2.20.28.10","_",585,634,0.0771654,{"v":8.2e-20,"d":"8.20E-20"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1220","_",434,566,0.207874,{"v":8.1e-43,"d":"8.10E-43"},"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",121,234,0.177953,{"v":3.6e-44,"d":"3.60E-44"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",235,394,0.250394,{"v":2.7e-54,"d":"2.70E-54"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",2,563,0.883465,{"v":1.2e-234,"d":"1.20E-234"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF25","_",2,563,0.883465,{"v":1.2e-234,"d":"1.20E-234"},"_","_","_","-"]
[null,"_","_","cd01158","_",7,377,0.582677,0,"_","_","_","-"]
[]
["CLOSTRIBL3_v1_11587","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037069","CATHGENE3D","G3DSA:1.10.540.10","G3DSA:1.10.540.10",1,119,0.311346,{"v":5.5e-38,"d":"5.50E-38"},"AcylCoA_DH/ox_N_sf","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR036250","SSF","SSF47203","SSF47203",227,378,0.398417,3.06E-56,"AcylCo_DH-like_C","Homologous_superfamily","Acyl-CoA dehydrogenase-like, C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR013786","PFAM","PF02771","Acyl-CoA_dh_N",6,117,0.292876,{"v":6.6e-31,"d":"6.60E-31"},"AcylCoA_DH/ox_N","Domain","Acyl-CoA dehydrogenase/oxidase, N-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR009100","SSF","SSF56645","SSF56645",1,242,0.635884,{"v":9.29e-85,"d":"9.29E-85"},"AcylCoA_DH/oxidase_NM_dom","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR009075","PFAM","PF00441","Acyl-CoA_dh_1",229,374,0.382586,{"v":1.9e-47,"d":"1.90E-47"},"AcylCo_DH/oxidase_C","Domain","Acyl-CoA dehydrogenase/oxidase C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006091","PFAM","PF02770","Acyl-CoA_dh_M",122,217,0.25066,{"v":2.3e-27,"d":"2.30E-27"},"Acyl-CoA_Oxase/DH_cen-dom","Domain","Acyl-CoA oxidase/dehydrogenase, central domain","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00072","ACYL_COA_DH_1",124,136,0.0316623,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PIRSF016578","_",5,97,0.242744,0.0025,"_","_","_","-"]
[null,"_","_","PIRSF016578","_",128,369,0.635884,5.2e-11,"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",121,234,0.298153,{"v":4.4e-45,"d":"4.40E-45"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",235,379,0.379947,{"v":5.2e-52,"d":"5.20E-52"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",2,378,0.992084,{"v":2.3e-145,"d":"2.30E-145"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",2,378,0.992084,{"v":2.3e-145,"d":"2.30E-145"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12012","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037069","CATHGENE3D","G3DSA:1.10.540.10","G3DSA:1.10.540.10",3,117,0.3,{"v":1.2E-26,"d":"1.20E-26"},"AcylCoA_DH/ox_N_sf","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR036250","SSF","SSF47203","SSF47203",227,378,0.397368,{"v":4.03e-57,"d":"4.03E-57"},"AcylCo_DH-like_C","Homologous_superfamily","Acyl-CoA dehydrogenase-like, C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR013786","PFAM","PF02771","Acyl-CoA_dh_N",6,107,0.265789,{"v":1.7e-20,"d":"1.70E-20"},"AcylCoA_DH/ox_N","Domain","Acyl-CoA dehydrogenase/oxidase, N-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR009100","SSF","SSF56645","SSF56645",2,238,0.621053,{"v":9.29e-70,"d":"9.29E-70"},"AcylCoA_DH/oxidase_NM_dom","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR009075","PFAM","PF00441","Acyl-CoA_dh_1",227,372,0.381579,{"v":4.4E-51,"d":"4.40E-51"},"AcylCo_DH/oxidase_C","Domain","Acyl-CoA dehydrogenase/oxidase C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006091","PFAM","PF02770","Acyl-CoA_dh_M",120,215,0.25,{"v":1.1E-23,"d":"1.10E-23"},"Acyl-CoA_Oxase/DH_cen-dom","Domain","Acyl-CoA oxidase/dehydrogenase, central domain","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00072","ACYL_COA_DH_1",122,134,0.0315789,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00073","ACYL_COA_DH_2",334,353,0.05,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PIRSF016578","_",2,375,0.981579,{"v":3.7e-17,"d":"3.70E-17"},"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",119,232,0.297368,{"v":4.1e-41,"d":"4.10E-41"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",233,380,0.386842,{"v":8.8e-57,"d":"8.80E-57"},"_","_","_","-"]
[null,"_","_","PTHR43516","_",2,376,0.984211,{"v":2.5e-124,"d":"2.50E-124"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12013","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037069","CATHGENE3D","G3DSA:1.10.540.10","G3DSA:1.10.540.10",3,115,0.28866,6e-15,"AcylCoA_DH/ox_N_sf","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR036250","SSF","SSF47203","SSF47203",227,381,0.396907,{"v":1.05e-41,"d":"1.05E-41"},"AcylCo_DH-like_C","Homologous_superfamily","Acyl-CoA dehydrogenase-like, C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR013786","PFAM","PF02771","Acyl-CoA_dh_N",8,114,0.273196,8.7e-12,"AcylCoA_DH/ox_N","Domain","Acyl-CoA dehydrogenase/oxidase, N-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR009100","SSF","SSF56645","SSF56645",6,239,0.600515,{"v":4.32e-53,"d":"4.32E-53"},"AcylCoA_DH/oxidase_NM_dom","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR009075","PFAM","PF00441","Acyl-CoA_dh_1",229,380,0.389175,{"v":1e-36,"d":"1.00E-36"},"AcylCo_DH/oxidase_C","Domain","Acyl-CoA dehydrogenase/oxidase C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006091","PFAM","PF02770","Acyl-CoA_dh_M",122,216,0.242268,{"v":1.2E-16,"d":"1.20E-16"},"Acyl-CoA_Oxase/DH_cen-dom","Domain","Acyl-CoA oxidase/dehydrogenase, central domain","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","G3DSA:2.40.110.10","_",121,233,0.28866,{"v":7.1e-30,"d":"7.10E-30"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",234,381,0.378866,{"v":2.4e-40,"d":"2.40E-40"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",7,381,0.963918,{"v":2.2e-86,"d":"2.20E-86"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",7,381,0.963918,{"v":2.2e-86,"d":"2.20E-86"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_20310","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037069","CATHGENE3D","G3DSA:1.10.540.10","G3DSA:1.10.540.10",1,120,0.313984,{"v":2.4e-41,"d":"2.40E-41"},"AcylCoA_DH/ox_N_sf","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR036250","SSF","SSF47203","SSF47203",227,378,0.398417,{"v":8.38e-57,"d":"8.38E-57"},"AcylCo_DH-like_C","Homologous_superfamily","Acyl-CoA dehydrogenase-like, C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR013786","PFAM","PF02771","Acyl-CoA_dh_N",6,118,0.295515,{"v":2.5E-36,"d":"2.50E-36"},"AcylCoA_DH/ox_N","Domain","Acyl-CoA dehydrogenase/oxidase, N-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR009100","SSF","SSF56645","SSF56645",1,242,0.635884,{"v":3.93e-86,"d":"3.93E-86"},"AcylCoA_DH/oxidase_NM_dom","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR009075","PFAM","PF00441","Acyl-CoA_dh_1",229,375,0.385224,{"v":2.8e-50,"d":"2.80E-50"},"AcylCo_DH/oxidase_C","Domain","Acyl-CoA dehydrogenase/oxidase C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006091","PFAM","PF02770","Acyl-CoA_dh_M",122,217,0.25066,{"v":3.2e-27,"d":"3.20E-27"},"Acyl-CoA_Oxase/DH_cen-dom","Domain","Acyl-CoA oxidase/dehydrogenase, central domain","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00072","ACYL_COA_DH_1",124,136,0.0316623,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00073","ACYL_COA_DH_2",336,355,0.0501319,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PIRSF016578","_",4,377,0.984169,{"v":5.3e-26,"d":"5.30E-26"},"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",121,234,0.298153,{"v":2e-44,"d":"2.00E-44"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",235,379,0.379947,{"v":5.1e-53,"d":"5.10E-53"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",2,378,0.992084,{"v":4.3e-157,"d":"4.30E-157"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",2,378,0.992084,{"v":4.3e-157,"d":"4.30E-157"},"_","_","_","-"]
[null,"_","_","cd01158","_",8,379,0.978892,0,"_","_","_","-"]
[]
["CLOSTRIBL3_v1_20311","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033948","CDD","cd01714","ETF_beta",2,202,0.772201,{"v":1.48247E-96,"d":"1.48E-96"},"ETF_beta_N","Domain","Electron transfer flavoprotein, beta subunit, N-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",23,206,0.706564,{"v":2.3E-51,"d":"2.30E-51"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",22,211,0.72973,{"v":4.1e-65,"d":"4.10E-65"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014729","CATHGENE3D","G3DSA:3.40.50.620","G3DSA:3.40.50.620",1,259,0.996139,{"v":1.2e-96,"d":"1.20E-96"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR012255","PANTHER","PTHR21294","PTHR21294",1,258,0.992278,{"v":3.1e-99,"d":"3.10E-99"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"IPR012255","PIRSF","PIRSF000090","Beta-ETF",1,259,0.996139,{"v":5.1e-94,"d":"5.10E-94"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"IPR000049","PROSITE","PS01065","ETF_BETA",155,175,0.0772201,"_","ET-Flavoprotein_bsu_CS","Conserved_site","Electron transfer flavoprotein, beta-subunit, conserved site","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"_","_","SSF52402","_",1,254,0.976834,{"v":2.79e-82,"d":"2.79E-82"},"_","_","_","-"]
[null,"_","_","PTHR21294:SF17","_",1,258,0.992278,{"v":3.1e-99,"d":"3.10E-99"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_20312","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033947","CDD","cd01715","ETF_alpha",8,180,0.516517,{"v":1.32753e-65,"d":"1.33E-65"},"ETF_alpha_N","Domain","Electron transfer flavoprotein, alpha subunit, N-terminal","-"]
[null,"IPR029035","SSF","SSF52467","SSF52467",209,328,0.357357,{"v":3.82e-47,"d":"3.82E-47"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR018206","PROSITE","PS00696","ETF_ALPHA",273,299,0.0780781,"_","ETF_asu_C_CS","Conserved_site","Electron transfer flavoprotein subunit alpha, conserved site","-"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",210,292,0.246246,{"v":1e-36,"d":"1.00E-36"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",9,188,0.537538,{"v":2.9e-53,"d":"2.90E-53"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",9,198,0.567568,{"v":4.9e-65,"d":"4.90E-65"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014729","CATHGENE3D","G3DSA:3.40.50.620","G3DSA:3.40.50.620",5,205,0.600601,{"v":7.5e-83,"d":"7.50E-83"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR001308","PIRSF","PIRSF000089","Electra_flavoP_a",5,333,0.984985,{"v":1.8E-124,"d":"1.80E-124"},"ETF_a/FixB","Family","Electron transfer flavoprotein alpha subunit/FixB","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: flavin adenine dinucleotide binding (GO:0050660)"]
[null,"_","_","G3DSA:3.40.50.1220","_",206,333,0.381381,{"v":4.9E-56,"d":"4.90E-56"},"_","_","_","-"]
[null,"_","_","SSF52402","_",7,202,0.585586,4.81E-62,"_","_","_","-"]
[null,"_","_","PTHR43153","_",1,332,0.993994,{"v":8.8e-149,"d":"8.80E-149"},"_","_","_","-"]
[null,"_","_","PTHR43153:SF9","_",1,332,0.993994,{"v":8.8e-149,"d":"8.80E-149"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_11710","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR023865","PROSITE","PS01075","ACETATE_KINASE_1",5,16,0.0307263,"_","Aliphatic_acid_kinase_CS","Conserved_site","Aliphatic acid kinase, short-chain, conserved site","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR023865","PROSITE","PS01076","ACETATE_KINASE_2",179,196,0.047486,"_","Aliphatic_acid_kinase_CS","Conserved_site","Aliphatic acid kinase, short-chain, conserved site","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR011245","HAMAP","MF_00542","Butyrate_kinase",1,358,0.997207,143.473,"Butyrate_kin","Family","Butyrate kinase","Molecular Function: ATP binding (GO:0005524); Cellular Component: cytoplasm (GO:0005737); Biological Process: phosphorylation (GO:0016310); Molecular Function: butyrate kinase activity (GO:0047761)"]
[null,"IPR011245","PANTHER","PTHR21060:SF3","PTHR21060:SF3",1,356,0.99162,{"v":2.6e-147,"d":"2.60E-147"},"Butyrate_kin","Family","Butyrate kinase","Molecular Function: ATP binding (GO:0005524); Cellular Component: cytoplasm (GO:0005737); Biological Process: phosphorylation (GO:0016310); Molecular Function: butyrate kinase activity (GO:0047761)"]
[null,"IPR011245","PIRSF","PIRSF036458","Butyrate_kin",1,356,0.99162,{"v":2.1E-147,"d":"2.10E-147"},"Butyrate_kin","Family","Butyrate kinase","Molecular Function: ATP binding (GO:0005524); Cellular Component: cytoplasm (GO:0005737); Biological Process: phosphorylation (GO:0016310); Molecular Function: butyrate kinase activity (GO:0047761)"]
[null,"IPR011245","TIGRFAMs","TIGR02707","butyr_kinase",4,353,0.97486,{"v":6.1e-147,"d":"6.10E-147"},"Butyrate_kin","Family","Butyrate kinase","Molecular Function: ATP binding (GO:0005524); Cellular Component: cytoplasm (GO:0005737); Biological Process: phosphorylation (GO:0016310); Molecular Function: butyrate kinase activity (GO:0047761)"]
[null,"IPR000890","PANTHER","PTHR21060","PTHR21060",1,356,0.99162,{"v":2.6e-147,"d":"2.60E-147"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PFAM","PF00871","Acetate_kinase",4,332,0.916201,{"v":3.1e-58,"d":"3.10E-58"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",179,200,0.0586592,{"v":2.3e-16,"d":"2.30E-16"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",5,16,0.0307263,{"v":2.3e-16,"d":"2.30E-16"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",295,311,0.0446927,{"v":2.3e-16,"d":"2.30E-16"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",272,285,0.0363128,{"v":2.3e-16,"d":"2.30E-16"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"_","_","cd00012","_",6,112,0.296089,0.00018417,"_","_","_","-"]
[null,"_","_","SSF53067","_",117,342,0.628492,{"v":1.06e-44,"d":"1.06E-44"},"_","_","_","-"]
[null,"_","_","SSF53067","_",3,173,0.47486,{"v":6.04e-63,"d":"6.04E-63"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",137,330,0.539106,{"v":4.1e-146,"d":"4.10E-146"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",4,355,0.980447,{"v":4.1e-146,"d":"4.10E-146"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_11711","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR012147","PIRSF","PIRSF000428","P_Ac_trans",1,301,0.996678,{"v":1.2E-81,"d":"1.20E-81"},"P_Ac_Bu_trans","Family","Phosphate acetyl/butyryltransferase","Molecular Function: transferase activity, transferring acyl groups (GO:0016746)"]
[null,"IPR002505","PFAM","PF01515","PTA_PTB",82,295,0.707641,{"v":1.2e-43,"d":"1.20E-43"},"PTA_PTB","Domain","Phosphate acetyl/butaryl transferase","Molecular Function: transferase activity, transferring acyl groups (GO:0016746)"]
[null,"_","_","SSF53659","_",18,298,0.930233,{"v":2.8e-58,"d":"2.80E-58"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.718.10","_",4,300,0.983389,{"v":4.8E-101,"d":"4.80E-101"},"_","_","_","-"]
[null,"_","_","PTHR43356","_",3,298,0.980066,{"v":1e-105,"d":"1.00E-105"},"_","_","_","-"]
[null,"_","_","PTHR43356:SF2","_",3,298,0.980066,{"v":1e-105,"d":"1.00E-105"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12016","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR012147","PIRSF","PIRSF000428","P_Ac_trans",3,300,0.99,{"v":9.1e-80,"d":"9.10E-80"},"P_Ac_Bu_trans","Family","Phosphate acetyl/butyryltransferase","Molecular Function: transferase activity, transferring acyl groups (GO:0016746)"]
[null,"IPR002505","PFAM","PF01515","PTA_PTB",64,296,0.773333,{"v":8.8e-49,"d":"8.80E-49"},"PTA_PTB","Domain","Phosphate acetyl/butaryl transferase","Molecular Function: transferase activity, transferring acyl groups (GO:0016746)"]
[null,"_","_","SSF53659","_",8,299,0.97,{"v":1.6E-53,"d":"1.60E-53"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.718.10","_",6,300,0.98,{"v":5.7e-95,"d":"5.70E-95"},"_","_","_","-"]
[null,"_","_","PTHR43356","_",1,298,0.99,{"v":4.8E-102,"d":"4.80E-102"},"_","_","_","-"]
[null,"_","_","PTHR43356:SF2","_",1,298,0.99,{"v":4.8E-102,"d":"4.80E-102"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12308","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR012147","PIRSF","PIRSF000428","P_Ac_trans",1,298,0.996644,{"v":1.2E-85,"d":"1.20E-85"},"P_Ac_Bu_trans","Family","Phosphate acetyl/butyryltransferase","Molecular Function: transferase activity, transferring acyl groups (GO:0016746)"]
[null,"IPR002505","PFAM","PF01515","PTA_PTB",52,293,0.808725,{"v":6.9e-47,"d":"6.90E-47"},"PTA_PTB","Domain","Phosphate acetyl/butaryl transferase","Molecular Function: transferase activity, transferring acyl groups (GO:0016746)"]
[null,"_","_","SSF53659","_",8,296,0.966443,2.88E-61,"_","_","_","-"]
[null,"_","_","G3DSA:3.40.718.10","_",2,298,0.993289,{"v":7E-105,"d":"7.00E-105"},"_","_","_","-"]
[null,"_","_","PTHR43356","_",1,297,0.993289,{"v":4.6e-123,"d":"4.60E-123"},"_","_","_","-"]
[null,"_","_","PTHR43356:SF2","_",1,297,0.993289,{"v":4.6e-123,"d":"4.60E-123"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_20086","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR023865","PROSITE","PS01075","ACETATE_KINASE_1",5,16,0.0304709,"_","Aliphatic_acid_kinase_CS","Conserved_site","Aliphatic acid kinase, short-chain, conserved site","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR011245","HAMAP","MF_00542","Butyrate_kinase",1,361,0.99723,148.568,"Butyrate_kin","Family","Butyrate kinase","Molecular Function: ATP binding (GO:0005524); Cellular Component: cytoplasm (GO:0005737); Biological Process: phosphorylation (GO:0016310); Molecular Function: butyrate kinase activity (GO:0047761)"]
[null,"IPR011245","PANTHER","PTHR21060:SF3","PTHR21060:SF3",1,357,0.98615,{"v":1.6e-156,"d":"1.60E-156"},"Butyrate_kin","Family","Butyrate kinase","Molecular Function: ATP binding (GO:0005524); Cellular Component: cytoplasm (GO:0005737); Biological Process: phosphorylation (GO:0016310); Molecular Function: butyrate kinase activity (GO:0047761)"]
[null,"IPR011245","PIRSF","PIRSF036458","Butyrate_kin",1,355,0.980609,{"v":5.4e-151,"d":"5.40E-151"},"Butyrate_kin","Family","Butyrate kinase","Molecular Function: ATP binding (GO:0005524); Cellular Component: cytoplasm (GO:0005737); Biological Process: phosphorylation (GO:0016310); Molecular Function: butyrate kinase activity (GO:0047761)"]
[null,"IPR011245","TIGRFAMs","TIGR02707","butyr_kinase",5,352,0.961219,{"v":4e-149,"d":"4.00E-149"},"Butyrate_kin","Family","Butyrate kinase","Molecular Function: ATP binding (GO:0005524); Cellular Component: cytoplasm (GO:0005737); Biological Process: phosphorylation (GO:0016310); Molecular Function: butyrate kinase activity (GO:0047761)"]
[null,"IPR000890","PANTHER","PTHR21060","PTHR21060",1,357,0.98615,{"v":1.6e-156,"d":"1.60E-156"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PFAM","PF00871","Acetate_kinase",5,341,0.930748,{"v":7.7e-61,"d":"7.70E-61"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",179,200,0.0581717,{"v":6.4e-18,"d":"6.40E-18"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",273,286,0.0360111,{"v":6.4e-18,"d":"6.40E-18"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",5,16,0.0304709,{"v":6.4e-18,"d":"6.40E-18"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",296,312,0.0443213,{"v":6.4e-18,"d":"6.40E-18"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"_","_","SSF53067","_",145,347,0.559557,{"v":6.02e-46,"d":"6.02E-46"},"_","_","_","-"]
[null,"_","_","SSF53067","_",4,172,0.465374,{"v":6.26e-63,"d":"6.26E-63"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",137,331,0.537396,{"v":1.5e-146,"d":"1.50E-146"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",5,354,0.966759,{"v":1.5e-146,"d":"1.50E-146"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_20087","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR023865","PROSITE","PS01076","ACETATE_KINASE_2",179,196,0.047486,"_","Aliphatic_acid_kinase_CS","Conserved_site","Aliphatic acid kinase, short-chain, conserved site","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR011245","HAMAP","MF_00542","Butyrate_kinase",1,358,0.997207,139.82,"Butyrate_kin","Family","Butyrate kinase","Molecular Function: ATP binding (GO:0005524); Cellular Component: cytoplasm (GO:0005737); Biological Process: phosphorylation (GO:0016310); Molecular Function: butyrate kinase activity (GO:0047761)"]
[null,"IPR011245","PANTHER","PTHR21060:SF3","PTHR21060:SF3",1,355,0.988827,{"v":1.2e-140,"d":"1.20E-140"},"Butyrate_kin","Family","Butyrate kinase","Molecular Function: ATP binding (GO:0005524); Cellular Component: cytoplasm (GO:0005737); Biological Process: phosphorylation (GO:0016310); Molecular Function: butyrate kinase activity (GO:0047761)"]
[null,"IPR011245","PIRSF","PIRSF036458","Butyrate_kin",1,355,0.988827,{"v":8.5e-141,"d":"8.50E-141"},"Butyrate_kin","Family","Butyrate kinase","Molecular Function: ATP binding (GO:0005524); Cellular Component: cytoplasm (GO:0005737); Biological Process: phosphorylation (GO:0016310); Molecular Function: butyrate kinase activity (GO:0047761)"]
[null,"IPR011245","TIGRFAMs","TIGR02707","butyr_kinase",4,351,0.969274,{"v":3.7e-145,"d":"3.70E-145"},"Butyrate_kin","Family","Butyrate kinase","Molecular Function: ATP binding (GO:0005524); Cellular Component: cytoplasm (GO:0005737); Biological Process: phosphorylation (GO:0016310); Molecular Function: butyrate kinase activity (GO:0047761)"]
[null,"IPR000890","PANTHER","PTHR21060","PTHR21060",1,355,0.988827,{"v":1.2e-140,"d":"1.20E-140"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PFAM","PF00871","Acetate_kinase",5,321,0.882682,{"v":5.1e-68,"d":"5.10E-68"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",297,313,0.0446927,{"v":4.6e-18,"d":"4.60E-18"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",5,16,0.0307263,{"v":4.6e-18,"d":"4.60E-18"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",179,200,0.0586592,{"v":4.6e-18,"d":"4.60E-18"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",274,287,0.0363128,{"v":4.6e-18,"d":"4.60E-18"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",149,162,0.0363128,{"v":4.6e-18,"d":"4.60E-18"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"_","_","SSF53067","_",120,340,0.614525,{"v":9.29e-50,"d":"9.29E-50"},"_","_","_","-"]
[null,"_","_","SSF53067","_",3,171,0.469274,{"v":3.56e-59,"d":"3.56E-59"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",4,354,0.977654,{"v":2.5e-135,"d":"2.50E-135"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",137,332,0.544693,{"v":2.5e-135,"d":"2.50E-135"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_13110","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR038460","CATHGENE3D","G3DSA:3.40.1080.20","G3DSA:3.40.1080.20",300,450,0.331858,{"v":1.8e-56,"d":"1.80E-56"},"AcetylCoA_hyd_C_sf","Homologous_superfamily","Acetyl-CoA hydrolase/transferase, C-terminal domain superfamily","-"]
[null,"IPR037171","SSF","SSF100950","SSF100950",9,230,0.488938,{"v":5.33e-31,"d":"5.33E-31"},"NagB/RpiA_transferase-like","Homologous_superfamily","NagB/RpiA transferase-like","-"]
[null,"IPR037171","SSF","SSF100950","SSF100950",198,448,0.553097,1.02E-57,"NagB/RpiA_transferase-like","Homologous_superfamily","NagB/RpiA transferase-like","-"]
[null,"IPR026888","PFAM","PF13336","AcetylCoA_hyd_C",282,438,0.345133,{"v":1.2E-58,"d":"1.20E-58"},"AcetylCoA_hyd_C","Domain","Acetyl-CoA hydrolase/transferase C-terminal domain","-"]
[null,"IPR003702","PFAM","PF02550","AcetylCoA_hydro",9,188,0.396018,{"v":4.5e-17,"d":"4.50E-17"},"ActCoA_hydro","Family","Acetyl-CoA hydrolase/transferase","Molecular Function: catalytic activity (GO:0003824); Biological Process: acetyl-CoA metabolic process (GO:0006084)"]
[null,"_","_","G3DSA:3.30.750.70","_",194,297,0.227876,{"v":1.1e-30,"d":"1.10E-30"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.1080.10","_",2,190,0.415929,{"v":5.7e-49,"d":"5.70E-49"},"_","_","_","-"]
[null,"_","_","PTHR21432","_",11,441,0.951327,{"v":1.6e-103,"d":"1.60E-103"},"_","_","_","-"]
[null,"_","_","PTHR21432:SF19","_",11,441,0.951327,{"v":1.6e-103,"d":"1.60E-103"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_11114","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033947","CDD","cd01715","ETF_alpha",73,243,0.420792,{"v":1.48894E-49,"d":"1.49E-49"},"ETF_alpha_N","Domain","Electron transfer flavoprotein, alpha subunit, N-terminal","-"]
[null,"IPR029035","SSF","SSF52467","SSF52467",275,393,0.292079,{"v":7.77e-44,"d":"7.77E-44"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",275,357,0.20297,{"v":5.4e-32,"d":"5.40E-32"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",76,252,0.435644,{"v":9.4e-40,"d":"9.40E-40"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",74,276,0.5,{"v":2.7e-38,"d":"2.70E-38"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014729","CATHGENE3D","G3DSA:3.40.50.620","G3DSA:3.40.50.620",61,264,0.502475,{"v":2.8E-62,"d":"2.80E-62"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR001308","PIRSF","PIRSF000089","Electra_flavoP_a",71,399,0.811881,{"v":9.3e-99,"d":"9.30E-99"},"ETF_a/FixB","Family","Electron transfer flavoprotein alpha subunit/FixB","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: flavin adenine dinucleotide binding (GO:0050660)"]
[null,"_","_","G3DSA:3.30.70.20","_",3,57,0.133663,1.7E-5,"_","_","_","-"]
[null,"_","_","SSF54862","_",17,58,0.101485,9.28e-06,"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1220","_",268,402,0.331683,{"v":2.3e-50,"d":"2.30E-50"},"_","_","_","-"]
[null,"_","_","SSF52402","_",72,269,0.487624,{"v":5.23e-51,"d":"5.23E-51"},"_","_","_","-"]
[null,"_","_","PTHR43153","_",68,399,0.819307,{"v":5.7e-129,"d":"5.70E-129"},"_","_","_","-"]
[null,"_","_","PTHR43153:SF9","_",68,399,0.819307,{"v":5.7e-129,"d":"5.70E-129"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_11115","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033948","CDD","cd01714","ETF_beta",3,205,0.770992,{"v":4.33633e-85,"d":"4.34E-85"},"ETF_beta_N","Domain","Electron transfer flavoprotein, beta subunit, N-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",22,198,0.671756,{"v":1e-44,"d":"1.00E-44"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",22,213,0.729008,{"v":4.2e-56,"d":"4.20E-56"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014729","CATHGENE3D","G3DSA:3.40.50.620","G3DSA:3.40.50.620",1,261,0.992366,{"v":2.8e-86,"d":"2.80E-86"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR012255","PANTHER","PTHR21294","PTHR21294",1,261,0.992366,{"v":3.9e-86,"d":"3.90E-86"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"IPR012255","PIRSF","PIRSF000090","Beta-ETF",1,262,0.996183,{"v":5e-85,"d":"5.00E-85"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"_","_","SSF52402","_",1,258,0.980916,2.23E-74,"_","_","_","-"]
[null,"_","_","PTHR21294:SF17","_",1,261,0.992366,{"v":3.9e-86,"d":"3.90E-86"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_11486","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036318","SSF","SSF56176","SSF56176",13,227,0.454352,{"v":3.55e-63,"d":"3.55E-63"},"FAD-bd_PCMH-like_sf","Homologous_superfamily","FAD-binding, type PCMH-like superfamily","Molecular Function: flavin adenine dinucleotide binding (GO:0050660)"]
[null,"IPR016171","CATHGENE3D","G3DSA:1.10.45.10","G3DSA:1.10.45.10",430,470,0.0849257,5.7e-09,"Vanillyl_alc_oxidase_C-sub2","Homologous_superfamily","Vanillyl-alcohol oxidase, C-terminal subdomain 2","-"]
[null,"IPR016169","CATHGENE3D","G3DSA:3.30.465.10","G3DSA:3.30.465.10",108,229,0.2569,{"v":1.2E-42,"d":"1.20E-42"},"FAD-bd_PCMH_sub2","Homologous_superfamily","FAD-binding, type PCMH, subdomain 2","-"]
[null,"IPR016167","CATHGENE3D","G3DSA:3.30.43.10","G3DSA:3.30.43.10",2,106,0.220807,{"v":1.6e-26,"d":"1.60E-26"},"FAD-bd_PCMH_sub1","Homologous_superfamily","FAD-binding, type PCMH, subdomain 1","-"]
[null,"IPR016166","PROFILE","PS51387","FAD_PCMH",50,229,0.380042,26.369,"FAD-bd_PCMH","Domain","FAD-binding domain, PCMH-type","Molecular Function: FAD binding (GO:0071949)"]
[null,"IPR016164","SSF","SSF55103","SSF55103",203,469,0.564756,{"v":2.29e-51,"d":"2.29E-51"},"FAD-linked_Oxase-like_C","Homologous_superfamily","FAD-linked oxidase-like, C-terminal","Molecular Function: catalytic activity (GO:0003824); Molecular Function: flavin adenine dinucleotide binding (GO:0050660)"]
[null,"IPR006094","PFAM","PF01565","FAD_binding_4",56,192,0.288747,{"v":6.7E-37,"d":"6.70E-37"},"Oxid_FAD_bind_N","Domain","FAD linked oxidase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR004113","PFAM","PF02913","FAD-oxidase_C",230,468,0.505308,{"v":1.7E-49,"d":"1.70E-49"},"FAD-linked_oxidase_C","Domain","FAD-linked oxidase, C-terminal","Molecular Function: catalytic activity (GO:0003824); Molecular Function: flavin adenine dinucleotide binding (GO:0050660)"]
[null,"_","_","G3DSA:3.30.70.2740","_",351,429,0.165605,3.9E-13,"_","_","_","-"]
[null,"_","_","PTHR42934","_",11,470,0.974522,{"v":3.8e-116,"d":"3.80E-116"},"_","_","_","-"]
[null,"_","_","PTHR42934:SF2","_",11,470,0.974522,{"v":3.8e-116,"d":"3.80E-116"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_11487","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033947","CDD","cd01715","ETF_alpha",7,182,0.533537,{"v":3.21436e-43,"d":"3.21E-43"},"ETF_alpha_N","Domain","Electron transfer flavoprotein, alpha subunit, N-terminal","-"]
[null,"IPR029035","SSF","SSF52467","SSF52467",202,321,0.362805,{"v":2.07e-46,"d":"2.07E-46"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",202,285,0.253049,{"v":2.6e-33,"d":"2.60E-33"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",9,183,0.530488,{"v":5.2E-42,"d":"5.20E-42"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",8,194,0.567073,{"v":2.3e-48,"d":"2.30E-48"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014729","CATHGENE3D","G3DSA:3.40.50.620","G3DSA:3.40.50.620",1,197,0.597561,{"v":2e-60,"d":"2.00E-60"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR001308","PIRSF","PIRSF000089","Electra_flavoP_a",4,327,0.984756,{"v":1.7E-108,"d":"1.70E-108"},"ETF_a/FixB","Family","Electron transfer flavoprotein alpha subunit/FixB","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: flavin adenine dinucleotide binding (GO:0050660)"]
[null,"_","_","SSF52402","_",6,194,0.573171,{"v":9.07e-48,"d":"9.07E-48"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1220","_",198,324,0.384146,{"v":1.8E-51,"d":"1.80E-51"},"_","_","_","-"]
[null,"_","_","PTHR43153","_",1,326,0.990854,{"v":6.5e-120,"d":"6.50E-120"},"_","_","_","-"]
[null,"_","_","PTHR43153:SF9","_",1,326,0.990854,{"v":6.5e-120,"d":"6.50E-120"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_11488","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033948","CDD","cd01714","ETF_beta",2,205,0.766038,{"v":6.36908e-77,"d":"6.37E-77"},"ETF_beta_N","Domain","Electron transfer flavoprotein, beta subunit, N-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",23,208,0.698113,{"v":1.5e-45,"d":"1.50E-45"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",22,213,0.720755,{"v":4.3e-55,"d":"4.30E-55"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014729","CATHGENE3D","G3DSA:3.40.50.620","G3DSA:3.40.50.620",1,265,0.996226,{"v":1.4E-87,"d":"1.40E-87"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR012255","PANTHER","PTHR21294","PTHR21294",1,264,0.992453,{"v":3.3e-76,"d":"3.30E-76"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"IPR012255","PIRSF","PIRSF000090","Beta-ETF",1,265,0.996226,{"v":7.7e-80,"d":"7.70E-80"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"_","_","SSF52402","_",1,258,0.969811,{"v":7.67e-71,"d":"7.67E-71"},"_","_","_","-"]
[null,"_","_","PTHR21294:SF17","_",1,264,0.992453,{"v":3.3e-76,"d":"3.30E-76"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12010","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033947","CDD","cd01715","ETF_alpha",9,177,0.5,{"v":2.82114e-43,"d":"2.82E-43"},"ETF_alpha_N","Domain","Electron transfer flavoprotein, alpha subunit, N-terminal","-"]
[null,"IPR029035","SSF","SSF52467","SSF52467",210,329,0.354167,{"v":3E-49,"d":"3.00E-49"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",210,293,0.247024,{"v":8e-38,"d":"8.00E-38"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",10,178,0.5,{"v":2.3e-33,"d":"2.30E-33"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",9,198,0.5625,{"v":2e-27,"d":"2.00E-27"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014729","CATHGENE3D","G3DSA:3.40.50.620","G3DSA:3.40.50.620",5,205,0.595238,{"v":1.4e-61,"d":"1.40E-61"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR001308","PIRSF","PIRSF000089","Electra_flavoP_a",5,335,0.982143,{"v":2.5e-118,"d":"2.50E-118"},"ETF_a/FixB","Family","Electron transfer flavoprotein alpha subunit/FixB","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: flavin adenine dinucleotide binding (GO:0050660)"]
[null,"_","_","SSF52402","_",7,199,0.571429,{"v":6.63e-45,"d":"6.63E-45"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1220","_",206,336,0.386905,{"v":1.1e-59,"d":"1.10E-59"},"_","_","_","-"]
[null,"_","_","PTHR43153","_",1,334,0.991071,{"v":1.1E-132,"d":"1.10E-132"},"_","_","_","-"]
[null,"_","_","PTHR43153:SF9","_",1,334,0.991071,{"v":1.1E-132,"d":"1.10E-132"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12011","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033948","CDD","cd01714","ETF_beta",2,203,0.767176,{"v":4.48687e-92,"d":"4.49E-92"},"ETF_beta_N","Domain","Electron transfer flavoprotein, beta subunit, N-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",24,207,0.698473,{"v":2.4e-49,"d":"2.40E-49"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",22,212,0.725191,{"v":2.6e-55,"d":"2.60E-55"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014729","CATHGENE3D","G3DSA:3.40.50.620","G3DSA:3.40.50.620",1,262,0.996183,{"v":1e-95,"d":"1.00E-95"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR012255","PANTHER","PTHR21294","PTHR21294",1,260,0.98855,{"v":2.9E-94,"d":"2.90E-94"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"IPR012255","PIRSF","PIRSF000090","Beta-ETF",1,262,0.996183,{"v":8.2e-89,"d":"8.20E-89"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"_","_","SSF52402","_",1,256,0.973282,1.05E-76,"_","_","_","-"]
[null,"_","_","PTHR21294:SF17","_",1,260,0.98855,{"v":2.9E-94,"d":"2.90E-94"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_20124","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033948","CDD","cd01714","ETF_beta",2,205,0.766038,{"v":3.67521e-85,"d":"3.68E-85"},"ETF_beta_N","Domain","Electron transfer flavoprotein, beta subunit, N-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",23,208,0.698113,{"v":1.2E-47,"d":"1.20E-47"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",22,213,0.720755,{"v":3.1e-57,"d":"3.10E-57"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014729","CATHGENE3D","G3DSA:3.40.50.620","G3DSA:3.40.50.620",1,265,0.996226,{"v":4.9E-89,"d":"4.90E-89"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR012255","PANTHER","PTHR21294","PTHR21294",1,252,0.94717,{"v":9.7e-91,"d":"9.70E-91"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"IPR012255","PIRSF","PIRSF000090","Beta-ETF",1,265,0.996226,{"v":5e-83,"d":"5.00E-83"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"_","_","SSF52402","_",1,259,0.973585,{"v":1.05e-72,"d":"1.05E-72"},"_","_","_","-"]
[null,"_","_","PTHR21294:SF17","_",1,252,0.94717,{"v":9.7e-91,"d":"9.70E-91"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_20125","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033947","CDD","cd01715","ETF_alpha",3,174,0.513514,{"v":2.41665e-50,"d":"2.42E-50"},"ETF_alpha_N","Domain","Electron transfer flavoprotein, alpha subunit, N-terminal","-"]
[null,"IPR029035","SSF","SSF52467","SSF52467",205,323,0.354354,{"v":2.24e-44,"d":"2.24E-44"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR018206","PROSITE","PS00696","ETF_ALPHA",269,295,0.0780781,"_","ETF_asu_C_CS","Conserved_site","Electron transfer flavoprotein subunit alpha, conserved site","-"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",207,288,0.243243,{"v":2.7e-34,"d":"2.70E-34"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",5,182,0.531532,{"v":1.4e-43,"d":"1.40E-43"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",4,193,0.567568,{"v":6e-43,"d":"6.00E-43"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014729","CATHGENE3D","G3DSA:3.40.50.620","G3DSA:3.40.50.620",1,202,0.603604,{"v":7.4E-64,"d":"7.40E-64"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR001308","PIRSF","PIRSF000089","Electra_flavoP_a",1,330,0.987988,{"v":1.4e-107,"d":"1.40E-107"},"ETF_a/FixB","Family","Electron transfer flavoprotein alpha subunit/FixB","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: flavin adenine dinucleotide binding (GO:0050660)"]
[null,"_","_","SSF52402","_",3,194,0.573574,{"v":1.19e-49,"d":"1.19E-49"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1220","_",203,333,0.39039,{"v":4.1e-54,"d":"4.10E-54"},"_","_","_","-"]
[null,"_","_","PTHR43153","_",2,330,0.984985,{"v":3.1e-121,"d":"3.10E-121"},"_","_","_","-"]
[null,"_","_","PTHR43153:SF9","_",2,330,0.984985,{"v":3.1e-121,"d":"3.10E-121"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_10629","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037225","CATHGENE3D","G3DSA:3.40.50.11540","G3DSA:3.40.50.11540",133,281,0.323851,1.9e-10,"Nuo51_FMN-bd_sf","Homologous_superfamily","NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily","-"]
[null,"IPR037225","SSF","SSF142019","SSF142019",85,292,0.452954,{"v":9.15e-61,"d":"9.15E-61"},"Nuo51_FMN-bd_sf","Homologous_superfamily","NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily","-"]
[null,"IPR026902","PFAM","PF13375","RnfC_N",4,102,0.214442,{"v":2.8E-38,"d":"2.80E-38"},"RnfC_N","Domain","RnfC Barrel sandwich hybrid domain","-"]
[null,"IPR019554","PFAM","PF10531","SLBB",286,333,0.102845,9.1e-14,"Soluble_ligand-bd","Domain","Soluble ligand binding domain","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",405,416,0.02407,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF13237","Fer4_10",363,416,0.115974,7.2E-9,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",353,386,0.0722101,8.029,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",396,427,0.0678337,7.928,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011538","PFAM","PF01512","Complex1_51K",128,272,0.315098,{"v":3.1e-52,"d":"3.10E-52"},"Nuo51_FMN-bd","Domain","NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain","-"]
[null,"IPR010208","HAMAP","MF_00461","RsxC_RnfC",1,457,0.997812,157.308,"Ion_transpt_RnfC/RsxC","Family","Ion-translocating oxidoreductase complex, subunit RnfC/RsxC","Molecular Function: electron transfer activity (GO:0009055); Cellular Component: membrane (GO:0016020); Molecular Function: 4 iron, 4 sulfur cluster binding (GO:0051539)"]
[null,"IPR010208","PANTHER","PTHR43034","PTHR43034",2,455,0.991247,{"v":5.3e-165,"d":"5.30E-165"},"Ion_transpt_RnfC/RsxC","Family","Ion-translocating oxidoreductase complex, subunit RnfC/RsxC","Molecular Function: electron transfer activity (GO:0009055); Cellular Component: membrane (GO:0016020); Molecular Function: 4 iron, 4 sulfur cluster binding (GO:0051539)"]
[null,"IPR010208","TIGRFAMs","TIGR01945","rnfC",3,431,0.936543,{"v":6.3e-177,"d":"6.30E-177"},"Ion_transpt_RnfC/RsxC","Family","Ion-translocating oxidoreductase complex, subunit RnfC/RsxC","Molecular Function: electron transfer activity (GO:0009055); Cellular Component: membrane (GO:0016020); Molecular Function: 4 iron, 4 sulfur cluster binding (GO:0051539)"]
[null,"IPR009051","SSF","SSF46548","SSF46548",323,434,0.242888,{"v":2.27e-19,"d":"2.27E-19"},"Helical_ferredxn","Homologous_superfamily","Alpha-helical ferredoxin","Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"_","_","G3DSA:3.10.20.600","_",283,361,0.170678,3.5e-05,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",362,420,0.126915,3e-08,"_","_","_","-"]
[null,"_","_","Coil","_",431,457,0.0568928,"_","_","_","_","-"]
[]
["CLOSTRIBL3_v1_10630","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR011303","HAMAP","MF_00462","RsxD_RnfD",11,330,0.963746,24.1,"RnfD","Family","Ion-translocating oxidoreductase complex Rnf, subunit D","Cellular Component: integral component of membrane (GO:0016021); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR011303","PANTHER","PTHR30578:SF0","PTHR30578:SF0",11,330,0.963746,{"v":1.9e-102,"d":"1.90E-102"},"RnfD","Family","Ion-translocating oxidoreductase complex Rnf, subunit D","Cellular Component: integral component of membrane (GO:0016021); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR011303","TIGRFAMs","TIGR01946","rnfD",16,328,0.942598,{"v":1.5E-98,"d":"1.50E-98"},"RnfD","Family","Ion-translocating oxidoreductase complex Rnf, subunit D","Cellular Component: integral component of membrane (GO:0016021); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR004338","PANTHER","PTHR30578","PTHR30578",11,330,0.963746,{"v":1.9e-102,"d":"1.90E-102"},"NqrB/RnfD","Family","Ion-translocating oxidoreductase NqrB/RnfD","Cellular Component: membrane (GO:0016020); Biological Process: transmembrane transport (GO:0055085)"]
[null,"IPR004338","PFAM","PF03116","NQR2_RnfD_RnfE",13,328,0.951662,{"v":9e-112,"d":"9.00E-112"},"NqrB/RnfD","Family","Ion-translocating oxidoreductase NqrB/RnfD","Cellular Component: membrane (GO:0016020); Biological Process: transmembrane transport (GO:0055085)"]
[]
["CLOSTRIBL3_v1_10631","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR010209","HAMAP","MF_00479","RsxG_RnfG",7,180,0.935135,22.289,"Ion_transpt_RnfG/RsxG","Family","Ion-translocating oxidoreductase complex, subunit RnfG/RsxG","Cellular Component: plasma membrane (GO:0005886); Molecular Function: electron transfer activity (GO:0009055); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR010209","PANTHER","PTHR36118","PTHR36118",15,179,0.886486,{"v":5.5e-41,"d":"5.50E-41"},"Ion_transpt_RnfG/RsxG","Family","Ion-translocating oxidoreductase complex, subunit RnfG/RsxG","Cellular Component: plasma membrane (GO:0005886); Molecular Function: electron transfer activity (GO:0009055); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR010209","PIRSF","PIRSF006091","E_trnsport_RnfG",1,183,0.983784,{"v":2.9e-35,"d":"2.90E-35"},"Ion_transpt_RnfG/RsxG","Family","Ion-translocating oxidoreductase complex, subunit RnfG/RsxG","Cellular Component: plasma membrane (GO:0005886); Molecular Function: electron transfer activity (GO:0009055); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR010209","TIGRFAMs","TIGR01947","rnfG",17,178,0.87027,{"v":1.6e-35,"d":"1.60E-35"},"Ion_transpt_RnfG/RsxG","Family","Ion-translocating oxidoreductase complex, subunit RnfG/RsxG","Cellular Component: plasma membrane (GO:0005886); Molecular Function: electron transfer activity (GO:0009055); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR007329","PFAM","PF04205","FMN_bind",90,175,0.459459,{"v":6.1e-21,"d":"6.10E-21"},"FMN-bd","Domain","FMN-binding","Molecular Function: FMN binding (GO:0010181); Cellular Component: membrane (GO:0016020)"]
[null,"IPR007329","SMART","SM00900","FMN_bind",90,178,0.475676,{"v":1E-26,"d":"1.00E-26"},"FMN-bd","Domain","FMN-binding","Molecular Function: FMN binding (GO:0010181); Cellular Component: membrane (GO:0016020)"]
[]
["CLOSTRIBL3_v1_10632","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR010968","HAMAP","MF_00478","RsxE_RnfE",1,196,0.919811,24.025,"RnfE","Family","Ion-translocating oxidoreductase complex subunit E","Cellular Component: membrane (GO:0016020); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR010968","TIGRFAMs","TIGR01948","rnfE",5,194,0.891509,{"v":6.6e-67,"d":"6.60E-67"},"RnfE","Family","Ion-translocating oxidoreductase complex subunit E","Cellular Component: membrane (GO:0016020); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR003667","PFAM","PF02508","Rnf-Nqr",4,185,0.853774,{"v":1.7e-57,"d":"1.70E-57"},"NqrDE/RnfAE","Family","NqrDE/RnfAE","Cellular Component: membrane (GO:0016020)"]
[null,"IPR003667","PIRSF","PIRSF006102","NQR_DE",1,204,0.957547,{"v":1.5e-67,"d":"1.50E-67"},"NqrDE/RnfAE","Family","NqrDE/RnfAE","Cellular Component: membrane (GO:0016020)"]
[null,"_","_","PTHR30586","_",3,197,0.915094,{"v":4.7E-67,"d":"4.70E-67"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_10633","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR011293","HAMAP","MF_00459","RsxA_RnfA",2,191,0.979275,23.718,"Ion_transpt_RnfA/RsxA","Family","Ion-translocating oxidoreductase complex, subunit  RnfA/RsxA","Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR011293","TIGRFAMs","TIGR01943","rnfA",4,191,0.968912,{"v":3.4E-70,"d":"3.40E-70"},"Ion_transpt_RnfA/RsxA","Family","Ion-translocating oxidoreductase complex, subunit  RnfA/RsxA","Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR003667","PFAM","PF02508","Rnf-Nqr",4,191,0.968912,{"v":9.1e-52,"d":"9.10E-52"},"NqrDE/RnfAE","Family","NqrDE/RnfAE","Cellular Component: membrane (GO:0016020)"]
[null,"IPR003667","PIRSF","PIRSF006102","NQR_DE",1,193,0.994819,{"v":2.7e-48,"d":"2.70E-48"},"NqrDE/RnfAE","Family","NqrDE/RnfAE","Cellular Component: membrane (GO:0016020)"]
[null,"_","_","PTHR30335","_",1,192,0.989637,{"v":1.8e-71,"d":"1.80E-71"},"_","_","_","-"]
[null,"_","_","PTHR30335:SF0","_",1,192,0.989637,{"v":1.8e-71,"d":"1.80E-71"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_10634","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",173,184,0.0383275,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",218,229,0.0383275,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF13237","Fer4_10",166,229,0.219512,2.5e-08,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",164,193,0.101045,11.079,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",208,238,0.10453,8.827,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",134,163,0.101045,8.029,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",239,272,0.114983,7.517,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR013283","PRINTS","PR01868","ABCEFAMILY",178,193,0.0522648,1.6e-05,"RLI1","Family","RLI1","-"]
[null,"IPR013283","PRINTS","PR01868","ABCEFAMILY",215,239,0.0836237,1.6e-05,"RLI1","Family","RLI1","-"]
[null,"IPR011005","CATHGENE3D","G3DSA:3.20.20.20","G3DSA:3.20.20.20",37,127,0.313589,1.8e-08,"Dihydropteroate_synth-like","Homologous_superfamily","Dihydropteroate synthase-like","Biological Process: cellular metabolic process (GO:0044237)"]
[null,"IPR010207","HAMAP","MF_00463","RsxB_RnfB",5,195,0.662021,28.468,"Elect_transpt_cplx_RnfB/RsxB","Family","Ion-translocating oxidoreductase complex, RnfB/RsxB","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"IPR010207","TIGRFAMs","TIGR01944","rnfB",4,95,0.317073,{"v":1.1E-23,"d":"1.10E-23"},"Elect_transpt_cplx_RnfB/RsxB","Family","Ion-translocating oxidoreductase complex, RnfB/RsxB","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"IPR007202","PFAM","PF04060","FeS",45,78,0.114983,9.3e-12,"4Fe-4S_dom","Domain","4Fe-4S domain","Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"IPR007202","PROFILE","PS51656","4FE4S",33,93,0.209059,25.221,"4Fe-4S_dom","Domain","4Fe-4S domain","Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"_","_","G3DSA:3.30.70.20","_",215,268,0.184669,7.2e-07,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",137,195,0.202091,7.6e-15,"_","_","_","-"]
[null,"_","_","SSF54862","_",135,268,0.463415,{"v":8.03e-19,"d":"8.03E-19"},"_","_","_","-"]
[null,"_","_","cd10549","_",136,267,0.456446,{"v":1.11917E-24,"d":"1.12E-24"},"_","_","_","-"]
[null,"_","_","PTHR43560","_",3,265,0.912892,{"v":6e-53,"d":"6.00E-53"},"_","_","_","-"]
[]
[]
["CLOSTRIBL3_v1_10096","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",91,102,0.0585106,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF12798","Fer4_3",144,164,0.106383,0.13,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PFAM","PF12800","Fer4_4",10,23,0.0691489,0.0077,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PFAM","PF13247","Fer4_11",56,110,0.287234,3.5e-09,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",82,111,0.154255,10.801,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",4,33,0.154255,7.618,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",137,170,0.175532,7.525,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",50,81,0.164894,6.71,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"_","_","G3DSA:3.30.70.20","_",1,83,0.43617,1.4E-11,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",84,186,0.542553,2.3e-15,"_","_","_","-"]
[null,"_","_","SSF54862","_",1,182,0.962766,{"v":4.6e-42,"d":"4.60E-42"},"_","_","_","-"]
[null,"_","_","PTHR42859","_",3,171,0.893617,{"v":9.5e-46,"d":"9.50E-46"},"_","_","_","-"]
[null,"_","_","PTHR42859:SF8","_",3,171,0.893617,{"v":9.5e-46,"d":"9.50E-46"},"_","_","_","-"]
[null,"_","_","cd10554","_",5,168,0.867021,{"v":3.90717e-68,"d":"3.91E-68"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_10095","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036991","CATHGENE3D","G3DSA:4.10.260.20","G3DSA:4.10.260.20",400,462,0.134199,{"v":8e-20,"d":"8.00E-20"},"Fe_hydrogenase_ssu_sf","Homologous_superfamily","Iron hydrogenase, small subunit superfamily","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",15,26,0.0238095,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF00037","Fer4",9,31,0.047619,8.3e-09,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",6,35,0.0627706,11.28,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",36,64,0.0606061,8.122,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR013352","TIGRFAMs","TIGR02512","FeFe_hydrog_A",85,395,0.670996,{"v":3.7e-131,"d":"3.70E-131"},"Fe_hydrogenase_subset","Domain","Iron hydrogenase, subset","Molecular Function: iron ion binding (GO:0005506); Molecular Function: ferredoxin hydrogenase activity (GO:0008901); Molecular Function: iron-sulfur cluster binding (GO:0051536); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR009016","SSF","SSF53920","SSF53920",44,456,0.891775,{"v":4.97e-130,"d":"4.97E-130"},"Fe_hydrogenase","Homologous_superfamily","Iron hydrogenase","-"]
[null,"IPR004108","PFAM","PF02906","Fe_hyd_lg_C",110,391,0.608225,{"v":4E-95,"d":"4.00E-95"},"Fe_hydrogenase_lsu_C","Domain","Iron hydrogenase, large subunit, C-terminal","-"]
[null,"IPR003149","PFAM","PF02256","Fe_hyd_SSU",406,458,0.112554,{"v":8.4e-22,"d":"8.40E-22"},"Fe_hydrogenase_ssu","Domain","Iron hydrogenase, small subunit","-"]
[null,"IPR003149","SMART","SM00902","Fe_hyd_SSU",400,459,0.127706,{"v":1.5E-24,"d":"1.50E-24"},"Fe_hydrogenase_ssu","Domain","Iron hydrogenase, small subunit","-"]
[null,"_","_","G3DSA:3.30.70.20","_",7,65,0.125541,6.7e-14,"_","_","_","-"]
[null,"_","_","SSF54862","_",5,56,0.11039,{"v":6.78e-16,"d":"6.78E-16"},"_","_","_","-"]
[null,"_","_","PTHR11615","_",84,459,0.811688,{"v":3.8e-93,"d":"3.80E-93"},"_","_","_","-"]
[null,"_","_","PTHR11615:SF124","_",84,459,0.811688,{"v":3.8e-93,"d":"3.80E-93"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1780","_",91,394,0.655844,{"v":4.4e-130,"d":"4.40E-130"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.950.10","_",156,385,0.495671,{"v":4.4e-130,"d":"4.40E-130"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_10094","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",96,107,0.0594595,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF12837","Fer4_6",8,28,0.108108,6e-06,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PFAM","PF13247","Fer4_11",60,111,0.275676,1.1e-08,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",87,116,0.156757,10.541,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",7,36,0.156757,9.239,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",56,86,0.162162,6.903,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",128,163,0.189189,6.786,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"_","_","G3DSA:3.30.70.20","_",1,41,0.216216,5.5e-06,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",50,182,0.713513,{"v":4.8e-24,"d":"4.80E-24"},"_","_","_","-"]
[null,"_","_","PTHR42859","_",6,170,0.886486,{"v":5.7e-37,"d":"5.70E-37"},"_","_","_","-"]
[null,"_","_","PTHR42859:SF4","_",6,170,0.886486,{"v":5.7e-37,"d":"5.70E-37"},"_","_","_","-"]
[null,"_","_","SSF54862","_",1,164,0.881081,{"v":2.72e-42,"d":"2.72E-42"},"_","_","_","-"]
[null,"_","_","cd10554","_",8,161,0.827027,{"v":9.55588e-61,"d":"9.56E-61"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_10091","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR042128","CDD","cd03064","TRX_Fd_NuoE",82,159,0.472393,{"v":1.23204e-36,"d":"1.23E-36"},"NuoE_dom","Domain","NuoE domain","-"]
[null,"IPR041921","CATHGENE3D","G3DSA:1.10.10.1590","G3DSA:1.10.10.1590",11,76,0.398773,8.6e-12,"NuoE_N","Homologous_superfamily","NADH-quinone oxidoreductase subunit E, N-terminal","-"]
[null,"IPR036249","SSF","SSF52833","SSF52833",17,163,0.895706,{"v":4.03e-47,"d":"4.03E-47"},"Thioredoxin-like_sf","Homologous_superfamily","Thioredoxin-like superfamily","-"]
[null,"IPR002023","PIRSF","PIRSF000216","NADH_DH_24kDa",7,163,0.957055,{"v":1.4E-49,"d":"1.40E-49"},"NuoE-like","Family","NADH-quinone oxidoreductase subunit E-like","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","G3DSA:3.40.30.10","_",77,159,0.503067,{"v":1.1E-31,"d":"1.10E-31"},"_","_","_","-"]
[null,"_","_","PF01257","_",18,159,0.865031,{"v":1.1e-50,"d":"1.10E-50"},"_","_","_","-"]
[null,"_","_","PTHR43342","_",16,162,0.895706,{"v":5.2e-57,"d":"5.20E-57"},"_","_","_","-"]
[null,"_","_","PTHR43342:SF1","_",16,162,0.895706,{"v":5.2e-57,"d":"5.20E-57"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_10092","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037225","CATHGENE3D","G3DSA:3.40.50.11540","G3DSA:3.40.50.11540",165,343,0.297162,{"v":2.9e-76,"d":"2.90E-76"},"Nuo51_FMN-bd_sf","Homologous_superfamily","NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily","-"]
[null,"IPR037225","SSF","SSF142019","SSF142019",113,348,0.392321,{"v":8.63e-86,"d":"8.63E-86"},"Nuo51_FMN-bd_sf","Homologous_superfamily","NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily","-"]
[null,"IPR037207","CATHGENE3D","G3DSA:1.20.1440.230","G3DSA:1.20.1440.230",440,541,0.168614,{"v":2.7e-33,"d":"2.70E-33"},"Nuop51_4Fe4S-bd_sf","Homologous_superfamily","NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain superfamily","-"]
[null,"IPR037207","SSF","SSF140490","SSF140490",439,540,0.168614,1.44E-36,"Nuop51_4Fe4S-bd_sf","Homologous_superfamily","NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain superfamily","-"]
[null,"IPR036249","SSF","SSF52833","SSF52833",4,99,0.158598,{"v":5.48e-19,"d":"5.48E-19"},"Thioredoxin-like_sf","Homologous_superfamily","Thioredoxin-like superfamily","-"]
[null,"IPR019575","PFAM","PF10589","NADH_4Fe-4S",443,527,0.140234,{"v":1.6e-30,"d":"1.60E-30"},"Nuop51_4Fe4S-bd","Domain","NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain","Molecular Function: 4 iron, 4 sulfur cluster binding (GO:0051539)"]
[null,"IPR019575","SMART","SM00928","NADH_4Fe-4S",442,487,0.0751252,{"v":6.4e-23,"d":"6.40E-23"},"Nuop51_4Fe4S-bd","Domain","NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain","Molecular Function: 4 iron, 4 sulfur cluster binding (GO:0051539)"]
[null,"IPR019554","PFAM","PF10531","SLBB",356,405,0.081803,1e-09,"Soluble_ligand-bd","Domain","Soluble ligand binding domain","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",551,562,0.0183639,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF00037","Fer4",575,596,0.0350584,1.4E-5,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",542,571,0.048414,9.793,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",572,599,0.0450751,9.424,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011538","PFAM","PF01512","Complex1_51K",160,331,0.285476,{"v":2.8e-46,"d":"2.80E-46"},"Nuo51_FMN-bd","Domain","NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain","-"]
[null,"IPR001949","PROSITE","PS00645","COMPLEX1_51K_2",455,466,0.0183639,"_","NADH-UbQ_OxRdtase_51kDa_CS","Conserved_site","NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site","Molecular Function: NADH dehydrogenase (ubiquinone) activity (GO:0008137); Molecular Function: FMN binding (GO:0010181); Molecular Function: 4 iron, 4 sulfur cluster binding (GO:0051539); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PF01257","_",4,81,0.128548,1.2e-06,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",546,596,0.0834725,4.6e-11,"_","_","_","-"]
[null,"_","_","SSF54862","_",538,597,0.0984975,1.05E-12,"_","_","_","-"]
[null,"_","_","cd02980","_",5,83,0.130217,2.07278e-14,"_","_","_","-"]
[null,"_","_","G3DSA:3.40.30.10","_",3,101,0.163606,{"v":6.8E-21,"d":"6.80E-21"},"_","_","_","-"]
[null,"_","_","SSF142984","_",354,437,0.138564,{"v":1.7e-26,"d":"1.70E-26"},"_","_","_","-"]
[null,"_","_","G3DSA:3.10.20.600","_",344,439,0.158598,{"v":1.9e-34,"d":"1.90E-34"},"_","_","_","-"]
[null,"_","_","PTHR43578","_",5,534,0.883139,{"v":1.4E-213,"d":"1.40E-213"},"_","_","_","-"]
[null,"_","_","Coil","_",17,37,0.033389,"_","_","_","_","-"]
[null,"_","_","Coil","_",238,258,0.033389,"_","_","_","_","-"]
[]
["CLOSTRIBL3_v1_10093","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036010","SSF","SSF54292","SSF54292",2,105,0.410359,{"v":7.73e-22,"d":"7.73E-22"},"2Fe-2S_ferredoxin-like_sf","Homologous_superfamily","2Fe-2S ferredoxin-like superfamily","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",166,177,0.0438247,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",156,186,0.119522,10.39,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",116,149,0.131474,8.592,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR001041","CDD","cd00207","fer2",6,53,0.187251,9.04311e-06,"2Fe-2S_ferredoxin-type","Domain","2Fe-2S ferredoxin-type iron-sulfur binding domain","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"IPR001041","PROFILE","PS51085","2FE2S_FER_2",1,79,0.310757,9.35,"2Fe-2S_ferredoxin-type","Domain","2Fe-2S ferredoxin-type iron-sulfur binding domain","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"_","_","G3DSA:3.30.70.20","_",124,181,0.227092,1.2E-8,"_","_","_","-"]
[null,"_","_","PF14697","_",123,182,0.23506,1.5E-9,"_","_","_","-"]
[null,"_","_","PF13510","_",2,77,0.298805,3e-12,"_","_","_","-"]
[null,"_","_","SSF54862","_",76,186,0.438247,1.32E-15,"_","_","_","-"]
[null,"_","_","G3DSA:3.10.20.740","_",1,123,0.486056,{"v":1.5e-25,"d":"1.50E-25"},"_","_","_","-"]
[null,"_","_","PTHR11615","_",2,182,0.717131,{"v":2.8e-29,"d":"2.80E-29"},"_","_","_","-"]
[null,"_","_","PTHR11615:SF225","_",2,182,0.717131,{"v":2.8e-29,"d":"2.80E-29"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_13020","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",119,130,0.0244989,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF00037","Fer4",113,134,0.0467706,6.1e-07,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",110,140,0.0668151,9.987,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",76,108,0.0712695,6.374,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR009016","SSF","SSF53920","SSF53920",118,432,0.699332,3.66E-75,"Fe_hydrogenase","Homologous_superfamily","Iron hydrogenase","-"]
[null,"IPR004108","PFAM","PF02906","Fe_hyd_lg_C",152,389,0.52784,{"v":2.8e-60,"d":"2.80E-60"},"Fe_hydrogenase_lsu_C","Domain","Iron hydrogenase, large subunit, C-terminal","-"]
[null,"_","_","G3DSA:3.30.70.20","_",78,144,0.146993,2.5e-11,"_","_","_","-"]
[null,"_","_","SSF54862","_",92,137,0.100223,1.67E-12,"_","_","_","-"]
[null,"_","_","PTHR11615","_",94,409,0.701559,{"v":2e-22,"d":"2.00E-22"},"_","_","_","-"]
[null,"_","_","PTHR11615:SF231","_",94,409,0.701559,{"v":2e-22,"d":"2.00E-22"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.950.20","_",190,431,0.536748,{"v":1.5e-38,"d":"1.50E-38"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_20317","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR027631","TIGRFAMs","TIGR04105","FeFe_hydrog_B1",5,458,0.913306,{"v":8.2e-179,"d":"8.20E-179"},"FeFe_hydrog_B1","Family","[FeFe] hydrogenase, group B1/B3","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",189,200,0.0221774,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF00037","Fer4",137,157,0.0403226,2.4e-06,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PFAM","PF12838","Fer4_7",164,203,0.078629,3.3e-07,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",180,209,0.0584677,10.642,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",133,162,0.0584677,10.23,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",101,132,0.0625,7.45,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR009016","SSF","SSF53920","SSF53920",188,459,0.546371,{"v":8.63e-66,"d":"8.63E-66"},"Fe_hydrogenase","Homologous_superfamily","Iron hydrogenase","-"]
[null,"IPR004108","PFAM","PF02906","Fe_hyd_lg_C",221,455,0.471774,{"v":3.3E-61,"d":"3.30E-61"},"Fe_hydrogenase_lsu_C","Domain","Iron hydrogenase, large subunit, C-terminal","-"]
[null,"_","_","G3DSA:3.30.70.20","_",163,208,0.0907258,3.2e-12,"_","_","_","-"]
[null,"_","_","SSF54862","_",91,157,0.133065,9.63e-13,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",104,162,0.116935,9.6e-14,"_","_","_","-"]
[null,"_","_","SSF54862","_",135,217,0.165323,{"v":7.96e-18,"d":"7.96E-18"},"_","_","_","-"]
[null,"_","_","PTHR11615","_",164,421,0.518145,{"v":3.8E-27,"d":"3.80E-27"},"_","_","_","-"]
[null,"_","_","PTHR11615:SF231","_",164,421,0.518145,{"v":3.8E-27,"d":"3.80E-27"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.950.20","_",261,482,0.445565,{"v":2.2E-37,"d":"2.20E-37"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12009","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR042099","CATHGENE3D","G3DSA:3.40.50.12780","G3DSA:3.40.50.12780",2,435,0.773214,{"v":6.6e-100,"d":"6.60E-100"},"AMP-dep_Synthh-like_sf","Homologous_superfamily","AMP-dependent synthetase-like superfamily","-"]
[null,"IPR025110","PFAM","PF13193","AMP-binding_C",452,526,0.132143,1.2e-11,"AMP-bd_C","Domain","AMP-binding enzyme, C-terminal domain","-"]
[null,"IPR000873","PFAM","PF00501","AMP-binding",33,440,0.726786,{"v":2.7E-90,"d":"2.70E-90"},"AMP-dep_Synth/Lig","Domain","AMP-dependent synthetase/ligase","Molecular Function: catalytic activity (GO:0003824)"]
[null,"_","_","G3DSA:3.30.300.310","_",436,541,0.1875,{"v":2.9e-25,"d":"2.90E-25"},"_","_","_","-"]
[null,"_","_","PTHR43767","_",12,539,0.941071,{"v":1.1E-109,"d":"1.10E-109"},"_","_","_","-"]
[null,"_","_","PTHR43767:SF1","_",12,539,0.941071,{"v":1.1E-109,"d":"1.10E-109"},"_","_","_","-"]
[null,"_","_","SSF56801","_",20,536,0.921429,{"v":5.23e-124,"d":"5.23E-124"},"_","_","_","-"]
[null,"_","_","cd05903","_",50,534,0.864286,{"v":5.92583e-175,"d":"5.93E-175"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_10745","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR042113","CATHGENE3D","G3DSA:3.40.50.10950","G3DSA:3.40.50.10950",10,329,0.963746,{"v":1.5e-141,"d":"1.50E-141"},"P_AcTrfase_dom1","Homologous_superfamily","Phosphate acetyltransferase, domain 1","-"]
[null,"IPR042112","CATHGENE3D","G3DSA:3.40.50.10750","G3DSA:3.40.50.10750",142,302,0.483384,{"v":1.5e-141,"d":"1.50E-141"},"P_AcTrfase_dom2","Homologous_superfamily","Phosphate acetyltransferase, domain 2","-"]
[null,"IPR012147","PIRSF","PIRSF000428","P_Ac_trans",1,331,0.996979,{"v":5.9e-114,"d":"5.90E-114"},"P_Ac_Bu_trans","Family","Phosphate acetyl/butyryltransferase","Molecular Function: transferase activity, transferring acyl groups (GO:0016746)"]
[null,"IPR004614","TIGRFAMs","TIGR00651","pta",18,326,0.930514,{"v":2.1e-123,"d":"2.10E-123"},"P_AcTrfase","Domain","Phosphate acetyltransferase","Molecular Function: acetyltransferase activity (GO:0016407)"]
[null,"IPR002505","PFAM","PF01515","PTA_PTB",3,326,0.975831,{"v":2.1e-137,"d":"2.10E-137"},"PTA_PTB","Domain","Phosphate acetyl/butaryl transferase","Molecular Function: transferase activity, transferring acyl groups (GO:0016746)"]
[null,"_","_","SSF53659","_",1,329,0.990937,{"v":1.69e-102,"d":"1.69E-102"},"_","_","_","-"]
[null,"_","_","PTHR43356","_",2,330,0.990937,{"v":1.3e-159,"d":"1.30E-159"},"_","_","_","-"]
[null,"_","_","PTHR43356:SF3","_",2,330,0.990937,{"v":1.3e-159,"d":"1.30E-159"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_10746","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR023865","PROSITE","PS01075","ACETATE_KINASE_1",3,14,0.0275689,"_","Aliphatic_acid_kinase_CS","Conserved_site","Aliphatic acid kinase, short-chain, conserved site","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR023865","PROSITE","PS01076","ACETATE_KINASE_2",203,220,0.0426065,"_","Aliphatic_acid_kinase_CS","Conserved_site","Aliphatic acid kinase, short-chain, conserved site","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR004372","HAMAP","MF_00020","Acetate_kinase",1,398,0.994987,200.227,"Ac/propionate_kinase","Family","Acetate/propionate kinase","Biological Process: organic acid metabolic process (GO:0006082); Molecular Function: kinase activity (GO:0016301); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR004372","PIRSF","PIRSF000722","Acetate_prop_kin",1,399,0.997494,{"v":1.6E-160,"d":"1.60E-160"},"Ac/propionate_kinase","Family","Acetate/propionate kinase","Biological Process: organic acid metabolic process (GO:0006082); Molecular Function: kinase activity (GO:0016301); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR004372","TIGRFAMs","TIGR00016","ackA",1,394,0.984962,{"v":9.3e-163,"d":"9.30E-163"},"Ac/propionate_kinase","Family","Acetate/propionate kinase","Biological Process: organic acid metabolic process (GO:0006082); Molecular Function: kinase activity (GO:0016301); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PANTHER","PTHR21060","PTHR21060",1,397,0.992481,{"v":9.7e-172,"d":"9.70E-172"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PFAM","PF00871","Acetate_kinase",2,389,0.969925,{"v":3.4e-163,"d":"3.40E-163"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",322,338,0.0401003,{"v":3.5e-46,"d":"3.50E-46"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",300,313,0.0325815,{"v":3.5e-46,"d":"3.50E-46"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",173,186,0.0325815,{"v":3.5e-46,"d":"3.50E-46"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",3,14,0.0275689,{"v":3.5e-46,"d":"3.50E-46"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",203,224,0.0526316,{"v":3.5e-46,"d":"3.50E-46"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",376,388,0.0300752,{"v":3.5e-46,"d":"3.50E-46"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"_","_","SSF53067","_",1,196,0.488722,{"v":4.53e-73,"d":"4.53E-73"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",1,195,0.486216,{"v":5E-80,"d":"5.00E-80"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",196,399,0.508772,{"v":9.1e-89,"d":"9.10E-89"},"_","_","_","-"]
[null,"_","_","SSF53067","_",157,395,0.596491,{"v":2.83e-95,"d":"2.83E-95"},"_","_","_","-"]
[null,"_","_","PTHR21060:SF15","_",1,397,0.992481,{"v":9.7e-172,"d":"9.70E-172"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_11881","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR039697","PANTHER","PTHR11496","PTHR11496",3,385,0.98708,{"v":1.9E-112,"d":"1.90E-112"},"Alcohol_dehydrogenase_Fe","Family","Iron-type alcohol dehydrogenase-like","-"]
[null,"IPR018211","PROSITE","PS00913","ADH_IRON_1",176,204,0.0723514,"_","ADH_Fe_CS","Conserved_site","Alcohol dehydrogenase, iron-type, conserved site","Molecular Function: oxidoreductase activity (GO:0016491); Molecular Function: metal ion binding (GO:0046872); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001670","PFAM","PF00465","Fe-ADH",12,378,0.945736,{"v":2.2e-111,"d":"2.20E-111"},"ADH_Fe/GldA","Domain","Alcohol dehydrogenase, iron-type/glycerol dehydrogenase GldA","Molecular Function: oxidoreductase activity (GO:0016491); Molecular Function: metal ion binding (GO:0046872); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","G3DSA:3.40.50.1970","_",1,187,0.48062,{"v":4.3e-51,"d":"4.30E-51"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.1090.10","_",188,385,0.509044,{"v":1.1E-64,"d":"1.10E-64"},"_","_","_","-"]
[null,"_","_","SSF56796","_",5,384,0.979328,{"v":4.84e-117,"d":"4.84E-117"},"_","_","_","-"]
[null,"_","_","cd08193","_",7,382,0.968992,{"v":4.94678E-173,"d":"4.95E-173"},"_","_","_","-"]
[]
["CLOSTRIBL3_v1_20137","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR039697","PANTHER","PTHR11496","PTHR11496",4,381,0.986911,{"v":4.5e-142,"d":"4.50E-142"},"Alcohol_dehydrogenase_Fe","Family","Iron-type alcohol dehydrogenase-like","-"]
[null,"IPR018211","PROSITE","PS00913","ADH_IRON_1",159,187,0.0732984,"_","ADH_Fe_CS","Conserved_site","Alcohol dehydrogenase, iron-type, conserved site","Molecular Function: oxidoreductase activity (GO:0016491); Molecular Function: metal ion binding (GO:0046872); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001670","PFAM","PF00465","Fe-ADH",8,372,0.95288,{"v":3.2e-116,"d":"3.20E-116"},"ADH_Fe/GldA","Domain","Alcohol dehydrogenase, iron-type/glycerol dehydrogenase GldA","Molecular Function: oxidoreductase activity (GO:0016491); Molecular Function: metal ion binding (GO:0046872); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","G3DSA:3.40.50.1970","_",1,170,0.442408,{"v":3.1e-46,"d":"3.10E-46"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.1090.10","_",172,382,0.549738,{"v":7.9E-76,"d":"7.90E-76"},"_","_","_","-"]
[null,"_","_","SSF56796","_",4,381,0.986911,{"v":7.33e-118,"d":"7.33E-118"},"_","_","_","-"]
[null,"_","_","PTHR11496:SF91","_",4,381,0.986911,{"v":4.5e-142,"d":"4.50E-142"},"_","_","_","-"]
[null,"_","_","cd08180","_",4,378,0.979058,0,"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12484","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR016163","CATHGENE3D","G3DSA:3.40.309.10","G3DSA:3.40.309.10",223,406,0.345283,{"v":4.2e-172,"d":"4.20E-172"},"Ald_DH_C","Homologous_superfamily","Aldehyde dehydrogenase, C-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor (GO:0016620); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR016162","CATHGENE3D","G3DSA:3.40.605.10","G3DSA:3.40.605.10",22,445,0.798113,{"v":4.2e-172,"d":"4.20E-172"},"Ald_DH_N","Homologous_superfamily","Aldehyde dehydrogenase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR016161","SSF","SSF53720","SSF53720",11,450,0.828302,7.72E-76,"Ald_DH/histidinol_DH","Homologous_superfamily","Aldehyde/histidinol dehydrogenase","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR015590","PFAM","PF00171","Aldedh",22,273,0.473585,{"v":3.1E-20,"d":"3.10E-20"},"Aldehyde_DH_dom","Domain","Aldehyde dehydrogenase domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR013357","TIGRFAMs","TIGR02518","EutH_ACDH",5,527,0.984906,{"v":1.8E-235,"d":"1.80E-235"},"Acetaldehyde_DH_acetylating","Family","Acetaldehyde dehydrogenase, acetylating","-"]
[null,"_","_","PTHR11699","_",2,463,0.869811,{"v":5.7E-186,"d":"5.70E-186"},"_","_","_","-"]
[null,"_","_","PTHR11699:SF68","_",2,463,0.869811,{"v":5.7E-186,"d":"5.70E-186"},"_","_","_","-"]
[null,"_","_","cd07122","_",14,447,0.816981,0,"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12496","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR016163","CATHGENE3D","G3DSA:3.40.309.10","G3DSA:3.40.309.10",223,407,0.370968,{"v":7.5E-163,"d":"7.50E-163"},"Ald_DH_C","Homologous_superfamily","Aldehyde dehydrogenase, C-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor (GO:0016620); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR016162","CATHGENE3D","G3DSA:3.40.605.10","G3DSA:3.40.605.10",17,445,0.862903,{"v":7.5E-163,"d":"7.50E-163"},"Ald_DH_N","Homologous_superfamily","Aldehyde dehydrogenase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR016161","SSF","SSF53720","SSF53720",11,450,0.885081,{"v":1.54e-69,"d":"1.54E-69"},"Ald_DH/histidinol_DH","Homologous_superfamily","Aldehyde/histidinol dehydrogenase","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR015590","PFAM","PF00171","Aldedh",16,272,0.516129,{"v":2.1e-21,"d":"2.10E-21"},"Aldehyde_DH_dom","Domain","Aldehyde dehydrogenase domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PTHR11699","_",1,467,0.939516,{"v":1.8e-177,"d":"1.80E-177"},"_","_","_","-"]
[null,"_","_","PTHR11699:SF68","_",1,467,0.939516,{"v":1.8e-177,"d":"1.80E-177"},"_","_","_","-"]
[null,"_","_","cd07122","_",15,448,0.872984,0,"_","_","_","-"]
[]
["CLOSTRIBL3_v1_12732","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036291","SSF","SSF51735","SSF51735",1,148,0.506897,5.49E-27,"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR015426","PFAM","PF09290","AcetDehyd-dimer",124,260,0.468966,{"v":5.8e-59,"d":"5.80E-59"},"Acetylaldehyde_DH_C","Domain","Acetaldehyde dehydrogenase, C-terminal","Molecular Function: acetaldehyde dehydrogenase (acetylating) activity (GO:0008774); Biological Process: aromatic compound catabolic process (GO:0019439); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR003361","HAMAP","MF_01657","Ac_ald_DH_ac",1,290,0.996552,116.306,"Acetaldehyde_dehydrogenase","Family","Acetaldehyde dehydrogenase","Molecular Function: acetaldehyde dehydrogenase (acetylating) activity (GO:0008774); Biological Process: aromatic compound catabolic process (GO:0019439); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR003361","PIRSF","PIRSF015689","Actaldh_dh_actl",1,290,0.996552,{"v":1.9e-124,"d":"1.90E-124"},"Acetaldehyde_dehydrogenase","Family","Acetaldehyde dehydrogenase","Molecular Function: acetaldehyde dehydrogenase (acetylating) activity (GO:0008774); Biological Process: aromatic compound catabolic process (GO:0019439); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR003361","TIGRFAMs","TIGR03215","ac_ald_DH_ac",3,285,0.972414,{"v":6.7e-137,"d":"6.70E-137"},"Acetaldehyde_dehydrogenase","Family","Acetaldehyde dehydrogenase","Molecular Function: acetaldehyde dehydrogenase (acetylating) activity (GO:0008774); Biological Process: aromatic compound catabolic process (GO:0019439); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR000534","PFAM","PF01118","Semialdhyde_dh",5,115,0.37931,8e-12,"Semialdehyde_DH_NAD-bd","Domain","Semialdehyde dehydrogenase, NAD-binding","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor (GO:0016620); Molecular Function: NAD binding (GO:0051287); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR000534","SMART","SM00859","Semialdhyde_dh",5,116,0.382759,1.7E-5,"Semialdehyde_DH_NAD-bd","Domain","Semialdehyde dehydrogenase, NAD-binding","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor (GO:0016620); Molecular Function: NAD binding (GO:0051287); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","SSF55347","_",124,261,0.472414,2.94E-57,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.360.10","_",124,274,0.517241,{"v":3.4e-117,"d":"3.40E-117"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.720","_",4,281,0.955172,{"v":3.4e-117,"d":"3.40E-117"},"_","_","_","-"]

{"sheet":"PSortB","index":12,"n_rows":70,"n_cols":4,"rows_kept":70}
["CDS","PsortB Localization","Score","Gram"]
["CLOSTRIBL3_v1_11086","Unknown",2.5,"+"]
["CLOSTRIBL3_v1_11116","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_11117","CytoplasmicMembrane",10,"+"]
["CLOSTRIBL3_v1_30024","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_10010","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_10012","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_12309","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_12417","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_12774","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_12775","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_12776","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_12777","Unknown",2.5,"+"]
["CLOSTRIBL3_v1_10343","Unknown",2.5,"+"]
["CLOSTRIBL3_v1_20129","Unknown",2.5,"+"]
["CLOSTRIBL3_v1_12838","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_13111","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_11283","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_11276","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_13113","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_20313","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_13112","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_11087","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_20109","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_20308","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_12502","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_11587","Cytoplasmic",9.67,"+"]
["CLOSTRIBL3_v1_12012","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_12013","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_20310","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_20311","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_20312","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_11710","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_11711","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_12016","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_12308","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_20086","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_20087","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_13110","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_11114","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_11115","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_11486","Unknown",2.5,"+"]
["CLOSTRIBL3_v1_11487","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_11488","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_12010","Unknown",2.5,"+"]
["CLOSTRIBL3_v1_12011","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_20124","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_20125","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_10629","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_10630","CytoplasmicMembrane",9.55,"+"]
["CLOSTRIBL3_v1_10631","Unknown",3.33,"+"]
["CLOSTRIBL3_v1_10632","CytoplasmicMembrane",10,"+"]
["CLOSTRIBL3_v1_10633","CytoplasmicMembrane",10,"+"]
["CLOSTRIBL3_v1_10634","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_10096","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_10095","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_10094","CytoplasmicMembrane",8.78,"+"]
["CLOSTRIBL3_v1_10091","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_10092","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_10093","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_13020","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_20317","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_12009","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_10745","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_10746","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_11881","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_20137","Cytoplasmic",9.97,"+"]
["CLOSTRIBL3_v1_12484","Unknown",2.5,"+"]
["CLOSTRIBL3_v1_12496","Cytoplasmic",7.5,"+"]
["CLOSTRIBL3_v1_12732","Cytoplasmic",7.5,"+"]