{"text_format":"3","workbook":"xlsx","n_sheets":14,"sheets":["reactions","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":"reactions","index":0,"n_rows":31,"n_cols":6,"rows_kept":31,"hidden":true,"merged":[[1,0,10,0],[4,5,5,5],[11,0,16,0],[17,0,19,0],[20,0,21,0],[22,0,24,0],[25,0,30,0]]}
["Predicted function","No.","Enzyme abbreviation","EC number","Enzyme","Reaction"]
["Acetyl-CoA formation",1,"LacA","5.1.2.1","lactate racemase","D-lactate <=> L-lactate"]
[null,2,"LacP",null,"L-lactate permease"]
[null,3,"LDH","1.1.1.27","lactate dehydrogenase","(S)-lactate + NAD+ → H+ + NADH + pyruvate"]
[null,4,"PFOR","1.2.7.1","pyruvate ferredoxin oxidoreductase","pyruvate + CoA + 2 oxidized ferredoxin → acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+"]
[null,null,"PorABCD","1.2.7.1","pyruvate synthase"]
[null,5,"ACoAS","6.2.1.1","acetyl-CoA synthetase","ATP + acetate + CoA → ADP + phosphate + acetyl-CoA"]
[null,6,"ACK","2.7.2.1","acetate kinase","ATP + acetate → ADP + acetyl phosphate"]
[null,7,"PTA","2.3.1.8","phosphate acetyltransferase","CoA + acetyl phosphate → acetyl-CoA + phosphate "]
[null,8,"ADH","1.1.1.1","Alcohol dehydrogenase","A primary alcohol + NAD(+) → an aldehyde + NADH"]
[null,9,"ADA","1.2.1.10","acetaldehyde dehydrogenase","Acetaldehyde + CoA + NAD(+) → acetyl-CoA + NADH"]
["reverse β-oxidation",10,"ACAT","2.3.1.9, 2.3.1.16 ","acetyl-CoA acetyltransferase","2 acetyl-CoA → acetoacetyl-CoA + coenzyme A "]
[null,11,"HAD","1.1.1.157","3-hydroxybutyryl-CoA dehydrogenase","acetoacetyl-CoA + NADPH + H+ → (S)-3-hydroxybutyryl-CoA + NADP+ "]
[null,12,"ECH","4.2.1.150, 4.2.1.55","enoyl-CoA hydratase","(S)-3-hydroxybutyryl-CoA → crotonyl-CoA + H2O"]
[null,13,"BCD","1.3.8.1","butyryl-CoA dehydrogenase","crotonyl-CoA + a reduced electron-transfer flavoprotein → butyryl-CoA + an oxidized electron-transfer flavoprotein + H+"]
[null,14,"EtfA,B",null,"electron transfer flavoprotein A,B"]
[null,15,"CoAT","2.8.3.-","Butyryl-CoA:acetate CoA-transferase","Acyl-CoA + acetate → a fatty acid anion + acetyl-CoA"]
["Butyrate formation",16,"ACT","3.1.2.20","acyl-CoA thioesterase","an acyl-CoA + H2O → a carboxylate + coenzyme A + H+"]
[null,17,"PTB","2.3.1.19","phosphate butyryltransferase","butyryl-CoA + phosphate → CoA + butyryl phosphate"]
[null,18,"BUK","2.7.2.7","butyrate kinase","ADP + butyryl phosphate → ATP + butyrate"]
["Energy conservation",19,"RnfABCDEG","7.1.1.1","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex"]
[null,20,"EchABCDEF",null,"energy-conserving hydrogenase"]
["H2 formation",21,"H2ase","1.12.7.2","hydrogen:ferredoxin oxidoreductase","2 reduced ferredoxin + 2 H+ → H2 + 2 oxidized ferredoxin "]
[null,22,"HndABCD","1.1.12.3","hydrogen:NADP+ oxidoreductase","2H+ + 2NADPH → H2 + 2NADP(+) "]
[null,23,"HydABC","1.12.1.4",null,"5 H+ + NADH + 2 reduced ferredoxin → 2 H2 + NAD+ + 2 oxidized ferredoxin"]
["Others",24,"BM","5.4.99.13","butyryl-CoA:isobutyryl-CoA mutase","butyryl-CoA → iso-butyryl-CoA"]
[null,25,"ACS","6.2.1.-","acyl-CoA synthetase","ATP + a medium-chain fatty acid + CoA → AMP + diphosphate + a medium-chain acyl-CoA"]
[null,26,"ACOCT","2.8.3.19","Acetyl-CoA:oxalate CoA-transferase","acetyl-CoA + oxalate → acetate + oxalyl-CoA"]
[null,27,"HadABC","4.2.1.157","(R)-2-hydroxyisocaproyl-CoA dehydratase activator, alpha subunit, beta subunit ","(R)-2-hydroxy-4-methylpentanoyl-CoA = 4-methylpent-2-enoyl-CoA + H2O"]
[null,28,"CarC","1.3.1.108","Caffeyl-CoA reductase-Etf complex subunit CarC","hydrocaffeoyl-CoA + 2 NAD+ + 2 reduced [2Fe-2S]-[ferredoxin] → (E)-caffeoyl-CoA + 2 NADH + 2 oxidized [2Fe-2S]-[ferredoxin]"]
[null,29,"HydN",null,"Electron transport protein"]

{"sheet":"instruction","index":1,"n_rows":14,"n_cols":2,"rows_kept":14,"merged":[[0,0,0,1]]}
["Additional file 7. Functional annotations of strain BL-6"]
["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":2,"n_rows":55,"n_cols":13,"rows_kept":55}
["CDS","Strand","length","Begin","End","AMIGene Start","AMIGene Lpcod","AMIGene Apcod","Matrix","Prodigal Begin","Prodigal End","Glimmer Begin","Glimmer End"]
["CLOSTRIBL6_v1_3221","R",1281,3148620,3149900,3149900,0.954447,0.954447,1,3148620,3149900,3148620,3149900]
["CLOSTRIBL6_v1_3223","D",1554,3150461,3152014,3150461,0.954376,0.954376,1,3150461,3152014,3150461,3152014]
["CLOSTRIBL6_v1_2713","D",954,2653597,2654550,2653597,0.917717,0.917717,1,2653597,2654550,2653597,2654550]
["CLOSTRIBL6_v1_0279","D",3558,312150,315707,312150,0.978898,0.978898,1,312150,315707,312150,315707]
["CLOSTRIBL6_v1_3009","D",582,2961537,2962124,2961537,0.81837,0.81837,1,2961546,2962124,2961543,2962124]
["CLOSTRIBL6_v1_3010","D",309,2962121,2962429,2962121,0.829628,0.829628,1,2962121,2962429,2962121,2962429]
["CLOSTRIBL6_v1_3011","D",1176,2962444,2963619,2962444,0.926825,0.926825,1,2962444,2963619,2962444,2963619]
["CLOSTRIBL6_v1_3012","D",933,2963634,2964566,2963634,0.915204,0.915204,1,2963634,2964566,2963634,2964566]
["CLOSTRIBL6_v1_0126","R",837,143170,144006,144006,0.923833,0.923833,1,143170,144006,143170,144006]
["CLOSTRIBL6_v1_0127","R",1188,144056,145396,145192,0.80766,0.918493,1,144056,145243,144056,145243]
["CLOSTRIBL6_v1_0555","R",900,598906,599814,599814,0.918807,0.918807,1,598906,599805,598906,599805]
["CLOSTRIBL6_v1_0556","R",1194,599847,601040,601040,0.909605,0.909605,1,599847,601040,599847,601040]
["CLOSTRIBL6_v1_0558","D",789,601625,602437,601625,0.89084,0.89084,1,601649,602437,601649,602437]
["CLOSTRIBL6_v1_0559","D",1203,602455,603723,602455,0.887777,0.887777,1,602521,603723,602521,603723]
["CLOSTRIBL6_v1_0560","D",798,603680,604540,603680,0.815721,0.815721,1,603743,604540,603743,604540]
["CLOSTRIBL6_v1_0561","D",1293,604524,605825,604524,0.925425,0.925425,1,604533,605825,604533,605825]
["CLOSTRIBL6_v1_0562","D",1131,605818,606948,605818,0.945506,0.945506,1,605818,606948,605818,606948]
["CLOSTRIBL6_v1_0871","D",945,896644,897588,896644,0.944834,0.944834,1,896644,897588,896644,897588]
["CLOSTRIBL6_v1_2953","R",1041,2894251,2895291,2895291,0.97202,0.97202,1,2894251,2895291,2894251,2895291]
["CLOSTRIBL6_v1_0031","R",810,29478,30308,30308,0.968383,0.968383,1,29478,30287,29478,30287]
["CLOSTRIBL6_v1_1904","R",1896,1903847,1905742,1905742,0.95307,0.95307,1,1903847,1905742,1903847,1905742]
["CLOSTRIBL6_v1_3062","R",1698,3006024,3007721,3007721,0.982019,0.982019,1,3006024,3007721,3006024,3007721]
["CLOSTRIBL6_v1_0135","D",1140,151798,152943,151798,0.913971,0.913971,1,151804,152943,151804,152943]
["CLOSTRIBL6_v1_0136","D",780,152943,153737,152943,0.930599,0.930599,1,152958,153737,152958,153737]
["CLOSTRIBL6_v1_0137","D",1041,153737,154777,153737,0.943882,0.943882,1,153737,154777,153758,154777]
["CLOSTRIBL6_v1_3216","R",1143,3143571,3144713,3144713,0.94242,0.94242,1,3143571,3144713,3143571,3144713]
["CLOSTRIBL6_v1_3217","R",1005,3145198,3146202,3146202,0.959788,0.959788,1,3145198,3146202,3145198,3146202]
["CLOSTRIBL6_v1_3218","R",807,3146219,3147025,3147025,0.906508,0.906508,1,3146219,3147025,3146219,3147025]
["CLOSTRIBL6_v1_3220","R",1428,3147140,3148723,3148723,0.901938,0.901938,1,3147140,3148567,3147140,3148567]
["CLOSTRIBL6_v1_2270","D",480,2274395,2274874,2274395,0.859105,0.859105,1,2274395,2274874,2274395,2274874]
["CLOSTRIBL6_v1_2820","R",987,2761155,2762141,2762141,0.927062,0.927062,1,2761155,2762141,2761155,2762141]
["CLOSTRIBL6_v1_2821","R",801,2762142,2762942,2762942,0.929106,0.929106,1,2762142,2762942,2762142,2762942]
["CLOSTRIBL6_v1_0258","R",1728,279898,281625,281625,0.972776,0.972776,1,279898,281625,279898,281625]
["CLOSTRIBL6_v1_0260","D",1416,282648,284063,282648,0.966255,0.966255,1,282648,284063,282648,284063]
["CLOSTRIBL6_v1_1906","R",1308,1907501,1908808,1908808,0.903606,0.903606,1,1907501,1908808,1907501,1908808]
["CLOSTRIBL6_v1_2017","R",1446,2029053,2030630,2030498,0.874001,0.950163,1,2029053,2030498,2029053,2030498]
["CLOSTRIBL6_v1_2260","R",1206,2263864,2265105,2265105,0.977413,0.977413,1,2263864,2265069,2263864,2265069]
["CLOSTRIBL6_v1_1872","R",972,1868519,1869520,1869520,0.935058,0.935058,1,1868519,1869490,1868519,1869490]
["CLOSTRIBL6_v1_0095","R",1164,103379,104542,104542,0.953769,0.953769,1,103379,104542,103379,104542]
["CLOSTRIBL6_v1_1804","D",1173,1796227,1797399,1796227,0.93451,0.93451,1,1796230,1797399,1796227,1797399]
["CLOSTRIBL6_v1_2186","D",2607,2189800,2192406,2189800,0.966573,0.966573,1,2189800,2192406,2189800,2192406]
["CLOSTRIBL6_v1_2879","R",1185,2829292,2830476,2830476,0.950282,0.950282,1,2829292,2830476,2829292,2830476]
["CLOSTRIBL6_v1_3434","D",1182,3364265,3365446,3364265,0.97402,0.97402,1,3364265,3365446,3364265,3365446]
["CLOSTRIBL6_v1_1351","D",1470,1392583,1394142,1392583,0.777885,0.777885,1,1392694,1394142,1392673,1394142]
["CLOSTRIBL6_v1_2699","D",1908,2638721,2640628,2638721,0.928253,0.928253,1,2638721,2640628,2638772,2640628]
["CLOSTRIBL6_v1_2700","D",867,2640037,2641494,2640628,0.542698,0.913688,1,2640628,2641494,2640628,2641494]
["CLOSTRIBL6_v1_2701","D",465,2641508,2641972,2641508,0.868363,0.868363,1,2641508,2641972,2641508,2641972]
["CLOSTRIBL6_v1_2702","D",348,2641969,2642319,2641969,0.901154,0.901154,1,2641972,2642319,2641972,2642319]
["CLOSTRIBL6_v1_2703","D",1080,2642322,2643401,2642322,0.954498,0.954498,1,2642322,2643401,2642322,2643401]
["CLOSTRIBL6_v1_2704","D",624,2643408,2644031,2643408,0.444847,0.444847,1,2643408,2644031,2643408,2644031]
["CLOSTRIBL6_v1_2705","D",2229,2644054,2646282,2644054,0.957816,0.957816,1,2644054,2646282,2644054,2646282]
["CLOSTRIBL6_v1_2706","D",213,2646304,2646516,2646304,0.668819,0.668819,1,2646304,2646516,2646304,2646516]
["CLOSTRIBL6_v1_2707","D",1035,2646513,2647547,2646513,0.941586,0.941586,1,2646513,2647547,2646513,2647547]
["CLOSTRIBL6_v1_2708","D",987,2647551,2648537,2647551,0.948747,0.948747,1,2647551,2648537,2647551,2648537]

{"sheet":"gene features","index":3,"n_rows":55,"n_cols":8,"rows_kept":55}
["CDS","GC Content","GC1 Content","GC2 Content","GC3 Content","CAI","GCskew","R/Y ratio"]
["CLOSTRIBL6_v1_3221",63.47,66.74,43.56,80.09,0.75,-0.028,1.066]
["CLOSTRIBL6_v1_3223",60.94,56.76,45.95,80.12,0.72,0.052,0.805]
["CLOSTRIBL6_v1_2713",61.11,59.75,41.51,82.08,0.76,0.005,1.017]
["CLOSTRIBL6_v1_0279",59.75,57.34,41.65,80.27,0.77,0.02,1.064]
["CLOSTRIBL6_v1_3009",61.86,60.31,42.27,82.99,0.68,-0.1,1.309]
["CLOSTRIBL6_v1_3010",58.25,50.49,44.66,79.61,0.73,-0.144,1.272]
["CLOSTRIBL6_v1_3011",62.42,58.16,43.62,85.46,0.76,0.016,1.074]
["CLOSTRIBL6_v1_3012",60.13,53.38,43.73,83.28,0.78,-0.016,1.18]
["CLOSTRIBL6_v1_0126",54.48,55.91,37.99,69.53,0.68,-0.013,1.197]
["CLOSTRIBL6_v1_0127",61.7,64.9,46.72,73.48,0.69,-0.048,1.129]
["CLOSTRIBL6_v1_0555",59.33,58.33,42.33,77.33,0.68,0.011,1.098]
["CLOSTRIBL6_v1_0556",64.07,62.56,48.49,81.16,0.68,-0.022,1.113]
["CLOSTRIBL6_v1_0558",61.47,63.12,44.49,76.81,0.67,-0.06,1.173]
["CLOSTRIBL6_v1_0559",58.6,59.6,43.39,72.82,0.64,-1E-3,1.015]
["CLOSTRIBL6_v1_0560",60.65,61.65,44.36,75.94,0.66,-0.066,1.151]
["CLOSTRIBL6_v1_0561",59.47,56.84,40.84,80.74,0.73,0.004,1.089]
["CLOSTRIBL6_v1_0562",59.33,57.56,40.32,80.11,0.71,0.01,1.027]
["CLOSTRIBL6_v1_0871",61.06,62.54,40,80.63,0.72,-0.165,1.316]
["CLOSTRIBL6_v1_2953",61.96,64.55,44.96,76.37,0.67,-0.113,1.22]
["CLOSTRIBL6_v1_0031",63.21,65.19,41.85,82.59,0.71,-0.082,1.143]
["CLOSTRIBL6_v1_1904",58.76,59.49,40.19,76.58,0.75,-0.039,1.194]
["CLOSTRIBL6_v1_3062",61.13,61.48,42.93,78.98,0.72,-0.058,1.169]
["CLOSTRIBL6_v1_0135",56.05,55.79,39.74,72.63,0.69,-0.058,1.192]
["CLOSTRIBL6_v1_0136",58.72,60,40.38,75.77,0.71,0,1.114]
["CLOSTRIBL6_v1_0137",59.46,61.1,40.06,77.23,0.76,-0.05,1.178]
["CLOSTRIBL6_v1_3216",59.14,58.01,42.52,76.9,0.77,-0.044,1.101]
["CLOSTRIBL6_v1_3217",64.18,66.27,45.67,80.6,0.76,-0.042,1.138]
["CLOSTRIBL6_v1_3218",60.59,63.57,42.75,75.46,0.72,-0.047,1.217]
["CLOSTRIBL6_v1_3220",60.78,60.29,37.18,84.87,0.83,-0.039,1.106]
["CLOSTRIBL6_v1_2270",57.92,60.62,38.12,75,0.72,-0.043,1.192]
["CLOSTRIBL6_v1_2820",65.25,69.6,43.77,82.37,0.73,-0.09,1.188]
["CLOSTRIBL6_v1_2821",64.92,66.67,43.45,84.64,0.74,-0.081,1.219]
["CLOSTRIBL6_v1_0258",55.27,54.51,37.67,73.61,0.69,1E-3,1.149]
["CLOSTRIBL6_v1_0260",57.49,57.2,40.25,75,0.69,-0.106,1.237]
["CLOSTRIBL6_v1_1906",60.7,58.94,45.41,77.75,0.66,-0.073,1.176]
["CLOSTRIBL6_v1_2017",62.52,60.37,44.81,82.37,0.73,-0.062,1.188]
["CLOSTRIBL6_v1_2260",59.04,57.96,39.3,79.85,0.73,-0.034,1.123]
["CLOSTRIBL6_v1_1872",58.85,56.79,41.36,78.4,0.75,-0.004,1.146]
["CLOSTRIBL6_v1_0095",62.03,60.82,40.98,84.28,0.79,0.111,0.966]
["CLOSTRIBL6_v1_1804",57.54,59.34,44.25,69.05,0.62,-0.022,1.133]
["CLOSTRIBL6_v1_2186",61.33,57.65,42.23,84.12,0.75,0.046,1.024]
["CLOSTRIBL6_v1_2879",59.75,60.25,39.75,79.24,0.71,-0.073,1.215]
["CLOSTRIBL6_v1_3434",63.11,60.41,44.42,84.52,0.76,0,1.099]
["CLOSTRIBL6_v1_1351",59.39,61.02,45.51,71.63,0.64,-0.026,1.062]
["CLOSTRIBL6_v1_2699",57.7,53.62,39.47,80.03,0.72,0.045,0.822]
["CLOSTRIBL6_v1_2700",56.75,52.94,38.06,79.24,0.73,0.049,0.791]
["CLOSTRIBL6_v1_2701",56.34,56.77,40.65,71.61,0.66,-0.046,1.143]
["CLOSTRIBL6_v1_2702",49.14,52.59,29.31,65.52,0.61,-0.076,1.305]
["CLOSTRIBL6_v1_2703",59.17,58.06,38.06,81.39,0.75,-0.014,1.077]
["CLOSTRIBL6_v1_2704",60.26,54.81,59.13,66.83,0.64,0.074,1.152]
["CLOSTRIBL6_v1_2705",63.48,63.93,45.9,80.62,0.69,0.013,1.015]
["CLOSTRIBL6_v1_2706",54.93,66.2,35.21,63.38,0.6,-0.179,1.219]
["CLOSTRIBL6_v1_2707",65.22,62.03,49.57,84.06,0.73,-0.019,1.033]
["CLOSTRIBL6_v1_2708",63.73,62.92,47.11,81.16,0.7,-0.04,1.155]

{"sheet":"protein features","index":4,"n_rows":55,"n_cols":14,"rows_kept":55}
["CDS","Mw (Da)","Hydrophobicity","Tiny","Small","Aliphatic","Aromatic","Non Polar","Polar","Charged","Basic","Acidic","pI","Oxyphobic Index"]
["CLOSTRIBL6_v1_3221",45787.86,0,31.46,54.93,24.88,7.75,58.69,41.31,27,14.55,12.44,6.22,9.52]
["CLOSTRIBL6_v1_3223",53563.4,1.08,38.1,56.29,31.53,8.12,73.5,26.5,8.7,5.8,2.9,9.4,8.37]
["CLOSTRIBL6_v1_2713",34339.14,0.07,33.12,52.68,24.61,9.46,58.04,41.96,23.34,12.93,10.41,7.05,9.23]
["CLOSTRIBL6_v1_0279",128941.11,-0.26,32.57,54.94,18.9,11.39,57.3,42.7,24.73,12.83,11.9,6.1,9.49]
["CLOSTRIBL6_v1_3009",21153.43,-0.28,29.02,53.37,21.76,8.81,56.48,43.52,27.46,15.54,11.92,9.12,9.68]
["CLOSTRIBL6_v1_3010",11302.68,-0.13,32.35,51.96,19.61,8.82,58.82,41.18,29.41,13.73,15.69,5.15,10.14]
["CLOSTRIBL6_v1_3011",42513.62,-0.11,34.02,53.2,19.95,9.46,57.8,42.2,24.04,10.49,13.56,4.83,9.87]
["CLOSTRIBL6_v1_3012",34797.48,-0.38,31.61,51.61,15.48,13.23,56.13,43.87,25.16,14.52,10.65,8.62,10.17]
["CLOSTRIBL6_v1_0126",29974.66,0.02,30.22,50.36,25.54,6.47,57.55,42.45,26.98,14.03,12.95,6.45,8.92]
["CLOSTRIBL6_v1_0127",41047.66,0.11,36.71,59.49,21.27,5.82,63.54,36.46,20.51,11.14,9.37,8.71,9.7]
["CLOSTRIBL6_v1_0555",32511.7,-0.19,32.11,54.18,21.74,8.36,55.52,44.48,24.75,13.04,11.71,7.78,9.54]
["CLOSTRIBL6_v1_0556",42114.81,0.03,37.03,55.67,21.91,6.05,60.2,39.8,21.66,11.84,9.82,8.13,10.18]
["CLOSTRIBL6_v1_0558",28306.7,-0.01,33.21,48.86,24.05,4.96,59.92,40.08,25.95,12.98,12.98,6.07,9.9]
["CLOSTRIBL6_v1_0559",44389.42,-0.31,30.25,53.25,19.75,13.25,56.75,43.25,25.25,13,12.25,5.76,9.89]
["CLOSTRIBL6_v1_0560",28076.93,0.04,36.98,54.34,23.4,7.17,56.23,43.77,24.15,12.08,12.08,5.47,9.16]
["CLOSTRIBL6_v1_0561",48519.04,-0.43,29.3,48.84,17.21,11.16,53.72,46.28,25.12,11.86,13.26,5.2,10.18]
["CLOSTRIBL6_v1_0562",42282.16,-0.19,27.93,48.4,20.21,10.37,58.24,41.76,22.61,11.17,11.44,5.49,10.37]
["CLOSTRIBL6_v1_0871",34743.48,-0.18,30.25,47.45,22.29,9.55,56.05,43.95,28.34,14.65,13.69,6.3,9.66]
["CLOSTRIBL6_v1_2953",36569.66,0.03,34.1,55.2,21.97,8.09,63.29,36.71,23.99,12.43,11.56,5.95,9.71]
["CLOSTRIBL6_v1_0031",29480.58,-0.11,30.48,50.56,23.42,7.81,56.51,43.49,29.37,14.13,15.24,5.23,9.34]
["CLOSTRIBL6_v1_1904",68209.06,-0.24,31.85,51.66,20.13,9.83,58,42,26.47,13.31,13.15,5.74,9.37]
["CLOSTRIBL6_v1_3062",60528.75,-0.11,33.63,51.15,21.24,9.73,60,40,23.89,12.57,11.33,6.59,9.17]
["CLOSTRIBL6_v1_0135",41306.9,-0.12,33.25,47.76,20.05,9.23,56.73,43.27,24.8,12.66,12.14,6.95,9.31]
["CLOSTRIBL6_v1_0136",28440.2,-0.26,29.73,52.9,23.94,7.72,52.51,47.49,27.8,13.51,14.29,5.31,8.96]
["CLOSTRIBL6_v1_0137",37326.44,-0.08,30.92,53.47,23.99,6.65,57.8,42.2,25.72,12.72,13.01,5.6,9.48]
["CLOSTRIBL6_v1_3216",41864.3,-0.14,34.47,48.16,17.37,11.32,57.11,42.89,24.74,11.84,12.89,5.26,9.77]
["CLOSTRIBL6_v1_3217",35349.82,-0.02,35.03,58.08,23.35,7.78,58.98,41.02,26.05,13.17,12.87,5.66,9.39]
["CLOSTRIBL6_v1_3218",28980.98,-0.16,31.34,55.6,23.13,7.46,55.97,44.03,27.61,13.81,13.81,5.64,9.55]
["CLOSTRIBL6_v1_3220",51902.64,-0.04,28.84,51.79,23.58,9.47,58.74,41.26,24.21,10.53,13.68,4.82,9.62]
["CLOSTRIBL6_v1_2270",17987.67,-0.39,26.42,50.31,23.9,9.43,48.43,51.57,27.67,15.72,11.95,7.2,10.26]
["CLOSTRIBL6_v1_2820",35272.25,-0.04,32.01,50.91,24.09,6.71,59.76,40.24,28.35,14.02,14.33,5.59,9.53]
["CLOSTRIBL6_v1_2821",28381.18,-0.08,31.95,57.14,23.68,6.39,57.52,42.48,27.07,12.78,14.29,5.17,9.36]
["CLOSTRIBL6_v1_0258",64350.81,-0.26,26.96,48,24,7.3,52.17,47.83,27.13,15.13,12,8.66,9.59]
["CLOSTRIBL6_v1_0260",50848.25,0.01,32.06,53.08,22.72,6.58,59.24,40.76,26.75,14.65,12.1,8.24,9.59]
["CLOSTRIBL6_v1_1906",48114.39,-0.23,31.26,52.41,20,8.51,55.4,44.6,28.05,14.48,13.56,6.01,10.29]
["CLOSTRIBL6_v1_2017",52658.75,-0.19,33.47,53.01,18.71,8.11,57.38,42.62,27.86,15.18,12.68,7.64,10.37]
["CLOSTRIBL6_v1_2260",43748.57,-0.08,31.17,49.88,23.44,9.73,56.11,43.89,26.43,14.71,11.72,6.97,9.36]
["CLOSTRIBL6_v1_1872",34532.48,-0.08,32.2,54.8,21.67,6.81,59.13,40.87,25.39,13.31,12.07,8.51,9.06]
["CLOSTRIBL6_v1_0095",41472.29,0.08,32.04,55.04,23.51,8.01,61.76,38.24,23.26,11.63,11.63,5.6,9.54]
["CLOSTRIBL6_v1_1804",41393.54,0.02,36.15,56.41,20.51,10.26,59.74,40.26,22.56,11.54,11.03,5.7,8.99]
["CLOSTRIBL6_v1_2186",95404.54,-0.13,31.11,52.42,21.54,10.71,56.91,43.09,24.77,13.13,11.64,6.33,9.57]
["CLOSTRIBL6_v1_2879",42419.42,0.06,31.73,53.05,23.6,8.38,60.91,39.09,23.86,12.44,11.42,6.03,9.65]
["CLOSTRIBL6_v1_3434",42870.15,-0.19,32.82,54.45,20.61,10.94,56.74,43.26,24.68,13.49,11.2,6.64,9.5]
["CLOSTRIBL6_v1_1351",52689.5,-0.03,33.74,54.19,22.29,8.59,59.3,40.7,24.13,12.47,11.66,6.15,9.51]
["CLOSTRIBL6_v1_2699",69230.78,0.86,32.28,48.03,30.55,14.49,70.08,29.92,14.17,8.82,5.35,8.69,8.53]
["CLOSTRIBL6_v1_2700",32035.04,0.78,29.51,44.44,30.56,14.24,67.36,32.64,14.93,8.68,6.25,8.37,8.44]
["CLOSTRIBL6_v1_2701",16577.46,-0.01,29.22,59.09,25.32,7.14,60.39,39.61,22.73,11.69,11.04,6.09,9.67]
["CLOSTRIBL6_v1_2702",13351.67,-0.47,23.48,34.78,23.48,13.91,50.43,49.57,31.3,13.91,17.39,4.95,9.46]
["CLOSTRIBL6_v1_2703",40640.64,-0.08,25.07,45.4,23.68,11.7,57.94,42.06,27.3,14.21,13.09,6.04,9.74]
["CLOSTRIBL6_v1_2704",21832.35,-0.52,41.55,62.32,9.66,5.8,55.56,44.44,23.67,15.46,8.21,9.44,9.79]
["CLOSTRIBL6_v1_2705",81220.22,-0.14,32.08,52.29,21.02,9.84,59.43,40.57,24.8,13.61,11.19,8.19,9.87]
["CLOSTRIBL6_v1_2706",7415.24,0.54,28.57,61.43,31.43,8.57,64.29,35.71,22.86,8.57,14.29,4.45,9.51]
["CLOSTRIBL6_v1_2707",36837.12,0.03,36.05,58.43,20.93,9.01,63.37,36.63,20.35,11.63,8.72,8.61,10.26]
["CLOSTRIBL6_v1_2708",34014.6,0.19,39.02,58.23,23.78,5.49,61.59,38.41,22.56,10.37,12.2,5.06,9.61]

{"sheet":"MaGe-Curated annotations","index":5,"n_rows":1058,"n_cols":26,"rows_kept":1058}
["CLOSTRIBL6_v1_3221","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",null,"Clostridiaceae BL-3","larA","Lactate racemase","LACTATE-RACEMASE-RXN ; RHEA:10960 ;",0.98357,0.98821,52.03,{"v":8e-152,"d":"8.00E-152"},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",5,422,426,6,423,424]
[null,"CD630_11700",null,"Clostridium difficile 630","_","Conserved hypothetical protein","_",0.98592,0.99057,50,{"v":6e-141,"d":"6.00E-141"},1,1,"_","_","1 : Unknown","_","u : unknown","_","4 : Unknown function but conserved in other organisms",5,423,426,6,424,424]
[]
["CLOSTRIBL6_v1_3223","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_11117",null,"Clostridiaceae BL-3","lctP","L-lactate permease","_",0.98839,1.00591,46.18,{"v":2E-165,"d":"2.00E-165"},1,1,"4.S.98 : lactate ;","_","11 : Membrane","_","t : transporter",10508058,"2a : Function from experimental evidences in other organisms",6,514,517,9,504,508]
[null,"ECED1_5018","_","Escherichia coli ED1a","_","L-lactate permease","_",0.9749,0.97679,42.57,{"v":1E-134,"d":"1.00E-134"},1,1,"_","_","1 : Unknown","7 : Transport and binding proteins ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,509,517,9,510,518]
[null,"ECS88_4020","_","Escherichia coli S88","lldP","L-lactate permease","_",0.94192,1.00387,35.84,{"v":4e-96,"d":"4.00E-96"},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",2,499,517,16,530,551]
[null,"ECUMN_4118","_","Escherichia coli UMN026","lldP","L-lactate permease","_",0.94192,1.00387,35.84,{"v":5e-96,"d":"5.00E-96"},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",2,499,517,16,530,551]
[null,"EFER_3597","_","Escherichia fergusonii ATCC 35469T","lldP","L-lactate permease","_",0.94192,1.00387,35.07,{"v":3e-94,"d":"3.00E-94"},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",2,499,517,16,530,551]
[null,"PP_4735","_","Pseudomonas putida KT2440","lldP","L-lactate permease","_",0.94424,1.01547,35.24,{"v":6e-92,"d":"6.00E-92"},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",2,503,517,16,537,556]
[null,"NLA0588","_","Neisseria lactamica ST640","lldP","L-lactate permease","_",0.9543,1.00967,36.02,{"v":8e-92,"d":"8.00E-92"},1,1,"_","_","5 : Inner membrane protein","_","t : transporter","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,509,517,17,528,547]
[null,"PSEEN0768","_","Pseudomonas entomophila L48","lldP","L-lactate permease","_",0.94424,1.01547,35.05,{"v":1E-89,"d":"1.00E-89"},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",2,503,517,16,537,556]
[]
["CLOSTRIBL6_v1_2713","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 ;",0.94081,0.95268,52.98,{"v":1e-110,"d":"1.00E-110"},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",7,308,317,8,308,321]
[null,"BN424_462","_","Carnobacterium maltaromaticum LMA28 v1","ldh1","L-lactate dehydrogenase 1","L-LACTATE-DEHYDROGENASE-RXN ; RHEA:23444 ;",0.95327,0.9653,45.75,{"v":6e-94,"d":"6.00E-94"},1,1,"_","1.1.1.27","2 : Cytoplasmic","6.8 : Glycolysis/gluconeogenesis ;","e : enzyme","6411465, 1768113","2a : Function from experimental evidences in other organisms",4,309,317,8,311,321]
[null,"BTCD_v1_2573","_","Brochothrix thermosphacta CD337","lctE","L-lactate dehydrogenase","L-LACTATE-DEHYDROGENASE-RXN ; RHEA:23444 ;",0.99369,1.01613,45.71,{"v":7e-93,"d":"7.00E-93"},1,1,"_","1.1.1.27","2 : Cytoplasmic","16.10 : Respire ;","e : enzyme","10809684, 16207915, 19383131, 10644484, 16085862, 15644899","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,315,317,1,310,310]
[null,"CD630_21640","_","Clostridium difficile 630","ldh","L-lactate dehydrogenase (L-LDH)","_",0.95963,0.97476,42.72,{"v":1e-86,"d":"1.00E-86"},1,1,"1.1.1.20 : Glycol degradation ; 1.3.4 : Tricarboxylic acid cycle ; 1.3.5 : Fermentation ; 1.3.7 : Anaerobic respiration ; 1.7.2 : Glyoxylate bypass ; 1.7.21 : Glyoxylate degradation ; 1.7.8 : Gluconeogenesis ;","1.1.1.27","2 : Cytoplasmic","6.3 : Anaerobic ; 6.7 : Fermentation ; 6.8 : Glycolysis/gluconeogenesis ; 6.12 : TCA cycle ;","e : enzyme","10644484, 16085862, 15644899","2a : Function from experimental evidences in other organisms",6,309,317,6,314,322]
[null,"SSV_v1_1093","_","Streptococcus sanguinis 2908","ldh","L-lactate dehydrogenase","L-LACTATE-DEHYDROGENASE-RXN ;",0.93293,0.9653,45.1,{"v":2E-85,"d":"2.00E-85"},1,1,"_","1.1.1.27","2 : Cytoplasmic","16.10 : Respire ;","e : enzyme","10809684, 16207915","2a : Function from experimental evidences in other organisms",5,308,317,7,310,328]
[null,"CLOSTRIBL4_v1_2205","_","Clostridiales BL-4","ldh","L-lactate dehydrogenase","L-LACTATE-DEHYDROGENASE-RXN ; RHEA:23444 ;",0.9653,0.97452,42.16,{"v":9e-82,"d":"9.00E-82"},1,1,"_","1.1.1.27","2 : Cytoplasmic","_","e : enzyme",15007569,"2a : Function from experimental evidences in other organisms",4,309,317,3,307,314]
[null,"AZOLI_2908","_","Azospirillum lipoferum 4B","ldh","L-lactate dehydrogenase","_",0.97476,0.97785,38.51,{"v":4E-70,"d":"4.00E-70"},1,1,"_","1.1.1.27","10 : Secreted","6.8 : Glycolysis/gluconeogenesis ;","e : enzyme",10809684,"2a : Function from experimental evidences in other organisms",7,315,317,2,309,316]
[null,"Ent638_2002","_","Enterobacter sp. 638","ldh","L-lactate dehydrogenase 2 (L-LDH 2)","_",0.90323,0.97161,37.66,{"v":4e-67,"d":"4.00E-67"},1,1,"_","1.1.1.27","2 : Cytoplasmic","6.8 : Glycolysis/gluconeogenesis ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,312,317,33,338,341]
[]
["CLOSTRIBL6_v1_0279","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,"CLOSTRIBL4_v1_0841",null,"Clostridiales BL-4","PFOF","Pyruvate:ferredoxin oxidoreductase","PYRUFLAVREDUCT-RXN ; RHEA:12768 ;",0.99747,0.99831,75.89,0,1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme",18631365,"2a : Function from experimental evidences in other organisms",2,1183,1185,3,1181,1184]
[null,"CLOSTRIBL3_v1_10343","_","Clostridiaceae BL-3","pfo","Pyruvate-flavodoxin oxidoreductase","PYFLAVOXRE-RXN ; RHEA:12765 ;",0.99662,1.01113,61.81,0,1,1,"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",4,1183,1185,3,1165,1168]
[null,"SBF1_v1_590008","_","Desulfosporosinus sp. SbF1","pfoA","pyruvate synthase","PYRUFLAVREDUCT-RXN ; RHEA:12768 ;",1,1.01196,59.83,0,1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",4,1185,1185,3,1168,1171]
[null,"CD630_26820","_","Clostridium difficile 630","pfo","Pyruvate-ferredoxin oxidoreductase","_",1.00844,1.01357,58.41,0,1,1,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"1c : Function from experimental evidences in the studied genus",1,1184,1185,1,1179,1179]
[null,"CLOAM0324","_","Candidatus Cloacamonas acidaminovorans Evry","_","putative pyruvate-ferredoxin oxidoreductase (por-like) or pyruvate-flavodoxin oxidoreductase (ydbK-like), 4Fe-4S domain","_",1.00506,1.01535,52.64,0,1,1,"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",1,1184,1185,1,1172,1173]
[null,"Ent638_2136","_","Enterobacter sp. 638","ydbK","Putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; 4Fe-4S cluster binding protein","_",1.01013,1.01959,47.37,0,1,1,"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)",5,1183,1185,1,1165,1174]
[null,"ECK1374","_","Escherichia coli K12","ydbK","putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; 4Fe-4S cluster binding protein","PYRUFLAVREDUCT-RXN ;",1.01097,1.02044,47.58,0,1,1,"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",5,1183,1185,1,1165,1174]
[null,"AZOLI_p30297","_","Azospirillum lipoferum 4B","_","putative pyruvate-ferredoxin/flavodoxin oxidoreductase","_",1.00506,1.01621,47.86,0,1,1,"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",8,1183,1185,1,1168,1172]
[null,"Spro_2604","_","Serratia proteamaculans 568","_","Putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; 4Fe-4S cluster binding protein (NifJ)","_",1.01097,1.01784,46.58,0,1,1,"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",5,1183,1185,1,1168,1177]
[null,"BN874v1_1210009","_","Candidatus Contendobacter odensis Run_B_J11","_","putative pyruvate-flavodoxin oxidoreductase (nifJ)","_",1.00168,1.00928,47.07,0,1,1,"_","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",3,1183,1185,4,1181,1194]
[null,"BN11v3_340013",null,"Tetrasphaera australiensis Ben110","_","putative pyruvate-flavodoxin oxidoreductase","_",1.00587,1.01266,46.25,0,1,1,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",8352652,"3 : Putative function from multiple computational evidences",7,1183,1185,8,1178,1193]
[null,"FRAAL3253","_","Frankia alni ACN14a","_","Pyruvate-flavodoxin oxidoreductase","_",1.00422,1.01277,46.13,0,1,1,"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)",6,1180,1185,4,1160,1175]
[null,"BN873v1_150048","_","Candidatus Competibacter denitrificans Run_A_D11","_","putative pyruvate-flavodoxin oxidoreductase (nifJ)","_",1.01174,1.01857,46.06,0,1,1,"_","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",3,1183,1185,4,1181,1193]
[null,"SBF1_v1_1030024",null,"Desulfosporosinus sp. SbF1","pfoA_3a","fragment of pyruvate synthase (part 1/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.58565,0.9844,62.1,0,3,1,"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",4,697,1185,3,694,705]
[null,"VCA0530","_","Vibrio cholerae N16961","_","putative Pyruvate-flavodoxin oxidoreductase","_",0.94515,1.038,39.29,0,1,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",9,1115,1185,6,1072,1079]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.38734,0.9766,62.96,0,2,1,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"2a : Function from experimental evidences in other organisms",1,459,1185,1,458,470]
[null,"SBF1_v1_1030023",null,"Desulfosporosinus sp. SbF1","pfoA_3b","fragment of pyruvate synthase (part 2/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.39916,1.01285,58.14,{"v":6E-175,"d":"6.00E-175"},5,1,"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",716,1185,1185,1,463,467]
[null,"NBG4_v1_230036",null,"Candidatus Sulfobium mesophilum","nifJ","Pyruvate:ferredoxin oxidoreductase","PYRUFLAVREDUCT-RXN ;",0.22869,0.99632,54.61,{"v":2e-94,"d":"2.00E-94"},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",1,271,1185,1,271,272]
[]
["CLOSTRIBL6_v1_3009","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_12777",null,"Clostridiaceae BL-3","porC","Pyruvate synthase subunit PorC","PYRUFLAVREDUCT-RXN ; RHEA:12765 ;",0.98964,0.98964,69.11,{"v":7e-96,"d":"7.00E-96"},1,1,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","8620891, 7608066, 9495749","2a : Function from experimental evidences in other organisms",1,191,193,1,191,193]
[null,"NBG4_v1_970004",null,"Candidatus Sulfobium mesophilum","porC","Pyruvate synthase subunit PorC","PYRUFLAVREDUCT-RXN ; RHEA:12765 ;",1,1.01047,49.22,{"v":3e-61,"d":"3.00E-61"},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",2,193,193,1,191,191]
[null,"HELPY_1077",null,"Helicobacter pylori B38","porG","Pyruvate synthase subunit porC (Pyruvate oxidoreductase gamma chain) (POR) (Pyruvic-ferredoxin oxidoreductase subunit gamma)","_",0.98446,1.02151,39.47,{"v":2E-35,"d":"2.00E-35"},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",7,191,193,3,186,186]
[null,"MGMSRv2_1071",null,"Magnetospirillum gryphiswaldense MSR-1 v2","porC","Pyruvate synthase subunit porC","_",0.97927,1.00532,35.98,{"v":9e-35,"d":"9.00E-35"},1,1,"_","1.2.7.1","1 : Unknown","_","e : enzyme",8688087,"2a : Function from experimental evidences in other organisms",5,193,193,1,180,188]
[]
["CLOSTRIBL6_v1_3010","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_12776",null,"Clostridiaceae BL-3","porD","Pyruvate synthase subunit PorD","PYRUFLAVREDUCT-RXN ; RHEA:12765 ;",0.88235,0.91837,50,{"v":9e-28,"d":"9.00E-28"},1,1,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","8620891, 7608066, 9495749","2a : Function from experimental evidences in other organisms",11,100,102,10,98,98]
[null,"NBG4_v1_970003",null,"Candidatus Sulfobium mesophilum","porD","Pyruvate synthase subunit PorD","PYRUFLAVREDUCT-RXN ; RHEA:12768 ;",0.91176,0.95876,47.31,{"v":5e-26,"d":"5.00E-26"},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",14,102,102,6,97,97]
[]
["CLOSTRIBL6_v1_3011","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_12775",null,"Clostridiaceae BL-3","porA","Pyruvate synthase subunit PorA","RHEA:12765 ;",1.00512,1.00512,58.78,{"v":5e-154,"d":"5.00E-154"},1,1,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","8620891, 7608066, 9495749","2a : Function from experimental evidences in other organisms",1,391,391,1,391,391]
[null,"NBG4_v1_970002",null,"Candidatus Sulfobium mesophilum","porA","Pyruvate synthase subunit PorA","PYRUFLAVREDUCT-RXN ; RHEA:12768 ;",0.98724,0.98977,49.87,{"v":1e-132,"d":"1.00E-132"},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",7,391,391,7,392,392]
[null,"HELPY_1079",null,"Helicobacter pylori B38","porA","Pyruvate synthase subunit porA (Pyruvate oxidoreductase alpha chain) (POR) (Pyruvic-ferredoxin oxidoreductase subunit alpha)","_",0.92383,0.96164,43.09,{"v":2E-95,"d":"2.00E-95"},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",9,380,391,15,389,407]
[null,"MGMSRv2_1070",null,"Magnetospirillum gryphiswaldense MSR-1 v2","porA","Pyruvate synthase subunit porA","_",0.93095,0.94057,40.38,{"v":5e-77,"d":"5.00E-77"},1,1,"_","1.2.7.1","1 : Unknown","_","e : enzyme","16980466, 8620891","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,367,391,3,363,387]
[null,"NIDE3874",null,"Candidatus Nitrospira defluvii","vorA","2-ketoisovalerate ferredoxin reductase, alpha subunit","_",0.92718,0.97698,35.34,{"v":6e-69,"d":"6.00E-69"},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)",5,382,391,4,381,412]
[null,"MAGMOv5_1648",null,"Magnetotactic ovoidal bacterium MO-1","_","Putative Pyruvate flavodoxin/ferredoxin oxidoreductase alfa subunit","_",0.57755,1,35.29,{"v":2e-57,"d":"2.00E-57"},1,2,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,373,391,16,403,677]
[]
["CLOSTRIBL6_v1_3012","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_12774",null,"Clostridiaceae BL-3","porB","Pyruvate synthase subunit PorB","RHEA:12765 ;",0.99355,0.99676,62.99,{"v":6E-152,"d":"6.00E-152"},1,1,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","8620891, 7608066, 9495749","2a : Function from experimental evidences in other organisms",1,308,310,1,307,309]
[null,"NBG4_v1_970001",null,"Candidatus Sulfobium mesophilum","porB","Pyruvate synthase subunit PorB","PYRUFLAVREDUCT-RXN ; RHEA:12765 ;",0.93226,0.98635,59.52,{"v":1e-124,"d":"1.00E-124"},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",5,293,310,7,292,293]
[null,"HELPY_1081",null,"Helicobacter pylori B38","porB","Pyruvate synthase subunit porB (Pyruvate oxidoreductase beta chain) (POR) (Pyruvic-ferredoxin oxidoreductase subunit beta)","_",0.96178,0.97419,45.7,{"v":8e-95,"d":"8.00E-95"},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",5,304,310,8,306,314]
[null,"MGMSRv2_1069",null,"Magnetospirillum gryphiswaldense MSR-1 v2","porB","Pyruvate synthase subunit porB","_",0.84098,0.8871,47.27,{"v":6e-83,"d":"6.00E-83"},1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme",8688087,"2a : Function from experimental evidences in other organisms",11,282,310,11,276,327]
[null,"SCFA_v1_3810002",null,"Ca. Propionivorax syntrophicum F70","porB","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit","_",0.99678,1,40.97,{"v":2e-69,"d":"2.00E-69"},1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,309,310,1,295,311]
[null,"NIDE3873",null,"Candidatus Nitrospira defluvii","vorB","2-ketoisovalerate ferredoxin reductase, beta subunit","_",0.94231,0.94839,40.82,{"v":1E-62,"d":"1.00E-62"},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)",12,301,310,16,304,312]
[]
["CLOSTRIBL6_v1_0126","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,"CLOSTRIBL4_v1_1869",null,"Clostridiales BL-4","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.99283,0.9964,72.56,{"v":3e-146,"d":"3.00E-146"},1,1,"_","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,277,278,1,277,279]
[null,"CLOSTRIBL3_v1_20313","_","Clostridiaceae BL-3","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.99291,1.00719,60.71,{"v":3e-114,"d":"3.00E-114"},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",2,277,278,3,280,282]
[null,"CD630_10580",null,"Clostridium difficile 630","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",1.00356,1.01439,55.32,{"v":7e-98,"d":"7.00E-98"},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",1,278,278,1,280,281]
[null,"AZOLI_p50301","_","Azospirillum lipoferum 4B","hbdA1","3-hydroxybutyryl-CoA dehydrogenase","_",0.9589,1.00719,50.71,{"v":2E-90,"d":"2.00E-90"},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",2,278,278,6,284,292]
[null,"BRADO3444","_","Bradyrhizobium sp. ORS278","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.98587,1.0036,52.33,{"v":5e-89,"d":"5.00E-89"},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",3,278,278,5,282,283]
[null,"AZCBGv1_p190002","_","Azospirillum brasilense CBG497","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.96233,1.01079,50.18,{"v":1e-88,"d":"1.00E-88"},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",2,278,278,6,284,292]
[null,"MGMSRv2_1554","_","Magnetospirillum gryphiswaldense MSR-1 v2","mmgB","3-hydroxybutyryl-CoA dehydrogenase,containing NAD(P)-binding domain","_",0.92739,1.01079,50.89,{"v":5e-87,"d":"5.00E-87"},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)",2,278,278,17,295,303]
[null,"NBG4_v1_200002",null,"Candidatus Sulfobium mesophilum","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:22432 ;",0.98936,1.0036,48.03,{"v":6e-87,"d":"6.00E-87"},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",2,277,278,5,281,282]
[null,"BSU24160",null,"Bacillus subtilis 168","mmgB","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.97213,1.0036,49.1,{"v":8e-87,"d":"8.00E-87"},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",2,277,278,5,282,287]
[null,"BBta_4257","_","Bradyrhizobium sp. BTAi1","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.97842,1.00369,51.84,{"v":8e-85,"d":"8.00E-85"},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",11,278,278,1,270,271]
[null,"PSHAa0399","_","Pseudoalteromonas haloplanktis TAC125","bhbD","3-hydroxybutyryl-CoA dehydrogenase (Beta- hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",1,1.01079,49.11,{"v":5e-84,"d":"5.00E-84"},1,1,"_","1.1.1.157","unknown","_","e : enzyme",8001771,"2a : Function from experimental evidences in other organisms",1,277,278,1,281,281]
[null,"BN381v2_100132","_","Candidatus Microthrix parvicella RN1","_","putative dehydrogenase","_",0.92409,1.00719,48.93,{"v":1e-81,"d":"1.00E-81"},1,1,"_","_","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","12846838, 8001771, 1699931","3 : Putative function from multiple computational evidences",2,278,278,24,302,303]
[null,"PSEEN3198",null,"Pseudomonas entomophila L48","paaH","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.99281,1.00364,47.83,{"v":1e-81,"d":"1.00E-81"},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)",5,277,278,1,275,275]
[null,"RALTA_A0220","_","Cupriavidus taiwanensis LMG19424","_","3-HYDROXYBUTYRYL-COA DEHYDROGENASE","_",0.98592,1.00719,47.14,{"v":2e-80,"d":"2.00E-80"},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)",3,278,278,6,283,284]
[null,"CMR15v5_0701","_","Ralstonia solanacearum CMR15","_","3-HYDROXYBUTYRYL-COA DEHYDROGENASE","_",0.98239,1.0036,48.03,{"v":3e-80,"d":"3.00E-80"},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)",3,277,278,6,282,284]
[null,"BDBv6_40067","_","Blood disease bacterium R229","_","3-HYDROXYBUTYRYL-COA DEHYDROGENASE","_",0.97887,1,47.84,{"v":3e-80,"d":"3.00E-80"},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)",3,277,278,6,282,284]
[null,"Rmet_0212","_","Cupriavidus metallidurans CH34","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.98239,1.0036,46.95,{"v":4e-80,"d":"4.00E-80"},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",3,278,278,6,283,284]
[null,"Mchl_1824","_","Methylobacterium extorquens CM4","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.94881,1,48.56,{"v":1E-79,"d":"1.00E-79"},1,1,"_","1.1.1.157","1 : Unknown","_","e : enzyme","2687255, 8655474","2a : Function from experimental evidences in other organisms",3,277,278,8,284,293]
[null,"METDI2209","_","Methylobacterium extorquens DM4","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.91749,1,48.56,{"v":2E-79,"d":"2.00E-79"},1,1,"_","1.1.1.157","1 : Unknown","_","e : enzyme","2687255, 8655474","2a : Function from experimental evidences in other organisms",3,277,278,18,294,303]
[null,"ADVE02_v2_10866","_","Methylosinus trichosporium OB3b","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.95563,1.00719,47.86,{"v":5E-79,"d":"5.00E-79"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,277,278,7,284,293]
[null,"RM41v1_680007","_","Sinorhizobium sp. Rm41","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta- hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.95862,1,48.2,{"v":1E-78,"d":"1.00E-78"},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)",3,277,278,5,281,290]
[null,"NIDE3117",null,"Candidatus Nitrospira defluvii","paaH","3-hydroxybutyryl-CoA dehydrogenase","_",0.94558,1,46.4,{"v":2e-76,"d":"2.00E-76"},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)",3,277,278,9,285,294]
[null,"BN12v2_1150036","_","Tetrasphaera japonica T1-X7","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD))","_",0.47297,1.00719,43.21,{"v":9e-72,"d":"9.00E-72"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,278,278,7,285,592]
[null,"BN11v3_1490005","_","Tetrasphaera australiensis Ben110","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD)","_",0.47466,1.01079,43.06,{"v":4e-71,"d":"4.00E-71"},1,1,"_","1.1.1.157","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",1444364,"3 : Putative function from multiple computational evidences",2,278,278,7,285,592]
[null,"FRAAL5917","_","Frankia alni ACN14a","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.4326,0.99281,46.74,{"v":1E-70,"d":"1.00E-70"},1,1,"1.7.1 : Unassigned reversible reactions ;","1.1.1.157","1 : Unknown","16.2 : Construct biomass (Anabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,277,278,1,275,638]
[null,"BN10v3_1170022","_","Tetrasphaera elongata Lp2","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD))","_",0.47547,1.01079,41.99,{"v":6e-70,"d":"6.00E-70"},1,1,"_","1.1.1.157","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",2,278,278,7,285,591]
[null,"BN13v1_460001","_","Tetrasphaera jenkinsii Ben74","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD))","_",0.47466,1.01079,43.06,{"v":6e-69,"d":"6.00E-69"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,278,278,7,285,592]
[null,"Npun_R3442","_","Nostoc punctiforme ATCC 29133; PCC 73102","_","3-hydroxybutyryl-CoA dehydrogenase","_",0.97222,1.00719,42.5,{"v":2e-67,"d":"2.00E-67"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,278,278,7,285,288]
[null,"BN874v1_720038","_","Candidatus Contendobacter odensis Run_B_J11","_","putative hydroxyacyl/hydroxybutyrl -CoA dehydrogenase","RXN0-2044 ;",0.94295,1.01079,42.35,{"v":4e-65,"d":"4.00E-65"},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",2,278,278,5,283,298]
[null,"NIDE3103",null,"Candidatus Nitrospira defluvii","_","putative 3-hydroxyacyl-CoA dehydrogenase","_",0.68796,1.00719,41.43,{"v":7e-65,"d":"7.00E-65"},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",2,278,278,5,281,407]
[null,"BN42v3_20192","_","Mycobacterium canettii STB-K","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98601,1.01439,41.49,{"v":2e-64,"d":"2.00E-64"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,277,278,7,286,286]
[null,"BN45v3_10517","_","Mycobacterium canettii STB-J","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98601,1.01439,40.78,{"v":7e-64,"d":"7.00E-64"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,277,278,7,286,286]
[null,"BN44v3_10518","_","Mycobacterium canettii STB-D","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98601,1.01439,41.13,{"v":7e-64,"d":"7.00E-64"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,277,278,7,286,286]
[null,"BN43v3_10507","_","Mycobacterium canettii STB-L","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98601,1.01439,41.13,{"v":7e-64,"d":"7.00E-64"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,277,278,7,286,286]
[null,"BN873v1_210050","_","Candidatus Competibacter denitrificans Run_A_D11","_","putative hydroxyacyl/hydroxybutyrl -CoA dehydrogenase","_",0.9396,1.00719,40.71,{"v":1E-61,"d":"1.00E-61"},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",2,278,278,5,283,298]
[null,"ABAYE2368",null,"Acinetobacter baumannii AYE","paaH","3-hydroxybutyryl-CoA dehydrogenase, phenylacetic acid degradation","_",0.54883,1.01079,40.57,{"v":3e-60,"d":"3.00E-60"},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",2,278,278,10,289,512]
[null,"AZOLI_p40260",null,"Azospirillum lipoferum 4B","paaH","3-hydroxybutyryl-CoA dehydrogenase","_",0.50722,1.01079,41.64,{"v":2e-59,"d":"2.00E-59"},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",3,278,278,10,288,554]
[null,"PP_3282",null,"Pseudomonas putida KT2440","paaH","3-hydroxyadipyl-CoA dehydrogenase","RXN0-2044 ; RHEA:16199 ;",0.55842,1.01439,40.43,{"v":4e-58,"d":"4.00E-58"},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",1,278,278,8,288,505]
[null,"PSEEN2793",null,"Pseudomonas entomophila L48","paaC","3-hydroxyacyl-CoA dehydrogenase phaC","_",0.55315,1.01079,39.15,{"v":3E-57,"d":"3.00E-57"},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",2,278,278,12,291,508]
[null,"NVIE_010920","_","Nitrososphaera viennensis EN76","_","hydroxyacyl-CoA dehydrogenase","_",0.73438,1.01439,39.72,{"v":7e-57,"d":"7.00E-57"},1,1,"_","1.1.1.35","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,277,278,9,287,384]
[null,"XDD1v4_3925",null,"Xenorhabdus doucetiae FRM16","paaH","protein PaaH; 3-hydroxybutyryl-CoA dehydrogenase","_",0.51005,1.0036,39.78,{"v":7e-56,"d":"7.00E-56"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,277,278,10,287,547]
[null,"THI_3559","_","Thiomonas sp. 3As","_","putative 3-hydroxybutyryl-CoA dehydrogenase PaaH","_",0.55118,1.00719,39.64,{"v":2E-55,"d":"2.00E-55"},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",2,277,278,10,288,508]
[null,"CLOSTRIBL4_v1_1158",null,"Clostridiales BL-4","hbd","3-hydroxybutyryl-CoA dehydrogenase","RXN-12570 ; RHEA:16200 ;",0.95623,1.02158,37.32,{"v":3e-55,"d":"3.00E-55"},2,3,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",3,278,278,9,292,297]
[null,"MGMSRv2_3175",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaH","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.55248,1.0036,39.07,{"v":4E-55,"d":"4.00E-55"},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",3,277,278,10,287,505]
[null,"THI_0464",null,"Thiomonas sp. 3As","_","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.55976,1.01079,39.15,{"v":3e-54,"d":"3.00E-54"},2,1,"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",2,278,278,12,290,502]
[null,"ACIAD1690",null,"Acinetobacter baylyi ADP1","dcaH","dehydrogenase","1.1.1.259-RXN ; METHELENE-THMPT-OXI-RXN ; RXN0-2044 ;",0.56238,1.02158,35.56,{"v":2E-52,"d":"2.00E-52"},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",2,277,278,7,285,505]
[null,"Spro_1832",null,"Serratia proteamaculans 568","paaH","3-hydroxyacyl-CoA dehydrogenase, NAD-binding","_",0.5501,1.00719,37.14,{"v":4E-52,"d":"4.00E-52"},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)",3,278,278,11,289,509]
[null,"ABAYE2306",null,"Acinetobacter baumannii AYE","dcaH","dehydrogenase","_",0.55819,1.01799,36.04,{"v":7e-52,"d":"7.00E-52"},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",3,277,278,8,285,507]
[null,"IBTHAUMv1_1140010","_","Ianthella basta symbiont thaum","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.85252,0.92578,39.66,{"v":7e-51,"d":"7.00E-51"},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)",3,234,278,6,241,256]
[null,"CLOSTRIBL3_v1_13113",null,"Clostridiaceae BL-3","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.98611,1.02158,37.68,{"v":7e-50,"d":"7.00E-50"},2,2,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 25112316","1c : Function from experimental evidences in the studied genus",2,277,278,5,287,288]
[null,"MARHY2087","_","Marinobacter hydrocarbonoclasticus ATCC 49840","fadB","bifunctional enzyme (PBE) (PBFE) [Includes: Enoyl-CoA hydratase ; 3,2-trans-enoyl-CoA isomerase ; 3-hydroxyacyl-CoA dehydrogenase ]","_",0.40057,1.00719,38.93,{"v":8e-50,"d":"8.00E-50"},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",2,277,278,293,567,699]
[null,"AZOLI_p30575","_","Azospirillum lipoferum 4B","pimF","Enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase","_",0.39463,1.0036,38.71,{"v":9e-50,"d":"9.00E-50"},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",2,277,278,307,581,707]
[null,"Rmet_4582","_","Cupriavidus metallidurans CH34","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)","_",0.4023,1.00719,40,{"v":6E-49,"d":"6.00E-49"},1,1,"_","1.1.1.35, 4.2.1.17","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,277,278,297,570,696]
[null,"METDI4031",null,"Methylobacterium extorquens DM4","_","putative fatty acid oxidation complex subunit alpha (enoyl-CoA hydratase and epimerase and isomerase ; 3-hydroxyacyl-CoA dehydrogenase) (fadJ-like; synonym yfcX)","_",0.38472,1.01439,37.23,{"v":3e-46,"d":"3.00E-46"},2,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17, 5.3.3.8, 5.1.2.3, 1.1.1.35","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",12535077,"3 : Putative function from multiple computational evidences",2,277,278,330,608,733]
[null,"plu3200","_","Photorhabdus luminescens TT01","fadJ","Anaerobic beta-oxidation complex II containing 3-hydroxyacyl-CoA dehydrogenase, putative beta-hydroxybutyryl-CoA epimerase, and enoyl-CoA hydratase activities; in FadR regulon (by similarity)","_",0.37685,1.00719,36.79,{"v":1e-45,"d":"1.00E-45"},1,1,"_","_","_","_","_","_","_",3,278,278,342,617,743]
[null,"VIBNIv4_A0766","_","Vibrio nigripulchritudo SFn1","fadJ","Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase ; 3-hydroxyacyl-CoA dehydrogenase]","_",0.39574,1.0036,36.2,{"v":1e-45,"d":"1.00E-45"},1,1,"1.1.2.4 : Anaerobic fatty acid oxidation pathway ; 7.1 : Cytoplasm ;","4.2.1.17, 5.1.2.3, 1.1.1.35","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","9205837, 9278503, 16738553, 12270828, 12535077","2a : Function from experimental evidences in other organisms",2,277,278,311,586,705]
[null,"MARHY2411",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","fadJ","Fatty acid oxidation complex subunit alpha","_",0.39804,1.02518,36.84,{"v":2E-45,"d":"2.00E-45"},2,1,"_","4.2.1.17, 1.1.1.35, 5.1.2.3","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,277,278,317,598,716]
[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)","_",0.40548,1.01079,38.79,{"v":4e-45,"d":"4.00E-45"},3,2,"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",2,277,278,294,567,693]
[null,"BBta_0817",null,"Bradyrhizobium sp. BTAi1","_","putative bifunctional anaerobic fatty acid oxidation complex protein (fadJ/fadB-like): enoyl-CoA hydratase/epimerase/isomerase ; 3-hydroxyacyl-CoA dehydrogenase","_",0.38806,1.02878,36.36,{"v":7E-45,"d":"7.00E-45"},3,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17, 1.1.1.35, 5.3.3.8","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,277,278,329,607,737]
[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","_",0.40404,1.00719,37.5,{"v":8e-45,"d":"8.00E-45"},3,1,"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",2,277,278,294,567,693]
[null,"Rmet_5110",null,"Cupriavidus metallidurans CH34","fadB1","short chain enoyl-CoA hydratase / 3-hydroxyacyl-CoA dehydrogenase","_",0.39021,1.0036,36.56,{"v":1e-44,"d":"1.00E-44"},2,2,"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)",2,277,278,313,587,715]
[null,"CMR15v5_2681",null,"Ralstonia solanacearum CMR15","fadB","fused 3-hydroxybutyryl-CoA epimerase, delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase, enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase","_",0.4026,1.0036,38.71,{"v":5e-44,"d":"5.00E-44"},3,2,"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",3,277,278,295,567,693]
[null,"PP_2136",null,"Pseudomonas putida KT2440","fadB","enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase","OHACYL-COA-DEHYDROG-RXN ; ENOYL-COA-HYDRAT-RXN ;",0.39161,1.00719,36.79,{"v":7e-43,"d":"7.00E-43"},3,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17, 1.1.1.35","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","12115060, 11251808","1b : Function from experimental evidences in the studied species",2,277,278,316,592,715]
[null,"ACIAD0335",null,"Acinetobacter baylyi ADP1","fadB","fatty oxidation complex alpha subunit [Includes: Enoyl-CoA hydratase ; Delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase ; 3-hydroxyacyl-CoA dehydrogenase; 3- hydroxybutyryl-CoA epimerase]","OHACYL-COA-DEHYDROG-RXN ; 3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; OHBUTYRYL-COA-EPIM-RXN ; METHYLACYLYLCOA-HYDROXY-RXN ; RXN-902 ; TIGLYLCOA-HYDROXY-RXN ; RXN0-5391 ; RXN0-5393 ; RXN-11662 ; 5.1.2.3-RXN ; RXN-12570 ; RXN-7931 ; ENOYL-COA-DELTA-ISOM-RXN ; ENOYL-COA-HYDRAT-RXN ; RHEA:23719 ; RHEA:21763 ; RHEA:22435 ; RHEA:17850 ; RHEA:34086 ; RHEA:31178 ; RHEA:31122 ; RHEA:30802 ; RHEA:16107 ;",0.3947,1.01799,37.1,{"v":1E-42,"d":"1.00E-42"},2,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17, 5.3.3.8, 1.1.1.35, 5.1.2.3","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","1699931, 1712230, 12115060, 1438362","2a : Function from experimental evidences in other organisms",2,277,278,317,593,717]
[null,"LMIv2_1447","_","Legionella micdadei","_","3-hydroxybutyryl-CoA epimerase","_",0.42645,1.03237,35.89,{"v":2e-42,"d":"2.00E-42"},1,1,"_","5.1.2.3","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,277,278,310,577,673]
[null,"VS_0041",null,"Vibrio tasmaniensis LGP32","_","3-hydroxybutyryl-CoA epimerase, Fatty acid oxidation complex subunit alpha","_",0.39142,1.01799,35.69,{"v":3e-42,"d":"3.00E-42"},2,1,"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",2,278,278,316,594,723]
[null,"SCFA_v1_1540002",null,"Ca. Phosphitivorax butyraticus R76","_","Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase / 3-hydroxyacyl-CoA dehydrogenase","_",0.35694,0.88849,35.63,{"v":4e-42,"d":"4.00E-42"},4,1,"_","1.1.1.35, 4.2.1.17, 5.1.2.3, 5.3.3.8","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,244,278,324,568,692]
[null,"VCR9J2v1_150068",null,"Vibrio crassostreae J2-9","fadB","Putative 3-hydroxybutyryl-CoA epimerase","OHBUTYRYL-COA-EPIM-RXN ; RHEA:21760 ;",0.39415,1.01799,36.04,{"v":6e-42,"d":"6.00E-42"},2,1,"1.1.2.6 : Aerobic fatty acid oxidation pathway ; 7.1 : Cytoplasm ;","5.1.2.3","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","1699931, 1712230, 2204034","2a : Function from experimental evidences in other organisms",2,277,278,319,595,718]
[null,"PSEEN3728",null,"Pseudomonas entomophila L48","fadB","fatty oxidation complex alpha subunit [Includes: Enoyl-CoA hydratase ; Delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase ; 3-hydroxyacyl-CoA dehydrogenase; 3- hydroxybutyryl-CoA epimerase]","_",0.38199,1.00719,36.07,{"v":2E-41,"d":"2.00E-41"},3,1,"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","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,277,278,334,610,733]
[null,"MARHY2136",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","fadB","Fatty acid oxidation complex subunit alpha","_",0.39161,1.00719,35.36,{"v":1e-40,"d":"1.00E-40"},3,1,"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",11251808,"2a : Function from experimental evidences in other organisms",5,277,278,319,592,715]
[null,"BRADO0981",null,"Bradyrhizobium sp. ORS278","pimF","Enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase","_",0.40746,1.02158,36.62,{"v":5e-38,"d":"5.00E-38"},4,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17, 1.1.1.35","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme",15758219,"2a : Function from experimental evidences in other organisms",2,277,278,297,564,697]
[]
["CLOSTRIBL6_v1_0127","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,"CLOSTRIBL4_v1_1867",null,"Clostridiales BL-4","thlA","acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.93365,0.99747,70.05,0,1,1,"_","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","7867955, 11075929","2a : Function from experimental evidences in other organisms",1,394,395,27,418,422]
[null,"Rmet_1357",null,"Cupriavidus metallidurans CH34","phaA","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.98734,0.99237,61.79,{"v":8e-172,"d":"8.00E-172"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,394,395,4,391,393]
[null,"RALTA_A1351","_","Cupriavidus taiwanensis LMG19424","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.98734,0.99237,60.77,{"v":2E-167,"d":"2.00E-167"},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",5,394,395,4,391,393]
[null,"CLOSTRIBL3_v1_12838","_","Clostridiaceae BL-3","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99241,1,60.71,{"v":4e-166,"d":"4.00E-166"},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",3,394,395,2,391,392]
[null,"CMR15v5_2547","_","Ralstonia solanacearum CMR15","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.98734,0.99237,59.74,{"v":6e-164,"d":"6.00E-164"},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",5,394,395,4,391,393]
[null,"PP_4636","_","Pseudomonas putida KT2440","yqeF","acetyl-CoA acetyltransferase","METHYLACETOACETYLCOATHIOL-RXN ; RXN-12561 ; ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",0.98734,0.9949,60.26,{"v":5e-163,"d":"5.00E-163"},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",5,394,395,4,391,392]
[null,"THI_1641","_","Thiomonas sp. 3As","phbA1","acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.98734,0.9949,59.74,{"v":2e-161,"d":"2.00E-161"},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",5,394,395,4,391,392]
[null,"PSEEN4635","_","Pseudomonas entomophila L48","phbA","acetyl-CoA acetyltransferase","_",0.96069,0.98987,58.31,{"v":8e-161,"d":"8.00E-161"},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",4,394,395,17,405,407]
[null,"HEAR0577","_","Herminiimonas arsenicoxydans","phbA","acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.98246,0.99241,58.16,{"v":3E-158,"d":"3.00E-158"},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)",3,394,395,10,398,399]
[null,"MARHY3102","_","Marinobacter hydrocarbonoclasticus ATCC 49840","phbA","acetyl-CoA acetyltransferase with thiolase domain, PHB biosynthesis","_",0.99241,1,56.63,{"v":3E-157,"d":"3.00E-157"},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",3,394,395,2,391,392]
[null,"Spro_0592","_","Serratia proteamaculans 568","atoB","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.97756,0.99241,56.63,{"v":1e-151,"d":"1.00E-151"},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)",3,394,395,10,399,401]
[null,"CD630_26760","_","Clostridium difficile 630","thlA2","Acetoacetyl-CoA thiolase 2","_",0.98987,0.99745,55.75,{"v":1e-149,"d":"1.00E-149"},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",3,393,395,2,390,392]
[null,"METDI4272","_","Methylobacterium extorquens DM4","phaA","beta-ketothiolase","_",0.99241,0.99492,55.87,{"v":1e-148,"d":"1.00E-148"},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",3,394,395,5,392,394]
[null,"AZOLI_2388","_","Azospirillum lipoferum 4B","phbA3","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98987,1,56.27,{"v":8e-147,"d":"8.00E-147"},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",4,394,395,3,389,391]
[null,"BRADO0562","_","Bradyrhizobium sp. ORS278","phbA","acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.99494,0.99746,56.49,{"v":1E-146,"d":"1.00E-146"},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)",1,393,395,3,391,394]
[null,"CD630_10590",null,"Clostridium difficile 630","thlA1","Acetoacetyl-CoA thiolase 1","_",0.99241,1.00256,55.36,{"v":1E-146,"d":"1.00E-146"},2,1,"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",3,394,395,2,390,391]
[null,"BN873v1_100077","_","Candidatus Competibacter denitrificans Run_A_D11","phaA","Acetyl-CoA acetyltransferase","_",0.99241,0.99746,53.32,{"v":3e-144,"d":"3.00E-144"},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",3,394,395,2,391,393]
[null,"BN874v1_850028","_","Candidatus Contendobacter odensis Run_B_J11","phaA","Acetyl-CoA acetyltransferase","_",0.99241,0.99746,53.83,{"v":5e-144,"d":"5.00E-144"},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)",3,394,395,2,391,393]
[null,"ECK2842","_","Escherichia coli K12","yqeF","Acetyl-CoA acetyltransferase","_",0.99241,0.99746,53.06,{"v":1e-143,"d":"1.00E-143"},1,1,"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",3,394,395,2,390,393]
[null,"RM41v1_110012","_","Sinorhizobium sp. Rm41","phbA","acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98734,0.99237,54.1,{"v":4e-139,"d":"4.00E-139"},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",5,394,395,6,391,393]
[null,"MGMSRv2_1838","_","Magnetospirillum gryphiswaldense MSR-1 v2","phbA","acetyl-CoA acetyltransferase containing thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98734,1,53.85,{"v":4e-139,"d":"4.00E-139"},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)",5,394,395,4,389,390]
[null,"NT26v4_3604","_","Rhizobium sp. NT-26","phbA","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98734,0.99237,53.33,{"v":4e-137,"d":"4.00E-137"},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)",5,394,395,6,391,393]
[null,"AZOLI_p10676","_","Azospirillum lipoferum 4B","phbA2","Acetyl-CoA acetyltransferase with thiolase domain (Beta-ketothiolase)","_",1,1.00509,50.63,{"v":4e-131,"d":"4.00E-131"},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",1,394,395,1,391,393]
[null,"HELPY_0683","_","Helicobacter pylori B38","atoB","Acetyl coenzyme A acetyltransferase","_",0.98987,1,49.62,{"v":1E-127,"d":"1.00E-127"},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",4,394,395,3,389,391]
[null,"NBG4_v1_200004",null,"Candidatus Sulfobium mesophilum","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99747,0.99747,47.97,{"v":3e-127,"d":"3.00E-127"},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",1,394,395,7,394,395]
[null,"SCFA_v1_120020",null,"Ca. Phosphitivorax anaerolimi F81","yqeF","Acetyl-CoA acetyltransferase","_",0.99241,1,50.26,{"v":4e-126,"d":"4.00E-126"},3,1,"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",3,394,395,2,390,392]
[null,"NIDE3116",null,"Candidatus Nitrospira defluvii","atoB","Acetyl-CoA acetyltransferase","_",0.98481,0.98731,49.1,{"v":5e-124,"d":"5.00E-124"},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",6,394,395,8,393,394]
[null,"RPSI07_1730",null,"Ralstonia solanacearum PSI07","phaA","acetyl-CoA acetyltransferase, thiolase-like","_",1,1.00254,48.1,{"v":1e-123,"d":"1.00E-123"},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)",1,394,395,1,392,394]
[null,"Rmet_1362",null,"Cupriavidus metallidurans CH34","bktB","acetyl-CoA acetyltransferase","_",1,1.00254,49.37,{"v":1e-122,"d":"1.00E-122"},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",1,394,395,1,392,394]
[null,"VIBNIv4_B1306","_","Vibrio nigripulchritudo SFn1","phbA","acetyl-CoA acetyltransferase","_",1.00499,1.02025,47.89,{"v":4e-122,"d":"4.00E-122"},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",1,394,395,1,399,401]
[null,"VIBNIv4_A1234","_","Vibrio nigripulchritudo SFn1","phbA","Acetyl-CoA acetyltransferase","_",0.99747,1,44.92,{"v":5e-121,"d":"5.00E-121"},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",2,395,395,3,392,394]
[null,"PSEEN3197",null,"Pseudomonas entomophila L48","_","putative Acetoacetyl-CoA thiolase","_",1.00253,1.00508,47.47,{"v":1e-120,"d":"1.00E-120"},2,1,"1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.9","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,394,395,5,392,394]
[null,"CLOSTRIBL4_v1_1159",null,"Clostridiales BL-4","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",1.00756,1.01266,48.5,{"v":4e-118,"d":"4.00E-118"},2,2,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","7867955, 11075929, 11466286, 1685080","2a : Function from experimental evidences in other organisms",1,394,395,1,395,397]
[null,"METUNv2_520573","_","Methyloversatilis universalis FAM5","phbA","Acetyl-CoA acetyltransferase","_",0.99747,0.99747,47.46,{"v":6e-117,"d":"6.00E-117"},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",2,394,395,4,393,395]
[null,"BN424_3179","_","Carnobacterium maltaromaticum LMA28 v1","thlA","Acetoacetyl-CoA thiolase","METHYLACETOACETYLCOATHIOL-RXN ; RXN-12561 ; ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99241,1.00771,47.7,{"v":1e-116,"d":"1.00E-116"},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)",3,394,395,2,387,389]
[null,"BN381v2_150043","_","Candidatus Microthrix parvicella RN1","phaA","acetyl-CoA acetyltransferase","_",0.98481,0.98982,49.61,{"v":3e-115,"d":"3.00E-115"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","18246303, 10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",6,393,395,5,390,393]
[null,"VS_II0585","_","Vibrio tasmaniensis LGP32","_","Acetyl-CoA C acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",1.00248,1.02278,45.05,{"v":1e-112,"d":"1.00E-112"},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",1,394,395,1,399,403]
[null,"BSU24170",null,"Bacillus subtilis 168","mmgA","degradative acetoacetyl-CoA thiolase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99494,1,43.26,{"v":7e-112,"d":"7.00E-112"},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",3,395,395,2,392,393]
[null,"CLOSTRIBL3_v1_13111",null,"Clostridiaceae BL-3","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",1.00759,1.0179,45.73,{"v":2e-111,"d":"2.00E-111"},2,2,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","7867955, 11075929, 11466286, 1685080","1c : Function from experimental evidences in the studied genus",3,395,395,2,391,391]
[null,"MARHY1170",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","thlA","acetyl-CoA acetyltransferase, Acetoacetyl-CoA thiolase","_",0.98987,0.99491,46.8,{"v":8e-111,"d":"8.00E-111"},2,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",7867955,"2a : Function from experimental evidences in other organisms",5,395,395,6,392,393]
[null,"BN12v2_3170003","_","Tetrasphaera japonica T1-X7","phaA","acetyl-CoA acetyltransferase (fadA) (Acetoacetyl-CoA thiolase) (beta-ketothiolase)","_",0.98744,0.99494,47.33,{"v":1e-110,"d":"1.00E-110"},1,1,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",5,395,395,7,395,398]
[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 ;",0.99241,1.00256,44.64,{"v":1e-109,"d":"1.00E-109"},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",4,395,395,3,390,391]
[null,"CMR15v5_0670",null,"Ralstonia solanacearum CMR15","_","putative acetyl-CoA acetyltransferase with thiolase domain","_",1.00253,1.00763,44.19,{"v":4E-109,"d":"4.00E-109"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,395,395,1,392,393]
[null,"BTCD_v1_1714","_","Brochothrix thermosphacta CD337","mevB","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.98987,1.00773,46.55,{"v":4E-109,"d":"4.00E-109"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme",7763384,"2a : Function from experimental evidences in other organisms",3,393,395,2,385,388]
[null,"ABAYE2367",null,"Acinetobacter baumannii AYE","paaJ","beta-ketoadipyl CoA thiolase with thiolase-like domain, phenylacetic acid degradation","_",0.99502,1.01266,47.5,{"v":2e-108,"d":"2.00E-108"},2,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","1 : Unknown","_","e : enzyme",9748275,"2b : Function from indirect experimental evidences (e.g. phenotypes)",3,394,395,2,399,402]
[null,"THI_0462",null,"Thiomonas sp. 3As","pcaF1","Beta-ketoadipyl CoA thiolase","_",0.9925,1.00506,46.85,{"v":2e-108,"d":"2.00E-108"},2,2,"1 : Metabolism ;","2.3.1.-","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",7961399,"2a : Function from experimental evidences in other organisms",7,394,395,6,398,400]
[null,"RCFBPv4_3139",null,"Ralstonia solanacearum CFBP2957","_","putative acetyl-CoA acetyltransferase with thiolase domain","_",1.00253,1.00763,44.19,{"v":1E-107,"d":"1.00E-107"},3,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,395,395,1,392,393]
[null,"RPSI07_3138",null,"Ralstonia solanacearum PSI07","_","putative acetyl-CoA acetyltransferase with thiolase domain","_",1.00253,1.00763,43.69,{"v":3e-107,"d":"3.00E-107"},3,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,395,395,1,392,393]
[null,"BN13v1_460011","_","Tetrasphaera jenkinsii Ben74","_","putative Acetyl-CoA acetyltransferase (beta-ketothiolase) (phaA)","_",0.98744,0.99494,47.33,{"v":1e-106,"d":"1.00E-106"},1,1,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","3 : Putative function from multiple computational evidences",5,395,395,7,395,398]
[null,"AZOLI_p40258",null,"Azospirillum lipoferum 4B","paaJ","beta-ketoadipyl CoA thiolase","_",0.99502,1.01266,44.5,{"v":2e-106,"d":"2.00E-106"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",3,394,395,2,400,402]
[null,"LEPBIa0355","_","Leptospira biflexa serovar Patoc Patoc 1","thiL1","Putative acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.99494,1,44.27,{"v":7E-105,"d":"7.00E-105"},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",3,394,395,2,389,393]
[null,"THI_3549",null,"Thiomonas sp. 3As","pcaF2","Beta-ketoadipyl CoA thiolase","_",0.99257,1.01519,44.14,{"v":1e-104,"d":"1.00E-104"},3,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","10766858, 12846838, 7961399, 9748275","2a : Function from experimental evidences in other organisms",2,394,395,4,402,404]
[null,"BN11v3_1860009","_","Tetrasphaera australiensis Ben110","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.98747,0.99747,47.46,{"v":6e-104,"d":"6.00E-104"},1,1,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",5,395,395,8,396,399]
[null,"MGMSRv2_3177",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaE","beta-ketoadipyl CoA thiolase","_",0.99501,1.01013,44.11,{"v":1e-103,"d":"1.00E-103"},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",5,394,395,4,399,401]
[null,"NIDE3104",null,"Candidatus Nitrospira defluvii","fadA","3-ketoacyl-CoA thiolase","_",1,1.00253,43.18,{"v":1e-103,"d":"1.00E-103"},2,2,"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)",3,394,395,2,394,396]
[null,"Atu3475",null,"Agrobacterium tumefaciens C58","fadAx","acetyl-CoA C-acetyltransferase","_",0.94903,0.98987,45.52,{"v":2e-102,"d":"2.00E-102"},1,1,"1 : Metabolism ;","_","2 : Cytoplasmic","_","e : enzyme",11251808,"2b : Function from indirect experimental evidences (e.g. phenotypes)",5,394,395,32,410,412]
[null,"pRALTA_0081","_","Cupriavidus taiwanensis LMG19424","_","acetyl-CoA acetyltransferase","_",0.9875,1,44.05,{"v":1e-101,"d":"1.00E-101"},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)",5,395,395,9,399,400]
[null,"PSEEN2795",null,"Pseudomonas entomophila L48","pcaF-2","beta-ketoadipyl CoA thiolase","_",0.97783,1.00506,44.58,{"v":5e-101,"d":"5.00E-101"},5,2,"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",6,394,395,10,404,406]
[null,"BN45v3_30404","_","Mycobacterium canettii STB-J","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98734,1.00257,45.9,{"v":2E-100,"d":"2.00E-100"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,393,395,1,386,389]
[null,"BN42v3_21228","_","Mycobacterium canettii STB-K","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98734,1.00257,46.15,{"v":2E-100,"d":"2.00E-100"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,393,395,1,386,389]
[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 ;",0.97783,1.00506,44.33,{"v":3e-100,"d":"3.00E-100"},5,2,"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",6,394,395,10,404,406]
[null,"BN44v3_11488","_","Mycobacterium canettii STB-D","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98734,1.00257,45.9,{"v":5e-100,"d":"5.00E-100"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,393,395,1,386,389]
[null,"AZOLI_p10029",null,"Azospirillum lipoferum 4B","atoB","acetyl-CoA acetyltransferase with thiolase domain","_",1,1.00509,45.57,{"v":5e-100,"d":"5.00E-100"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1 : Carbon compound utilization ; 1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ; 6.2 : Amino acids and amines ;","e : enzyme",7867955,"2a : Function from experimental evidences in other organisms",1,394,395,1,391,393]
[null,"FRAAL5910","_","Frankia alni ACN14a","atoB","acetyl-CoA acetyltransferase with thiolase domain","_",1.00253,1.00253,45.71,{"v":6e-100,"d":"6.00E-100"},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)",1,395,395,1,392,395]
[null,"RALTA_A0113",null,"Cupriavidus taiwanensis LMG19424","_","putative acetyl-CoA acetyltransferase with thiolase domain","_",0.99747,1.0051,41.37,{"v":8e-100,"d":"8.00E-100"},3,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,395,395,2,391,392]
[null,"BN43v3_30420","_","Mycobacterium canettii STB-L","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98734,1.00257,45.9,{"v":1E-99,"d":"1.00E-99"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,393,395,1,386,389]
[null,"ECK1394",null,"Escherichia coli K12","paaE","beta-ketoadipyl CoA thiolase","RXN-3641 ; RXN0-6512 ;",0.99751,1.01266,43.5,{"v":1E-99,"d":"1.00E-99"},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",3,394,395,2,399,401]
[null,"XDD1v4_3927",null,"Xenorhabdus doucetiae FRM16","paaJ","protein PaaJ; Beta-ketoadipyl-CoA thiolase","_",0.98515,1.00759,43.47,{"v":3e-97,"d":"3.00E-97"},1,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.174","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",7,394,395,6,401,404]
[null,"ACIAD1689",null,"Acinetobacter baylyi ADP1","dcaF","beta-ketoadipyl CoA thiolase","2.3.1.155-RXN ; KETOACYLCOATHIOL-RXN ; RXN-3641 ;",0.98005,0.99494,41.48,{"v":3e-94,"d":"3.00E-94"},5,2,"_","2.3.1.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921, 11571189","1a : Function from experimental evidences in the studied strain",11,394,395,10,398,401]
[null,"ABAYE2307",null,"Acinetobacter baumannii AYE","dcaF","beta-ketoadipyl CoA thiolase","_",0.98005,0.99494,40.71,{"v":4e-93,"d":"4.00E-93"},5,2,"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",11,394,395,10,398,401]
[null,"Pars_0309","_","Pyrobaculum arsenaticum DSM 13514","thlA","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.97297,1.00253,42.17,{"v":4E-92,"d":"4.00E-92"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11075929, 11466286, 1685080, 7867955","2a : Function from experimental evidences in other organisms",4,395,395,15,406,407]
[null,"BN11v3_1360003",null,"Tetrasphaera australiensis Ben110","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase)","_",1.00253,1.02326,40.66,{"v":5e-89,"d":"5.00E-89"},2,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",17189250,"3 : Putative function from multiple computational evidences",2,395,395,3,386,387]
[null,"THI_3278",null,"Thiomonas sp. 3As","phbA2","acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",1.00253,1.0102,42.42,{"v":2E-87,"d":"2.00E-87"},4,1,"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",1,395,395,1,391,392]
[null,"MARHY2135",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","fadA","3-ketoacyl-CoA thiolase; (thiolase I, acetyl-CoA transferase), in complex with FadB catalyzes Catalyzes the final step of fatty acid oxidation","_",1.00759,1.0179,40.7,{"v":1e-86,"d":"1.00E-86"},5,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 7.1 : Cytoplasm ;","2.3.1.16","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",12115060,"2a : Function from experimental evidences in other organisms",3,394,395,6,389,391]
[null,"RALTA_A1469",null,"Cupriavidus taiwanensis LMG19424","_","putative 3-ketoacyl-CoA thiolase / acetyl-CoA acetyltransferase","_",1.02278,1.03061,39.6,{"v":4e-84,"d":"4.00E-84"},4,1,"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",4,395,395,3,391,392]
[null,"CMR15v5_2683",null,"Ralstonia solanacearum CMR15","_","acetyl-CoA acetyltransferase","_",1.02278,1.03061,38.86,{"v":6e-83,"d":"6.00E-83"},4,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,395,395,3,391,392]
[null,"Rmet_1853",null,"Cupriavidus metallidurans CH34","atoB","acetyl-CoA acetyltransferase / thiolase","_",1.02278,1.03061,39.11,{"v":3e-81,"d":"3.00E-81"},5,1,"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",4,395,395,3,391,392]
[null,"HEAR2836",null,"Herminiimonas arsenicoxydans","fadA","3-ketoacyl-CoA thiolase (Fatty acid oxidation complex beta subunit) (Beta-ketothiolase) (Acetyl-CoA acyltransferase)","_",1.03266,1.04051,39.9,{"v":5e-81,"d":"5.00E-81"},2,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.16","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","11356168, 11696182, 14630959, 15979881, 9490742","2a : Function from experimental evidences in other organisms",1,394,395,1,396,398]
[null,"CMR15v5_0432",null,"Ralstonia solanacearum CMR15","fadA","3-ketoacyl-CoA thiolase (Fatty acid oxidation complex beta subunit) (Beta-ketothiolase) (Acetyl-CoA acyltransferase)","_",1.00251,1.01266,39.5,{"v":2e-80,"d":"2.00E-80"},5,2,"1 : Metabolism ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.16","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","11356168, 11696182, 14630959, 15979881, 9490742","2a : Function from experimental evidences in other organisms",7,394,395,10,397,399]
[null,"BN11v3_1350015",null,"Tetrasphaera australiensis Ben110","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",1.00985,1.03797,40,{"v":1E-79,"d":"1.00E-79"},3,2,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",4,394,395,3,403,406]
[null,"PSEEN3727",null,"Pseudomonas entomophila L48","fadA","3-ketoacyl-CoA thiolase (Fatty oxidation complex beta subunit) (Beta-ketothiolase) (Acetyl-CoA acyltransferase)","_",1.00759,1.0179,39.95,{"v":1E-79,"d":"1.00E-79"},6,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16","Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,394,395,6,389,391]
[null,"AZCBGv1_p150132","_","Azospirillum brasilense CBG497","phaA","Beta-ketothiolase (acetyl-CoA acetyltransferase with thiolase domain)(Acetyl-CoA C-acyltransferase)","_",0.99241,1.01292,39.29,{"v":2E-79,"d":"2.00E-79"},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",5,394,395,13,385,387]
[null,"BRADO0983",null,"Bradyrhizobium sp. ORS278","pimB","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",1.01772,1.01772,38.56,{"v":4e-77,"d":"4.00E-77"},5,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",2883171,"2a : Function from experimental evidences in other organisms",6,395,395,5,393,395]
[null,"BBta_7072",null,"Bradyrhizobium sp. BTAi1","pimB","Acetyl-CoA acetyltransferase with thiolase domain","_",1.02278,1.02278,38.12,{"v":1e-75,"d":"1.00E-75"},6,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",6,395,395,5,393,395]
[null,"ACIAD0334",null,"Acinetobacter baylyi ADP1","fadA","3-ketoacyl-CoA thiolase (Fatty oxidation complex beta subunit) (Beta-ketothiolase) (Acetyl-CoA acyltransferase)","2.3.1.155-RXN ; KETOACYLCOATHIOL-RXN ; METHYLACETOACETYLCOATHIOL-RXN ;",1.00253,1.01538,37.37,{"v":1e-74,"d":"1.00E-74"},8,2,"1.1.2 : fatty acids ;","2.3.1.16","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,394,395,7,388,390]
[null,"MARHY2410",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","paaJ","ketoadipyl CoA thiolase subunit","_",1.03234,1.05063,38.8,{"v":9e-74,"d":"9.00E-74"},6,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.16","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,395,1,400,402]
[null,"Atu0502",null,"Agrobacterium tumefaciens C58","fadA","acetyl-CoA acetyltransferase","_",1,1.01772,36.07,{"v":6e-69,"d":"6.00E-69"},2,2,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",16,394,395,17,400,402]
[null,"METDI4034",null,"Methylobacterium extorquens DM4","_","putative acetyl-CoA acyltransferase (Fatty oxidation complex beta subunit) (3-ketoacyl-CoA thiolase) (Beta-ketothiolase) (fadA-like)","_",0.96627,1.01519,35.66,{"v":4e-68,"d":"4.00E-68"},2,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.16","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","1699931, 7961399","3 : Putative function from multiple computational evidences",16,394,395,30,413,415]
[]
["CLOSTRIBL6_v1_0555","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,"CLOSTRIBL4_v1_1158",null,"Clostridiales BL-4","hbd","3-hydroxybutyryl-CoA dehydrogenase","RXN-12570 ; RHEA:16200 ;",0.98997,0.99663,82.09,0,1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,296,299,1,296,297]
[null,"CLOSTRIBL3_v1_13113",null,"Clostridiaceae BL-3","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.95652,0.99306,44.06,{"v":2E-85,"d":"2.00E-85"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 25112316","1c : Function from experimental evidences in the studied genus",6,291,299,3,287,288]
[null,"CLOSTRIBL3_v1_20313",null,"Clostridiaceae BL-3","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.95652,1.01418,38.46,{"v":2e-65,"d":"2.00E-65"},2,2,"_","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286, 8001771","1c : Function from experimental evidences in the studied genus",6,291,299,1,280,282]
[null,"CLOSTRIBL4_v1_1869",null,"Clostridiales BL-4","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.9398,1.00717,38.79,{"v":9e-59,"d":"9.00E-59"},2,2,"_","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",11,291,299,5,277,279]
[null,"CLOSTRIBL6_v1_0126",null,"Clostridiales BL-6","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.94314,1.01439,38.65,{"v":1E-56,"d":"1.00E-56"},2,1,"_","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8759838, 18461320, 28956599","2a : Function from experimental evidences in other organisms",11,292,299,5,278,278]
[null,"NBG4_v1_200002",null,"Candidatus Sulfobium mesophilum","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:22432 ;",0.95652,1.01418,35.31,{"v":3e-56,"d":"3.00E-56"},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",6,291,299,3,281,282]
[null,"BSU24160",null,"Bacillus subtilis 168","mmgB","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.95987,1,35.54,{"v":3e-55,"d":"3.00E-55"},1,2,"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",5,291,299,2,282,287]
[null,"AZOLI_p40260",null,"Azospirillum lipoferum 4B","paaH","3-hydroxybutyryl-CoA dehydrogenase","_",0.52888,0.97993,38.23,{"v":1E-50,"d":"1.00E-50"},1,2,"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",8,297,299,9,293,554]
[null,"MGMSRv2_3175",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaH","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.56238,0.94983,37.32,{"v":7e-50,"d":"7.00E-50"},2,2,"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",9,291,299,10,287,505]
[null,"PSEEN3198",null,"Pseudomonas entomophila L48","paaH","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.9398,1.02182,35.23,{"v":4e-49,"d":"4.00E-49"},1,3,"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)",11,291,299,1,275,275]
[null,"CMR15v5_2681",null,"Ralstonia solanacearum CMR15","fadB","fused 3-hydroxybutyryl-CoA epimerase, delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase, enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase","_",0.42857,0.99331,35.35,{"v":8e-46,"d":"8.00E-46"},3,1,"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",3,298,299,289,573,693]
[null,"PP_3282",null,"Pseudomonas putida KT2440","paaH","3-hydroxyadipyl-CoA dehydrogenase","RXN0-2044 ; RHEA:16199 ;",0.56832,0.95987,38.68,{"v":2E-45,"d":"2.00E-45"},2,2,"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",9,292,299,10,288,505]
[null,"PSEEN2793",null,"Pseudomonas entomophila L48","paaC","3-hydroxyacyl-CoA dehydrogenase phaC","_",0.57283,0.97324,36.43,{"v":2E-45,"d":"2.00E-45"},2,3,"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",3,292,299,7,291,508]
[null,"THI_0464",null,"Thiomonas sp. 3As","_","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.56773,0.95318,35.44,{"v":2e-42,"d":"2.00E-42"},1,3,"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",9,292,299,13,290,502]
[null,"XDD1v4_3925",null,"Xenorhabdus doucetiae FRM16","paaH","protein PaaH; 3-hydroxybutyryl-CoA dehydrogenase","_",0.52285,0.95652,35.31,{"v":2e-40,"d":"2.00E-40"},3,2,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",9,291,299,10,287,547]
[null,"LMIv2_1447",null,"Legionella micdadei","_","3-hydroxybutyryl-CoA epimerase","_",0.41902,0.94314,36.52,{"v":4e-38,"d":"4.00E-38"},1,2,"_","5.1.2.3","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",11,291,299,312,577,673]
[]
["CLOSTRIBL6_v1_0556","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,"CLOSTRIBL4_v1_1159",null,"Clostridiales BL-4","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",1,1,76.32,0,1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","7867955, 11075929, 11466286, 1685080","2a : Function from experimental evidences in other organisms",1,397,397,1,397,397]
[null,"CLOSTRIBL4_v1_1867",null,"Clostridiales BL-4","thlA","acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.93602,0.99496,49.11,{"v":3e-125,"d":"3.00E-125"},2,2,"_","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","7867955, 11075929","2a : Function from experimental evidences in other organisms",4,395,397,29,418,422]
[null,"CLOSTRIBL6_v1_0127",null,"Clostridiales BL-6","phaA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",1.00504,1.01013,48.62,{"v":2e-123,"d":"2.00E-123"},1,1,"_","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","16352833, 18246303, 19016856, 28956599","2a : Function from experimental evidences in other organisms",4,395,397,3,394,395]
[null,"RPSI07_1730",null,"Ralstonia solanacearum PSI07","phaA","acetyl-CoA acetyltransferase, thiolase-like","_",1.01763,1.02538,48.76,{"v":7e-120,"d":"7.00E-120"},1,2,"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)",1,397,397,1,394,394]
[null,"CD630_10590",null,"Clostridium difficile 630","thlA1","Acetoacetyl-CoA thiolase 1","_",0.99748,1.01279,47.73,{"v":1E-119,"d":"1.00E-119"},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",3,396,397,1,391,391]
[null,"Rmet_1362",null,"Cupriavidus metallidurans CH34","bktB","acetyl-CoA acetyltransferase","_",1.01763,1.02538,49.01,{"v":7e-119,"d":"7.00E-119"},1,2,"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",1,397,397,1,394,394]
[null,"Rmet_1357",null,"Cupriavidus metallidurans CH34","phaA","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",1,1.01018,47.1,{"v":7e-118,"d":"7.00E-118"},2,2,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,396,397,1,392,393]
[null,"CLOSTRIBL3_v1_13111",null,"Clostridiaceae BL-3","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99748,1.01279,46.21,{"v":2E-116,"d":"2.00E-116"},2,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","7867955, 11075929, 11466286, 1685080","1c : Function from experimental evidences in the studied genus",3,395,397,1,390,391]
[null,"AZOLI_p40026","_","Azospirillum lipoferum 4B","pcaF","Beta-ketoadipyl CoA thiolase","_",0.98768,1.01008,47.88,{"v":1e-114,"d":"1.00E-114"},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",3,397,397,8,406,406]
[null,"ABSDF2022","_","Acinetobacter baumannii SDF","pcaF","beta-ketoadipyl CoA thiolase","_",1.00248,1.01763,45.79,{"v":3e-114,"d":"3.00E-114"},1,1,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme",8125318,"2a : Function from experimental evidences in other organisms",1,397,397,1,403,403]
[null,"ABAYE1675","_","Acinetobacter baumannii AYE","pcaF","beta-ketoadipyl CoA thiolase","_",1.00248,1.01763,45.79,{"v":5e-114,"d":"5.00E-114"},1,1,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme",8125318,"2a : Function from experimental evidences in other organisms",1,397,397,1,403,403]
[null,"ACIAD1706","_","Acinetobacter baylyi ADP1","pcaF","beta-ketoadipyl CoA thiolase","2.3.1.155-RXN ; KETOACYLCOATHIOL-RXN ; RXN-3641 ;",1.00249,1.01259,46.02,{"v":5e-114,"d":"5.00E-114"},1,1,"_","2.3.1.-","1 : Unknown","_","e : enzyme","8125318, 7883173, 8063101, 3036773","1a : Function from experimental evidences in the studied strain",3,397,397,1,401,401]
[null,"Rmet_3669","_","Cupriavidus metallidurans CH34","pcaF","acetyl-CoA acetyltransferase","_",1.0025,1.01008,47.38,{"v":5e-114,"d":"5.00E-114"},1,1,"1.1.2.7 : Acetoacetate degradation ;","_","1 : Unknown","_","c : carrier","_","2a : Function from experimental evidences in other organisms",3,397,397,1,400,400]
[null,"PSEEN3197",null,"Pseudomonas entomophila L48","_","putative Acetoacetyl-CoA thiolase","_",1.00252,1.01015,44.47,{"v":6e-114,"d":"6.00E-114"},2,2,"1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.9","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,397,397,1,394,394]
[null,"THI_0462",null,"Thiomonas sp. 3As","pcaF1","Beta-ketoadipyl CoA thiolase","_",1.0025,1.01008,46.63,{"v":2E-113,"d":"2.00E-113"},2,1,"1 : Metabolism ;","2.3.1.-","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",7961399,"2a : Function from experimental evidences in other organisms",3,397,397,1,400,400]
[null,"ABAYE2367",null,"Acinetobacter baumannii AYE","paaJ","beta-ketoadipyl CoA thiolase with thiolase-like domain, phenylacetic acid degradation","_",1.01741,1.03023,46.94,{"v":2e-112,"d":"2.00E-112"},3,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","1 : Unknown","_","e : enzyme",9748275,"2b : Function from indirect experimental evidences (e.g. phenotypes)",3,397,397,1,401,402]
[null,"RALTA_B0208","_","Cupriavidus taiwanensis LMG19424","pcaF","Beta-ketoadipyl CoA thiolase","_",1.0025,1.01008,46.63,{"v":3e-112,"d":"3.00E-112"},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",3,397,397,1,400,400]
[null,"PSHAa1586","_","Pseudoalteromonas haloplanktis TAC125","atoB","acetyl-CoA acetyltransferase with thiolase domain, Acetoacetyl-CoA thiolase","_",0.96822,0.99748,44.44,{"v":2e-111,"d":"2.00E-111"},1,1,"_","2.3.1.9","cytoplasm (undefined)","_","e : enzyme",7867955,"2a : Function from experimental evidences in other organisms",5,397,397,20,409,409]
[null,"NIDE3104",null,"Candidatus Nitrospira defluvii","fadA","3-ketoacyl-CoA thiolase","_",1.01259,1.01515,46.52,{"v":3e-111,"d":"3.00E-111"},1,1,"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)",3,397,397,1,396,396]
[null,"PSEEN2795",null,"Pseudomonas entomophila L48","pcaF-2","beta-ketoadipyl CoA thiolase","_",1.00493,1.02771,46.81,{"v":2E-109,"d":"2.00E-109"},4,1,"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",3,397,397,6,406,406]
[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 ;",0.97783,1,47.1,{"v":6e-109,"d":"6.00E-109"},4,1,"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",8,397,397,11,406,406]
[null,"XPG1v4_0713","_","Xenorhabdus poinarii G6","pcaF","Beta-ketoadipyl-CoA thiolase","_",1.0225,1.03023,46.21,{"v":1E-108,"d":"1.00E-108"},1,1,"_","2.3.1.174","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,397,397,1,400,400]
[null,"MGMSRv2_3177",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaE","beta-ketoadipyl CoA thiolase","_",1,1.01008,46.38,{"v":7E-106,"d":"7.00E-106"},2,1,"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",3,397,397,1,401,401]
[null,"XDD1v4_3927",null,"Xenorhabdus doucetiae FRM16","paaJ","protein PaaJ; Beta-ketoadipyl-CoA thiolase","_",1,1.01763,45.3,{"v":8e-105,"d":"8.00E-105"},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",3,397,397,1,403,404]
[null,"ECK1394",null,"Escherichia coli K12","paaE","beta-ketoadipyl CoA thiolase","RXN-3641 ; RXN0-6512 ;",1,1.01008,44.64,{"v":1e-103,"d":"1.00E-103"},3,1,"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",3,397,397,1,401,401]
[null,"NBG4_v1_200004",null,"Candidatus Sulfobium mesophilum","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99496,1,42.28,{"v":5e-103,"d":"5.00E-103"},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",4,396,397,9,395,395]
[null,"AZOLI_p40258",null,"Azospirillum lipoferum 4B","paaJ","beta-ketoadipyl CoA thiolase","_",1,1.01259,44.28,{"v":6e-100,"d":"6.00E-100"},2,2,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",3,397,397,1,402,402]
[null,"ACIAD1689",null,"Acinetobacter baylyi ADP1","dcaF","beta-ketoadipyl CoA thiolase","2.3.1.155-RXN ; KETOACYLCOATHIOL-RXN ; RXN-3641 ;",1,1.01008,42.14,{"v":5e-99,"d":"5.00E-99"},3,1,"_","2.3.1.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921, 11571189","1a : Function from experimental evidences in the studied strain",3,397,397,1,400,401]
[null,"SCFA_v1_120020",null,"Ca. Phosphitivorax anaerolimi F81","yqeF","Acetyl-CoA acetyltransferase","_",1,1.01276,42.07,{"v":9e-99,"d":"9.00E-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",3,396,397,1,391,392]
[null,"ABAYE2307",null,"Acinetobacter baumannii AYE","dcaF","beta-ketoadipyl CoA thiolase","_",1.00748,1.01763,42.57,{"v":2e-97,"d":"2.00E-97"},4,1,"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",3,397,397,1,400,401]
[null,"BN42v3_90051","_","Mycobacterium canettii STB-K","fadA","Putative Acetyl-CoA Acetyltransferase FadA6 (Acetoacetyl-CoA Thiolase)","_",1.00504,1.03368,42.11,{"v":6e-94,"d":"6.00E-94"},1,1,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","11929527, 12657046, 12775759, 15928073","3 : Putative function from multiple computational evidences",3,397,397,1,386,386]
[null,"BN45v3_100051","_","Mycobacterium canettii STB-J","fadA","Putative Acetyl-CoA Acetyltransferase FadA6 (Acetoacetyl-CoA Thiolase)","_",1.00504,1.03368,42.11,{"v":3e-93,"d":"3.00E-93"},1,1,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","11929527, 12657046, 12775759, 15928073","3 : Putative function from multiple computational evidences",3,397,397,1,386,386]
[null,"BN44v3_110048","_","Mycobacterium canettii STB-D","fadA","Putative Acetyl-CoA Acetyltransferase FadA6 (Acetoacetyl-CoA Thiolase)","_",1.00504,1.03368,41.85,{"v":7e-93,"d":"7.00E-93"},1,1,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","11929527, 12657046, 12775759, 15928073","3 : Putative function from multiple computational evidences",3,397,397,1,386,386]
[null,"BN43v3_90054","_","Mycobacterium canettii STB-L","fadA","Putative Acetyl-CoA Acetyltransferase FadA6 (Acetoacetyl-CoA Thiolase)","_",1.00504,1.03368,41.85,{"v":7e-93,"d":"7.00E-93"},1,1,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","11929527, 12657046, 12775759, 15928073","3 : Putative function from multiple computational evidences",3,397,397,1,386,386]
[null,"BSU24170",null,"Bacillus subtilis 168","mmgA","degradative acetoacetyl-CoA thiolase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",1,1.01018,40.55,{"v":4E-92,"d":"4.00E-92"},2,2,"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",3,395,397,1,391,393]
[null,"BN42v3_20922",null,"Mycobacterium canettii STB-K","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",1.01728,1.03778,40.05,{"v":4E-90,"d":"4.00E-90"},2,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",3,397,397,1,404,405]
[null,"BN12v2_1200011","_","Tetrasphaera japonica T1-X7","_","Putative 3-ketoacyl-CoA thiolase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",1.02469,1.04534,39.76,{"v":7e-90,"d":"7.00E-90"},1,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","3 : Putative function from multiple computational evidences",3,397,397,1,404,405]
[null,"BN44v3_11190",null,"Mycobacterium canettii STB-D","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",1.00488,1.03778,40.05,{"v":7e-90,"d":"7.00E-90"},2,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",3,397,397,6,409,410]
[null,"BN43v3_30127",null,"Mycobacterium canettii STB-L","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",1.00488,1.03778,40.05,{"v":7e-90,"d":"7.00E-90"},2,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",3,397,397,6,409,410]
[null,"BN45v3_30114",null,"Mycobacterium canettii STB-J","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",1.00488,1.03778,40.05,{"v":1E-89,"d":"1.00E-89"},2,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",3,397,397,6,409,410]
[null,"AZOLI_p30161","_","Azospirillum lipoferum 4B","phbA4","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.99244,1.01285,41.37,{"v":2e-89,"d":"2.00E-89"},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",8,395,397,7,387,389]
[null,"BN10v3_920035","_","Tetrasphaera elongata Lp2","_","Putative 3-ketoacyl-CoA thiolase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",0.99509,1.02015,39.51,{"v":4e-88,"d":"4.00E-88"},1,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",8,397,397,6,406,407]
[null,"PSEEN3547",null,"Pseudomonas entomophila L48","fadAx","acetyl-CoA acetyltransferase with thiolase domain FadAx","_",0.99244,0.99244,40.86,{"v":5e-88,"d":"5.00E-88"},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)",6,397,397,8,396,397]
[null,"Pars_1071","_","Pyrobaculum arsenaticum DSM 13514","_","putative acetyl-CoA acetyltransferase","_",1,1.01259,38.06,{"v":8e-88,"d":"8.00E-88"},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",3,397,397,8,402,402]
[null,"PP_2215",null,"Pseudomonas putida KT2440","_","acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",1.00504,1.00504,40.35,{"v":3e-87,"d":"3.00E-87"},5,2,"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",1,397,397,3,396,397]
[null,"BN13v1_250034","_","Tetrasphaera jenkinsii Ben74","_","Putative 3-ketoacyl-CoA thiolase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",1.02723,1.04534,39.76,{"v":3e-87,"d":"3.00E-87"},1,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","3 : Putative function from multiple computational evidences",3,397,397,1,403,404]
[null,"BN11v3_1350015",null,"Tetrasphaera australiensis Ben110","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",1.00739,1.03023,38.63,{"v":1e-86,"d":"1.00E-86"},1,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",3,397,397,1,405,406]
[null,"ACIAD1612",null,"Acinetobacter baylyi ADP1","_","putative acetyl-CoA C-acetyltransferase with thiolase domain","_",0.98741,0.99746,38.27,{"v":1e-85,"d":"1.00E-85"},5,2,"1.1.1 : carbon compounds ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",6,395,397,5,391,393]
[null,"BN11v3_1360003",null,"Tetrasphaera australiensis Ben110","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase)","_",0.98741,1.01292,40.05,{"v":2e-84,"d":"2.00E-84"},2,2,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",17189250,"3 : Putative function from multiple computational evidences",8,397,397,8,387,387]
[null,"RALTA_B0598",null,"Cupriavidus taiwanensis LMG19424","_","putative ACETYL-COA ACETYLTRANSFERASE (ACETOACETYL-COA THIOLASE) PROTEIN","_",1.00252,1.0179,38.69,{"v":2e-84,"d":"2.00E-84"},4,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 7.1 : Cytoplasm ;","_","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,397,397,1,391,391]
[null,"CMR15v5_2683",null,"Ralstonia solanacearum CMR15","_","acetyl-CoA acetyltransferase","_",1.02015,1.03316,37.78,{"v":7e-81,"d":"7.00E-81"},5,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,395,397,1,390,392]
[null,"RALTA_A1580",null,"Cupriavidus taiwanensis LMG19424","fadA","3-ketoacyl-CoA thiolase; (thiolase I, acetyl-CoA transferase)","_",1.03023,1.04337,38.88,{"v":5e-77,"d":"5.00E-77"},6,2,"1.1.2.1 : Degradation of short-chain fatty acids ; 7.1 : Cytoplasm ;","2.3.1.16","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,397,397,1,392,392]
[null,"RALSYv5_mp0378","_","Ralstonia syzygii R24","_","putative 3-ketoacyl-CoA thiolase / acetyl-CoA acetyltransferase (fragment)","_",0.43073,0.93443,38.01,{"v":8e-35,"d":"8.00E-35"},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",225,395,397,12,181,183]
[]
["CLOSTRIBL6_v1_0558","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,"CLOSTRIBL4_v1_1161",null,"Clostridiales BL-4","crt","Short-chain-enoyl-CoA hydratase","ENOYL-COA-HYDRAT-RXN ; RHEA:16108 ;",0.93841,0.98855,81.47,{"v":1e-149,"d":"1.00E-149"},1,1,"1 : Metabolism ;","4.2.1.50, 4.2.17.150","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","8655474, 11466286, 5057466","2a : Function from experimental evidences in other organisms",3,261,262,17,275,276]
[null,"CLOSTRIBL3_v1_20308",null,"Clostridiaceae BL-3","crt","Short-chain-enoyl-CoA hydratase","ENOYL-COA-HYDRAT-RXN ; RHEA:16105 ;",1,1.01158,48.85,{"v":3e-76,"d":"3.00E-76"},1,2,"_","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 5057466","1c : Function from experimental evidences in the studied genus",3,262,262,1,259,259]
[null,"BSU18220","_","Bacillus subtilis 168","ldeF","methylglutaconyl-CoA hydratase (leucine degradation)","METHYLGLUTACONYL-COA-HYDRATASE-RXN ; RHEA:21536 ;",0.99618,1.00385,50.96,{"v":7e-74,"d":"7.00E-74"},1,1,"_","4.2.1.18","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",19935659,"2b : Function from indirect experimental evidences (e.g. phenotypes)",6,261,262,3,259,260]
[null,"PP_3284",null,"Pseudomonas putida KT2440","paaF","enoyl-CoA hydratase-isomerase","RXN0-6513 ; RHEA:34866 ;",0.94656,0.96498,48.79,{"v":7e-70,"d":"7.00E-70"},1,1,"_","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","12846838, 15137080, 18437357","2a : Function from experimental evidences in other organisms",15,262,262,13,257,257]
[null,"CD630_10570",null,"Clostridium difficile 630","crt2","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.97736,0.98855,46.72,{"v":8E-70,"d":"8.00E-70"},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",5,259,262,9,262,265]
[null,"Rmet_2603","_","Cupriavidus metallidurans CH34","paaG1","Enoyl-CoA hydratase/isomerase","_",1.01141,1.01527,45.86,{"v":2e-69,"d":"2.00E-69"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,262,262,1,263,263]
[null,"CD630_08000",null,"Clostridium difficile 630","crt1","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.98473,0.99231,43.02,{"v":4e-68,"d":"4.00E-68"},2,2,"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",7,262,262,6,260,260]
[null,"IBTHAUMv1_18460003","_","Ianthella basta symbiont thaum","crt","3-hydroxybutyryl-CoA dehydratase","_",0.9542,0.99206,47.2,{"v":5e-67,"d":"5.00E-67"},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)",8,255,262,3,250,252]
[null,"BN11v3_3200006","_","Tetrasphaera australiensis Ben110","_","putative enoyl-CoA hydratase echA8","_",0.99618,1.00772,45.21,{"v":1E-62,"d":"1.00E-62"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,262,262,3,259,259]
[null,"BN874v1_720037","_","Candidatus Contendobacter odensis Run_B_J11","_","putative enoyl-CoA hydratase-isomerase","_",0.99618,1.01163,42.53,{"v":2e-62,"d":"2.00E-62"},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",3,262,262,1,258,258]
[null,"NVIE_008340","_","Nitrososphaera viennensis EN76","_","3-hydroxybutyryl-CoA dehydratase","_",0.89967,1.02672,42.01,{"v":6e-61,"d":"6.00E-61"},1,1,"_","4.2.1.55","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",16,254,262,28,296,299]
[null,"PSEEN2791",null,"Pseudomonas entomophila L48","phaA","enoyl-CoA hydratase/isomerase PhaA","_",0.94656,0.96498,43.55,{"v":6e-61,"d":"6.00E-61"},1,1,"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",14,261,262,12,256,257]
[null,"BN873v1_210051","_","Candidatus Competibacter denitrificans Run_A_D11","_","putative enoyl-CoA hydratase-isomerase","_",0.99618,1.01163,42.91,{"v":1e-60,"d":"1.00E-60"},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",3,262,262,1,258,258]
[null,"RM41v1_60029","_","Sinorhizobium sp. Rm41","_","Putative enoyl-CoA hydratase","_",0.99237,1.01167,41.92,{"v":2e-60,"d":"2.00E-60"},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",3,262,262,1,257,257]
[null,"BRADO2663","_","Bradyrhizobium sp. ORS278","_","Putative enoyl-CoA hydratase","_",0.97368,0.98855,41.7,{"v":2e-60,"d":"2.00E-60"},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",5,262,262,11,266,266]
[null,"BN13v1_100067","_","Tetrasphaera jenkinsii Ben74","_","putative enoyl-CoA hydratase echA8","_",1.00382,1.01544,44.11,{"v":1E-59,"d":"1.00E-59"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,262,262,3,259,259]
[null,"BN10v3_570010","_","Tetrasphaera elongata Lp2","_","putative enoyl-CoA hydratase echA8","_",0.99618,1.01163,44.44,{"v":2e-59,"d":"2.00E-59"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,262,262,3,258,258]
[null,"BN44v3_11186",null,"Mycobacterium canettii STB-D","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",0.98473,1.00389,41.09,{"v":4e-59,"d":"4.00E-59"},1,2,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",5,262,262,3,257,257]
[null,"BN43v3_30123",null,"Mycobacterium canettii STB-L","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",0.98473,1.00389,41.09,{"v":4e-59,"d":"4.00E-59"},1,2,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",5,262,262,3,257,257]
[null,"ABAYE2304",null,"Acinetobacter baumannii AYE","dcaE","enoyl-CoA hydratase","_",0.9631,0.99618,41.76,{"v":5e-59,"d":"5.00E-59"},1,1,"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",2,262,262,15,271,271]
[null,"AZOLI_3178","_","Azospirillum lipoferum 4B","paaF1","Enoyl-CoA hydratase-isomerase","_",0.99618,1.01163,40.61,{"v":5e-59,"d":"5.00E-59"},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",3,262,262,1,258,258]
[null,"MGMSRv2_2895","_","Magnetospirillum gryphiswaldense MSR-1 v2","paaF","enoyl-CoA hydratase-isomerase","_",0.98855,1.00388,40.54,{"v":8e-59,"d":"8.00E-59"},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",5,262,262,3,258,258]
[null,"Rru_A3801","_","Rhodospirillum rubrum ATCC 11170","fadB","short chain enoyl-CoA hydratase","_",0.98855,1.00388,40.54,{"v":3e-58,"d":"3.00E-58"},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)",5,262,262,3,258,258]
[null,"BN45v3_30109",null,"Mycobacterium canettii STB-J","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",0.98473,1.00389,40.31,{"v":1e-57,"d":"1.00E-57"},1,2,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",5,262,262,3,257,257]
[null,"PSEEN3545",null,"Pseudomonas entomophila L48","fadB1x","enoyl-CoA hydratase, FadB1x","_",0.96183,1.008,39.68,{"v":2e-57,"d":"2.00E-57"},2,1,"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",11,262,262,2,250,250]
[null,"XDD1v4_3923",null,"Xenorhabdus doucetiae FRM16","paaF","protein PaaF; enoyl-CoA hydratase-isomerase","_",0.9771,0.99611,40.23,{"v":2e-57,"d":"2.00E-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",6,261,262,4,256,257]
[null,"BN42v3_20918",null,"Mycobacterium canettii STB-K","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",0.98473,1.00389,39.92,{"v":2e-57,"d":"2.00E-57"},1,2,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",5,262,262,3,257,257]
[null,"HEAR0207","_","Herminiimonas arsenicoxydans","ech","Enoyl-CoA hydratase","_",0.98855,1.00388,42.08,{"v":5e-57,"d":"5.00E-57"},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",3,260,262,1,256,258]
[null,"RALTA_A2759","_","Cupriavidus taiwanensis LMG19424","badK","cyclohex-1-ene-1-carboxyl-CoA hydratase","_",0.99618,1.01163,41.76,{"v":8e-57,"d":"8.00E-57"},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)",5,262,262,3,258,258]
[null,"VIBNIv4_A1764","_","Vibrio nigripulchritudo SFn1","_","putative Enoyl-CoA hydratase","_",1.03435,1.04231,39.48,{"v":2e-56,"d":"2.00E-56"},1,1,"_","4.2.1.17","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",6,262,262,3,260,260]
[null,"BN12v2_350029","_","Tetrasphaera japonica T1-X7","_","putative enoyl-CoA hydratase echA8","_",0.9771,0.9771,41.02,{"v":1e-55,"d":"1.00E-55"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",8,258,262,5,256,262]
[null,"NIDE3102",null,"Candidatus Nitrospira defluvii","paaF","putative Enoyl-CoA hydratase","_",0.93511,0.93511,44.49,{"v":2E-55,"d":"2.00E-55"},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",21,262,262,22,262,262]
[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 ;",0.94275,0.94636,40.89,{"v":2E-55,"d":"2.00E-55"},1,1,"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",16,262,262,18,261,261]
[null,"BDBv6_60063","_","Blood disease bacterium R229","paaF","enoyl-CoA hydratase-isomerase","_",0.96947,0.9845,40.94,{"v":1E-54,"d":"1.00E-54"},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",3,255,262,1,251,258]
[null,"CMR15v5_1457","_","Ralstonia solanacearum CMR15","paaF","enoyl-CoA hydratase-isomerase","_",0.99618,1.01163,40.23,{"v":3e-54,"d":"3.00E-54"},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",3,262,262,1,258,258]
[null,"CLOSTRIBL4_v1_1868",null,"Clostridiales BL-4","crt","Short-chain-enoyl-CoA hydratase","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; RHEA:17852 ;",0.97328,0.98837,40,{"v":3e-54,"d":"3.00E-54"},2,2,"_","4.2.1.55","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286, 5057466","2a : Function from experimental evidences in other organisms",8,255,262,4,250,258]
[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 ;",0.9771,0.99611,38.67,{"v":1E-53,"d":"1.00E-53"},2,2,"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",5,260,262,3,255,257]
[null,"MGMSRv2_3173",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaF","enoyl-CoA hydratase-isomerase","_",0.93893,0.94981,39.43,{"v":6E-52,"d":"6.00E-52"},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",16,261,262,16,258,259]
[null,"CLOSTRIBL3_v1_13112",null,"Clostridiaceae BL-3","crt","Short-chain-enoyl-CoA hydratase","RXN-11667 ; RHEA:52664 ;",0.98473,1.01176,37.6,{"v":8e-52,"d":"8.00E-52"},2,2,"_","4.2.1.150","2 : Cytoplasmic","_","e : enzyme","8655474, 5057466","1c : Function from experimental evidences in the studied genus",6,262,262,2,255,255]
[null,"AZCBGv1_p1100088","_","Azospirillum brasilense CBG497","_","enoyl-CoA hydratase-isomerase","_",0.91321,0.92366,41.32,{"v":2E-51,"d":"2.00E-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)",19,260,262,25,263,265]
[null,"PSHAa0882","_","Pseudoalteromonas haloplanktis TAC125","paaF","putative enoyl-CoA hydratase-isomerase","_",0.94656,0.95019,38.31,{"v":1e-48,"d":"1.00E-48"},1,1,"2 : Intermediary metabolism ;","4.2.1.17","unknown","_","e : enzyme",9748275,"3 : Putative function from multiple computational evidences",15,262,262,17,261,261]
[null,"Rmet_5557","_","Cupriavidus metallidurans CH34","_","Enoyl-CoA hydratase/isomerase","_",1.01136,1.01908,35.21,{"v":3e-48,"d":"3.00E-48"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,262,262,1,264,264]
[null,"ECS88_4526","_","Escherichia coli S88","_","putative Enoyl-CoA hydratase/carnithine racemase","_",0.9542,0.96525,39.6,{"v":6e-48,"d":"6.00E-48"},1,1,"_","4.2.1.17","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",16,262,262,14,259,259]
[null,"ABAYE2370",null,"Acinetobacter baumannii AYE","paaF","enoyl-CoA hydratase, phenylacetic acid degradation","_",0.94656,0.96498,36.69,{"v":4e-47,"d":"4.00E-47"},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)",14,261,262,12,256,257]
[null,"CMR15v5_mp0937","_","Ralstonia solanacearum CMR15","_","putative enoyl-CoA hydratase/isomerase (paaF)","_",0.95489,0.96947,40.94,{"v":9E-47,"d":"9.00E-47"},1,1,"1 : Metabolism ;","4.2.1.-","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",12,261,262,7,257,266]
[null,"VIBNIv4_A2696",null,"Vibrio nigripulchritudo SFn1","_","putative Enoyl-CoA hydratase","_",0.89855,0.94656,36.69,{"v":1E-46,"d":"1.00E-46"},3,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",16,259,262,17,260,276]
[null,"RALTA_B0546","_","Cupriavidus taiwanensis LMG19424","_","putative Enoyl-CoA hydratase/isomerase","_",1,1.01158,36.64,{"v":1e-45,"d":"1.00E-45"},1,1,"1 : Metabolism ;","4.2.1.17","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,260,262,2,256,259]
[null,"AGR4A_v2_Lc60051","_","Agrobacterium genomosp. 4 B6","_","putative enoyl-CoA hydratase/isomerase","_",0.96947,0.98069,37.8,{"v":2e-44,"d":"2.00E-44"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",11,261,262,9,257,259]
[null,"Rmet_5150",null,"Cupriavidus metallidurans CH34","_","enoyl-CoA hydratase","_",1.00379,1.01145,38.87,{"v":3e-44,"d":"3.00E-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)",10,261,262,7,264,264]
[null,"RALTA_A1578",null,"Cupriavidus taiwanensis LMG19424","_","putative Enoyl-CoA hydratase/isomerase","_",1.00755,1.01908,37.08,{"v":7e-42,"d":"7.00E-42"},3,3,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",8,261,262,5,264,265]
[null,"RALTA_B0595",null,"Cupriavidus taiwanensis LMG19424","_","Putative acyl-CoA hydratase, phenylacetic acid degradation","_",0.92096,1.0229,36.94,{"v":2e-39,"d":"2.00E-39"},3,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.5.4 : Fatty acid and phosphatidic acid ;","4.2.1.17","1 : Unknown","3.1 : Biosynthesis ;  6 : Energy metabolism ;","e : enzyme","10766858, 9748275","3 : Putative function from multiple computational evidences",5,259,262,8,270,291]
[null,"Spro_1828",null,"Serratia proteamaculans 568","caiD","Crotonobetainyl CoA hydratase","_",0.81679,0.89167,35.98,{"v":6e-33,"d":"6.00E-33"},3,1,"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)",8,219,262,8,213,240]
[null,"NBG4_v1_200001",null,"Candidatus Sulfobium mesophilum","echA","3-hydroxybutyryl-CoA dehydratase (fragment)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; RHEA:17849 ;",0.4542,0.84397,39.5,{"v":9e-23,"d":"9.00E-23"},1,2,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",19,135,262,23,139,141]
[]
["CLOSTRIBL6_v1_0559","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,"CLOSTRIBL4_v1_1162",null,"Clostridiales BL-4","_","Putative acyl-CoA transferase (fragment)","_",0.99751,1.0025,69.83,0,1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,399,400,1,401,402]
[null,"CD630_03950",null,"Clostridium difficile 630","hadA","Isocaprenoyl-CoA:2-hydroxyisocaproate CoA-transferase","_",0.9975,1,37.59,{"v":5e-93,"d":"5.00E-93"},1,1,"1.1.3.12 : Leucine degradation ;","2.8.3.-","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","24484910, 15654892, 15374661, 16957230","1b : Function from experimental evidences in the studied species",4,400,400,3,398,399]
[null,"CD630_08020",null,"Clostridium difficile 630","_","Putative CoA-transferase, family III","_",0.96117,0.99,37.37,{"v":3e-85,"d":"3.00E-85"},2,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,396,400,6,399,412]
[]
["CLOSTRIBL6_v1_0560","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,"CLOSTRIBL4_v1_1163",null,"Clostridiales BL-4","hadI","2-hydroxyisocaproyl-CoA dehydratase activator","_",0.98491,0.99618,76.63,{"v":5e-144,"d":"5.00E-144"},1,1,"_","3.-.-.-","2 : Cytoplasmic","_","e : enzyme","15654892, 22827463","2a : Function from experimental evidences in other organisms",1,261,265,1,261,262]
[null,"CD630_03960",null,"Clostridium difficile 630","hadI","Activator of 2-hydroxyisocaproyl-CoA dehydratase","_",0.96654,0.98113,56.92,{"v":3e-101,"d":"3.00E-101"},1,1,"1.1.3.12 : Leucine degradation ; 1.3.5 : Fermentation ;","_","2 : Cytoplasmic","6.7 : Fermentation ;","e : enzyme","24484910, 16957230, 15654892, 11106419","1b : Function from experimental evidences in the studied species",1,260,265,4,263,269]
[null,"SCFA_v1_1140005",null,"Ca. Phosphitivorax anaerolimi F81","hgdC","2-hydroxyglutaryl-CoA dehydratase activator protein","_",0.97358,0.98099,39.53,{"v":5e-66,"d":"5.00E-66"},3,2,"_","3.6.1.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,255,265,1,256,263]
[null,"ECK4325","_","Escherichia coli K12","hgdC","ATPase, activator of (R)-hydroxyglutaryl-CoA dehydratase","_",0.96981,1.00784,40.08,{"v":3e-54,"d":"3.00E-54"},1,1,"3.1.4 : Regulation level unknown ;","_","1 : Unknown","12 : Regulatory functions ;","e : enzyme","15654892, 7607244, 8365476","2a : Function from experimental evidences in other organisms",2,258,265,3,254,255]
[]
["CLOSTRIBL6_v1_0561","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,"CLOSTRIBL4_v1_1164",null,"Clostridiales BL-4","hadB","(R)-2-hydroxyisocaproyl-CoA dehydratase alpha subunit","_",0.9838,0.98837,86.82,0,1,1,"_","4.2.1.-","2 : Cytoplasmic","_","e : enzyme","15654892, 21366233","2a : Function from experimental evidences in other organisms",5,429,430,7,431,432]
[null,"CD630_03970",null,"Clostridium difficile 630","hadB","Subunit of oxygen-sensitive 2-hydroxyisocaproyl-CoA dehydratase B","_",0.94884,0.99512,46.32,{"v":5e-124,"d":"5.00E-124"},1,2,"1.1.3.12 : Leucine degradation ; 1.3.5 : Fermentation ; 7.1 : Cytoplasm ;","_","2 : Cytoplasmic","6.7 : Fermentation ;","e : enzyme","24484910, 16957230, 15654892, 11106419","2a : Function from experimental evidences in other organisms",21,425,430,6,404,410]
[]
["CLOSTRIBL6_v1_0562","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,"CLOSTRIBL4_v1_1165",null,"Clostridiales BL-4","hadC","(R)-2-hydroxyisocaproyl-CoA dehydratase beta subunit","_",0.99734,1,77.07,0,1,1,"_","4.2.1.157","2 : Cytoplasmic","_","e : enzyme","15654892, 21366233","2a : Function from experimental evidences in other organisms",1,375,376,1,375,375]
[null,"CD630_03980",null,"Clostridium difficile 630","hadC","Subunit of oxygen-sensitive 2-hydroxyisocaproyl-CoA dehydratase C","_",0.98138,0.984,49.86,{"v":6e-129,"d":"6.00E-129"},1,1,"1.1.3.12 : Leucine degradation ; 1.3.5 : Fermentation ; 7.1 : Cytoplasm ;","_","2 : Cytoplasmic","6.7 : Fermentation ;","e : enzyme","24484910, 16957230, 15654892, 11106419","2a : Function from experimental evidences in other organisms",8,375,376,5,372,375]
[]
["CLOSTRIBL6_v1_0871","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_11276","_","Clostridiaceae BL-3","_","putative 3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16200 ;",0.90446,0.91318,39.79,{"v":6E-65,"d":"6.00E-65"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",6,288,314,5,288,311]
[null,"Spro_0593","_","Serratia proteamaculans 568","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.93312,0.9544,35.84,{"v":2e-61,"d":"2.00E-61"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,300,314,5,297,307]
[null,"CLOSTRIBL6_v1_0555","_","Clostridiales BL-6","hbd","3-hydroxybutyryl-CoA dehydrogenase","RXN-12705 ; RHEA:16200 ;",0.94268,0.98997,35.47,{"v":7e-61,"d":"7.00E-61"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 25112316","2a : Function from experimental evidences in other organisms",1,290,314,1,293,299]
[null,"BN43v3_30839","_","Mycobacterium canettii STB-L","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB3 (beta-hydroxybutyryl-CoA dehydrogenase) (BhbD)","_",0.91401,0.94408,36.93,{"v":4e-57,"d":"4.00E-57"},1,1,"1 : lipid metabolism ;","1.1.1.157","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",8,294,314,9,281,304]
[null,"BN45v3_40195","_","Mycobacterium canettii STB-J","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB3 (beta-hydroxybutyryl-CoA dehydrogenase) (BhbD)","_",0.91401,0.94408,36.93,{"v":6E-57,"d":"6.00E-57"},1,1,"1 : lipid metabolism ;","1.1.1.157","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",8,294,314,9,281,304]
[null,"BN44v3_20286","_","Mycobacterium canettii STB-D","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB3 (beta-hydroxybutyryl-CoA dehydrogenase) (BhbD)","_",0.92038,0.95066,36.68,{"v":6E-57,"d":"6.00E-57"},1,1,"1 : lipid metabolism ;","1.1.1.157","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",8,294,314,9,281,304]
[null,"BN42v3_21646","_","Mycobacterium canettii STB-K","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB3 (beta-hydroxybutyryl-CoA dehydrogenase) (BhbD)","_",0.91401,0.94408,36.93,{"v":6E-57,"d":"6.00E-57"},1,1,"1 : lipid metabolism ;","1.1.1.157","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",8,294,314,9,281,304]
[]
["CLOSTRIBL6_v1_2953","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,"BSU12320","_","Bacillus subtilis 168","yjmC","putative oxidoreductase","_",0.91908,0.94362,36.79,{"v":7e-68,"d":"7.00E-68"},1,1,"_","1.1.1.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","9579062, 9882655, 16788182","3 : Putative function from multiple computational evidences",17,333,346,19,334,337]
[null,"EFER_2959","_","Escherichia fergusonii ATCC 35469T","_","Ureidoglycolate dehydrogenase","_",0.95665,0.98512,35.65,{"v":3e-66,"d":"3.00E-66"},1,1,"1.1.5.2 : Ethanol degradation ; 1.7.26 : Allantoin assimilation ; 1.8.3 : Nitrogen metabolism ;","1.1.1.154","1 : Unknown","5.7 : Nitrogen metabolism ;  6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,333,346,6,333,336]
[null,"ECS88_3400","_","Escherichia coli S88","_","putative Ureidoglycolate dehydrogenase","_",0.95665,0.98512,35.95,{"v":7e-66,"d":"7.00E-66"},1,1,"1.1.5.2 : Ethanol degradation ; 1.7.26 : Allantoin assimilation ; 1.8.3 : Nitrogen metabolism ;","1.1.1.154","1 : Unknown","5.7 : Nitrogen metabolism ;  6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,333,346,6,333,336]
[null,"VIBNIv4_B2041","_","Vibrio nigripulchritudo SFn1","_","putative Malate/L-lactate dehydrogenase","_",0.95954,0.98516,36.14,{"v":2e-64,"d":"2.00E-64"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","6.11 : Sugars ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,333,346,5,333,337]
[]
["CLOSTRIBL6_v1_0031","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,"BN873v1_20056","_","Candidatus Competibacter denitrificans Run_A_D11","_","putative enoyl-CoA hydratase/isomerase","_",0.9145,0.93536,38.21,{"v":1E-51,"d":"1.00E-51"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,245,269,6,245,263]
[null,"MARHY3771","_","Marinobacter hydrocarbonoclasticus ATCC 49840","echA8","enoyl-CoA hydratase","_",0.83271,0.90688,38.84,{"v":6e-50,"d":"6.00E-50"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",45,268,269,30,247,247]
[null,"NT26v4_0182","_","Rhizobium sp. NT-26","_","Putative enoyl-CoA hydratase/isomerase","_",0.86296,0.86617,38.63,{"v":2E-41,"d":"2.00E-41"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","4.2.1.17","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",7,238,269,19,244,270]
[]
["CLOSTRIBL6_v1_1904","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_12502",null,"Clostridiaceae BL-3","bcd","Acyl-CoA dehydrogenase, short-chain specific","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47199 ; RHEA:24004 ;",0.99843,1.00475,79.65,0,1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286, 8399220, 7857927","2a : Function from experimental evidences in other organisms",1,630,631,1,634,635]
[null,"CLOSTRIBL4_v1_2140",null,"Clostridiales BL-4","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47196 ;",1.00157,1.00951,75.67,0,1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286, 8399220, 7857927","2a : Function from experimental evidences in other organisms",1,631,631,1,636,636]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.58479,0.98138,45.53,{"v":1e-111,"d":"1.00E-111"},1,3,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,374,631,4,372,376]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.59113,0.98939,44.5,{"v":5E-110,"d":"5.00E-110"},1,3,"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",6,378,631,4,376,377]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.58479,0.98138,44.44,{"v":3e-109,"d":"3.00E-109"},1,3,"_","1.3.99.2","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,374,631,4,372,376]
[null,"CMR15v5_0672",null,"Ralstonia solanacearum CMR15","_","putative acyl CoA dehydrogenase oxidoreductase protein","_",0.58479,0.98138,43.63,{"v":6e-106,"d":"6.00E-106"},1,2,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,374,631,4,372,376]
[null,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.58479,0.984,44.72,{"v":2e-103,"d":"2.00E-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",6,374,631,4,372,375]
[null,"BN13v1_430010","_","Tetrasphaera jenkinsii Ben74","_","putative acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.61648,0.98731,44.47,{"v":1E-99,"d":"1.00E-99"},1,1,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,377,631,2,390,394]
[null,"BN12v2_410044","_","Tetrasphaera japonica T1-X7","_","putative acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.61014,0.98465,43.38,{"v":1E-97,"d":"1.00E-97"},1,1,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,377,631,2,386,391]
[null,"VIBNIv4_B0452","_","Vibrio nigripulchritudo SFn1","_","putative Acyl-CoA dehydrogenase","_",0.58954,0.96373,42.74,{"v":2E-90,"d":"2.00E-90"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",9,378,631,12,380,386]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.59429,0.96154,39.47,{"v":3e-89,"d":"3.00E-89"},2,3,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,377,631,11,385,390]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.60697,0.97455,40.47,{"v":2E-87,"d":"2.00E-87"},2,3,"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",3,380,631,9,391,393]
[null,"CMR15v5_0667",null,"Ralstonia solanacearum CMR15","_","putative acyl-CoA dehydrogenase oxidoreductase","_",0.60222,0.96692,39.47,{"v":8e-87,"d":"8.00E-87"},2,3,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,377,631,9,388,393]
[null,"RALTA_A0110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL-COA DEHYDROGENASE OXIDOREDUCTASE","_",0.60697,0.97455,39.95,{"v":8e-87,"d":"8.00E-87"},2,3,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,380,631,9,391,393]
[null,"THI_3281",null,"Thiomonas sp. 3As","ivd","Isovaleryl-CoA dehydrogenase","_",0.60697,0.97704,39.43,{"v":9e-86,"d":"9.00E-86"},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)",3,380,631,8,390,392]
[null,"Rmet_2531",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase (IVDHase)","_",0.5832,0.97098,36.41,{"v":8e-66,"d":"8.00E-66"},6,3,"1.1.1 : Carbohydrates/Carbon compounds ;","1.3.99.10","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,374,631,10,376,379]
[null,"Rmet_2530",null,"Cupriavidus metallidurans CH34","ivd","isovaleryl-CoA dehydrogenase (IVDHase)","_",0.58162,0.9709,35.69,{"v":8e-62,"d":"8.00E-62"},8,4,"1.1.1 : Carbohydrates/Carbon compounds ;","1.3.99.10","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,373,631,10,374,378]
[null,"NMA1201",null,"Neisseria meningitidis Z2491","rubA","rubredoxin (Rd)","_",0.0729,0.82143,50,6e-13,1,2,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",583,628,631,4,49,56]
[null,"CAGGBEG34_v5_20065",null,"Candidatus Glomeribacter gigasporarum BEG34","rubA","Rubredoxin (Rd)","_",0.07607,0.82759,43.75,8e-11,1,2,"_","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier",7670642,"2a : Function from experimental evidences in other organisms",581,628,631,6,53,58]
[null,"HEAR0645",null,"Herminiimonas arsenicoxydans","rubA1","Rubredoxin (Rd)","_",0.0729,0.85185,47.83,3E-10,2,2,"1.4.3 : electron carrier ;","_","1 : Unknown","6 : Energy metabolism ;","c : carrier",7670642,"2a : Function from experimental evidences in other organisms",583,628,631,4,49,54]
[null,"THI_2938",null,"Thiomonas sp. 3As","rub","Rubredoxin Rd","_",0.07132,0.9,44.44,6E-9,9,2,"1.4.3 : Electron carrier ;","_","1 : Unknown","6 : Energy metabolism ;","c : carrier",11160086,"2a : Function from experimental evidences in other organisms",584,628,631,1,45,50]
[null,"HEAR2748",null,"Herminiimonas arsenicoxydans","rubA2","Rubredoxin (Rd)","_",0.07132,0.9,42.22,1e-07,3,2,"1.4.3 : electron carrier ;","_","1 : Unknown","6 : Energy metabolism ;","c : carrier",7670642,"2a : Function from experimental evidences in other organisms",584,628,631,1,45,50]
[]
["CLOSTRIBL6_v1_3062","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,"CLOSTRIBL6_v1_1904","_","Clostridiales BL-6","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47199 ;",0.89699,1.00177,65.72,0,1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,563,565,1,554,631]
[null,"CLOSTRIBL3_v1_11587",null,"Clostridiaceae BL-3","bcd","Acyl-CoA dehydrogenase, short-chain specific","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24004 ; RHEA:47196 ;",0.66726,0.99472,51.46,{"v":9e-129,"d":"9.00E-129"},3,2,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,377,565,1,377,379]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.66195,0.99204,47.59,{"v":8e-121,"d":"8.00E-121"},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",5,378,565,3,376,377]
[null,"PSEEN3546",null,"Pseudomonas entomophila L48","fadFx","acyl-CoA dehydrogenase protein FadFx","_",0.65487,0.98667,48.92,{"v":3e-119,"d":"3.00E-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",5,374,565,3,372,375]
[null,"PP_2216","_","Pseudomonas putida KT2440","acd","short-chain acyl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24007 ;",0.64956,0.97867,48.77,{"v":4e-117,"d":"4.00E-117"},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",8,374,565,6,372,375]
[null,"MGMSRv2_0193","_","Magnetospirillum gryphiswaldense MSR-1 v2","_","Acyl-CoA dehydrogenase","_",0.65487,0.97368,48.11,{"v":2e-115,"d":"2.00E-115"},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",5,374,565,3,372,380]
[null,"ACIAD1607","_","Acinetobacter baylyi ADP1","acads","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; RXN0-2301 ; RHEA:24007 ; RHEA:12277 ;",0.65664,0.98933,47.44,{"v":2e-114,"d":"2.00E-114"},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",4,374,565,2,372,375]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.65487,0.98404,47.3,{"v":2E-113,"d":"2.00E-113"},1,1,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,374,565,3,372,376]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.65487,0.98404,46.49,{"v":1e-111,"d":"1.00E-111"},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)",5,374,565,3,372,376]
[null,"CMR15v5_0672",null,"Ralstonia solanacearum CMR15","_","putative acyl CoA dehydrogenase oxidoreductase protein","_",0.65487,0.98404,45.41,{"v":3e-107,"d":"3.00E-107"},1,1,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,374,565,3,372,376]
[null,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.65487,0.98667,43.78,{"v":5e-100,"d":"5.00E-100"},1,3,"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",5,374,565,3,372,375]
[null,"MARHY1099","_","Marinobacter hydrocarbonoclasticus ATCC 49840","_","acyl-CoA dehydrogenase","_",0.67257,0.97938,41.32,{"v":1e-93,"d":"1.00E-93"},1,1,"_","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,378,565,1,379,388]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.66018,0.95641,39.95,{"v":1e-88,"d":"1.00E-88"},2,4,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,373,565,9,381,390]
[null,"THI_3281",null,"Thiomonas sp. 3As","ivd","Isovaleryl-CoA dehydrogenase","_",0.66903,0.96429,38.89,{"v":3e-84,"d":"3.00E-84"},2,4,"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)",1,373,565,6,383,392]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.66903,0.96183,39.15,{"v":2e-83,"d":"2.00E-83"},2,4,"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",1,373,565,7,384,393]
[null,"CMR15v5_0667",null,"Ralstonia solanacearum CMR15","_","putative acyl-CoA dehydrogenase oxidoreductase","_",0.66549,0.95674,38.3,{"v":8e-82,"d":"8.00E-82"},2,4,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,373,565,9,384,393]
[null,"RALTA_A0110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL-COA DEHYDROGENASE OXIDOREDUCTASE","_",0.66903,0.96183,38.36,{"v":4e-81,"d":"4.00E-81"},3,4,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,373,565,7,384,393]
[null,"SCFA_v1_30011",null,"Ca. Phosphitivorax anaerolimi F81","bcd","Acyl-CoA dehydrogenase (fragment)","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24004 ; RHEA:47196 ;",0.42655,0.9877,51.45,{"v":7e-71,"d":"7.00E-71"},6,3,"_","1.3.8.1","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",139,378,565,3,243,244]
[null,"Rmet_6103","_","Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase-like protein (fragment)","_",0.36814,0.97196,35.1,{"v":3E-34,"d":"3.00E-34"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",171,378,565,3,209,214]
[]
["CLOSTRIBL6_v1_0135","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","_",0.98681,0.98942,72.73,0,1,1,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",6,379,379,5,378,378]
[null,"CLOSTRIBL3_v1_20310",null,"Clostridiaceae BL-3","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24004 ;",1,1,69.66,0,1,1,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286","1c : Function from experimental evidences in the studied genus",1,379,379,1,379,379]
[null,"CLOSTRIBL4_v1_1870",null,"Clostridiales BL-4","bcd","butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24007 ;",0.99221,1.00792,68.85,0,1,1,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","2a : Function from experimental evidences in other organisms",1,377,379,1,382,385]
[null,"BSU37170","_","Bacillus subtilis 168","acdA","acyl-CoA dehydrogenase","ACYLCOADEHYDROG-RXN ;",0.99472,0.99472,59.42,{"v":5e-156,"d":"5.00E-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",1,377,379,1,377,379]
[null,"CD630_08030",null,"Clostridium difficile 630","_","Putative acyl-CoA dehydrogenase","_",1,1.00264,55.53,{"v":1e-140,"d":"1.00E-140"},2,1,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,378,379,1,379,380]
[null,"CD630_03990",null,"Clostridium difficile 630","acdB","Acyl-CoA dehydrogenase, short-chain specific","_",0.98681,0.99204,55.61,{"v":4e-140,"d":"4.00E-140"},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",6,379,379,4,377,377]
[null,"SCFA_v1_190035","_","Ca. Phosphitivorax anaerolimi F81","bcd","acyl-CoA dehydrogenase, short-chain specific (Butyryl-CoA dehydrogenase)","_",0.99215,1,52.77,{"v":7E-139,"d":"7.00E-139"},1,1,"_","1.3.8.1","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,378,379,1,379,382]
[null,"SCFA_v1_2690009","_","Ca. Phosphitivorax butyraticus R76","acdA","Acyl-CoA dehydrogenase (Butyryl-CoA dehydrogenase)","_",0.99215,1,52.51,{"v":4e-138,"d":"4.00E-138"},1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,378,379,1,379,382]
[null,"SCFA_v1_500014",null,"Ca. Phosphitivorax anaerolimi F81","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.98956,1,50.13,{"v":6e-132,"d":"6.00E-132"},2,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,378,379,1,379,383]
[null,"SCFA_v1_1080002",null,"Ca. Phosphitivorax butyraticus R76","acdA","Acyl-CoA dehydrogenase","_",0.98956,1,50.92,{"v":8e-132,"d":"8.00E-132"},2,1,"_","1.3.8.-","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,378,379,1,379,383]
[null,"BSU18260",null,"Bacillus subtilis 168","ldeJ","isovaleryl-CoA dehydrogenase (leucine degradation)","RXN0-2301 ;",1,1.00264,51.32,{"v":4e-131,"d":"4.00E-131"},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,"BN44v3_70065","_","Mycobacterium canettii STB-D","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.97172,0.99736,48.41,{"v":7e-124,"d":"7.00E-124"},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,"BN45v3_60311","_","Mycobacterium canettii STB-J","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.97172,0.99736,48.41,{"v":8e-124,"d":"8.00E-124"},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","_",0.97172,0.99736,48.41,{"v":8e-124,"d":"8.00E-124"},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","_",0.97172,0.99736,48.15,{"v":1e-122,"d":"1.00E-122"},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,"CLOSTRIBL3_v1_10853",null,"Clostridiaceae BL-3","carC","Caffeyl-CoA reductase-Etf complex subunit CarC","RHEA:46956 ;",0.99208,0.99208,47.87,{"v":9e-118,"d":"9.00E-118"},4,1,"_","1.3.1.108","2 : Cytoplasmic","_","e : enzyme",23479729,"2a : Function from experimental evidences in other organisms",5,379,379,3,378,379]
[null,"PSEEN3546",null,"Pseudomonas entomophila L48","fadFx","acyl-CoA dehydrogenase protein FadFx","_",0.97625,0.98667,44.86,{"v":3e-117,"d":"3.00E-117"},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",5,374,379,3,372,375]
[null,"PP_2216",null,"Pseudomonas putida KT2440","acd","short-chain acyl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24007 ;",0.97625,0.98667,44.59,{"v":5E-117,"d":"5.00E-117"},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",5,374,379,3,372,375]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.98945,0.99469,44.53,{"v":1e-116,"d":"1.00E-116"},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",5,379,379,3,377,377]
[null,"RSK60v3_mp750032",null,"Ralstonia solanacearum K60","_","putative Butyryl-CoA dehydrogenase","_",0.97361,0.97878,46.34,{"v":5e-114,"d":"5.00E-114"},1,3,"1 : Metabolism ;","1.3.8.1","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,374,379,6,374,377]
[null,"CMR15v5_mp0941",null,"Ralstonia solanacearum CMR15","_","putative Butyryl-CoA dehydrogenase","_",0.97361,0.97878,45.8,{"v":7E-114,"d":"7.00E-114"},1,3,"1 : Metabolism ;","1.3.99.2","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,374,379,6,374,377]
[null,"RALSYv5_mp0315",null,"Ralstonia syzygii R24","_","putative Butyryl-CoA dehydrogenase","_",0.97361,0.97878,45.8,{"v":1e-113,"d":"1.00E-113"},1,3,"1 : Metabolism ;","1.3.99.2","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,374,379,6,374,377]
[null,"BN12v2_410006","_","Tetrasphaera japonica T1-X7","_","acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.98191,1.00264,45.79,{"v":4e-113,"d":"4.00E-113"},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,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.98417,0.99202,42.9,{"v":5e-113,"d":"5.00E-113"},1,2,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,377,379,3,375,376]
[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 ;",0.98681,0.99733,43.58,{"v":4e-112,"d":"4.00E-112"},1,3,"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",4,377,379,2,375,375]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.98417,0.99202,42.9,{"v":4e-111,"d":"4.00E-111"},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)",5,377,379,3,375,376]
[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":6e-111,"d":"6.00E-111"},2,1,"_","1.3.8.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,377,379,3,375,375]
[null,"BN873v1_590034","_","Candidatus Competibacter denitrificans Run_A_D11","_","putative acyl-CoA dehydrogenase","_",0.98417,0.98417,43.7,{"v":3e-110,"d":"3.00E-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",5,377,379,3,375,379]
[null,"BN13v1_920006","_","Tetrasphaera jenkinsii Ben74","_","putative acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.98705,1.00528,44.36,{"v":8e-110,"d":"8.00E-110"},1,1,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,379,379,8,386,386]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.97179,1,44.33,{"v":1e-109,"d":"1.00E-109"},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,"MARHY1166",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","ivdA","Isovaleryl-coenzyme A dehydrogenase","_",0.97165,0.99472,44.03,{"v":3e-108,"d":"3.00E-108"},1,2,"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",1,377,379,8,384,388]
[null,"RALTA_B1110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.96834,1,44.69,{"v":7e-108,"d":"7.00E-108"},1,2,"1 : Metabolism ;","1.3.99.-","2 : Cytoplasmic","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",11,377,379,1,367,367]
[null,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.98417,0.99467,42.9,{"v":2e-105,"d":"2.00E-105"},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",5,377,379,3,375,375]
[null,"MGMSRv2_0409",null,"Magnetospirillum gryphiswaldense MSR-1 v2","_","Acyl-CoA dehydrogenase/oxidase","_",0.97933,1,42.74,{"v":6e-105,"d":"6.00E-105"},2,2,"1.1.3.12 : Leucine degradation ;","1.3.8.4","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17540897, 8759838, 8655474","2a : Function from experimental evidences in other organisms",1,379,379,6,384,387]
[null,"CMR15v5_0672",null,"Ralstonia solanacearum CMR15","_","putative acyl CoA dehydrogenase oxidoreductase protein","_",0.98417,0.99202,40.75,{"v":1e-103,"d":"1.00E-103"},1,3,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,377,379,3,375,376]
[null,"LEPBIa0057","_","Leptospira biflexa serovar Patoc Patoc 1","acdA2","Acyl-CoA dehydrogenase","_",0.96392,0.98681,41.71,{"v":1e-101,"d":"1.00E-101"},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",1,374,379,2,374,388]
[null,"lpl1788",null,"Legionella pneumophila Lens","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.97429,1,40.9,{"v":2E-100,"d":"2.00E-100"},1,2,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,8,386,389]
[null,"lpg1824",null,"Legionella pneumophila subsp. pneumophila Philadelphia 1","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.97429,1,40.63,{"v":8e-100,"d":"8.00E-100"},1,2,"_","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",null,"Legionella pneumophila subsp. pneumophila HL06041035","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.98187,1,40.63,{"v":8e-100,"d":"8.00E-100"},1,2,"_","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",null,"Legionella pneumophila subsp. pneumophila Lorraine","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.98187,1,40.63,{"v":8e-100,"d":"8.00E-100"},1,2,"_","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",null,"Legionella pneumophila Corby","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.98187,1,40.63,{"v":8e-100,"d":"8.00E-100"},1,2,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,5,383,386]
[null,"lpp1787",null,"Legionella pneumophila Paris","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.97429,1,40.63,{"v":9e-100,"d":"9.00E-100"},1,2,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,8,386,389]
[null,"PP_4064",null,"Pseudomonas putida KT2440","ivd","isovaleryl-CoA dehydrogenase","_",0.88915,0.99472,41.91,{"v":6e-99,"d":"6.00E-99"},3,2,"1.1.3.12 : Leucine degradation ;","1.3.8.4","1 : Unknown","6.2 : Amino acids and amines ;","e : enzyme","11231285, 2777793","2a : Function from experimental evidences in other organisms",1,377,379,43,419,424]
[null,"MGMSRv2_0204",null,"Magnetospirillum gryphiswaldense MSR-1 v2","_","acyl-CoA dehydrogenase","_",0.99736,0.99736,41.01,{"v":5e-98,"d":"5.00E-98"},3,2,"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",1,377,379,1,376,379]
[null,"ABAYE2303",null,"Acinetobacter baumannii AYE","dcaA","acyl-CoA dehydrogenase","_",0.95052,0.96306,42.74,{"v":5e-98,"d":"5.00E-98"},3,1,"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",17,379,379,16,380,384]
[null,"PSEEN3386",null,"Pseudomonas entomophila L48","ivd","isovaleryl-CoA dehydrogenase","_",0.9425,0.99472,41.38,{"v":9e-98,"d":"9.00E-98"},3,2,"1.1.3.12 : Leucine degradation ;","1.3.99.10","Unknown","6 : Energy metabolism ;","e : enzyme","11231285, 2777793, 3446585","2a : Function from experimental evidences in other organisms",1,377,379,19,395,400]
[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 ;",0.96875,0.98153,41.67,{"v":9e-98,"d":"9.00E-98"},3,1,"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","1a : Function from experimental evidences in the studied strain",10,379,379,9,380,384]
[null,"THI_3281",null,"Thiomonas sp. 3As","ivd","Isovaleryl-CoA dehydrogenase","_",0.97449,1.00792,41.88,{"v":1E-97,"d":"1.00E-97"},2,2,"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)",1,377,379,6,387,392]
[null,"BN45v3_50884",null,"Mycobacterium canettii STB-J","fadE","Putative acyl-CoA dehydrogenase FadE19 (MMGC)","_",0.96684,1,42.74,{"v":3e-96,"d":"3.00E-96"},2,4,"1 : lipid metabolism ;","1.3.99.-","1 : Unknown","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",5,377,379,11,389,392]
[null,"BN43v3_40166",null,"Mycobacterium canettii STB-L","fadE","Putative acyl-CoA dehydrogenase FadE19 (MMGC)","_",0.96193,1,42.74,{"v":4e-96,"d":"4.00E-96"},2,4,"1 : lipid metabolism ;","1.3.99.-","1 : Unknown","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",5,377,379,13,391,394]
[null,"BN42v3_40456",null,"Mycobacterium canettii STB-K","fadE","Putative acyl-CoA dehydrogenase FadE19 (MMGC)","_",0.96193,1,42.74,{"v":4e-96,"d":"4.00E-96"},2,4,"1 : lipid metabolism ;","1.3.99.-","1 : Unknown","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",5,377,379,13,391,394]
[null,"CLOSTRIBL3_v1_12012",null,"Clostridiaceae BL-3","carC","Caffeyl-CoA reductase-Etf complex subunit CarC","RHEA:46956 ;",0.99211,0.99472,41.64,{"v":5e-96,"d":"5.00E-96"},5,1,"_","1.3.1.108","2 : Cytoplasmic","_","e : enzyme",23479729,"2a : Function from experimental evidences in other organisms",1,377,379,1,375,380]
[null,"ABAYE2288",null,"Acinetobacter baumannii AYE","_","putative citronelloyl-CoA dehydrogenase (liuA/gnyD)","_",0.97436,1.00264,39.74,{"v":3e-95,"d":"3.00E-95"},4,2,"1.1 : Carbon compound utilization ;","_","1 : Unknown","_","e : enzyme","15345388, 16517656, 18625020","3 : Putative function from multiple computational evidences",1,377,379,6,385,390]
[null,"BN44v3_50491",null,"Mycobacterium canettii STB-D","fadE","Putative acyl-CoA dehydrogenase FadE19 (MMGC)","_",0.96306,0.98383,43.29,{"v":1e-94,"d":"1.00E-94"},2,4,"1 : lipid metabolism ;","1.3.99.-","1 : Unknown","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",19,377,379,4,368,371]
[null,"RALTA_A0110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL-COA DEHYDROGENASE OXIDOREDUCTASE","_",0.97201,1.00792,40.05,{"v":2e-94,"d":"2.00E-94"},3,1,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,377,379,7,388,393]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.97201,1.00792,39.53,{"v":4e-94,"d":"4.00E-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",1,377,379,7,388,393]
[null,"CMR15v5_0667",null,"Ralstonia solanacearum CMR15","_","putative acyl-CoA dehydrogenase oxidoreductase","_",0.97201,1.00792,38.74,{"v":7E-94,"d":"7.00E-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",1,377,379,7,388,393]
[null,"BN873v1_590016",null,"Candidatus Competibacter denitrificans Run_A_D11","_","putative acyl-CoA dehydrogenase","_",0.97436,1.00264,40.79,{"v":4E-92,"d":"4.00E-92"},2,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.8.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,377,379,6,385,390]
[null,"MARHY1099",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","_","acyl-CoA dehydrogenase","_",0.97938,1.00264,39.47,{"v":1e-90,"d":"1.00E-90"},2,4,"_","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,378,379,1,379,388]
[null,"NBG4_v1_200003",null,"Candidatus Sulfobium mesophilum","acdA","Acyl-CoA dehydrogenase","RHEA:47196 ; RHEA:24004 ;",0.93316,0.95778,41.32,{"v":2E-87,"d":"2.00E-87"},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",19,379,379,31,387,389]
[null,"VIBNIv4_A0948",null,"Vibrio nigripulchritudo SFn1","ACAD8","Isobutyryl-CoA dehydrogenase","_",0.99219,1.00528,39.11,{"v":9e-87,"d":"9.00E-87"},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",1,379,379,1,378,384]
[null,"Rmet_5908","_","Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase-like protein","_",0.97662,0.99208,39.89,{"v":1e-86,"d":"1.00E-86"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",11,379,379,10,384,385]
[null,"Npun_R3440","_","Nostoc punctiforme ATCC 29133; PCC 73102","_","putative acyl-CoA dehydrogenase","_",0.95431,0.99208,39.63,{"v":8e-86,"d":"8.00E-86"},1,1,"_","1.3.99.2","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,374,379,1,370,394]
[null,"SCFA_v1_350006",null,"Ca. Phosphitivorax butyraticus R76","_","Butyryl-CoA dehydrogenase","_",0.97927,0.99736,37.57,{"v":2e-83,"d":"2.00E-83"},5,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,377,379,1,377,386]
[null,"LEPBIa1138",null,"Leptospira biflexa serovar Patoc Patoc 1","_","Putative acyl-CoA dehydrogenase, short-chain specific (SCAD) (Butyryl-CoA dehydrogenase)","_",0.96193,1,39.58,{"v":8e-83,"d":"8.00E-83"},3,1,"_","1.3.8.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,379,379,14,390,394]
[null,"Rmet_2599",null,"Cupriavidus metallidurans CH34","acdA","acyl-CoA dehydrogenase","_",0.99738,1.00528,37.8,{"v":3e-82,"d":"3.00E-82"},4,1,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,378,379,1,376,382]
[null,"SCFA_v1_1630002",null,"Ca. Propionivorax syntrophicum F70","acdB","Acyl-CoA dehydrogenase, short-chain specific","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47196 ; RHEA:24004 ;",0.96429,0.99736,38.36,{"v":4e-81,"d":"4.00E-81"},1,2,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,379,379,16,391,392]
[null,"VIBNIv4_B0452",null,"Vibrio nigripulchritudo SFn1","_","putative Acyl-CoA dehydrogenase","_",0.95078,0.96834,38.15,{"v":6e-81,"d":"6.00E-81"},1,4,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",13,379,379,16,381,386]
[null,"XNC1_1707","_","Xenorhabdus nematophila ATCC19061","xcnE","Acyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",0.96084,0.97098,38.59,{"v":2E-78,"d":"2.00E-78"},1,1,"_","1.3.99.2","1 : Unknown","_","e : enzyme","16349198, 1955881","1a : Function from experimental evidences in the studied strain",14,379,379,11,373,383]
[null,"XDD1v4_1795","_","Xenorhabdus doucetiae FRM16","xcnE","Acyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",0.96084,0.97098,38.04,{"v":7e-78,"d":"7.00E-78"},1,1,"_","1.3.8.1","1 : Unknown","_","e : enzyme","16349198, 1955881","2a : Function from experimental evidences in other organisms",14,379,379,11,373,383]
[null,"MARHY1169",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","fadE","long chain acyl coenzyme A dehydrogenase","_",0.97906,0.98681,37.17,{"v":2e-77,"d":"2.00E-77"},5,2,"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)",8,378,379,9,380,382]
[null,"FRAAL3144",null,"Frankia alni ACN14a","_","Acyl-CoA dehydrogenase, long-chain specific","_",0.92875,0.96306,38.36,{"v":3e-77,"d":"3.00E-77"},5,1,"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)",13,377,379,26,390,393]
[null,"BN381v2_250102","_","Candidatus Microthrix parvicella RN1","_","putative Acyl-CoA dehydrogenase","_",0.97317,1.05277,38.6,{"v":1e-75,"d":"1.00E-75"},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",5,377,379,8,404,410]
[null,"Rmet_2531",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase (IVDHase)","_",0.97889,0.97889,36.93,{"v":2e-74,"d":"2.00E-74"},5,1,"1.1.1 : Carbohydrates/Carbon compounds ;","1.3.99.10","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,377,379,11,379,379]
[null,"META1_2223","_","Methylobacterium extorquens AM1","mcd","methylsuccinyl-CoA dehydrogenase, putative isobutyryl-CoA dehydrogenase","_",0.68861,1.02111,37.21,{"v":8E-73,"d":"8.00E-73"},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","_",0.98425,0.98945,35.73,{"v":2e-72,"d":"2.00E-72"},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]
[null,"METDI3005","_","Methylobacterium extorquens DM4","msd","methylsuccinyl-CoA dehydrogenase","_",0.68861,1.02111,36.95,{"v":1e-71,"d":"1.00E-71"},1,1,"_","1.3.8.4","2 : Cytoplasmic","_","e : enzyme","16856937, 17548827","1c : Function from experimental evidences in the studied genus",5,379,379,177,561,562]
[null,"Rmet_2530",null,"Cupriavidus metallidurans CH34","ivd","isovaleryl-CoA dehydrogenase (IVDHase)","_",0.96834,0.9709,35.69,{"v":1E-70,"d":"1.00E-70"},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)",8,374,379,11,375,378]
[null,"XBJ1_1749","_","Xenorhabdus bovienii SS2004","fadE","acyl coenzyme A dehydrogenase","_",0.99736,1,35.19,{"v":2e-68,"d":"2.00E-68"},1,1,"_","1.3.99.13","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,377,379,1,376,378]
[null,"BN874v1_280009","_","Candidatus Contendobacter odensis Run_B_J11","_","putative acyl-CoA dehydrogenase","_",0.6719,1.01583,35.32,{"v":3e-66,"d":"3.00E-66"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme",19703103,"3 : Putative function from multiple computational evidences",5,367,379,167,550,573]
[]
["CLOSTRIBL6_v1_0136","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_10550",null,"Clostridium difficile 630","etfB","Electron transfer flavoproteins subunit beta","_",0.98113,1.00386,64.23,{"v":2E-120,"d":"2.00E-120"},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",1,259,259,6,265,265]
[null,"CLOSTRIBL3_v1_20311",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1,1,57.92,{"v":2e-105,"d":"2.00E-105"},1,1,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286, 9694853","2a : Function from experimental evidences in other organisms",1,259,259,1,259,259]
[null,"CD630_04000",null,"Clostridium difficile 630","etfB1","Beta-subunit of electron transfer flavoprotein","_",1,1.00772,54.41,{"v":4e-96,"d":"4.00E-96"},2,1,"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_08040",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein beta-subunit, core","_",0.98864,1.00772,54.79,{"v":1E-89,"d":"1.00E-89"},3,1,"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",1,255,259,1,260,264]
[null,"CLOSTRIBL4_v1_1871",null,"Clostridiales BL-4","etfB","Electron transfer flavoprotein subunit beta","_",1,1.02703,48.12,{"v":1E-79,"d":"1.00E-79"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,259,259,1,266,266]
[null,"CLOSTRIBL3_v1_12011",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1,1.01158,49.24,{"v":4E-79,"d":"4.00E-79"},3,2,"1.3 : Energy metabolism (carbon) ;","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,259,259,1,262,262]
[null,"pRALTA_0381",null,"Cupriavidus taiwanensis LMG19424","fixA","Electron transfer flavoprotein beta-subunit","_",0.85106,0.92664,48.33,{"v":9e-67,"d":"9.00E-67"},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",1,232,259,1,240,282]
[null,"AZOLI_0535",null,"Azospirillum lipoferum 4B","fixA","electron transfer flavoprotein beta subunit","_",0.90106,0.98456,43.53,{"v":2E-66,"d":"2.00E-66"},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",1,245,259,1,255,283]
[null,"CLOSTRIBL3_v1_20124",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.93962,0.96139,42.97,{"v":4e-66,"d":"4.00E-66"},4,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,247,259,1,249,265]
[null,"BURPHP2_0599",null,"Burkholderia phymatum STM815","fixA","protein fixA, electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.83333,0.90734,47.66,{"v":4e-65,"d":"4.00E-65"},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",1,227,259,1,235,282]
[null,"SBF1_v1_470015",null,"Desulfosporosinus sp. SbF1","fixA","electron-transferring flavoprotein, subunit FixA","_",0.87726,0.93822,44.03,{"v":4e-64,"d":"4.00E-64"},1,2,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,238,259,1,243,277]
[null,"BRADO5386",null,"Bradyrhizobium sp. ORS278","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.94662,1.02703,43.61,{"v":4e-62,"d":"4.00E-62"},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)",1,253,259,1,263,281]
[null,"SCFA_v1_500013",null,"Ca. Phosphitivorax anaerolimi F81","etfB","Electron transfer flavoprotein, beta subunit","_",0.94872,1,40.15,{"v":9e-62,"d":"9.00E-62"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,256,259,2,260,273]
[null,"MGMSRv2_1063",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.88129,0.94595,44.9,{"v":4e-61,"d":"4.00E-61"},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)",1,234,259,1,245,278]
[null,"CLOSTRIBL3_v1_11115",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1.00763,1.01931,41.29,{"v":8e-57,"d":"8.00E-57"},5,3,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,258,259,1,262,262]
[null,"MGMSRv2_0362",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","Electron transfer flavoprotein, beta-subunit","_",0.83099,0.9112,44.49,{"v":1E-56,"d":"1.00E-56"},2,2,"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",1,227,259,1,236,284]
[null,"RM41v1_psym670028",null,"Sinorhizobium sp. Rm41","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.80822,0.9112,44.07,{"v":1e-55,"d":"1.00E-55"},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)",1,227,259,1,236,292]
[null,"CD630_11710",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein subunit alpha","_",0.97358,0.99614,39.53,{"v":1e-55,"d":"1.00E-55"},4,2,"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",1,255,259,4,261,265]
[null,"SCFA_v1_1630003",null,"Ca. Propionivorax syntrophicum F70","FixA","Electron transfer flavoproteins subunit beta","_",0.85606,0.87259,42.48,{"v":6e-54,"d":"6.00E-54"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,222,259,1,226,264]
[null,"SBF1_v1_6700003",null,"Desulfosporosinus sp. SbF1","etfB_2","electron-transferring flavoprotein, beta subunit EtfB (lutD-associated)","_",0.89575,0.917,43.1,{"v":2e-53,"d":"2.00E-53"},2,3,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,227,259,1,230,253]
[null,"CLOSTRIBL3_v1_11488",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.99623,1.01931,37.88,{"v":3e-53,"d":"3.00E-53"},6,3,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,259,259,1,264,265]
[null,"FRAAL5878",null,"Frankia alni ACN14a","fixA","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.92337,0.9305,36.51,{"v":3e-48,"d":"3.00E-48"},1,1,"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,"SCFA_v1_3390002",null,"Ca. Phosphitivorax butyraticus R76","etfB","Electron transfer flavoprotein subunit beta","_",1.00772,1.01163,37.55,{"v":1E-42,"d":"1.00E-42"},1,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,256,259,1,254,258]
[null,"SCFA_v1_1080001",null,"Ca. Phosphitivorax butyraticus R76","etfB","Electron transfer flavoprotein subunit beta (fragment)","_",0.6834,0.9779,42.37,{"v":1E-42,"d":"1.00E-42"},2,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,175,259,2,178,181]
[null,"SCFA_v1_130010",null,"Ca. Phosphitivorax anaerolimi F81","etfB","Electron transfer flavoprotein subunit beta","_",1.01158,1.0155,37.79,{"v":5e-41,"d":"5.00E-41"},2,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,256,259,1,254,258]
[null,"BRADO6492",null,"Bradyrhizobium sp. ORS278","etfB","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.81853,0.85141,36.32,{"v":3e-30,"d":"3.00E-30"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8599534,"2a : Function from experimental evidences in other organisms",1,210,259,1,210,249]
[null,"BBta_1140",null,"Bradyrhizobium sp. BTAi1","etfB","Electron transfer flavoprotein beta-subunit","_",0.81853,0.85141,35.38,{"v":5e-30,"d":"5.00E-30"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,210,259,1,210,249]
[null,"Rmet_5519",null,"Cupriavidus metallidurans CH34","etfB","electron transfer flavoprotein beta-subunit","_",0.82625,0.85944,35.51,{"v":8e-29,"d":"8.00E-29"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier","10026281, 1576992, 8376381, 8599534","2a : Function from experimental evidences in other organisms",1,210,259,1,210,249]
[null,"HEAR0619",null,"Herminiimonas arsenicoxydans","etfB","electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.83012,0.86345,35.35,{"v":1e-28,"d":"1.00E-28"},1,2,"1.4.3 : electron carrier ;","_","1 : Unknown","6 : Energy metabolism ;","c : carrier","10026281, 1576992, 8376381, 8599534","2a : Function from experimental evidences in other organisms",1,210,259,1,210,249]
[null,"Mchl_1822",null,"Methylobacterium extorquens CM4","etfB","electron transfer flavoprotein subunit beta","_",0.82625,0.85944,35.51,{"v":2e-28,"d":"2.00E-28"},1,2,"1.4.3 : Electron carrier ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,210,259,1,210,249]
[null,"METDI2207",null,"Methylobacterium extorquens DM4","etfB","electron transfer flavoprotein, subunit beta (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.82625,0.85944,35.51,{"v":6e-28,"d":"6.00E-28"},1,2,"_","_","1 : Unknown","_","e : enzyme",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,210,259,1,210,249]
[null,"AZOLI_0088",null,"Azospirillum lipoferum 4B","etfB3","Electron transfer flavoprotein beta-subunit","_",0.83012,0.86345,35.81,{"v":4e-27,"d":"4.00E-27"},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)",1,210,259,1,210,249]
[null,"NT26v4_3413",null,"Rhizobium sp. NT-26","etfB","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.83012,0.86345,36.28,{"v":2e-26,"d":"2.00E-26"},1,2,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6 : Energy metabolism ;","c : carrier",8599534,"2a : Function from experimental evidences in other organisms",1,210,259,1,210,249]
[]
["CLOSTRIBL6_v1_0137","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","_",0.95376,0.99099,60.61,{"v":4e-141,"d":"4.00E-141"},1,1,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","c : carrier","17189250, 20059546, 21398533, 8655474, 11466286","2a : Function from experimental evidences in other organisms",8,337,346,1,330,333]
[null,"CD630_10560",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.92775,0.95536,59.19,{"v":1e-132,"d":"1.00E-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",16,336,346,4,324,336]
[null,"CD630_04010",null,"Clostridium difficile 630","etfA1","Alpha-subunit of electron transfer flavoprotein","_",0.93642,0.93913,56.79,{"v":2e-127,"d":"2.00E-127"},2,1,"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",13,336,346,10,333,345]
[null,"CLOSTRIBL4_v1_1872",null,"Clostridiales BL-4","etfA","Electron transfer flavoprotein subunit alpha","_",0.97011,1.03179,49.86,{"v":1e-114,"d":"1.00E-114"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",13,343,346,12,368,368]
[null,"CD630_08050",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein alpha-subunit","_",0.9711,0.98824,49.4,{"v":1e-114,"d":"1.00E-114"},3,1,"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",3,338,346,5,340,340]
[null,"SBF1_v1_470014",null,"Desulfosporosinus sp. SbF1","fixB","electron-transferring flavoprotein, subunit FixB","_",0.73589,0.9422,48.47,{"v":3E-103,"d":"3.00E-103"},1,1,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",13,338,346,110,435,443]
[null,"CLOSTRIBL3_v1_12010",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.95665,0.98512,46.53,{"v":9E-103,"d":"9.00E-103"},3,2,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",8,337,346,1,331,336]
[null,"BURPHP2_0598",null,"Burkholderia phymatum STM815","fixB","Protein fixB, Electron transfer flavoprotein, alpha subunit","_",0.86898,0.93931,48,{"v":8e-101,"d":"8.00E-101"},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",13,333,346,32,356,374]
[null,"pRALTA_0380",null,"Cupriavidus taiwanensis LMG19424","fixB","Electron transfer flavoprotein, alpha subunit","_",0.90133,0.97688,46.75,{"v":3e-99,"d":"3.00E-99"},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",13,345,346,32,368,375]
[null,"MGMSRv2_1064",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.9235,0.97688,45.56,{"v":5e-98,"d":"5.00E-98"},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)",13,346,346,28,365,366]
[null,"MGMSRv2_0361",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","Electron transfer flavoprotein, alpha subunit","_",0.9212,0.97977,45.72,{"v":5e-95,"d":"5.00E-95"},2,1,"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",12,346,346,30,367,368]
[null,"CLOSTRIBL3_v1_20125",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.96532,1.003,45.21,{"v":5e-95,"d":"5.00E-95"},4,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",14,346,346,2,333,333]
[null,"AZOLI_0536",null,"Azospirillum lipoferum 4B","fixB","electron transfer flavoprotein alpha chain","_",0.91922,0.95376,46.67,{"v":2E-92,"d":"2.00E-92"},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",13,334,346,21,346,359]
[null,"SBF1_v1_6700004",null,"Desulfosporosinus sp. SbF1","etfA_2","electron-transferring flavoprotein, alpha subunit EtfA (lutD-associated)","_",0.8408,0.97688,44.67,{"v":2E-90,"d":"2.00E-90"},3,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",5,342,346,63,398,402]
[null,"CLOSTRIBL3_v1_11114",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.82921,0.96821,42.69,{"v":2E-90,"d":"2.00E-90"},5,1,"_","_","2 : Cytoplasmic","_","c : carrier",17189250,"2a : Function from experimental evidences in other organisms",5,337,346,63,395,404]
[null,"CLOSTRIBL3_v1_11487",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.95665,1.00915,47.43,{"v":6e-90,"d":"6.00E-90"},6,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",10,337,346,2,323,328]
[null,"BRADO5385",null,"Bradyrhizobium sp. ORS278","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.88587,0.9422,43.87,{"v":1e-85,"d":"1.00E-85"},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)",13,334,346,28,352,368]
[null,"BSU28520",null,"Bacillus subtilis 168","etfA","electron transfer flavoprotein (alpha subunit)","_",0.9422,1.00308,40.8,{"v":1e-85,"d":"1.00E-85"},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",14,338,346,3,320,325]
[null,"SCFA_v1_130009",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",0.94509,1.01553,44.04,{"v":2e-82,"d":"2.00E-82"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",15,338,346,3,319,322]
[null,"RM41v1_psym670029",null,"Sinorhizobium sp. Rm41","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.94334,0.96243,41.74,{"v":4e-82,"d":"4.00E-82"},1,1,"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",11,338,346,10,341,353]
[null,"CD630_11720",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.83498,0.97977,38.94,{"v":7e-81,"d":"7.00E-81"},4,1,"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",7,340,346,63,394,406]
[null,"SCFA_v1_2400007","_","Ca. Phosphitivorax butyraticus R76","etfA","Electron transfer flavoprotein subunit alpha","_",0.94798,0.98498,39.33,{"v":2E-78,"d":"2.00E-78"},1,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",11,338,346,3,329,333]
[null,"SCFA_v1_500012",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",0.93931,0.97598,38.15,{"v":2e-75,"d":"2.00E-75"},2,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",14,338,346,6,329,333]
[null,"FRAAL5877",null,"Frankia alni ACN14a","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.94798,1.025,40.24,{"v":3e-69,"d":"3.00E-69"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","16.1 : Circulate ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",16,341,346,4,319,320]
[null,"LEPBIa1132",null,"Leptospira biflexa serovar Patoc Patoc 1","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.93931,1.01881,40,{"v":5e-69,"d":"5.00E-69"},1,2,"1.4.3 : Electron carrier ;","_","1 : Unknown","16.10 : Respire ;","c : carrier","_","2a : Function from experimental evidences in other organisms",16,338,346,4,316,319]
[null,"MARHY1802",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","etfA","electron transfer flavoprotein alpha-subunit","_",0.94509,1.04473,39.14,{"v":2e-65,"d":"2.00E-65"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6 : Energy metabolism ;","c : carrier",3415685,"2a : Function from experimental evidences in other organisms",16,338,346,3,311,313]
[null,"AZOLI_0089",null,"Azospirillum lipoferum 4B","etfA3","Electron transfer flavoprotein alpha-subunit","_",0.85838,0.96429,39.73,{"v":6e-64,"d":"6.00E-64"},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)",42,336,346,25,308,308]
[null,"AZOLI_p50300","_","Azospirillum lipoferum 4B","etfA2","Electron transfer flavoprotein alpha-subunit","_",0.85549,0.94872,42.91,{"v":2e-63,"d":"2.00E-63"},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)",42,336,346,26,311,312]
[null,"BN45v3_60005",null,"Mycobacterium canettii STB-J","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.93642,1.01887,38.27,{"v":2e-61,"d":"2.00E-61"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",16,337,346,4,314,318]
[null,"BN44v3_60522",null,"Mycobacterium canettii STB-D","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.93642,1.01887,38.27,{"v":3e-61,"d":"3.00E-61"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",16,337,346,4,314,318]
[null,"BN43v3_60007",null,"Mycobacterium canettii STB-L","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.93642,1.01887,38.27,{"v":3e-61,"d":"3.00E-61"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",16,337,346,4,314,318]
[null,"BN42v3_41031",null,"Mycobacterium canettii STB-K","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.93642,1.01887,38.27,{"v":3e-61,"d":"3.00E-61"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",16,337,346,4,314,318]
[null,"BN11v3_3200004",null,"Tetrasphaera australiensis Ben110","etfA","Electron transfer flavoprotein subunit alpha","_",0.93931,1.02201,35.38,{"v":3e-60,"d":"3.00E-60"},1,1,"_","_","1 : Unknown","6.5 : Electron transport ;","e : enzyme","10026281, 9694853","2a : Function from experimental evidences in other organisms",16,340,346,4,317,318]
[null,"BURPHK2_1883","_","Burkholderia phymatum STM815","etfA","electron transfer flavoprotein, alpha subunit","_",0.93064,1.03205,39.13,{"v":4e-59,"d":"4.00E-59"},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",16,332,346,3,306,312]
[null,"AZCBGv1_p190001","_","Azospirillum brasilense CBG497","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.83526,0.93226,41.52,{"v":3e-58,"d":"3.00E-58"},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)",52,339,346,33,310,310]
[null,"METDI2208",null,"Methylobacterium extorquens DM4","etfA","electron transfer flavoprotein, NAD/FAD-binding domain and ETFP adenine nucleotide-binding domain-like","_",0.95376,1.04101,37.27,{"v":6e-58,"d":"6.00E-58"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","15188393, 16926146, 8599534","2a : Function from experimental evidences in other organisms",18,340,346,5,315,317]
[null,"Mchl_1823",null,"Methylobacterium extorquens CM4","etfA","electron transfer flavoprotein alpha subunit","_",0.95376,1.04101,36.97,{"v":2e-57,"d":"2.00E-57"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","15188393, 16926146, 8599534","2a : Function from experimental evidences in other organisms",18,340,346,5,315,317]
[null,"PSHAa1617","_","Pseudoalteromonas haloplanktis TAC125","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.8526,0.95779,39.66,{"v":5e-57,"d":"5.00E-57"},1,1,"2.5.4 : Menaquinone and ubiquinone ;","_","unknown","_","u : unknown",8599534,"2a : Function from experimental evidences in other organisms",42,334,346,25,306,308]
[null,"HEAR0620",null,"Herminiimonas arsenicoxydans","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.85549,0.95793,39.86,{"v":6E-57,"d":"6.00E-57"},1,2,"1.4.3 : electron carrier ;","_","1 : Unknown","6 : Energy metabolism ;","c : carrier","10026281, 1576992, 8376381, 8599534","2a : Function from experimental evidences in other organisms",42,336,346,25,308,309]
[null,"NT26v4_3414",null,"Rhizobium sp. NT-26","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.8815,0.98706,38.36,{"v":3e-54,"d":"3.00E-54"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",37,336,346,20,309,309]
[null,"Rmet_0738",null,"Cupriavidus metallidurans CH34","etfA","Electron transfer flavoprotein subunit alpha (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.85549,0.95177,40.54,{"v":6e-54,"d":"6.00E-54"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",42,332,346,25,306,311]
[null,"PSEEN3657","_","Pseudomonas entomophila L48","etfA","electron transfer flavoprotein alpha-subunit","_",0.83237,1.04348,39.93,{"v":1E-53,"d":"1.00E-53"},1,1,"1.4.3 : Electron carrier ;","_","Unknown","6 : Energy metabolism ;","c : carrier","_","2a : Function from experimental evidences in other organisms",52,336,346,2,276,276]
[null,"BRADO6491",null,"Bradyrhizobium sp. ORS278","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.8815,0.98071,39.02,{"v":2e-53,"d":"2.00E-53"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",37,338,346,20,311,311]
[null,"CMR15v5_3436","_","Ralstonia solanacearum CMR15","etfA","Electron transfer flavoprotein, alpha-subunit","_",0.8526,0.94855,39.32,{"v":2e-53,"d":"2.00E-53"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",42,332,346,25,306,311]
[null,"Rmet_5518",null,"Cupriavidus metallidurans CH34","etfA","electron transfer flavoprotein, alpha subunit","_",0.85549,0.95484,39.19,{"v":2e-53,"d":"2.00E-53"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier","10026281, 1576992, 8376381, 8599534","2a : Function from experimental evidences in other organisms",42,332,346,25,306,310]
[null,"BBta_1141",null,"Bradyrhizobium sp. BTAi1","etfA","Electron transfer flavoprotein alpha-subunit","_",0.88728,0.97771,38.76,{"v":3e-53,"d":"3.00E-53"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",37,338,346,20,311,314]
[null,"RALTA_A0796","_","Cupriavidus taiwanensis LMG19424","etfA","ELECTRON TRANSFER FLAVOPROTEIN, ALPHA-SUBUNIT","_",0.84971,0.94534,40.82,{"v":3E-52,"d":"3.00E-52"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",42,332,346,25,306,311]
[null,"ACIAD2654","_","Acinetobacter baylyi ADP1","etfA","electron transfer flavoprotein alpha-subunit","_",0.87283,0.97106,37.75,{"v":9e-52,"d":"9.00E-52"},1,1,"1.4.3 : electron carrier ;","_","1 : Unknown","_","f : factor","_","2a : Function from experimental evidences in other organisms",40,336,346,23,311,311]
[null,"THI_1679",null,"Thiomonas sp. 3As","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF)(Electron transfer flavoprotein large subunit) (ETFLS)","_",0.84682,0.94516,37.88,{"v":2E-51,"d":"2.00E-51"},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",48,336,346,31,310,310]
[]
["CLOSTRIBL6_v1_3216","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,"CLOSTRIBL4_v1_1870",null,"Clostridiales BL-4","bcd","butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24007 ;",1,1.01316,63.9,{"v":1E-169,"d":"1.00E-169"},1,2,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","2a : Function from experimental evidences in other organisms",1,380,380,1,385,385]
[null,"CD630_10540",null,"Clostridium difficile 630","bcd2","Butyryl-CoA dehydrogenase","_",0.96316,0.96825,63.93,{"v":4e-162,"d":"4.00E-162"},1,2,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",10,375,380,9,374,378]
[null,"CLOSTRIBL6_v1_0135",null,"Clostridiales BL-6","bcd","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47199 ;",0.98684,0.98945,61.6,{"v":7e-162,"d":"7.00E-162"},1,1,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","2a : Function from experimental evidences in other organisms",1,375,380,1,375,379]
[null,"CLOSTRIBL3_v1_20310",null,"Clostridiaceae BL-3","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24004 ;",0.98684,0.98945,60.8,{"v":2e-157,"d":"2.00E-157"},1,2,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286","1c : Function from experimental evidences in the studied genus",1,375,380,1,375,379]
[null,"CD630_03990",null,"Clostridium difficile 630","acdB","Acyl-CoA dehydrogenase, short-chain specific","_",0.96842,0.97613,53.26,{"v":4e-128,"d":"4.00E-128"},2,2,"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",8,374,380,5,372,377]
[null,"CD630_08030",null,"Clostridium difficile 630","_","Putative acyl-CoA dehydrogenase","_",0.98947,0.98947,48.94,{"v":9e-122,"d":"9.00E-122"},3,2,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,374,380,1,375,380]
[null,"CMR15v5_mp0941","_","Ralstonia solanacearum CMR15","_","putative Butyryl-CoA dehydrogenase","_",0.98421,0.99204,48.4,{"v":2E-120,"d":"2.00E-120"},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",1,374,380,1,374,377]
[null,"RALSYv5_mp0315","_","Ralstonia syzygii R24","_","putative Butyryl-CoA dehydrogenase","_",0.98421,0.99204,48.13,{"v":2E-120,"d":"2.00E-120"},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",1,374,380,1,374,377]
[null,"RSK60v3_mp750032","_","Ralstonia solanacearum K60","_","putative Butyryl-CoA dehydrogenase","_",0.98421,0.99204,48.66,{"v":5e-120,"d":"5.00E-120"},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",1,374,380,1,374,377]
[null,"SCFA_v1_1080002",null,"Ca. Phosphitivorax butyraticus R76","acdA","Acyl-CoA dehydrogenase","_",0.94256,0.95,48.75,{"v":9e-112,"d":"9.00E-112"},3,4,"_","1.3.8.-","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",16,374,380,16,375,383]
[null,"RALTA_B1110","_","Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.95526,0.9891,47.11,{"v":2e-111,"d":"2.00E-111"},1,1,"1 : Metabolism ;","1.3.99.-","2 : Cytoplasmic","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",12,374,380,2,364,367]
[null,"SCFA_v1_500014",null,"Ca. Phosphitivorax anaerolimi F81","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.93995,0.94737,47.5,{"v":4e-110,"d":"4.00E-110"},3,4,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",16,374,380,16,375,383]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.97105,0.97878,44.44,{"v":9e-110,"d":"9.00E-110"},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",6,374,380,4,372,377]
[null,"lpl1788","_","Legionella pneumophila Lens","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.96144,0.98421,44.39,{"v":2E-109,"d":"2.00E-109"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,373,380,8,380,389]
[null,"lpg1824","_","Legionella pneumophila subsp. pneumophila Philadelphia 1","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.96144,0.98421,44.39,{"v":2E-109,"d":"2.00E-109"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,373,380,8,380,389]
[null,"lpp1787","_","Legionella pneumophila Paris","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.96144,0.98421,44.39,{"v":2E-109,"d":"2.00E-109"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,373,380,8,380,389]
[null,"LPVv2_2096","_","Legionella pneumophila subsp. pneumophila HL06041035","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.96891,0.98421,44.39,{"v":2E-109,"d":"2.00E-109"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,373,380,5,377,386]
[null,"LPOv2_1885","_","Legionella pneumophila subsp. pneumophila Lorraine","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.96891,0.98421,44.39,{"v":2E-109,"d":"2.00E-109"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,373,380,5,377,386]
[null,"LPC_1268","_","Legionella pneumophila Corby","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.96891,0.98421,44.39,{"v":2E-109,"d":"2.00E-109"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,373,380,5,377,386]
[null,"MARHY1166",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","ivdA","Isovaleryl-coenzyme A dehydrogenase","_",0.94845,0.96842,44.29,{"v":4E-109,"d":"4.00E-109"},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",7,373,380,13,380,388]
[null,"PSEEN2889","_","Pseudomonas entomophila L48","acdA","acyl-CoA dehydrogenase","_",0.97389,0.98158,45.04,{"v":2e-108,"d":"2.00E-108"},1,1,"_","1.3.99.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,374,380,3,375,383]
[null,"MGMSRv2_0409","_","Magnetospirillum gryphiswaldense MSR-1 v2","_","Acyl-CoA dehydrogenase/oxidase","_",0.9509,0.96842,44.57,{"v":7e-107,"d":"7.00E-107"},1,1,"1.1.3.12 : Leucine degradation ;","1.3.8.4","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17540897, 8759838, 8655474","2a : Function from experimental evidences in other organisms",7,373,380,11,378,387]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.94359,0.96842,43.48,{"v":2e-106,"d":"2.00E-106"},2,2,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",7,373,380,14,381,390]
[null,"BRADO1447","_","Bradyrhizobium sp. ORS278","ivd2","isovaleryl-CoA dehydrogenase","_",0.94359,0.96842,44.84,{"v":4e-105,"d":"4.00E-105"},1,1,"1.1.3.12 : Leucine degradation ;","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",7,373,380,14,381,390]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.98421,0.99468,43.05,{"v":3e-104,"d":"3.00E-104"},1,4,"_","1.3.99.2","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,378,380,4,376,376]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.97368,0.98404,43.51,{"v":7e-104,"d":"7.00E-104"},1,4,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,374,380,4,372,376]
[null,"CMR15v5_0672",null,"Ralstonia solanacearum CMR15","_","putative acyl CoA dehydrogenase oxidoreductase protein","_",0.97368,0.98404,43.51,{"v":7e-102,"d":"7.00E-102"},1,4,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,374,380,4,372,376]
[null,"THI_3281",null,"Thiomonas sp. 3As","ivd","Isovaleryl-CoA dehydrogenase","_",0.96429,0.99474,42.06,{"v":3e-99,"d":"3.00E-99"},1,1,"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)",1,373,380,6,383,392]
[null,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.95526,0.968,43.8,{"v":9e-97,"d":"9.00E-97"},2,4,"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",12,374,380,10,372,375]
[null,"AZOLI_p40074","_","Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.98425,0.98684,41.6,{"v":6e-95,"d":"6.00E-95"},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)",1,374,380,1,373,381]
[null,"CLOSTRIBL3_v1_10853",null,"Clostridiaceae BL-3","carC","Caffeyl-CoA reductase-Etf complex subunit CarC","RHEA:46956 ;",0.97368,0.97625,41.08,{"v":2e-94,"d":"2.00E-94"},4,4,"_","1.3.1.108","2 : Cytoplasmic","_","e : enzyme",23479729,"2a : Function from experimental evidences in other organisms",6,374,380,4,373,379]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.95165,0.98421,41.18,{"v":5e-92,"d":"5.00E-92"},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",7,373,380,12,384,393]
[null,"RALTA_A0110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL-COA DEHYDROGENASE OXIDOREDUCTASE","_",0.95165,0.98421,41.18,{"v":2E-91,"d":"2.00E-91"},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",7,373,380,12,384,393]
[null,"CMR15v5_0667",null,"Ralstonia solanacearum CMR15","_","putative acyl-CoA dehydrogenase oxidoreductase","_",0.95165,0.98421,39.84,{"v":3e-90,"d":"3.00E-90"},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",7,373,380,12,384,393]
[null,"CLOSTRIBL3_v1_12012",null,"Clostridiaceae BL-3","carC","Caffeyl-CoA reductase-Etf complex subunit CarC","RHEA:46956 ;",0.98684,0.98684,38.13,{"v":1E-87,"d":"1.00E-87"},5,3,"_","1.3.1.108","2 : Cytoplasmic","_","e : enzyme",23479729,"2a : Function from experimental evidences in other organisms",1,375,380,1,373,380]
[null,"SCFA_v1_1630002","_","Ca. Propionivorax syntrophicum F70","acdB","Acyl-CoA dehydrogenase, short-chain specific","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47196 ; RHEA:24004 ;",0.95408,0.98421,39.84,{"v":4e-87,"d":"4.00E-87"},1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,375,380,16,387,392]
[null,"VIBNIv4_B0452",null,"Vibrio nigripulchritudo SFn1","_","putative Acyl-CoA dehydrogenase","_",0.9456,0.96053,39.18,{"v":2e-81,"d":"2.00E-81"},1,3,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",10,374,380,13,376,386]
[null,"MARHY1169",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","fadE","long chain acyl coenzyme A dehydrogenase","_",0.9712,0.97632,38.27,{"v":5e-81,"d":"5.00E-81"},4,1,"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)",9,374,380,6,376,382]
[null,"SCFA_v1_350006",null,"Ca. Phosphitivorax butyraticus R76","_","Butyryl-CoA dehydrogenase","_",0.97409,0.98947,36.7,{"v":1e-80,"d":"1.00E-80"},5,2,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,374,380,1,374,386]
[]
["CLOSTRIBL6_v1_3217","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_12010",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.97917,0.98503,54.71,{"v":7e-124,"d":"7.00E-124"},1,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",6,333,334,7,334,336]
[null,"CLOSTRIBL3_v1_20312",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.98503,0.98799,54.71,{"v":4e-117,"d":"4.00E-117"},2,2,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","c : carrier","17189250, 20059546, 21398533, 8655474, 11466286","2a : Function from experimental evidences in other organisms",6,333,334,7,333,333]
[null,"CD630_04010",null,"Clostridium difficile 630","etfA1","Alpha-subunit of electron transfer flavoprotein","_",0.94203,0.97305,53.85,{"v":3e-116,"d":"3.00E-116"},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",6,329,334,11,333,345]
[null,"CLOSTRIBL6_v1_0137",null,"Clostridiales BL-6","etfA","electron transfer flavoprotein (alpha subunit)","_",0.95376,0.98802,48.79,{"v":5e-107,"d":"5.00E-107"},1,1,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 20059546, 21398533","2a : Function from experimental evidences in other organisms",6,333,334,14,340,346]
[null,"CD630_08050",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein alpha-subunit","_",0.95294,0.97006,50,{"v":1e-105,"d":"1.00E-105"},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",8,331,334,18,340,340]
[null,"SBF1_v1_470014",null,"Desulfosporosinus sp. SbF1","fixB","electron-transferring flavoprotein, subunit FixB","_",0.73363,0.97305,49.85,{"v":4e-98,"d":"4.00E-98"},1,2,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,331,334,113,435,443]
[null,"CLOSTRIBL4_v1_1872",null,"Clostridiales BL-4","etfA","Electron transfer flavoprotein subunit alpha","_",0.95652,1.05389,46.59,{"v":4e-97,"d":"4.00E-97"},1,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",6,330,334,13,362,368]
[null,"CD630_10560",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.97321,0.97904,45.26,{"v":4e-89,"d":"4.00E-89"},3,2,"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",10,333,334,6,328,336]
[null,"CLOSTRIBL3_v1_20125",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.98802,0.99099,42.73,{"v":1e-88,"d":"1.00E-88"},4,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",6,333,334,2,329,333]
[null,"MGMSRv2_1064",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.89617,0.98204,44.82,{"v":6e-86,"d":"6.00E-86"},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)",8,331,334,31,357,366]
[null,"BURPHP2_0598",null,"Burkholderia phymatum STM815","fixB","Protein fixB, Electron transfer flavoprotein, alpha subunit","_",0.86364,0.96707,44.89,{"v":6e-84,"d":"6.00E-84"},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",8,326,334,35,356,374]
[null,"pRALTA_0380",null,"Cupriavidus taiwanensis LMG19424","fixB","Electron transfer flavoprotein, alpha subunit","_",0.86667,0.97305,44.62,{"v":9e-84,"d":"9.00E-84"},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",6,326,334,33,356,375]
[null,"BRADO5385",null,"Bradyrhizobium sp. ORS278","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.88587,0.97605,44.48,{"v":6e-80,"d":"6.00E-80"},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)",6,326,334,29,351,368]
[null,"RM41v1_psym670029",null,"Sinorhizobium sp. Rm41","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.94051,0.99401,42.47,{"v":2E-79,"d":"2.00E-79"},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",6,331,334,13,341,353]
[null,"MGMSRv2_0361",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","Electron transfer flavoprotein, alpha subunit","_",0.89674,0.98802,42.73,{"v":4E-79,"d":"4.00E-79"},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",6,331,334,32,359,368]
[null,"AZOLI_0536",null,"Azospirillum lipoferum 4B","fixB","electron transfer flavoprotein alpha chain","_",0.91086,0.97904,44.34,{"v":4E-79,"d":"4.00E-79"},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",6,326,334,22,345,359]
[null,"CLOSTRIBL3_v1_11487",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.99102,1.00915,43.81,{"v":1e-74,"d":"1.00E-74"},5,3,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,330,334,1,323,328]
[null,"CLOSTRIBL3_v1_11114",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.82921,1.00299,38.81,{"v":3e-71,"d":"3.00E-71"},6,3,"_","_","2 : Cytoplasmic","_","c : carrier",17189250,"2a : Function from experimental evidences in other organisms",6,333,334,68,398,404]
[null,"LEPBIa1132","_","Leptospira biflexa serovar Patoc Patoc 1","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.97305,1.01881,41.54,{"v":2E-70,"d":"2.00E-70"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","16.10 : Respire ;","c : carrier","_","2a : Function from experimental evidences in other organisms",7,331,334,3,316,319]
[null,"SCFA_v1_500012",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",1,1.003,39.22,{"v":1e-69,"d":"1.00E-69"},2,2,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,331,334,1,329,333]
[null,"SBF1_v1_6700004",null,"Desulfosporosinus sp. SbF1","etfA_2","electron-transferring flavoprotein, alpha subunit EtfA (lutD-associated)","_",0.83333,1.00299,39.4,{"v":4e-69,"d":"4.00E-69"},3,3,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",6,333,334,68,396,402]
[null,"CD630_11720",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.81773,0.99401,37.95,{"v":1e-67,"d":"1.00E-67"},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",6,333,334,66,394,406]
[null,"BN45v3_60005","_","Mycobacterium canettii STB-J","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.99102,1.04088,42.6,{"v":4e-65,"d":"4.00E-65"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",7,333,334,3,317,318]
[null,"BN44v3_60522","_","Mycobacterium canettii STB-D","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.99102,1.04088,42.6,{"v":6E-65,"d":"6.00E-65"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",7,333,334,3,317,318]
[null,"BN43v3_60007","_","Mycobacterium canettii STB-L","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.99102,1.04088,42.6,{"v":6E-65,"d":"6.00E-65"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",7,333,334,3,317,318]
[null,"BN42v3_41031","_","Mycobacterium canettii STB-K","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.99102,1.04088,42.3,{"v":2e-64,"d":"2.00E-64"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",7,333,334,3,317,318]
[null,"HEAR0620",null,"Herminiimonas arsenicoxydans","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.87725,0.94822,41.3,{"v":4e-57,"d":"4.00E-57"},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",39,329,334,29,308,309]
[null,"METDI2208",null,"Methylobacterium extorquens DM4","etfA","electron transfer flavoprotein, NAD/FAD-binding domain and ETFP adenine nucleotide-binding domain-like","_",0.9012,0.94953,39.53,{"v":2E-55,"d":"2.00E-55"},1,2,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","15188393, 16926146, 8599534","2a : Function from experimental evidences in other organisms",35,333,334,25,315,317]
[null,"BURPHK2_1883",null,"Burkholderia phymatum STM815","etfA","electron transfer flavoprotein, alpha subunit","_",0.87725,0.9391,39.25,{"v":6e-55,"d":"6.00E-55"},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",35,325,334,25,306,312]
[null,"Mchl_1823",null,"Methylobacterium extorquens CM4","etfA","electron transfer flavoprotein alpha subunit","_",0.9012,0.94953,39.2,{"v":1E-54,"d":"1.00E-54"},1,2,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","15188393, 16926146, 8599534","2a : Function from experimental evidences in other organisms",35,333,334,25,315,317]
[null,"NMV_2368",null,"Neisseria meningitidis NEM8013","etfA","electron transfer flavoprotein alpha-subunit (alpha-ETF; electron transfer flavoprotein large subunit; ETFLS)","_",0.88323,0.94855,40.68,{"v":2e-53,"d":"2.00E-53"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","f : factor","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",40,330,334,29,310,311]
[null,"AZOLI_p50300",null,"Azospirillum lipoferum 4B","etfA2","Electron transfer flavoprotein alpha-subunit","_",0.88623,0.94872,39.53,{"v":2e-53,"d":"2.00E-53"},1,2,"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)",35,329,334,26,311,312]
[null,"CMR15v5_3436",null,"Ralstonia solanacearum CMR15","etfA","Electron transfer flavoprotein, alpha-subunit","_",0.87725,0.94212,38.91,{"v":5E-52,"d":"5.00E-52"},1,2,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",39,329,334,29,310,311]
[null,"RALTA_A0796",null,"Cupriavidus taiwanensis LMG19424","etfA","ELECTRON TRANSFER FLAVOPROTEIN, ALPHA-SUBUNIT","_",0.88323,0.94855,40.34,{"v":1E-51,"d":"1.00E-51"},1,2,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",39,329,334,29,310,311]
[null,"PSHAa1617",null,"Pseudoalteromonas haloplanktis TAC125","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.79341,0.86039,37.74,{"v":3e-50,"d":"3.00E-50"},1,2,"2.5.4 : Menaquinone and ubiquinone ;","_","unknown","_","u : unknown",8599534,"2a : Function from experimental evidences in other organisms",61,325,334,52,304,308]
[null,"ACIAD2654",null,"Acinetobacter baylyi ADP1","etfA","electron transfer flavoprotein alpha-subunit","_",0.94311,1.01286,39.37,{"v":2e-49,"d":"2.00E-49"},1,2,"1.4.3 : electron carrier ;","_","1 : Unknown","_","f : factor","_","2a : Function from experimental evidences in other organisms",35,329,334,25,311,311]
[null,"PSEEN3657",null,"Pseudomonas entomophila L48","etfA","electron transfer flavoprotein alpha-subunit","_",0.83533,1.01087,39.43,{"v":7e-49,"d":"7.00E-49"},1,2,"1.4.3 : Electron carrier ;","_","Unknown","6 : Energy metabolism ;","c : carrier","_","2a : Function from experimental evidences in other organisms",47,325,334,8,272,276]
[null,"VIBNIv4_B0455",null,"Vibrio nigripulchritudo SFn1","etfA","Electron transfer flavoprotein subunit alpha","_",0.85329,0.91935,38.25,{"v":9e-49,"d":"9.00E-49"},1,1,"1.4.1 : Electron donor ;","_","1 : Unknown","5.8 : Electron carrier regeneration ;","c : carrier","8599534, 12597275","2a : Function from experimental evidences in other organisms",52,330,334,40,308,310]
[null,"NT26v4_3414",null,"Rhizobium sp. NT-26","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.86527,0.93528,39.1,{"v":6e-48,"d":"6.00E-48"},1,2,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",39,325,334,29,305,309]
[]
["CLOSTRIBL6_v1_3218","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_12011",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.98507,1.00763,50,{"v":6e-82,"d":"6.00E-82"},1,1,"1.3 : Energy metabolism (carbon) ;","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,260,268,1,258,262]
[null,"CD630_08040",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein beta-subunit, core","_",0.98881,1.00379,51.32,{"v":1e-81,"d":"1.00E-81"},1,2,"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",1,262,268,1,258,264]
[null,"CD630_04000",null,"Clostridium difficile 630","etfB1","Beta-subunit of electron transfer flavoprotein","_",1,1.02682,47.39,{"v":6e-73,"d":"6.00E-73"},2,2,"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",1,268,268,1,261,261]
[null,"MGMSRv2_0362",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","Electron transfer flavoprotein, beta-subunit","_",0.88732,0.9403,48.41,{"v":1e-71,"d":"1.00E-71"},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",1,246,268,1,248,284]
[null,"CLOSTRIBL3_v1_20311",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.98134,1.01544,48.29,{"v":4E-70,"d":"4.00E-70"},3,2,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286, 9694853","2a : Function from experimental evidences in other organisms",1,261,268,1,253,259]
[null,"CLOSTRIBL6_v1_0136",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein subunit beta","_",0.94776,0.98069,48.03,{"v":1e-69,"d":"1.00E-69"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,254,268,1,246,259]
[null,"SBF1_v1_470015",null,"Desulfosporosinus sp. SbF1","fixA","electron-transferring flavoprotein, subunit FixA","_",0.89892,0.9291,43.37,{"v":4e-69,"d":"4.00E-69"},1,1,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,246,268,1,243,277]
[null,"CD630_10550",null,"Clostridium difficile 630","etfB","Electron transfer flavoproteins subunit beta","_",1,1.01132,43.28,{"v":8e-69,"d":"8.00E-69"},3,2,"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",1,268,268,6,265,265]
[null,"AZOLI_0535",null,"Azospirillum lipoferum 4B","fixA","electron transfer flavoprotein beta subunit","_",0.92226,0.97388,44.83,{"v":3e-67,"d":"3.00E-67"},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",1,255,268,1,257,283]
[null,"BRADO5386",null,"Bradyrhizobium sp. ORS278","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",1,1.04851,44.13,{"v":5e-67,"d":"5.00E-67"},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)",1,266,268,1,279,281]
[null,"pRALTA_0381",null,"Cupriavidus taiwanensis LMG19424","fixA","Electron transfer flavoprotein beta-subunit","_",0.93617,0.98507,43.94,{"v":1e-66,"d":"1.00E-66"},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",1,261,268,1,257,282]
[null,"MGMSRv2_1063",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.91727,0.95149,43.14,{"v":9e-66,"d":"9.00E-66"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,252,268,1,248,278]
[null,"SBF1_v1_6700003",null,"Desulfosporosinus sp. SbF1","etfB_2","electron-transferring flavoprotein, beta subunit EtfB (lutD-associated)","_",0.8806,0.93281,42.8,{"v":6e-63,"d":"6.00E-63"},2,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,235,268,1,230,253]
[null,"RM41v1_psym670028",null,"Sinorhizobium sp. Rm41","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.83562,0.91045,45.49,{"v":2e-62,"d":"2.00E-62"},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)",1,241,268,1,242,292]
[null,"CLOSTRIBL4_v1_1871",null,"Clostridiales BL-4","etfB","Electron transfer flavoprotein subunit beta","_",1.01493,1.02256,44.12,{"v":3e-61,"d":"3.00E-61"},1,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,268,268,1,266,266]
[null,"BURPHP2_0599",null,"Burkholderia phymatum STM815","fixA","protein fixA, electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.85106,0.89552,44.58,{"v":4e-61,"d":"4.00E-61"},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",1,237,268,1,237,282]
[null,"CLOSTRIBL3_v1_11115",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.98881,1.01145,40.38,{"v":5e-61,"d":"5.00E-61"},4,2,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,261,268,1,259,262]
[null,"CD630_11710",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein subunit alpha","_",0.98881,1,40.75,{"v":8e-59,"d":"8.00E-59"},4,1,"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",1,261,268,4,262,265]
[null,"CLOSTRIBL3_v1_20124",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1,1.01132,38.43,{"v":5E-56,"d":"5.00E-56"},5,3,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,264,268,1,261,265]
[null,"CLOSTRIBL3_v1_11488",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1.00746,1.01887,40,{"v":1e-55,"d":"1.00E-55"},6,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,268,268,1,264,265]
[null,"SCFA_v1_1080001",null,"Ca. Phosphitivorax butyraticus R76","etfB","Electron transfer flavoprotein subunit beta (fragment)","_",0.6791,1.00552,37.36,{"v":5e-35,"d":"5.00E-35"},2,2,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,182,268,2,178,181]
[null,"BN77v1_0452","_","Rhizobium mesoamericanum STM3625","etfB","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.64925,0.87,36.78,{"v":5e-22,"d":"5.00E-22"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier",10026281,"2a : Function from experimental evidences in other organisms",1,173,268,34,199,200]
[]
["CLOSTRIBL6_v1_3220","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)","_",0.94316,0.96137,49.55,{"v":1e-158,"d":"1.00E-158"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",23,470,475,24,465,466]
[null,"CD630_11730",null,"Clostridium difficile 630","_","Putative FAD-linked oxidase","_",0.94316,0.9676,49.55,{"v":6e-154,"d":"6.00E-154"},1,1,"_","1.1.-.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",22,469,475,21,462,463]
[null,"BSU28680","_","Bacillus subtilis 168","glcD","glycolate oxidase subunit","GLYCOLATEDEHYDRO-RXN ; RHEA:21264 ;",0.92632,0.93617,40.68,{"v":5e-103,"d":"5.00E-103"},1,1,"2.1.1 : Specific pathways ;","1.1.99.14","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8606183, 25217009","2a : Function from experimental evidences in other organisms",33,469,475,29,457,470]
[null,"SBF1_v1_320003",null,"Desulfosporosinus sp. SbF1","lutD","D-lactate, L-lactate, and/or glycolate dehydrogenase, FAD-linked subunit","_",0.98737,1.01515,36.67,{"v":1e-94,"d":"1.00E-94"},2,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",7,472,475,2,461,462]
[null,"HELPY_0844","_","Helicobacter pylori B38","glcD","Glycolate oxidase subunit","_",0.89895,0.93028,37.94,{"v":9e-86,"d":"9.00E-86"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","1.1.2.4","1 : Unknown","6.11 : TCA cycle ;","e : enzyme","11283302, 8606183","2a : Function from experimental evidences in other organisms",45,469,475,39,457,459]
[null,"THI_0812","_","Thiomonas sp. 3As","_","putative D-lactate dehydrogenase","_",0.95579,0.97009,35.24,{"v":2e-71,"d":"2.00E-71"},1,1,"1 : Metabolism ;","1.1.2.4","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",25,469,475,32,466,468]
[]
["CLOSTRIBL6_v1_2270","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,"CLOSTRIBL4_v1_1443","_","Clostridiales BL-4","_","putative Acyl-CoA thioesterase","_",1,1,79.87,{"v":3e-90,"d":"3.00E-90"},1,1,"_","3.1.2.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,159,159,1,159,159]
[null,"LEPBIa0300","_","Leptospira biflexa serovar Patoc Patoc 1","_","Acetyl-CoA hydrolase","_",0.90533,0.96226,40.52,{"v":1e-30,"d":"1.00E-30"},1,1,"_","3.1.2.1","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,153,159,5,157,169]
[null,"BTCD_v1_0785","_","Brochothrix thermosphacta CD337","ykhA","promiscuous acyl-CoA thioesterase","ACYL-COA-HYDROLASE-RXN ;",0.88953,0.96226,37.91,{"v":3E-28,"d":"3.00E-28"},1,1,"_","3.1.2.-","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","12426338, 18247525, 24623648, 24722906","2a : Function from experimental evidences in other organisms",7,158,159,5,157,172]
[null,"BSU13030","_","Bacillus subtilis 168","ykhA","promiscuous acyl-CoA thioesterase","ACYL-COA-HYDROLASE-RXN ;",0.91279,0.98742,36.94,{"v":1E-25,"d":"1.00E-25"},1,1,"2.4 : Metabolism of lipids ;","3.1.2.-","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","12426338, 18247525, 24623648, 24722906","2a : Function from experimental evidences in other organisms",1,151,159,1,157,172]
[null,"Deide_20410","_","Deinococcus deserti VCD115","_","putative acyl-CoA hydrolase","_",0.76101,0.83448,36.36,{"v":6e-21,"d":"6.00E-21"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",12,131,159,11,131,145]
[null,"BN424_2932","_","Carnobacterium maltaromaticum LMA28 v1","_","putative acyl-CoA hydrolase","_",0.81183,0.94969,35.1,{"v":2e-17,"d":"2.00E-17"},1,1,"_","3.1.2.-","2 : Cytoplasmic","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",7,155,159,10,160,186]
[]
["CLOSTRIBL6_v1_2820","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_11487",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.98171,0.98171,64.91,{"v":7e-149,"d":"7.00E-149"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,322,328,1,322,328]
[null,"CLOSTRIBL6_v1_0137",null,"Clostridiales BL-6","etfA","electron transfer flavoprotein (alpha subunit)","_",0.95087,1.00305,43.16,{"v":8E-79,"d":"8.00E-79"},1,2,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 20059546, 21398533","2a : Function from experimental evidences in other organisms",6,328,328,14,342,346]
[null,"SBF1_v1_6700004",null,"Desulfosporosinus sp. SbF1","etfA_2","electron-transferring flavoprotein, alpha subunit EtfA (lutD-associated)","_",0.82338,1.00915,45.02,{"v":2E-78,"d":"2.00E-78"},1,2,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",2,328,328,68,398,402]
[null,"CLOSTRIBL3_v1_20312",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.98198,0.99695,43.12,{"v":2E-78,"d":"2.00E-78"},2,3,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","c : carrier","17189250, 20059546, 21398533, 8655474, 11466286","2a : Function from experimental evidences in other organisms",6,326,328,7,333,333]
[null,"CD630_08050",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein alpha-subunit","_",0.96176,0.99695,44.04,{"v":3e-78,"d":"3.00E-78"},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",7,323,328,17,339,340]
[null,"CD630_04010",null,"Clostridium difficile 630","etfA1","Alpha-subunit of electron transfer flavoprotein","_",0.93623,0.98476,43.34,{"v":2e-76,"d":"2.00E-76"},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",6,322,328,11,333,345]
[null,"CLOSTRIBL3_v1_11114",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.82178,1.0122,43.07,{"v":2e-74,"d":"2.00E-74"},3,2,"_","_","2 : Cytoplasmic","_","c : carrier",17189250,"2a : Function from experimental evidences in other organisms",2,326,328,68,398,404]
[null,"CD630_11720",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.80049,0.99085,40.62,{"v":3e-74,"d":"3.00E-74"},3,2,"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",6,326,328,70,394,406]
[null,"CD630_10560",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.99107,1.01524,41.14,{"v":1E-73,"d":"1.00E-73"},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",8,328,328,4,330,336]
[null,"CLOSTRIBL3_v1_20125",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.99099,1.0061,41.52,{"v":1e-72,"d":"1.00E-72"},4,3,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",6,328,328,2,331,333]
[null,"BURPHP2_0598",null,"Burkholderia phymatum STM815","fixB","Protein fixB, Electron transfer flavoprotein, alpha subunit","_",0.87968,1.00305,39.51,{"v":1e-64,"d":"1.00E-64"},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",3,318,328,30,355,374]
[null,"pRALTA_0380",null,"Cupriavidus taiwanensis LMG19424","fixB","Electron transfer flavoprotein, alpha subunit","_",0.87733,1.00305,38.6,{"v":2e-62,"d":"2.00E-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",3,318,328,30,355,375]
[null,"CLOSTRIBL3_v1_12010",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.97619,1,38.72,{"v":3e-62,"d":"3.00E-62"},6,3,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",6,326,328,7,334,336]
[null,"AZOLI_0536",null,"Azospirillum lipoferum 4B","fixB","electron transfer flavoprotein alpha chain","_",0.91643,1.00305,36.47,{"v":6e-62,"d":"6.00E-62"},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",3,318,328,19,344,359]
[null,"CLOSTRIBL6_v1_3217",null,"Clostridiales BL-6","etfA","Electron transfer flavoprotein subunit alpha","_",0.98503,1.00305,41.34,{"v":4e-61,"d":"4.00E-61"},2,2,"_","_","2 : Cytoplasmic","_","e : enzyme",9694853,"2a : Function from experimental evidences in other organisms",6,326,328,6,333,334]
[null,"BRADO5385",null,"Bradyrhizobium sp. ORS278","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.90761,1.01829,35.03,{"v":1E-59,"d":"1.00E-59"},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)",3,324,328,26,356,368]
[null,"MGMSRv2_1064",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.87978,0.98171,36.02,{"v":1E-58,"d":"1.00E-58"},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)",7,318,328,30,351,366]
[null,"SBF1_v1_470014",null,"Desulfosporosinus sp. SbF1","fixB","electron-transferring flavoprotein, subunit FixB","_",0.73815,0.99695,39.14,{"v":1e-57,"d":"1.00E-57"},3,3,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,318,328,109,429,443]
[null,"SCFA_v1_500012",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",0.96697,0.98171,36.02,{"v":1e-57,"d":"1.00E-57"},1,3,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,322,328,6,327,333]
[null,"MGMSRv2_0361",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","Electron transfer flavoprotein, alpha subunit","_",0.88859,0.99695,35.17,{"v":8e-56,"d":"8.00E-56"},2,3,"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",6,318,328,32,353,368]
[null,"CLOSTRIBL4_v1_1872",null,"Clostridiales BL-4","etfA","Electron transfer flavoprotein subunit alpha","_",0.97554,1.09451,35.38,{"v":2e-54,"d":"2.00E-54"},1,3,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",6,327,328,13,366,368]
[null,"BN42v3_41031",null,"Mycobacterium canettii STB-K","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.99085,1.02201,35.69,{"v":1E-46,"d":"1.00E-46"},1,3,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",8,326,328,4,317,318]
[]
["CLOSTRIBL6_v1_2821","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","_",1,1.00377,60.9,{"v":2e-110,"d":"2.00E-110"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,266,266,1,264,265]
[null,"CLOSTRIBL3_v1_20124",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.97744,0.98113,42.69,{"v":3e-63,"d":"3.00E-63"},2,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,260,266,1,255,265]
[null,"CLOSTRIBL3_v1_11115",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1.00376,1.01908,39.7,{"v":2e-61,"d":"2.00E-61"},3,1,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,266,266,1,262,262]
[null,"CD630_08040",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein beta-subunit, core","_",0.98872,0.99621,41.44,{"v":3e-59,"d":"3.00E-59"},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",1,256,266,1,258,264]
[null,"CLOSTRIBL6_v1_3218",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein subunit beta","_",0.95149,0.95865,43.53,{"v":1E-58,"d":"1.00E-58"},1,2,"_","_","2 : Cytoplasmic","_","e : enzyme",9694853,"2a : Function from experimental evidences in other organisms",1,250,266,1,252,268]
[null,"SBF1_v1_6700003",null,"Desulfosporosinus sp. SbF1","etfB_2","electron-transferring flavoprotein, beta subunit EtfB (lutD-associated)","_",0.86842,0.91304,41.56,{"v":2e-57,"d":"2.00E-57"},1,2,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,231,266,1,229,253]
[null,"CLOSTRIBL4_v1_1871",null,"Clostridiales BL-4","etfB","Electron transfer flavoprotein subunit beta","_",0.8985,0.8985,43.1,{"v":3e-55,"d":"3.00E-55"},1,3,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,235,266,1,237,266]
[null,"CD630_11710",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein subunit alpha","_",0.93985,0.9434,39.6,{"v":4E-55,"d":"4.00E-55"},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",1,250,266,4,250,265]
[null,"CD630_04000",null,"Clostridium difficile 630","etfB1","Beta-subunit of electron transfer flavoprotein","_",0.8797,0.89655,41.03,{"v":1E-54,"d":"1.00E-54"},3,3,"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",1,234,266,1,231,261]
[null,"CLOSTRIBL3_v1_12011",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1,1.01527,37.59,{"v":5e-54,"d":"5.00E-54"},5,3,"1.3 : Energy metabolism (carbon) ;","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,266,266,1,262,262]
[null,"CLOSTRIBL6_v1_0136",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein subunit beta","_",0.86466,0.88803,42.61,{"v":1E-53,"d":"1.00E-53"},2,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,230,266,1,225,259]
[null,"CD630_10550",null,"Clostridium difficile 630","etfB","Electron transfer flavoproteins subunit beta","_",1.01128,1.01509,38.66,{"v":2e-48,"d":"2.00E-48"},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",1,266,266,6,265,265]
[null,"CLOSTRIBL3_v1_20311",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.86466,0.88803,40,{"v":4e-47,"d":"4.00E-47"},6,3,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286, 9694853","2a : Function from experimental evidences in other organisms",1,230,266,1,225,259]
[null,"SBF1_v1_470015",null,"Desulfosporosinus sp. SbF1","fixA","electron-transferring flavoprotein, subunit FixA","_",0.87004,0.90602,38.17,{"v":8e-47,"d":"8.00E-47"},2,3,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,238,266,1,238,277]
[null,"BURPHP2_0599",null,"Burkholderia phymatum STM815","fixA","protein fixA, electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.86525,0.91729,38.52,{"v":3e-45,"d":"3.00E-45"},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",1,234,266,1,237,282]
[null,"AZOLI_0535",null,"Azospirillum lipoferum 4B","fixA","electron transfer flavoprotein beta subunit","_",0.95406,1.01504,35.19,{"v":5e-45,"d":"5.00E-45"},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",1,259,266,1,267,283]
[null,"MGMSRv2_1063",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.96043,1.00376,35.58,{"v":9e-45,"d":"9.00E-45"},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)",1,260,266,1,265,278]
[null,"pRALTA_0381",null,"Cupriavidus taiwanensis LMG19424","fixA","Electron transfer flavoprotein beta-subunit","_",0.85461,0.90602,37.34,{"v":5e-43,"d":"5.00E-43"},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",1,234,266,1,237,282]
[null,"MGMSRv2_0362",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","Electron transfer flavoprotein, beta-subunit","_",0.95423,1.0188,35.06,{"v":3e-42,"d":"3.00E-42"},2,3,"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",1,259,266,1,269,284]
[null,"BRADO5386",null,"Bradyrhizobium sp. ORS278","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.86477,0.91353,35.8,{"v":2e-39,"d":"2.00E-39"},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)",1,236,266,1,240,281]
[null,"SCFA_v1_1630003",null,"Ca. Propionivorax syntrophicum F70","FixA","Electron transfer flavoproteins subunit beta","_",0.86466,0.87121,36.09,{"v":2e-38,"d":"2.00E-38"},1,2,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,227,266,1,226,264]
[null,"SCFA_v1_500013",null,"Ca. Phosphitivorax anaerolimi F81","etfB","Electron transfer flavoprotein, beta subunit","_",0.88278,0.90602,37.34,{"v":5E-36,"d":"5.00E-36"},1,3,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,236,266,2,235,273]
[null,"BN42v3_41032",null,"Mycobacterium canettii STB-K","fixA","Putative electron transfer flavoprotein (beta-subunit) FixA (beta-ETF) (electron transfer flavoprotein small subunit) (ETFSS)","_",0.95113,0.96198,35.57,{"v":2e-34,"d":"2.00E-34"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,252,266,3,250,263]
[]
["CLOSTRIBL6_v1_0258","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_1550009",null,"Ca. Phosphitivorax anaerolimi F81","_","putative ferredoxin","_",0.08696,0.87719,38,9e-06,1,9,"_","_","9 : Periplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",6,55,575,4,53,57]
[]
["CLOSTRIBL6_v1_0260","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_08930",null,"Clostridium difficile 630","_","Putative iron-dependent hydrogenase","_",0.93124,1.00637,44.09,{"v":3E-131,"d":"3.00E-131"},1,2,"_","1.12.7.2","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",4,455,471,17,482,509]
[null,"CD630_08940",null,"Clostridium difficile 630","_","Putative iron-dependent hydrogenase","_",0.95582,1.01062,41.18,{"v":7E-126,"d":"7.00E-126"},2,1,"_","1.12.7.2","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",4,456,471,4,474,498]
[null,"SCFA_v1_1550009",null,"Ca. Phosphitivorax anaerolimi F81","_","putative ferredoxin","_",0.10403,0.85965,42.86,1e-07,3,4,"_","_","9 : Periplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",95,143,471,8,54,57]
[null,"RM41v1_psym670036",null,"Sinorhizobium sp. Rm41","fdxN","Ferredoxin-like protein in nif region","_",0.11253,0.82812,35.85,0.0006,1,3,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ; 6.5 : Electron transport ; 16.15 : Symbiosis ;","c : carrier","6389527, 2842320, 2747618, 1603075","1c : Function from experimental evidences in the studied genus",93,139,471,6,56,64]
[]
["CLOSTRIBL6_v1_1906","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_13020","_","Clostridiaceae BL-3","hyd","Ferredoxin hydrogenase","HYDROG-RXN ; RHEA:17445 ;",0.78619,0.81149,44.76,{"v":2E-107,"d":"2.00E-107"},1,1,"_","1.12.7.2","2 : Cytoplasmic","_","e : enzyme","10368269, 9836629","2a : Function from experimental evidences in other organisms",80,430,435,90,441,449]
[null,"CD630_32580","_","Clostridium difficile 630","_","Iron hydrogenase","_",0.74686,0.82069,40.62,{"v":2e-93,"d":"2.00E-93"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","10368269, 9836629","2a : Function from experimental evidences in other organisms",74,429,435,111,456,478]
[]
["CLOSTRIBL6_v1_2017","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_08930",null,"Clostridium difficile 630","_","Putative iron-dependent hydrogenase","_",0.9725,1.02911,42.02,{"v":5e-132,"d":"5.00E-132"},1,1,"_","1.12.7.2","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,479,481,16,509,509]
[null,"CLOSTRIBL6_v1_0260","_","Clostridiales BL-6","_","putative Periplasmic (Fe) hydrogenase","_",0.921,0.94055,44.02,{"v":3e-130,"d":"3.00E-130"},1,1,"_","1.12.7.2","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,438,481,4,440,471]
[null,"CLOSTRIBL3_v1_20317","_","Clostridiaceae BL-3","_","putative Ferredoxin hydrogenase","_",0.95161,0.98129,42.37,{"v":2e-127,"d":"2.00E-127"},1,1,"_","1.12.7.2","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,454,481,2,469,496]
[null,"CD630_08940",null,"Clostridium difficile 630","_","Putative iron-dependent hydrogenase","_",0.91566,0.94802,41.67,{"v":1e-121,"d":"1.00E-121"},2,2,"_","1.12.7.2","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,438,481,3,458,498]
[null,"CLOSTRIBL4_v1_2149","_","Clostridiales BL-4","_","putative Ferredoxin hydrogenase","_",0.9521,0.99168,38.16,{"v":2e-110,"d":"2.00E-110"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",9,460,481,10,486,501]
[]
["CLOSTRIBL6_v1_2260","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,"CLOSTRIBL4_v1_2217",null,"Clostridiales BL-4","ackA","Acetate kinase","ACETATEKIN-RXN ; RHEA:11355 ;",0.95683,0.99501,68.42,0,1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","10360571, 10074080","2a : Function from experimental evidences in other organisms",1,398,401,1,398,417]
[null,"CLOSTRIBL3_v1_10746",null,"Clostridiaceae BL-3","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ; RHEA:11352 ;",1,1.00501,57.11,{"v":1E-156,"d":"1.00E-156"},1,1,"_","2.7.2.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8226682, 9811655, 11244084, 16995897, 19019159, 26098117","2a : Function from experimental evidences in other organisms",1,401,401,1,398,399]
[null,"SBF1_v1_800074","_","Desulfosporosinus sp. SbF1","ackA","acetate kinase","ACETATEKIN-RXN ; RHEA:11355 ;",0.99501,1.00504,52.13,{"v":2E-150,"d":"2.00E-150"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,399,401,1,397,397]
[null,"CD630_11750",null,"Clostridium difficile 630","ackA","Acetate kinase (Acetokinase)","_",1,1.00754,51.37,{"v":3e-143,"d":"3.00E-143"},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",1,399,401,1,398,398]
[null,"BSU29470","_","Bacillus subtilis 168","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ; RHEA:11352 ;",0.97756,0.99241,51.79,{"v":2E-140,"d":"2.00E-140"},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",2,393,401,3,389,395]
[null,"SSV_v1_0105","_","Streptococcus sanguinis 2908","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ;",0.98753,0.99748,50.25,{"v":7e-133,"d":"7.00E-133"},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",2,395,401,3,392,397]
[null,"BTCD_v1_0691","_","Brochothrix thermosphacta CD337","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ;",0.99002,0.99002,47.36,{"v":3e-130,"d":"3.00E-130"},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",2,397,401,3,397,401]
[null,"NMA1718","_","Neisseria meningitidis Z2491","ackA1","acetate kinase 1 (acetokinase 1)","_",0.97059,0.98753,46.21,{"v":6e-119,"d":"6.00E-119"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,394,401,16,402,408]
[null,"NMV_0875","_","Neisseria meningitidis NEM8013","ackA1","acetate kinase 1 (acetokinase 1)","_",0.98753,0.99497,46.21,{"v":6e-119,"d":"6.00E-119"},1,1,"1.3.5 : Fermentation ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,394,401,6,392,398]
[null,"EFER_2027","_","Escherichia fergusonii ATCC 35469T","_","putative acetate/propionate kinase pduW","_",0.9802,0.98753,45.45,{"v":2E-118,"d":"2.00E-118"},1,1,"_","2.7.2.1","1 : Unknown","_","e : enzyme",10498708,"3 : Putative function from multiple computational evidences",2,397,401,4,392,404]
[null,"BN12v2_1100005","_","Tetrasphaera japonica T1-X7","ackA","Acetate kinase","_",0.99002,1,45.09,{"v":2e-112,"d":"2.00E-112"},1,1,"_","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",3,398,401,6,395,397]
[null,"BN13v1_910016","_","Tetrasphaera jenkinsii Ben74","ackA","Acetate kinase","_",0.99002,1.00761,45.09,{"v":4E-109,"d":"4.00E-109"},1,1,"_","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",2,398,401,3,392,394]
[null,"VIBNIv4_B1211","_","Vibrio nigripulchritudo SFn1","ackA","Acetate kinase","_",0.98254,0.99244,44.16,{"v":8e-108,"d":"8.00E-108"},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",3,394,401,6,393,397]
[null,"VC1098","_","Vibrio cholerae N16961","ackA","acetate kinase","_",0.98005,0.98744,42.49,{"v":3e-105,"d":"3.00E-105"},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",3,394,401,5,392,398]
[null,"VIBNIv4_A2401","_","Vibrio nigripulchritudo SFn1","ackA","acetate kinase","_",0.98005,0.98744,41.98,{"v":2e-103,"d":"2.00E-103"},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",3,394,401,5,392,398]
[null,"ECS88_4678","_","Escherichia coli S88","_","Putative Acetate/propionate kinase","_",0.90805,0.98504,40.51,{"v":9E-103,"d":"9.00E-103"},1,1,"_","2.7.2.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,397,401,43,431,435]
[null,"ECED1_3455","_","Escherichia coli ED1a","_","Putative Acetate/propionate kinase","_",0.90805,0.98504,40.51,{"v":1e-102,"d":"1.00E-102"},1,1,"_","2.7.2.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,397,401,43,431,435]
[null,"BN45v3_10447","_","Mycobacterium canettii STB-J","ackA","Putative acetate kinase AckA (acetokinase)","_",0.97506,1.01558,41.94,{"v":2e-101,"d":"2.00E-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",3,393,401,5,375,385]
[null,"BN44v3_10450","_","Mycobacterium canettii STB-D","ackA","Putative acetate kinase AckA (acetokinase)","_",0.97506,1.01558,41.94,{"v":7e-101,"d":"7.00E-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",3,393,401,5,375,385]
[null,"VS_II1135","_","Vibrio tasmaniensis LGP32","ackA-2","Acetate kinase","ACETATEKIN-RXN ; RXN-7958 ;",0.98753,0.99748,42.17,{"v":2E-100,"d":"2.00E-100"},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",3,394,401,6,393,397]
[null,"BN43v3_10442","_","Mycobacterium canettii STB-L","ackA","Putative acetate kinase AckA (acetokinase)","_",0.97506,1.01558,41.69,{"v":3e-100,"d":"3.00E-100"},1,1,"7 : intermediary metabolism and respiration ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",3,393,401,5,375,385]
[null,"BN11v3_1350008","_","Tetrasphaera australiensis Ben110","ackA","acetate kinase A and propionate kinase 2","_",0.97756,0.98246,44.13,{"v":5e-100,"d":"5.00E-100"},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",2,393,401,7,391,399]
[null,"BN42v3_20130","_","Mycobacterium canettii STB-K","ackA","Putative acetate kinase AckA (acetokinase)","_",0.97506,1.01558,41.43,{"v":3e-99,"d":"3.00E-99"},1,1,"7 : intermediary metabolism and respiration ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",3,393,401,5,375,385]
[null,"MARHY2148","_","Marinobacter hydrocarbonoclasticus ATCC 49840","ackA","acetate kinase A and propionate kinase 2","_",0.99501,0.99501,40.1,{"v":8e-99,"d":"8.00E-99"},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",3,400,401,5,394,401]
[null,"BN10v3_560037","_","Tetrasphaera elongata Lp2","ackA","Acetate kinase","_",0.99002,1.05585,43.58,{"v":1e-98,"d":"1.00E-98"},1,1,"_","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",3,398,401,5,370,376]
[null,"ABAYE3282","_","Acinetobacter baumannii AYE","ack","acetate kinase (propionate kinase)","_",0.99002,0.9925,40.81,{"v":2e-94,"d":"2.00E-94"},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",3,399,401,5,388,400]
[null,"ACIAD0541","_","Acinetobacter baylyi ADP1","ack","acetate kinase (propionate kinase)","ACETATEKIN-RXN ; PROPKIN-RXN ; RXN-7958 ; RHEA:11355 ; RHEA:23151 ;",0.99252,0.99252,40.7,{"v":2E-90,"d":"2.00E-90"},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",3,399,401,5,389,401]
[null,"BN874v1_640030","_","Candidatus Contendobacter odensis Run_B_J11","ackA","Acetate/propionate kinase","_",1.01995,1.04337,39.61,{"v":2e-89,"d":"2.00E-89"},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",3,398,401,5,391,392]
[null,"HELPY_0888",null,"Helicobacter pylori B38","_","Fragment of putative acetate kinase AckA (Part 1)","_",0.7182,0.96,47.92,{"v":1E-87,"d":"1.00E-87"},1,1,"1.3.5 : Fermentation ;","2.7.2.1","1 : Unknown","6.7 : Fermentation ;","e : enzyme","12634340, 15755952, 17465479, 18223085","5 : Unknown function",1,285,401,1,286,300]
[null,"MGMSRv2_1019","_","Magnetospirillum gryphiswaldense MSR-1 v2","ackA","Acetate kinase","_",0.96403,1.00249,39.05,{"v":2E-87,"d":"2.00E-87"},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",3,401,401,22,412,417]
[null,"AZOLI_p20461","_","Azospirillum lipoferum 4B","ackA2","Acetate kinase","_",0.99265,1.00998,40.49,{"v":7e-86,"d":"7.00E-86"},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",4,400,401,13,401,408]
[null,"HP0903",null,"Helicobacter pylori 26695","ackA","Fragment of putative acetate kinase (Part 1)","_",0.7182,0.9863,47.22,{"v":2E-85,"d":"2.00E-85"},1,1,"6.7 : Fermentation ;","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,285,401,1,286,292]
[null,"NIDE3516","_","Candidatus Nitrospira defluvii","ackA","Acetate kinase","_",0.9703,0.97756,40.05,{"v":1E-84,"d":"1.00E-84"},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",3,392,401,11,392,404]
[null,"p2METDI0002","_","Methylobacterium extorquens DM4","ackA","acetate kinase","_",1.00249,1.02813,38.56,{"v":3e-84,"d":"3.00E-84"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme",10094701,"2a : Function from experimental evidences in other organisms",4,395,401,7,388,391]
[null,"BN873v1_460010","_","Candidatus Competibacter denitrificans Run_A_D11","ackA","Acetate/propionate kinase","_",1.019,1.06983,36.36,{"v":2e-83,"d":"2.00E-83"},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",3,398,401,5,419,421]
[null,"METDI0790","_","Methylobacterium extorquens DM4","_","putative acetate kinase (ackA)","_",0.99501,1.01269,39.1,{"v":2e-83,"d":"2.00E-83"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,398,401,9,391,394]
[null,"BRADO1872","_","Bradyrhizobium sp. ORS278","tdcD","propionate kinase/acetate kinase C, anaerobic","_",0.99751,1.01266,38,{"v":6e-81,"d":"6.00E-81"},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, 2.7.2.-","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,399,401,6,392,395]
[null,"Rmet_0562","_","Cupriavidus metallidurans CH34","ackA2","acetate kinase","_",1.01235,1.02244,40.98,{"v":2e-80,"d":"2.00E-80"},1,1,"_","2.7.2.1","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,398,401,8,401,405]
[null,"RALTA_A1397","_","Cupriavidus taiwanensis LMG19424","_","Acetate kinase","_",1.00998,1.02273,37.78,{"v":2e-80,"d":"2.00E-80"},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)",3,400,401,5,393,396]
[null,"RPSI07_mp1366","_","Ralstonia solanacearum PSI07","ackA","Acetate kinase","_",0.99751,1.02041,39.75,{"v":5E-80,"d":"5.00E-80"},1,1,"_","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",10094701,"2a : Function from experimental evidences in other organisms",3,392,401,4,384,392]
[null,"MT37II_v2_a0110","_","Ca. Spiroplasma holothuricola MT37","ackA","acetate kinase (possibly promiscuous)","RXN-7958 ; ACETATEKIN-RXN ; RHEA:11352 ;",0.98765,0.99751,38.25,{"v":8e-80,"d":"8.00E-80"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,396,401,7,396,405]
[null,"AZOLI_0599","_","Azospirillum lipoferum 4B","ackA1","Acetate kinase","_",1.00249,1.0203,39.55,{"v":2E-79,"d":"2.00E-79"},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",3,398,401,5,391,394]
[null,"RCFBPv5_mp0810","_","Ralstonia solanacearum CFBP2957","ackA","acetate kinase","_",0.98753,1.0102,40.15,{"v":5e-77,"d":"5.00E-77"},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",3,392,401,4,384,392]
[null,"BN77v1_3277","_","Rhizobium mesoamericanum STM3625","ackA","Acetate kinase","_",1.00998,1.03846,37.28,{"v":7e-75,"d":"7.00E-75"},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",3,400,401,4,390,390]
[null,"RM41v1_580008","_","Sinorhizobium sp. Rm41","ackA","Acetate kinase","_",1,1.01777,35.41,{"v":2E-73,"d":"2.00E-73"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 1.7.29 : Acetate catabolism ; 7.1 : Cytoplasm ;","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.2 : Construct biomass (Anabolism) ;","e : enzyme",10094701,"1c : Function from experimental evidences in the studied genus",3,400,401,4,391,394]
[null,"HEAR1515","_","Herminiimonas arsenicoxydans","ackA","Acetate kinase (Acetokinase)","_",0.96602,0.99252,36.18,{"v":1e-71,"d":"1.00E-71"},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)",3,398,401,21,407,412]
[null,"HPP12_0900",null,"Helicobacter pylori P12","ackA-2","Fragment of acetate kinase (Part 2)","_",0.4788,0.9505,51.04,{"v":6e-62,"d":"6.00E-62"},1,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",94,285,401,4,195,202]
[null,"HPB8_649",null,"Helicobacter pylori B8","_","Fragment of acetate kinase AckA (Part 2)","_",0.43142,0.94536,54.91,{"v":6e-60,"d":"6.00E-60"},1,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",113,285,401,4,176,183]
[null,"HPAG1_0884",null,"Helicobacter pylori HPAG1","_","Fragment of acetate kinase (Part 1)","_",0.38653,0.89595,41.29,{"v":2e-32,"d":"2.00E-32"},1,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,152,401,2,154,173]
[null,"HPP12_0899",null,"Helicobacter pylori P12","ackA-3","Fragment of acetate kinase (Part 3)","_",0.28678,0.97458,46.09,{"v":8e-26,"d":"8.00E-26"},2,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",285,399,401,2,115,118]
[null,"HPG27_856","_","Helicobacter pylori G27","_","Fragment of putative acetate kinase AckA (Part 2)","_",0.28678,0.95041,45.22,{"v":2e-25,"d":"2.00E-25"},1,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",285,399,401,5,118,121]
[null,"HPB8_650",null,"Helicobacter pylori B8","_","Fragment of acetate kinase AckA (Part 3)","_",0.29177,0.99153,46.15,{"v":6e-25,"d":"6.00E-25"},2,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",285,401,401,2,117,118]
[null,"HP0903",null,"Helicobacter pylori 26695","ackA","Fragment of putative acetate kinase (Part 2)","_",0.28678,0.97458,44.35,{"v":1e-24,"d":"1.00E-24"},2,1,"6.7 : Fermentation ;","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",285,399,401,2,115,118]
[null,"HPAG1_0883",null,"Helicobacter pylori HPAG1","_","Fragment of actetate kinase (Part 3)","_",0.202,0.92045,44.44,{"v":3e-17,"d":"3.00E-17"},2,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",285,365,401,5,85,88]
[null,"HPB8_648",null,"Helicobacter pylori B8","_","Fragment of acetate kinase AckA (Part 1)","_",0.24688,0.95192,40.4,{"v":4e-17,"d":"4.00E-17"},3,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,96,401,1,97,104]
[null,"HPP12_0901",null,"Helicobacter pylori P12","ackA-1","Fragment of acetate kinase (Part 1)","_",0.24688,1.0102,40.4,{"v":4e-17,"d":"4.00E-17"},3,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,96,401,1,97,98]
[null,"HELPY_0887",null,"Helicobacter pylori B38","_","Fragment of putative acetate kinase AckA (Part 2)","_",0.202,0.92045,44.44,{"v":6e-17,"d":"6.00E-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",285,365,401,5,85,88]
[]
["CLOSTRIBL6_v1_1872","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_1100027","_","Desulfosporosinus sp. SbF1","pta","phosphate acetyltransferase","PHOSACETYLTRANS-RXN ; RHEA:19521 ;",1,1,74.92,{"v":7e-173,"d":"7.00E-173"},1,1,"_","2.3.1.8","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,323,323,1,323,323]
[null,"CLOSTRIBL4_v1_2331","_","Clostridiales BL-4","pta","phosphotransacetylase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.96997,1,70.28,{"v":2E-159,"d":"2.00E-159"},1,1,"_","2.3.1.8","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme","4201530, 10559153, 10809684, 16283428, 17183215, 17233734, 21453533, 23468065, 25355936","2a : Function from experimental evidences in other organisms",1,322,323,10,332,333]
[null,"BSU37660","_","Bacillus subtilis 168","pta","phosphotransacetylase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.94737,0.94737,54.9,{"v":6e-114,"d":"6.00E-114"},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",15,320,323,18,319,323]
[null,"CDIV41_v1_140089","_","Carnobacterium divergens V41","pta","Phosphate acetyltransferase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.9816,0.99071,52.5,{"v":6e-114,"d":"6.00E-114"},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",1,320,323,3,320,326]
[null,"SSV_v1_1079","_","Streptococcus sanguinis 2908","pta","phosphate acetyltransferase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ;",0.98769,0.99381,53.27,{"v":2e-112,"d":"2.00E-112"},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",1,320,323,3,318,325]
[null,"BN424_559","_","Carnobacterium maltaromaticum LMA28 v1","pta","phosphate acetyltransferase","PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.89164,0.9863,53.12,{"v":2e-103,"d":"2.00E-103"},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",33,320,323,1,286,292]
[null,"BTCD_v1_2175","_","Brochothrix thermosphacta CD337","pta","phosphotransacetylase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ;",0.94154,0.94737,50,{"v":3e-100,"d":"3.00E-100"},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",15,320,323,18,319,325]
[null,"CLOSTRIBL3_v1_10745","_","Clostridiaceae BL-3","pta","Phosphate acetyltransferase","PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.97885,1.0031,44.75,{"v":1e-86,"d":"1.00E-86"},1,1,"_","2.3.1.8","2 : Cytoplasmic","_","e : enzyme","8702268, 11466286","2a : Function from experimental evidences in other organisms",1,320,323,3,326,331]
[null,"BN43v3_10441","_","Mycobacterium canettii STB-L","pta","Putative phosphate acetyltransferase Pta (phosphotransacetylase)","_",0.45942,0.98142,43.22,{"v":1e-77,"d":"1.00E-77"},1,1,"7 : intermediary metabolism and respiration ;","2.3.1.8","1 : Unknown","_","e : enzyme",17443846,"3 : Putative function from multiple computational evidences",5,320,323,370,682,690]
[null,"BN13v1_910015","_","Tetrasphaera jenkinsii Ben74","pta","Phosphate acetyltransferase","_",0.46802,0.9969,41.61,{"v":2e-77,"d":"2.00E-77"},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",1,320,323,364,681,688]
[null,"BN44v3_10449","_","Mycobacterium canettii STB-D","pta","Putative phosphate acetyltransferase Pta (phosphotransacetylase)","_",0.44648,0.98142,42.9,{"v":6e-77,"d":"6.00E-77"},1,1,"7 : intermediary metabolism and respiration ;","2.3.1.8","1 : Unknown","_","e : enzyme",17443846,"3 : Putative function from multiple computational evidences",5,320,323,390,702,710]
[null,"BN45v3_10446","_","Mycobacterium canettii STB-J","pta","Putative phosphate acetyltransferase Pta (phosphotransacetylase)","_",0.44648,0.98142,42.9,{"v":1e-76,"d":"1.00E-76"},1,1,"7 : intermediary metabolism and respiration ;","2.3.1.8","1 : Unknown","_","e : enzyme",17443846,"3 : Putative function from multiple computational evidences",5,320,323,390,702,710]
[null,"NMV_1777","_","Neisseria meningitidis NEM8013","pta","phosphate acetyltransferase (phosphotransacetylase)","_",0.638,0.98762,41.07,{"v":4e-76,"d":"4.00E-76"},1,1,"1.3.5 : Fermentation ;","2.3.1.8","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",4,320,323,180,492,500]
[null,"VIBNIv4_A2402","_","Vibrio nigripulchritudo SFn1","pta","phosphate acetyltransferase","_",0.43096,0.95666,42.72,{"v":9e-76,"d":"9.00E-76"},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",14,320,323,404,706,717]
[null,"NMCC_0579","_","Neisseria meningitidis 053442","_","putative phosphate acetyltransferase (phosphotransacetylase)","_",0.5864,0.98762,40.75,{"v":5e-75,"d":"5.00E-75"},1,1,"_","2.3.1.8","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",4,320,323,224,536,544]
[null,"RALTA_B1570","_","Cupriavidus taiwanensis LMG19424","pta","phosphate acetyltransferase (taurine catabolism pathway)","_",0.93314,0.99381,39.56,{"v":5e-75,"d":"5.00E-75"},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",5,319,323,7,325,344]
[null,"ABAYE3283","_","Acinetobacter baumannii AYE","pta","phosphate acetyltransferase","_",0.43557,0.96285,43.09,{"v":2e-74,"d":"2.00E-74"},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",11,320,323,400,704,714]
[null,"BN42v3_20129","_","Mycobacterium canettii STB-K","pta","Putative phosphate acetyltransferase Pta (phosphotransacetylase)","_",0.45942,0.98142,41.64,{"v":3e-74,"d":"3.00E-74"},1,1,"7 : intermediary metabolism and respiration ;","2.3.1.8","1 : Unknown","_","e : enzyme",17443846,"3 : Putative function from multiple computational evidences",5,320,323,370,682,690]
[null,"BN11v3_1350009","_","Tetrasphaera australiensis Ben110","pta","Phosphate acetyltransferase","_",0.47007,0.9969,40.68,{"v":2E-73,"d":"2.00E-73"},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",1,320,323,363,680,685]
[null,"BN10v3_560038","_","Tetrasphaera elongata Lp2","pta","Phosphate acetyltransferase","_",0.46734,0.9969,40.68,{"v":7e-73,"d":"7.00E-73"},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",1,320,323,366,683,689]
[null,"ACIAD0540","_","Acinetobacter baylyi ADP1","pta","phosphate acetyltransferase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ; RHEA:19524 ; RHEA:28049 ;",0.43194,0.96285,42.44,{"v":8E-73,"d":"8.00E-73"},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",11,320,323,400,704,720]
[null,"MARHY2149","_","Marinobacter hydrocarbonoclasticus ATCC 49840","pta","phosphate acetyltransferase","_",0.47496,0.96904,41.21,{"v":2e-72,"d":"2.00E-72"},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",10,320,323,341,647,659]
[null,"BN873v1_160014","_","Candidatus Competibacter denitrificans Run_A_D11","pta","phosphate acetyltransferase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ;",0.46696,0.98452,41.19,{"v":7e-71,"d":"7.00E-71"},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",5,320,323,362,673,681]
[null,"BN874v1_910011","_","Candidatus Contendobacter odensis Run_B_J11","pta","Phosphate acetyltransferase","_",0.44167,0.98452,39.94,{"v":2E-70,"d":"2.00E-70"},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",5,320,323,394,705,720]
[null,"VIBNIv4_B0182","_","Vibrio nigripulchritudo SFn1","pta","Phosphate acetyltransferase","_",0.97892,1.00619,36.92,{"v":5e-70,"d":"5.00E-70"},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",3,319,323,5,325,332]
[null,"HELPY_0889","_","Helicobacter pylori B38","pta","Phosphotransacetylase","_",0.60425,0.96904,40.58,{"v":6e-70,"d":"6.00E-70"},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",10,320,323,206,513,518]
[null,"RM41v1_pld1620006","_","Sinorhizobium sp. Rm41","pta","Phosphate acetyltransferase","_",0.97879,1,39.94,{"v":4e-66,"d":"4.00E-66"},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",3,319,323,5,325,330]
[null,"BN12v2_1100006","_","Tetrasphaera japonica T1-X7","pta","phosphate acetyltransferase (fragment)","_",0.66234,0.94737,38.89,{"v":7e-66,"d":"7.00E-66"},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",16,320,323,155,456,462]
[null,"PSEEN0916","_","Pseudomonas entomophila L48","pta","phosphate acetyltransferase","_",0.44915,0.98452,37.42,{"v":1e-64,"d":"1.00E-64"},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",5,320,323,390,701,708]
[null,"HPP12_0902","_","Helicobacter pylori P12","pta-2","Fragment of phosphotransacetylase (Part 2)","_",0.54489,0.98324,44.32,{"v":3e-44,"d":"3.00E-44"},1,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",145,320,323,3,174,179]
[null,"HPAG1_0885","_","Helicobacter pylori HPAG1","_","Fragment of phosphotransacetylase (Part 3)","_",0.54489,0.98324,44.32,{"v":4e-44,"d":"4.00E-44"},1,1,"_","2.3.1.8","1 : Unknown","_","u : unknown","_","5 : Unknown function",145,320,323,3,174,179]
[null,"HP0904",null,"Helicobacter pylori 26695","pta","Fragment of putative phosphotransacetylase (Part 3)","_",0.39009,1.02439,37.3,{"v":4e-20,"d":"4.00E-20"},1,1,"6.7 : Fermentation ;","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",145,270,323,3,123,123]
[null,"HP0904",null,"Helicobacter pylori 26695","pta","Fragment of putative phosphotransacetylase (Part 4)","_",0.20124,0.89041,55.38,{"v":2e-18,"d":"2.00E-18"},2,1,"6.7 : Fermentation ;","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",256,320,323,4,68,73]
[]
["CLOSTRIBL6_v1_0095","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,"ECS88_0712",null,"Escherichia coli S88","_","putative alcohol dehydrogenase","_",0.96899,0.97403,40.8,{"v":4e-89,"d":"4.00E-89"},1,1,"_","1.1.1.1","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",13,387,387,8,378,385]
[null,"RCFBPv5_mp0504",null,"Ralstonia solanacearum CFBP2957","_","putative iron-containing alcohol dehydrogenase","_",0.90746,0.91214,41.08,{"v":4e-86,"d":"4.00E-86"},1,1,"_","1.1.1.1","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",32,383,387,34,384,389]
[null,"CLOSTRIBL3_v1_11881",null,"Clostridiaceae BL-3","adh","Alcohol dehydrogenase","RHEA:25290 ;",1.0155,1.0155,35.88,{"v":1e-80,"d":"1.00E-80"},1,1,"_","1.1.1.1","2 : Cytoplasmic","_","e : enzyme","2308827, 21725006","2a : Function from experimental evidences in other organisms",1,386,387,1,385,387]
[null,"Rmet_4943","_","Cupriavidus metallidurans CH34","_","putative iron-containing alcohol dehydrogenase","_",0.9199,0.92468,37.08,{"v":7E-72,"d":"7.00E-72"},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",33,387,387,34,385,385]
[null,"p1METDI0061","_","Methylobacterium extorquens DM4","_","putative iron-containing alcohol dehydrogenase","_",0.91214,0.91688,36.26,{"v":2E-66,"d":"2.00E-66"},1,1,"_","1.1.1.-","1 : Unknown","_","e : enzyme",2935393,"3 : Putative function from multiple computational evidences",33,383,387,32,381,385]
[null,"ASXYv1_3260061","_","Agrobacterium radiobacter DSM 30147","AttL","Gamma-hydroxybutyrate dehydrogenase","ALCOHOL-DEHYDROG-RXN ; ALCOHOL-DEHYDROG-GENERIC-RXN ;",0.93282,0.93523,35.46,{"v":3e-66,"d":"3.00E-66"},1,1,"_","1.1.1.1","1 : Unknown","_","e : enzyme","_","1c : Function from experimental evidences in the studied genus",33,387,387,35,386,386]
[]
["CLOSTRIBL6_v1_1804","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,"CLOSTRIBL4_v1_2290","_","Clostridiales BL-4","adh","Alcohol dehydrogenase","RXN-12448 ;",0.99744,1.01302,62.47,{"v":2e-166,"d":"2.00E-166"},1,1,"_","1.1.1.1","2 : Cytoplasmic","_","e : enzyme",2673928,"2a : Function from experimental evidences in other organisms",2,390,390,1,384,384]
[]
["CLOSTRIBL6_v1_2186","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_2152","_","Streptococcus sanguinis 2908","adhE","aldehyde-alcohol dehydrogenase [includes: alcohol dehydrogenase ; acetaldehyde dehydrogenase]","_",0.99095,1.00922,56.62,0,1,1,"_","1.1.1.1, 1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,867,868,1,875,884]
[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 ;",0.95565,0.99309,49.54,0,1,1,"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",18,868,868,8,864,902]
[null,"VIBNIv4_A0888","_","Vibrio nigripulchritudo SFn1","adhE","Aldehyde-alcohol dehydrogenase [Includes: Alcohol dehydrogenase ; Acetaldehyde dehydrogenase [acetylating] ; Pyruvate-formate-lyase deactivase]","_",0.95249,0.99309,49.54,0,1,1,"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",18,868,868,8,864,905]
[null,"AZOLI_p20688","_","Azospirillum lipoferum 4B","adhE","Aldehyde-alcohol dehydrogenase","_",0.94323,0.99539,49.42,0,1,1,"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",14,868,868,34,891,916]
[null,"AZOLI_p10253","_","Azospirillum lipoferum 4B","adhE2","Aldehyde-alcohol dehydrogenase","_",0.95344,0.99078,49.65,0,1,1,"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",18,868,868,10,863,902]
[null,"CD630_03340","_","Clostridium difficile 630","adhE","Aldehyde-alcohol dehydrogenase","_",0.98977,1.00346,48.56,0,1,1,"1.1.5.2 : Ethanol degradation ; 1.3.5 : Fermentation ;","1.1.1.1, 1.2.1.10","2 : Cytoplasmic","6.7 : Fermentation ; 15.10 : Adaptations to atypical conditions ;","e : enzyme","7980441, 8300540","1c : Function from experimental evidences in the studied genus",9,868,868,21,880,880]
[null,"SCFA_v1_940003","_","Ca. Propionivorax syntrophicum F70","adhE","Alcohol dehydrogenase / Acetaldehyde dehydrogenase [acetylating] / Pyruvate-formate-lyase deactivase (fragment)","ALCOHOL-DEHYDROG-RXN ;",0.4182,0.88971,66.12,{"v":5e-163,"d":"5.00E-163"},1,1,"_","1.1.1.1, 1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",10,372,868,46,408,408]
[null,"BTCD_v1_1045",null,"Brochothrix thermosphacta CD337","_","putative acetaldehyde dehydrogenase (Acetylating)","_",0.50115,0.96667,43.68,{"v":3e-117,"d":"3.00E-117"},1,1,"_","1.2.1.10","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",19,452,868,15,446,450]
[null,"BTCD_v1_1042",null,"Brochothrix thermosphacta CD337","_","putative succinate-semialdehyde dehydrogenase (acetylating)","RXN-8891 ;",0.5023,0.97758,44.72,{"v":5e-116,"d":"5.00E-116"},2,1,"_","1.2.1.76","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",18,452,868,10,442,446]
[null,"EFER_1992",null,"Escherichia fergusonii ATCC 35469T","_","putative Aldehyde dehydrogenase","_",0.50346,0.81989,41.88,{"v":2e-110,"d":"2.00E-110"},2,1,"_","1.2.1.10","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",16,452,868,16,450,533]
[null,"ECIAI39_4208",null,"Escherichia coli IAI39","_","putative Aldehyde dehydrogenase","_",0.50346,0.81989,41.65,{"v":5E-110,"d":"5.00E-110"},2,1,"_","_","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",16,452,868,16,450,533]
[null,"CLOSTRIBL3_v1_12484","_","Clostridiaceae BL-3","_","putative acetaldehyde dehydrogenase","ACETALD-DEHYDROG-RXN ; RHEA:23288 ;",0.5023,0.82264,43.12,{"v":1e-109,"d":"1.00E-109"},1,1,"_","1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",17,452,868,12,444,530]
[null,"EFER_1994",null,"Escherichia fergusonii ATCC 35469T","_","putative Alcohol dehydrogenase, iron-dependent","_",0.4735,1.05928,44.77,{"v":7e-97,"d":"7.00E-97"},3,1,"_","1.1.1.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",459,867,868,5,382,388]
[null,"ECIAI39_4210",null,"Escherichia coli IAI39","_","putative Alcohol dehydrogenase, iron-dependent","_",0.4735,1.05928,44.53,{"v":6e-96,"d":"6.00E-96"},3,1,"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",459,867,868,5,382,388]
[null,"CD630_19070",null,"Clostridium difficile 630","eutG","Ethanolamine iron-dependent Alcohol dehydrogenase","_",0.46083,1.06383,42.5,{"v":3e-94,"d":"3.00E-94"},5,1,"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",462,860,868,4,371,376]
[]
["CLOSTRIBL6_v1_2879","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,"VIBNIv4_B0861","_","Vibrio nigripulchritudo SFn1","adhB","Alcohol dehydrogenase 2","_",0.95685,0.98691,43.77,{"v":2e-102,"d":"2.00E-102"},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","3584063, 2308827, 15592456, 2935393","2a : Function from experimental evidences in other organisms",9,376,394,5,381,382]
[null,"ACIAD2015","_","Acinetobacter baylyi ADP1","_","putative alcohol dehydrogenase","ALCOHOL-DEHYDROG-RXN ; ALCOHOL-DEHYDROG-GENERIC-RXN ;",0.96701,0.97692,44.36,{"v":4e-102,"d":"4.00E-102"},1,1,"_","1.1.1.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,376,394,9,389,390]
[null,"PSEEN2959","_","Pseudomonas entomophila L48","adhB","alcohol dehydrogenase II (","_",0.95939,0.98953,42.33,{"v":9e-101,"d":"9.00E-101"},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)",9,377,394,5,382,382]
[null,"plu1563","_","Photorhabdus luminescens TT01","yiaY","_","_",0.95685,0.98433,43.24,{"v":7e-99,"d":"7.00E-99"},1,1,"_","_","_","_","_","_","_",9,376,394,6,382,383]
[null,"ECK3578","_","Escherichia coli K12","yiaY","Fe-containing alcohol dehydrogenase","_",0.95685,0.98433,41.91,{"v":9e-98,"d":"9.00E-98"},1,1,"1.7.1 : Unassigned reversible reactions ;","1.1.1.1","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",2935393,"2a : Function from experimental evidences in other organisms",9,376,394,6,382,383]
[null,"SSV_v1_1926","_","Streptococcus sanguinis 2908","_","probable alcohol dehydrogenase","_",0.94162,0.96867,42.86,{"v":1E-91,"d":"1.00E-91"},1,1,"_","1.1.1.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,368,394,4,374,383]
[null,"VIBNIv4_A1969","_","Vibrio nigripulchritudo SFn1","_","putative Alcohol dehydrogenase","_",0.86881,0.89086,37.04,{"v":4e-68,"d":"4.00E-68"},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",11,348,394,26,374,404]
[null,"ECK2448",null,"Escherichia coli K12","eutG","putative alcohol dehydrogenase in ethanolamine utilization; ethanolaminosome","_",0.97215,0.97462,35.42,{"v":2e-67,"d":"2.00E-67"},3,1,"1.1.4 : Amines ; 6.1 : Membrane ;","_","11 : Membrane","6.2 : Amino acids and amines ;","e : enzyme","10464203, 16291677","3 : Putative function from multiple computational evidences",3,376,394,17,394,395]
[null,"ECED1_3448",null,"Escherichia coli ED1a","_","putative propanol dehydrogenase","_",0.95685,1.01344,35.54,{"v":5e-64,"d":"5.00E-64"},4,3,"_","1.1.1.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",7,370,394,4,364,372]
[null,"EFER_1994",null,"Escherichia fergusonii ATCC 35469T","_","putative Alcohol dehydrogenase, iron-dependent","_",0.92893,0.9433,35.52,{"v":2e-63,"d":"2.00E-63"},4,3,"_","1.1.1.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",29,381,394,24,384,388]
[null,"ECS88_4685",null,"Escherichia coli S88","_","putative propanol dehydrogenase","_",0.95685,1.01344,35.28,{"v":2e-63,"d":"2.00E-63"},4,3,"_","1.1.1.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",7,370,394,4,364,372]
[null,"ECIAI39_4210",null,"Escherichia coli IAI39","_","putative Alcohol dehydrogenase, iron-dependent","_",0.92893,0.9433,35.52,{"v":4e-63,"d":"4.00E-63"},4,3,"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",29,381,394,24,384,388]
[null,"EFER_2022",null,"Escherichia fergusonii ATCC 35469T","_","putative Propanediol utilization propanol dehydrogenase pduQ","_",0.83503,0.88919,37.08,{"v":7e-61,"d":"7.00E-61"},5,3,"_","1.1.1.1","1 : Unknown","6 : Energy metabolism ;","e : enzyme",10498708,"3 : Putative function from multiple computational evidences",39,361,394,30,354,370]
[]
["CLOSTRIBL6_v1_3434","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,"BSU31370",null,"Bacillus subtilis 168","bdhJ","NADH-dependent butanol dehydrogenase","ENZRXN-161-RXN ;",0.99491,1.01034,36.57,{"v":6E-79,"d":"6.00E-79"},1,1,"2.1.1 : Specific pathways ;","1.1.1.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","1385386, 2673038, 9643546, 11466286, 15317791","2a : Function from experimental evidences in other organisms",1,389,393,1,384,387]
[null,"BSU31360",null,"Bacillus subtilis 168","bdhK","NADH-dependent butanol dehydrogenase subunit","ENZRXN-161-RXN ;",1.00254,1.01026,35.53,{"v":8e-76,"d":"8.00E-76"},2,1,"2.1.1 : Specific pathways ;","1.1.1.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","1385386, 1809209, 2673038","2a : Function from experimental evidences in other organisms",1,389,393,1,387,390]
[null,"SCFA_v1_990008","_","Ca. Phosphitivorax anaerolimi F81","yqhD","alcohol dehydrogenase, NAD(P)-dependent","RXN0-6487 ; ALCOHOL-DEHYDROGENASE-NADPORNOP+-RXN ; ALDEHYDE-DEHYDROGENASE-NADP+-RXN ;",0.89822,0.91688,37.39,{"v":3E-68,"d":"3.00E-68"},1,1,"1.7.1 : Unassigned reversible reactions ;","_","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",15327949,"2a : Function from experimental evidences in other organisms",1,350,393,1,346,385]
[]
["CLOSTRIBL6_v1_1351","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,"VIBNIv4_B0977","_","Vibrio nigripulchritudo SFn1","_","putative Aldehyde dehydrogenase","_",0.96319,1.00213,43.1,{"v":5e-121,"d":"5.00E-121"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",20,489,489,2,470,470]
[null,"AZCBGv1_p140064","_","Azospirillum brasilense CBG497","gabD","succinate-semialdehyde dehydrogenase I, NADP-dependent","_",0.94479,0.95062,40.26,{"v":3e-104,"d":"3.00E-104"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","2254272, 8297211","2a : Function from experimental evidences in other organisms",30,488,489,26,484,486]
[null,"THI_1017","_","Thiomonas sp. 3As","gabD","Succinate-semialdehyde dehydrogenase [NADP+] (SSDH)","_",0.94366,0.9591,38.59,{"v":3E-103,"d":"3.00E-103"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",8297211,"2a : Function from experimental evidences in other organisms",20,482,489,22,488,497]
[null,"p1METDI0060","_","Methylobacterium extorquens DM4","_","succinate-semialdehyde dehydrogenase I, NADP-dependent, GabD-like","_",0.93047,0.93621,40,{"v":1e-102,"d":"1.00E-102"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","1 : Unknown","_","e : enzyme",8297211,"2a : Function from experimental evidences in other organisms",30,482,489,27,478,486]
[null,"AZOLI_p30377","_","Azospirillum lipoferum 4B","gabD1","Succinate-semialdehyde dehydrogenase","_",0.94479,0.95062,38.1,{"v":1e-101,"d":"1.00E-101"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","2254272, 8297211","2a : Function from experimental evidences in other organisms",30,488,489,26,484,486]
[null,"MGMSRv2_0730","_","Magnetospirillum gryphiswaldense MSR-1 v2","gabD","Succinate-semialdehyde dehydrogenase [NADP+] (SSDH)","_",0.95501,0.96091,39.19,{"v":2e-101,"d":"2.00E-101"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",8297211,"2a : Function from experimental evidences in other organisms",20,482,489,15,478,486]
[null,"NT26v4_p10280","_","Rhizobium sp. NT-26","gabD","Succinate-semialdehyde dehydrogenase (SSDH) [NADP+]","_",0.95092,0.96273,38.92,{"v":3e-101,"d":"3.00E-101"},1,1,"1.3.4 : Tricarboxylic acid cycle ;","1.2.1.16","2 : Cytoplasmic","6.12 : TCA cycle ;","e : enzyme","2188954, 8297211","2a : Function from experimental evidences in other organisms",20,482,489,15,476,483]
[null,"BTCD_v1_0267","_","Brochothrix thermosphacta CD337","gabD","succinate-semialdehyde dehydrogenase","_",0.94297,0.94683,37.58,{"v":4e-101,"d":"4.00E-101"},1,1,"_","1.2.1.24","2 : Cytoplasmic","_","e : enzyme","12534463, 11679348, 10984043, 17388807","2a : Function from experimental evidences in other organisms",30,486,489,29,487,491]
[null,"BTTAP_v1_90074","_","Brochothrix thermosphacta TAP175","gabD","succinate-semialdehyde dehydrogenase","SUCCINATE-SEMIALDEHYDE-DEHYDROGENASE-RXN ;",0.94297,0.94683,37.58,{"v":1E-100,"d":"1.00E-100"},1,1,"4.S.111 : lysine ;","1.2.1.24","2 : Cytoplasmic","_","e : enzyme","12534463, 11679348, 10984043, 17388807","2a : Function from experimental evidences in other organisms",30,486,489,29,487,491]
[null,"RCFBPv4_2628","_","Ralstonia solanacearum CFBP2957","gabD","succinate-semialdehyde dehydrogenase I, NADP-dependent","_",0.93267,0.96319,38,{"v":2E-99,"d":"2.00E-99"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme",8297211,"2a : Function from experimental evidences in other organisms",18,482,489,29,498,505]
[null,"RPSI07_2632","_","Ralstonia solanacearum PSI07","gabD","succinate-semialdehyde dehydrogenase I, NADP-dependent","_",0.93069,0.96115,38.51,{"v":7e-99,"d":"7.00E-99"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.24","1 : Unknown","6.2 : Amino acids and amines ;","e : enzyme",8297211,"2a : Function from experimental evidences in other organisms",20,482,489,31,498,505]
[null,"RALSYv5_0856","_","Ralstonia syzygii R24","gabD","succinate-semialdehyde dehydrogenase I, NADP-dependent","_",0.88847,0.96115,38.51,{"v":1e-98,"d":"1.00E-98"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.24","1 : Unknown","6.2 : Amino acids and amines ;","e : enzyme",8297211,"2a : Function from experimental evidences in other organisms",20,482,489,55,522,529]
[null,"RALTA_B1086","_","Cupriavidus taiwanensis LMG19424","gabD2","succinate-semialdehyde dehydrogenase I, NADP-dependent, similar to gabD","_",0.99796,1,37.22,{"v":5e-98,"d":"5.00E-98"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme",8297211,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,482,489,2,482,490]
[null,"XDD1v4_1021","_","Xenorhabdus doucetiae FRM16","gabD","Succinate-semialdehyde dehydrogenase, NADP-dependent","_",0.94343,0.95501,37.47,{"v":9e-98,"d":"9.00E-98"},1,1,"_","1.2.1.16","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",20,482,489,20,483,495]
[null,"CMR15v5_mp0266","_","Ralstonia solanacearum CMR15","gabD","succinate-semialdehyde dehydrogenase I, NADP-dependent","_",0.95538,0.96319,38.85,{"v":1E-97,"d":"1.00E-97"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","1 : Unknown","6.2 : Amino acids and amines ;","e : enzyme","2254272, 8297211","2b : Function from indirect experimental evidences (e.g. phenotypes)",21,482,489,20,485,493]
[null,"Rmet_4942","_","Cupriavidus metallidurans CH34","gabD","succinate-semialdehyde dehydrogenase I, NADP-dependent","_",0.99182,1.00622,36.49,{"v":1E-97,"d":"1.00E-97"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ; 1.3.4 : Tricarboxylic acid cycle ;","1.2.1.16","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,482,489,1,476,482]
[null,"Spro_2470","_","Serratia proteamaculans 568","gabD","Succinate-semialdehyde dehydrogenase [NADP+] (SSDH)","_",0.91411,0.92547,38.7,{"v":1e-96,"d":"1.00E-96"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",38,482,489,30,473,483]
[null,"PP_0213","_","Pseudomonas putida KT2440","gabD-I","succinate-semialdehyde dehydrogenase (NADP+)","SUCCSEMIALDDEHYDROG-RXN ; RHEA:13214 ;",0.9591,0.97708,37.31,{"v":2e-96,"d":"2.00E-96"},1,1,"1.5.1.1 : Glutamate ; 1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.79","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","3355840, 7011797","1b : Function from experimental evidences in the studied species",20,482,489,14,474,480]
[null,"HEAR2670","_","Herminiimonas arsenicoxydans","gabD","Succinate-semialdehyde dehydrogenase [NADP+] (SSDH)","_",0.95935,0.96524,37.29,{"v":2e-96,"d":"2.00E-96"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",8297211,"2a : Function from experimental evidences in other organisms",16,482,489,18,485,492]
[null,"XNC3_v3_1049","_","Xenorhabdus nematophila F1","gabD","Succinate-semialdehyde dehydrogenase [NADP+] GabD","_",0.95306,0.95501,36.4,{"v":4E-95,"d":"4.00E-95"},1,1,"_","1.2.1.79","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",20,482,489,15,478,490]
[null,"PSEEN0189","_","Pseudomonas entomophila L48","gabD","Succinate-semialdehyde dehydrogenase","_",0.9591,0.97708,36.89,{"v":2e-94,"d":"2.00E-94"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","Unknown","5 : Central intermediary metabolism ;","e : enzyme","8297211, 9205837, 9278503","2a : Function from experimental evidences in other organisms",20,482,489,14,474,480]
[null,"BN873v1_470018","_","Candidatus Competibacter denitrificans Run_A_D11","gabD","succinate-semialdehyde dehydrogenase","_",1,1.01452,36.61,{"v":3e-94,"d":"3.00E-94"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.-","1 : Unknown","6.2 : Amino acids and amines ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,487,489,2,480,482]
[null,"RALTA_A1423","_","Cupriavidus taiwanensis LMG19424","gabD1","succinate-semialdehyde dehydrogenase I, NADP-dependent","_",0.93047,0.93814,38.24,{"v":3e-94,"d":"3.00E-94"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","1 : Unknown","6.2 : Amino acids and amines ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",30,482,489,25,476,485]
[null,"Ent638_3676","_","Enterobacter sp. 638","gabD","Succinate-semialdehyde dehydrogenase [NADP+] (SSDH)","_",0.96115,0.97107,38.3,{"v":7E-94,"d":"7.00E-94"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",23,486,489,15,481,484]
[null,"BSU03910","_","Bacillus subtilis 168","gabD","succinate-semialdehyde dehydrogenase","SUCCINATE-SEMIALDEHYDE-DEHYDROGENASE-RXN ; RHEA:13217 ;",0.93865,0.99351,36.38,{"v":1e-92,"d":"1.00E-92"},1,1,"2.2 : Metabolism of amino acids and related molecules ;","1.2.1.24","2 : Cytoplasmic","16.8 : Protect ;","e : enzyme","12354229, 15590624, 9723923, 12123465, 24529384, 24809290, 25911692","1a : Function from experimental evidences in the studied strain",33,488,489,5,462,462]
[null,"CMR15v5_0879","_","Ralstonia solanacearum CMR15","gabD","succinate-semialdehyde dehydrogenase I, NADP-dependent","_",0.91751,0.93252,37.06,{"v":2E-92,"d":"2.00E-92"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme",8297211,"2a : Function from experimental evidences in other organisms",30,482,489,35,489,497]
[null,"NMV_0900","_","Neisseria meningitidis NEM8013","gabD","succinate-semialdehyde dehydrogenase [NADP+] (SSDH)","_",0.91411,0.93711,36.02,{"v":1e-90,"d":"1.00E-90"},1,1,"1.7.31 : Aminobutyrate catabolism ;","1.2.1.24","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",38,482,489,27,470,477]
[null,"BRADO0028","_","Bradyrhizobium sp. ORS278","gabD","Succinate-semialdehyde dehydrogenase [NADP+] (SSDH)","_",0.93561,0.95092,38.06,{"v":1E-89,"d":"1.00E-89"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",8297211,"2a : Function from experimental evidences in other organisms",20,482,489,31,490,497]
[null,"VIBNIv4_A1507","_","Vibrio nigripulchritudo SFn1","_","putative Succinate-semialdehyde dehydrogenase","_",0.94012,0.96319,35.46,{"v":4e-88,"d":"4.00E-88"},1,1,"1.1.3 : Amino acids ; 7.1 : Cytoplasm ;","1.2.1.16","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","_","3 : Putative function from multiple computational evidences",20,485,489,22,490,501]
[null,"BN874v1_1760012","_","Candidatus Contendobacter odensis Run_B_J11","gabD","succinate-semialdehyde dehydrogenase","_",0.96728,0.97727,36.15,{"v":2E-87,"d":"2.00E-87"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.-","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",20,488,489,14,483,484]
[null,"BN12v2_450014","_","Tetrasphaera japonica T1-X7","_","putative succinate-semialdehyde dehydrogenase I, NADP-dependent (or putative aldehyde dehydrogenase)","_",0.94479,0.95062,36.8,{"v":5e-87,"d":"5.00E-87"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","_","3 : Putative function from multiple computational evidences",30,487,489,28,485,486]
[null,"BN11v3_3600001","_","Tetrasphaera australiensis Ben110","gabD","succinate-semialdehyde dehydrogenase I, NADP-dependent","_",0.98978,0.99384,36.36,{"v":9e-87,"d":"9.00E-87"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.24","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",11,488,489,12,487,487]
[null,"PSHAa2665","_","Pseudoalteromonas haloplanktis TAC125","gabD","succinate-semialdehyde dehydrogenase I, NADP-dependent","_",0.82836,0.90798,35.14,{"v":2e-86,"d":"2.00E-86"},1,1,"2.2.3.3 : Degradation of polyamines ;","1.2.1.16","cytoplasm (undefined)","16.11 : Scavenge (Catabolism) ;","e : enzyme","2254272, 8297211","2a : Function from experimental evidences in other organisms",38,478,489,88,526,536]
[null,"LEPBIa2654","_","Leptospira biflexa serovar Patoc Patoc 1","gabD","Succinate-semialdehyde dehydrogenase [NADP+] (SSDH)","_",0.92843,0.93608,35.68,{"v":3e-86,"d":"3.00E-86"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","12446648, 2254272, 8297211","2a : Function from experimental evidences in other organisms",31,482,489,27,477,485]
[null,"BN13v1_180036","_","Tetrasphaera jenkinsii Ben74","_","putative succinate-semialdehyde dehydrogenase I, NADP-dependent (or putative aldehyde dehydrogenase)","_",0.98978,0.99384,37.19,{"v":5e-86,"d":"5.00E-86"},1,1,"1.7.31 : Aminobutyrate catabolism ; 1.7.32 : Putrescine catabolism ;","1.2.1.16","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","_","3 : Putative function from multiple computational evidences",11,488,489,12,487,487]
[null,"BN10v3_840014","_","Tetrasphaera elongata Lp2","gabD","succinate-semialdehyde dehydrogenase","_",0.94683,0.95464,36.29,{"v":2e-83,"d":"2.00E-83"},1,1,"_","1.2.1.24","2 : Cytoplasmic","_","e : enzyme","2254272, 8297211","2a : Function from experimental evidences in other organisms",30,488,489,27,485,485]
[null,"BN43v3_20204","_","Mycobacterium canettii STB-L","aldA","Putative aldehyde dehydrogenase NAD dependent AldA (aldehyde dehydrogenase[NAD+])","_",0.96728,0.96728,36.15,{"v":2E-79,"d":"2.00E-79"},1,1,"7 : intermediary metabolism and respiration ;","1.2.1.-","2 : Cytoplasmic","_","e : enzyme","12368446, 12657046, 12775759","3 : Putative function from multiple computational evidences",21,482,489,13,482,489]
[null,"FRAAL0200","_","Frankia alni ACN14a","_","NAD+-dependent betaine aldehyde dehydrogenase","_",0.92293,0.97955,35.7,{"v":3E-79,"d":"3.00E-79"},1,1,"_","1.2.1.3","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",20,489,489,23,498,519]
[null,"BN44v3_10838","_","Mycobacterium canettii STB-D","aldA","Putative aldehyde dehydrogenase NAD dependent AldA (aldehyde dehydrogenase[NAD+])","_",0.96728,0.96728,36.36,{"v":8E-79,"d":"8.00E-79"},1,1,"7 : intermediary metabolism and respiration ;","1.2.1.-","2 : Cytoplasmic","_","e : enzyme","12368446, 12657046, 12775759","3 : Putative function from multiple computational evidences",21,482,489,13,482,489]
[null,"BN42v3_20527","_","Mycobacterium canettii STB-K","aldA","Putative aldehyde dehydrogenase NAD dependent AldA (aldehyde dehydrogenase[NAD+])","_",0.96728,0.96728,36.15,{"v":7e-78,"d":"7.00E-78"},1,1,"7 : intermediary metabolism and respiration ;","1.2.1.-","2 : Cytoplasmic","_","e : enzyme","12368446, 12657046, 12775759","3 : Putative function from multiple computational evidences",21,482,489,13,482,489]
[null,"BN45v3_20037","_","Mycobacterium canettii STB-J","aldA","Putative aldehyde dehydrogenase NAD dependent AldA (aldehyde dehydrogenase[NAD+])","_",0.96728,0.96728,36.15,{"v":9e-78,"d":"9.00E-78"},1,1,"7 : intermediary metabolism and respiration ;","1.2.1.-","2 : Cytoplasmic","_","e : enzyme","12368446, 12657046, 12775759","3 : Putative function from multiple computational evidences",21,482,489,13,482,489]
[]
["CLOSTRIBL6_v1_2699","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_3090001","_","Ca. Propionivorax syntrophicum F70","MrpA","NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunit","_",0.53386,0.811,36.87,{"v":2e-54,"d":"2.00E-54"},1,1,"_","_","5 : Inner membrane protein","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",123,439,635,77,408,418]
[]
["CLOSTRIBL6_v1_2701","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,"NVIE_007050",null,"Nitrososphaera viennensis EN76","_","NADH ubiquinone oxidoreductase 20 kDa subunit","_",0.44928,0.80519,50,{"v":2e-43,"d":"2.00E-43"},1,1,"4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ;","1.6.99.5","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",14,137,154,151,274,276]
[null,"AZOLI_p30022",null,"Azospirillum lipoferum 4B","hycG","hydrogenase 3 and formate hydrogenase complex, HycG subunit","_",0.50936,0.88312,43.38,{"v":6e-42,"d":"6.00E-42"},1,1,"1.3.5 : Fermentation ; 1.3.7 : Anaerobic respiration ; 6.1 : Membrane ; 7.3 : Inner membrane ;","1.12.7.2","5 : Inner membrane protein","6.3 : Anaerobic ; 6.7 : Fermentation ;","e : enzyme",2187144,"2a : Function from experimental evidences in other organisms",1,136,154,31,166,267]
[null,"AZOLI_p20532",null,"Azospirillum lipoferum 4B","cooL1","carbon monoxide-induced hydrogenase, CooL subunit","_",0.88679,0.91558,43.97,{"v":3e-41,"d":"3.00E-41"},1,1,"_","1.6.99.5","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",8892819,"2a : Function from experimental evidences in other organisms",6,145,154,14,154,159]
[null,"AZOLI_p40581",null,"Azospirillum lipoferum 4B","cooL2","carbon monoxide-induced hydrogenase, CooL subunit","_",0.87097,0.87662,44.44,{"v":3e-41,"d":"3.00E-41"},1,1,"_","1.6.99.5","2 : Cytoplasmic","6.16 : Chemoautotrophy ;","e : enzyme",16311624,"2b : Function from indirect experimental evidences (e.g. phenotypes)",6,139,154,14,148,155]
[null,"IBTHAUMv1_20160010",null,"Ianthella basta symbiont thaum","nuoB","NADH-quinone oxidoreductase, B subunit","1.6.99.5-RXN ;",0.78161,0.88312,46.32,{"v":1E-35,"d":"1.00E-35"},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 ; 7.3 : Inner membrane ;","1.6.99.5","6 : Inner membrane-associated","6 : Energy metabolism ; 6.1 : Aerobic ; 6.3 : Anaerobic ; 6.5 : Electron transport ;","e : enzyme","12730198, 1637825, 17157874, 7690854, 8366049, 9020134, 9030257, 9593861","2a : Function from experimental evidences in other organisms",7,141,154,41,169,174]
[null,"IBTHAUMv1_13940026",null,"Ianthella basta symbiont thaum","nuoB","NADH-quinone oxidoreductase, B subunit","_",0.78161,0.88312,46.32,{"v":1E-35,"d":"1.00E-35"},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 ; 7.3 : Inner membrane ;","1.6.99.5","6 : Inner membrane-associated","6 : Energy metabolism ; 6.1 : Aerobic ; 6.3 : Anaerobic ; 6.5 : Electron transport ;","e : enzyme","12730198, 1637825, 17157874, 7690854, 8366049, 9020134, 9030257, 9593861","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,141,154,41,169,174]
[null,"NVIE_011660",null,"Nitrososphaera viennensis EN76","nuoB","NADH-quinone oxidoreductase subunit B","_",0.79769,0.8961,44.93,{"v":2E-35,"d":"2.00E-35"},2,1,"4.3.D.1 : The Proton- or sodium ion-translocating NADH Dehydrogenase (NDH) Family ;","1.6.99.5","11 : Membrane","6 : Energy metabolism ;","m : membrane component","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,141,154,43,173,173]
[null,"MGMSRv2_2682","_","Magnetospirillum gryphiswaldense MSR-1 v2","hycG","hydrogenase 3 and formate hydrogenase complex, HycG subunit","_",0.71591,0.81818,42.06,{"v":3e-33,"d":"3.00E-33"},1,1,"1.3.5 : Fermentation ; 1.3.7 : Anaerobic respiration ; 6.1 : Membrane ; 7.3 : Inner membrane ;","1.12.7.2","5 : Inner membrane protein","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,127,154,43,168,176]
[null,"AZCBGv1_p160211",null,"Azospirillum brasilense CBG497","hyfI","Hydrogenase-4 subunit I","_",0.72832,0.81818,39.68,{"v":6e-33,"d":"6.00E-33"},1,1,"1.3.5 : Fermentation ; 1.3.7 : Anaerobic respiration ;","_","2 : Cytoplasmic","6.3 : Anaerobic ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,127,154,39,164,173]
[null,"NIDE0235",null,"Candidatus Nitrospira defluvii","nuoB","NADH-quinone oxidoreductase, subunit B","_",0.68132,0.80519,41.13,{"v":1e-32,"d":"1.00E-32"},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 ; 7.3 : Inner membrane ;","1.6.99.5","6 : Inner membrane-associated","6 : Energy metabolism ; 6.5 : Electron transport ; 6.1 : Aerobic ; 6.3 : Anaerobic ;","e : enzyme","12730198, 1637825, 17157874, 7690854, 8366049, 9020134, 9030257, 9593861","2a : Function from experimental evidences in other organisms",15,137,154,47,167,182]
[null,"MAGMOv5_3368",null,"Magnetotactic ovoidal bacterium MO-1","nuoB","NADH-quinone oxidoreductase chain B (NADH dehydrogenase I, chain B) (NDH-1, chain B)","_",0.79042,0.85714,36.36,{"v":7e-31,"d":"7.00E-31"},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 ;","1.6.99.5, 1.6.5.3","2 : Cytoplasmic","16.7 : Manage energy ; 16.10 : Respire ; 6.1 : Aerobic ; 6.3 : Anaerobic ; 6.5 : Electron transport ; 7.4 : Cations and iron carrying compounds ;","e : enzyme","12118882, 12923180, 12975362, 15175326, 15368583, 7565112, 7730262","2a : Function from experimental evidences in other organisms",5,136,154,28,156,167]
[null,"BN45v3_60152",null,"Mycobacterium canettii STB-J","nuoB","Putative NadH dehydrogenase I (chain b) NuoB (NADH-ubiquinone oxidoreductase chain b)","_",0.69022,0.82468,41.73,{"v":2e-30,"d":"2.00E-30"},2,1,"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",15,140,154,34,153,184]
[null,"BN44v3_60653",null,"Mycobacterium canettii STB-D","nuoB","Putative NadH dehydrogenase I (chain b) NuoB (NADH-ubiquinone oxidoreductase chain b)","_",0.69022,0.82468,41.73,{"v":2e-30,"d":"2.00E-30"},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",15,140,154,34,153,184]
[null,"BN43v3_60132",null,"Mycobacterium canettii STB-L","nuoB","Putative NadH dehydrogenase I (chain b) NuoB (NADH-ubiquinone oxidoreductase chain b)","_",0.69022,0.82468,41.73,{"v":2e-30,"d":"2.00E-30"},2,1,"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",15,140,154,34,153,184]
[null,"BN42v3_41189",null,"Mycobacterium canettii STB-K","nuoB","Putative NadH dehydrogenase I (chain b) NuoB (NADH-ubiquinone oxidoreductase chain b)","_",0.69022,0.82468,41.73,{"v":2e-30,"d":"2.00E-30"},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",15,140,154,34,153,184]
[null,"HELPY_1237",null,"Helicobacter pylori B38","nuoB","NADH-ubiquinone oxidoreductase, NQO6 subunit","_",0.90566,0.93506,38.19,{"v":3e-29,"d":"3.00E-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 ;","1.6.5.3","2 : Cytoplasmic","6.1 : Aerobic ;","e : enzyme","11695831, 12923180, 12975362, 15215104, 16645316","2a : Function from experimental evidences in other organisms",5,148,154,20,155,159]
[null,"PSEEN3485",null,"Pseudomonas entomophila L48","nuoB","NADH dehydrogenase I chain B","_",0.56444,0.82468,37.01,{"v":4e-25,"d":"4.00E-25"},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","Inner membrane protein","6 : Energy metabolism ; 7 : Transport and binding proteins ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",15,140,154,65,188,225]
[]
["CLOSTRIBL6_v1_2703","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,"AZOLI_p20528",null,"Azospirillum lipoferum 4B","cooH1","Carbon monoxide-induced hydrogenase, CooH subunit","_",0.99164,0.99164,42.7,{"v":2e-94,"d":"2.00E-94"},1,1,"_","1.6.99.5","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","1644755, 8626276","2a : Function from experimental evidences in other organisms",8,359,359,6,359,359]
[null,"AZOLI_p40577",null,"Azospirillum lipoferum 4B","cooH2","Carbon monoxide-induced hydrogenase, CooH subunit","_",0.99443,0.99443,41.18,{"v":1e-88,"d":"1.00E-88"},1,1,"1.7.1 : Unassigned reversible reactions ;","1.6.99.-","2 : Cytoplasmic","6.16 : Chemoautotrophy ;","e : enzyme","8626276, 16311624","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,359,359,6,359,359]
[null,"AZOLI_p30024",null,"Azospirillum lipoferum 4B","hycE","hydrogenase 3, large subunit","_",0.62697,0.99721,36.03,{"v":5E-74,"d":"5.00E-74"},1,1,"1.3.5 : Fermentation ; 1.3.7 : Anaerobic respiration ; 6.1 : Membrane ; 7.3 : Inner membrane ;","1.12.7.2","5 : Inner membrane protein","6.3 : Anaerobic ; 6.7 : Fermentation ;","e : enzyme","2187144, 8125094","2a : Function from experimental evidences in other organisms",6,359,359,183,539,571]
[]
["CLOSTRIBL6_v1_2705","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,"BBta_0471",null,"Bradyrhizobium sp. BTAi1","hypF","carbamoyl phosphate phosphatase, [NiFe] Hydrogenase maturation protein","_",0.94903,1.05391,37.85,{"v":3E-148,"d":"3.00E-148"},1,1,"1.3.7 : Anaerobic respiration ; 2.3.4 : Chaperoning, folding ; 7.1 : Cytoplasm ; 1.8 : Metabolism of other compounds ;","_","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",5,740,742,23,799,824]
[null,"BBta_p0172",null,"Bradyrhizobium sp. BTAi1","hypF","Hydrogenase maturation protein hypF (Carbamoyltransferase)","_",0.98278,1,37.47,{"v":3e-144,"d":"3.00E-144"},1,1,"1.3.7 : Anaerobic respiration ; 2.3.4 : Chaperoning, folding ;","2.1.3.-","1 : Unknown","16.13 : Shape ; 16.7 : Manage energy ;","e : enzyme",9492269,"2b : Function from indirect experimental evidences (e.g. phenotypes)",5,736,742,15,745,755]
[null,"MALCv4_1970",null,"Methylomicrobium alcaliphilum 20Z","hypF","nickel-iron hydrogenase, carbamoyltransferase maturation factor","_",0.98943,1.00943,36.18,{"v":2e-141,"d":"2.00E-141"},1,1,"_","2.1.3.-","1 : Unknown","_","e : enzyme","12377778, 15291820","2a : Function from experimental evidences in other organisms",5,735,742,17,750,757]
[null,"BRADO1697",null,"Bradyrhizobium sp. ORS278","hypF","carbamoyl phosphate phosphatase, [NiFe] Hydrogenase maturation protein","_",1.00266,1.01617,37.27,{"v":6e-141,"d":"6.00E-141"},1,1,"2.3.4 : Chaperoning, folding ;","_","2 : Cytoplasmic","16.15 : Symbiosis ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,738,742,15,736,752]
[null,"BURPHP2_0031",null,"Burkholderia phymatum STM815","hypF2","carbamoyl phosphate phosphatase HypF2, [NiFe] Hydrogenase maturation protein","_",0.96334,1.02695,36.35,{"v":1e-137,"d":"1.00E-137"},1,1,"1.3.7 : Anaerobic respiration ; 2.3.4 : Chaperoning, folding ;","2.1.3.-","2 : Cytoplasmic","_","e : enzyme","9799289, 12948488","2a : Function from experimental evidences in other organisms",5,740,742,23,780,791]
[null,"AZCBGv1_p150158",null,"Azospirillum brasilense CBG497","hypF","Carbamoyl phosphate-converting enzyme hypF, [NiFe]-hydrogenase maturation factor hypF","_",1.01325,1.031,36.34,{"v":4e-137,"d":"4.00E-137"},1,1,"2.3.4 : Chaperoning, folding ; 1.3.7 : Anaerobic respiration ; 7.1 : Cytoplasm ;","_","2 : Cytoplasmic","11.3 : Protein folding and stabilization ; 6.3 : Anaerobic ;","e : enzyme","12206761, 12377778, 15291820, 15504408","2a : Function from experimental evidences in other organisms",3,738,742,4,735,755]
[null,"Rmet_1537",null,"Cupriavidus metallidurans CH34","hypF2","carbamoyl phosphate phosphatase and maturation protein for [NiFe] hydrogenases","_",0.97834,1.03504,36.72,{"v":2e-135,"d":"2.00E-135"},1,1,"1.3.7 : Anaerobic respiration ; 2.3.4 : Chaperoning, folding ; 7.1 : Cytoplasm ;","_","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",5,738,742,17,774,785]
[null,"AZOLI_p30072","_","Azospirillum lipoferum 4B","hypF","[NiFe]-hydrogenase maturation factor hypF (carbamoyl transferase)","_",1.03639,1.04626,36.8,{"v":8e-131,"d":"8.00E-131"},1,1,"2.3.4 : Chaperoning, folding ;","_","2 : Cytoplasmic","11.3 : Protein folding and stabilization ;","e : enzyme","12206761, 12377778, 15291820, 15504408","2a : Function from experimental evidences in other organisms",7,741,742,1,733,735]
[]
["CLOSTRIBL6_v1_2706","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,"MGMSRv2_2201",null,"Magnetospirillum gryphiswaldense MSR-1 v2","hypC","Hydrogenase expression/formation protein HypC","_",0.94737,1.02857,37.5,2E-8,1,1,"2.3.4 : Chaperoning, folding ;","_","2 : Cytoplasmic","16.15 : Symbiosis ;","ph : phenotype","_","2a : Function from experimental evidences in other organisms",1,70,70,1,72,76]
[null,"BURPHP2_0010",null,"Burkholderia phymatum STM815","hypC","Hydrogenase expression/formation protein HypC","_",0.75,0.94286,39.39,9e-08,1,1,"1.3.7 : Anaerobic respiration ; 2.3.4 : Chaperoning, folding ;","_","2 : Cytoplasmic","16.7 : Manage energy ; 16.3 : Control ;","f : factor","8163174, 8230232, 8326860","2a : Function from experimental evidences in other organisms",1,63,70,1,66,88]
[null,"AZOLI_p40340",null,"Azospirillum lipoferum 4B","hypC","Hydrogenase expression/formation protein hypC","_",0.94737,1.02857,36.11,2e-07,1,1,"2.3.4 : Chaperoning, folding ; 1.3.7 : Anaerobic respiration ;","_","2 : Cytoplasmic","11.3 : Protein folding and stabilization ; 6.3 : Anaerobic ;","f : factor","9485446, 11511872","2a : Function from experimental evidences in other organisms",1,70,70,1,72,76]
[null,"AZCBGv1_p150157",null,"Azospirillum brasilense CBG497","hypC","Hydrogenase isoenzymes formation protein hypC","_",0.89873,1.01429,40.85,9e-07,1,1,"2.3.4 : Chaperoning, folding ; 1.3.7 : Anaerobic respiration ;","_","2 : Cytoplasmic","11.3 : Protein folding and stabilization ; 6.3 : Anaerobic ;","f : factor","9485446, 11511872","2a : Function from experimental evidences in other organisms",1,65,70,1,68,79]
[null,"Rmet_1538",null,"Cupriavidus metallidurans CH34","hypC2","Hydrogenase expression/formation protein HypC","_",0.72857,0.82258,37.25,0.0003,2,1,"2.3.4 : Chaperoning, folding ; 1.3.7 : Anaerobic respiration ;","_","2 : Cytoplasmic","_","f : factor","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",17,66,70,2,52,62]
[]
["CLOSTRIBL6_v1_2707","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,"AZOLI_0851","_","Azospirillum lipoferum 4B","hypD","HypD Protein required for maturation of hydrogenase","_",0.90541,0.97384,41.19,{"v":2E-78,"d":"2.00E-78"},1,1,"2.3.3 : Posttranslational modification ; 1.8 : Metabolism of other compounds ;","_","2 : Cytoplasmic","5 : Central intermediary metabolism ; 11.2 : Protein modification and repair ;","ph : phenotype","1849603, 8352644, 12948488","2a : Function from experimental evidences in other organisms",18,339,344,32,362,370]
[null,"AZCBGv1_p150058","_","Azospirillum brasilense CBG497","hypD","protein required for maturation of hydrogenases, hydrogenase expression/formation protein","_",0.8971,0.98837,40.59,{"v":2E-78,"d":"2.00E-78"},1,1,"2.3.3 : Posttranslational modification ; 1.8 : Metabolism of other compounds ; 1.3.7 : Anaerobic respiration ;","_","2 : Cytoplasmic","6.3 : Anaerobic ; 11.2 : Protein modification and repair ;","f : factor","1849603, 8352644, 12948488","2a : Function from experimental evidences in other organisms",13,339,344,27,366,379]
[null,"BRADO1699",null,"Bradyrhizobium sp. ORS278","hypD","hydrogenase expression/formation protein","_",0.872,0.95058,39.76,{"v":3e-76,"d":"3.00E-76"},1,1,"2.3.3 : Posttranslational modification ; 1.8 : Metabolism of other compounds ;","_","2 : Cytoplasmic","16.15 : Symbiosis ;","ph : phenotype","_","2a : Function from experimental evidences in other organisms",17,335,344,31,357,375]
[null,"Rmet_1282",null,"Cupriavidus metallidurans CH34","hypD1","protein required for maturation of hydrogenases (CMGI-2)(ICE Tn4371 6054)","_",0.86305,0.97093,40.42,{"v":3e-76,"d":"3.00E-76"},1,1,"1.3.7 : Anaerobic respiration ; 2.3.3 : Posttranslational modification ;","_","2 : Cytoplasmic","_","f : factor","_","2a : Function from experimental evidences in other organisms",19,339,344,33,366,387]
[null,"MGMSRv2_2202",null,"Magnetospirillum gryphiswaldense MSR-1 v2","hypD","hydrogenase expression/formation protein","_",0.87335,0.96221,39.27,{"v":2E-73,"d":"2.00E-73"},1,1,"1.8 : Metabolism of other compounds ; 2.3.3 : Posttranslational modification ;","_","2 : Cytoplasmic","16.15 : Symbiosis ;","ph : phenotype","_","2a : Function from experimental evidences in other organisms",18,335,344,32,362,379]
[null,"Rmet_1539",null,"Cupriavidus metallidurans CH34","hypD2","protein required for maturation of hydrogenases","_",0.89474,0.98837,38.82,{"v":2E-73,"d":"2.00E-73"},2,1,"1.3.7 : Anaerobic respiration ; 2.3.3 : Posttranslational modification ;","_","1 : Unknown","6 : Energy metabolism ;","f : factor","_","2a : Function from experimental evidences in other organisms",13,339,344,27,366,380]
[null,"BURPHP2_0009",null,"Burkholderia phymatum STM815","hypD","Hydrogenase expression/formation protein HypD","_",0.89628,0.97965,39.17,{"v":4e-71,"d":"4.00E-71"},1,1,"1.3.7 : Anaerobic respiration ; 2.3.3 : Posttranslational modification ;","_","1 : Unknown","6.3 : Anaerobic ; 11.2 : Protein modification and repair ;","f : factor",1849603,"2a : Function from experimental evidences in other organisms",17,339,344,31,360,376]
[null,"HELPY_0882",null,"Helicobacter pylori B38","hypD","Hydrogenase expression/formation protein HypD","_",0.90811,0.97674,37.2,{"v":4E-70,"d":"4.00E-70"},1,1,"1.3.7 : Anaerobic respiration ; 2.3.3 : Posttranslational modification ;","_","1 : Unknown","11.3 : Protein folding and stabilization ;","f : factor","11123699, 14726233, 1482271, 15504408, 16814778","1a : Function from experimental evidences in the studied strain",16,343,344,34,369,370]
[null,"MALCv4_1971",null,"Methylomicrobium alcaliphilum 20Z","hypD","nickel-iron hydrogenase, metal-binding maturation protein","_",0.90374,0.98256,38.46,{"v":2e-68,"d":"2.00E-68"},1,1,"_","_","1 : Unknown","_","f : factor","11511872, 8326860","2a : Function from experimental evidences in other organisms",15,335,344,20,353,374]
[null,"MAGMOv5_0179",null,"Magnetotactic ovoidal bacterium MO-1","hypD","Hydrogenase expression/formation protein HypD","_",0.8708,0.97965,36.5,{"v":1e-67,"d":"1.00E-67"},1,1,"2.3.3 : Posttranslational modification ; 1.8 : Metabolism of other compounds ;","_","2 : Cytoplasmic","16.15 : Symbiosis ; 6.3 : Anaerobic ; 11.2 : Protein modification and repair ;","f : factor","1849603, 8326860","2a : Function from experimental evidences in other organisms",18,339,344,32,366,387]
[]
["CLOSTRIBL6_v1_2708","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,"AZCBGv1_p150156",null,"Azospirillum brasilense CBG497","hypE","carbamoyl phosphate phosphatase, hydrogenase 3 maturation protein","_",0.95115,1.00915,53.17,{"v":6e-106,"d":"6.00E-106"},1,1,"2.3.4 : Chaperoning, folding ; 1.3.7 : Anaerobic respiration ;","_","2 : Cytoplasmic","11.3 : Protein folding and stabilization ; 6.3 : Anaerobic ;","f : factor","12377778, 15291820, 1849603, 9485446","2a : Function from experimental evidences in other organisms",3,328,328,18,348,348]
[null,"BURPHP2_0008",null,"Burkholderia phymatum STM815","hypE","carbamoyl phosphate phosphatase, hydrogenase 3 maturation protein","_",0.95402,1.0122,50.6,{"v":6e-106,"d":"6.00E-106"},1,1,"1.3.7 : Anaerobic respiration ; 2.3.4 : Chaperoning, folding ;","_","1 : Unknown","6.3 : Anaerobic ; 11.3 : Protein folding and stabilization ;","e : enzyme","1849603, 9485446","2a : Function from experimental evidences in other organisms",2,328,328,17,348,348]
[null,"AZOLI_p40339",null,"Azospirillum lipoferum 4B","hypE","Hydrogenase expression/formation protein HypE","_",0.95402,1.0122,52.41,{"v":6e-105,"d":"6.00E-105"},1,1,"2.3.4 : Chaperoning, folding ; 1.3.7 : Anaerobic respiration ;","_","2 : Cytoplasmic","11.3 : Protein folding and stabilization ; 6.3 : Anaerobic ;","f : factor","12377778, 15291820, 1849603, 9485446","2a : Function from experimental evidences in other organisms",3,328,328,18,348,348]
[null,"Rmet_1281",null,"Cupriavidus metallidurans CH34","hypE1","carbamoyl phosphate phosphatase, hydrogenase 3 maturation protein (CMGI-2)(ICE Tn4371 6054)","_",0.91351,1.03049,51.48,{"v":3e-100,"d":"3.00E-100"},1,1,"_","_","2 : Cytoplasmic","6.16 : Chemoautotrophy ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,328,328,33,370,370]
[null,"MAGMOv5_0180",null,"Magnetotactic ovoidal bacterium MO-1","hypE","Hydrogenase maturation protein HypE","_",0.97353,1.00915,48.34,{"v":3E-98,"d":"3.00E-98"},1,1,"2.3.4 : Chaperoning, folding ; 1.3.7 : Anaerobic respiration ;","_","2 : Cytoplasmic","6.3 : Anaerobic ; 11.3 : Protein folding and stabilization ;","f : factor",7906310,"2a : Function from experimental evidences in other organisms",3,328,328,10,340,340]
[null,"MGMSRv2_2203",null,"Magnetospirillum gryphiswaldense MSR-1 v2","hypE","hydrogenase maturation protein HypE","_",0.95129,1.0122,46.99,{"v":2e-97,"d":"2.00E-97"},1,1,"2.3.4 : Chaperoning, folding ;","_","2 : Cytoplasmic","_","f : factor",7906310,"2a : Function from experimental evidences in other organisms",2,328,328,18,349,349]
[null,"BRADO1700",null,"Bradyrhizobium sp. ORS278","hypE","hydrogenase maturation protein HypE","_",0.95954,1.0122,49.4,{"v":7e-97,"d":"7.00E-97"},1,1,"2.3.4 : Chaperoning, folding ;","_","2 : Cytoplasmic","_","f : factor",7906310,"2a : Function from experimental evidences in other organisms",3,328,328,15,346,346]
[null,"Rmet_1540",null,"Cupriavidus metallidurans CH34","hypE2","carbamoyl phosphate phosphatase, hydrogenase 3 maturation protein","_",0.95129,1.0122,48.49,{"v":3e-96,"d":"3.00E-96"},2,1,"1.3.7 : Anaerobic respiration ; 2.3.4 : Chaperoning, folding ;","_","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,328,328,18,349,349]
[null,"BBta_p0171",null,"Bradyrhizobium sp. BTAi1","hypE","Hydrogenase expression/formation protein hypE","_",0.9711,1.02439,46.43,{"v":7e-85,"d":"7.00E-85"},1,1,"1.3.7 : Anaerobic respiration ; 2.3.4 : Chaperoning, folding ; 3.1.4 : Regulation level unknown ;","_","1 : Unknown","16.13 : Shape ; 16.7 : Manage energy ;","f : factor",1526470,"2b : Function from indirect experimental evidences (e.g. phenotypes)",2,328,328,15,346,346]
[null,"MAGMOv5_0785",null,"Magnetotactic ovoidal bacterium MO-1","hypE","hydrogenase maturation protein HypE","_",0.99702,1.02134,44.48,{"v":2e-82,"d":"2.00E-82"},2,1,"2.3.4 : Chaperoning, folding ;","_","2 : Cytoplasmic","_","f : factor",7906310,"2a : Function from experimental evidences in other organisms",3,328,328,6,336,336]
[null,"MALCv4_1964",null,"Methylomicrobium alcaliphilum 20Z","hypE","nickel-iron hydrogenase, metallocenter assembly protein","_",0.97654,1.01524,45.35,{"v":5e-81,"d":"5.00E-81"},1,1,"2.3.4 : Chaperoning, folding ;","_","1 : Unknown","11.3 : Protein folding and stabilization ;","f : factor","7906310, 1849603","2a : Function from experimental evidences in other organisms",3,328,328,12,341,341]
[null,"HELPY_0042",null,"Helicobacter pylori B38","hypE","Hydrogenase expression/formation protein","_",1,1.0122,38.55,{"v":2E-70,"d":"2.00E-70"},1,1,"1.3.7 : Anaerobic respiration ; 2.3.4 : Chaperoning, folding ;","_","1 : Unknown","11.3 : Protein folding and stabilization ;","f : factor","14726233, 1482271, 15291820, 16412426, 1849603","1a : Function from experimental evidences in the studied strain",3,328,328,4,332,332]

{"sheet":"SwissProt","index":6,"n_rows":845,"n_cols":22,"rows_kept":845}
["CLOSTRIBL6_v1_3221","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?",0.99531,0.99531,50.47,{"v":5e-143,"d":"5.00E-143"},1,1,"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)","_",2,424,426,3,425,426]
[null,"F9USS9","IPMed?",0.9108,0.91509,51.55,{"v":4e-132,"d":"4.00E-132"},2,1,"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",36,423,426,38,424,424]
[]
["CLOSTRIBL6_v1_3223","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?",0.89168,0.97257,39.91,{"v":1e-123,"d":"1.00E-123"},1,1,"lctP","L-lactate permease","_","Cell membrane, Membrane, Transmembrane, Transmembrane helix, Transport",10508058,"Streptococcus iniae","_",1,461,517,1,449,474]
[null,"P33231","IPMed?",0.95463,1.01741,35.74,{"v":2e-94,"d":"2.00E-94"},2,1,"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",2,506,517,16,537,551]
[null,"P65253","_",0.94192,1.00387,35.84,{"v":6e-94,"d":"6.00E-94"},3,1,"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",2,499,517,16,530,551]
[null,"P65254","_",0.94192,1.00387,35.84,{"v":6e-94,"d":"6.00E-94"},3,1,"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",2,499,517,16,530,551]
[null,"Q8ZL63","_",0.94192,1.00387,35.07,{"v":5e-92,"d":"5.00E-92"},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",2,499,517,16,530,551]
[null,"Q8Z2E3","_",0.94192,1.00387,34.68,{"v":7e-91,"d":"7.00E-91"},5,1,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Transmembrane, Transmembrane helix, Transport","11677608, 12644504","Salmonella typhi","CT18 / ATCC 700931 / Ty2",2,499,517,16,530,551]
[null,"P71067","IPMed?",0.95737,1.04255,33.58,{"v":1e-85,"d":"1.00E-85"},6,1,"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",1,506,517,15,549,563]
[null,"Q46839","IPMed?",0.9375,1.01547,34.1,{"v":1E-83,"d":"1.00E-83"},7,1,"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",2,499,517,16,538,560]
[null,"P55910","IPMed?",0.97782,1.02321,33.65,{"v":4E-79,"d":"4.00E-79"},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",2,506,517,14,531,541]
[null,"Q9K5Z9","_",0.9771,0.99033,29.88,{"v":8e-69,"d":"8.00E-69"},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",6,506,517,18,515,524]
[null,"Q57251","_",1.02068,1.05029,22.1,{"v":8e-32,"d":"8.00E-32"},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",1,514,517,1,528,532]
[null,"O68460","IPMed?",0.71083,0.96518,21.24,0.16,11,4,"hppA","K(+)-insensitive pyrophosphate-energized proton pump","7.1.3.1","Calcium, Cell membrane, Complete proteome, Hydrogen ion transport, Ion transport, Magnesium, Membrane, Metal-binding, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","9630689, 21886856, 15292143, 11956221","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",31,490,517,11,467,702]
[null,"Q7T2T1","IPMed?",0.22631,0.24174,24.79,0.24,12,1,"CELF2","CUGBP Elav-like family member 2","_","Alternative splicing, Complete proteome, Cytoplasm, mRNA processing, Nucleus, Reference proteome, Repeat, Repressor, RNA-binding","15226369, 15830352","Gallus gallus","_",352,465,517,228,344,484]
[null,"Q8LG88","IPMed?",0.30556,0.31915,26.67,0.58,13,4,"TDT","Tonoplast dicarboxylate transporter","_","Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport, Vacuole","12947042, 27862469, 14593172, 15728336","Arabidopsis thaliana","cv. Columbia / cv. Columbia",305,462,517,320,480,540]
[]
["CLOSTRIBL6_v1_2713","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q632G8","_",0.97161,0.98089,53.25,{"v":2e-111,"d":"2.00E-111"},1,1,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",16621833,"Bacillus cereus (strain ZK / E33L)","ZK / E33L",7,314,317,7,313,314]
[null,"Q6HC14","_",0.97161,0.98089,53.25,{"v":2e-111,"d":"2.00E-111"},1,1,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",16621833,"Bacillus thuringiensis subsp. konkukian (strain 97-27)","97-27",7,314,317,7,313,314]
[null,"Q81K80","_",0.97161,0.98089,53.25,{"v":2e-111,"d":"2.00E-111"},1,1,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","12721629, 18952800","Bacillus anthracis","Ames / isolate Porton / Ames ancestor",7,314,317,7,313,314]
[null,"Q816G3","_",0.97161,0.98089,52.92,{"v":2e-111,"d":"2.00E-111"},2,1,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","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",7,314,317,7,313,314]
[null,"P62048","_",0.97161,0.98089,53.25,{"v":3e-111,"d":"3.00E-111"},3,1,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",14960714,"Bacillus cereus (strain ATCC 10987 / NRS 248)","ATCC 10987 / NRS 248",7,314,317,7,313,314]
[null,"P13714","IPMed?",0.94375,0.95268,52.98,{"v":2e-108,"d":"2.00E-108"},4,1,"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",7,308,317,7,307,320]
[null,"A7Z152","_",0.95268,0.95268,53.31,{"v":3e-108,"d":"3.00E-108"},5,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",17704766,"Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42)","DSM 23117 / BGSC 10A6 / FZB42",7,308,317,8,308,317]
[null,"Q65NP0","_",0.94671,0.95268,52.65,{"v":2e-105,"d":"2.00E-105"},6,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","15383718, 15461803","Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)","ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46 / ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46",7,308,317,8,308,319]
[null,"C5D5V2","_",0.95925,0.9653,50.98,{"v":2e-105,"d":"2.00E-105"},7,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","_","Geobacillus sp. (strain WCH70)","_",7,312,317,8,312,319]
[null,"Q59244","IPMed?",0.9653,0.9653,50.33,{"v":6e-105,"d":"6.00E-105"},9,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",3675869,"Bacillus caldolyticus","_",3,308,317,4,308,317]
[null,"P00345","IPMed?",0.97799,0.98107,51.45,{"v":6e-105,"d":"6.00E-105"},8,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","3122782, 3118900","Bacillus megaterium","DSM 090",6,310,317,10,312,318]
[null,"Q81RW4","_",0.97161,0.98089,50.32,{"v":1e-104,"d":"1.00E-104"},10,1,"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",7,314,317,7,313,314]
[null,"P62047","_",0.97161,0.98089,50.32,{"v":1e-104,"d":"1.00E-104"},10,1,"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",7,314,317,7,313,314]
[null,"Q63CN1","_",0.97161,0.98089,50.32,{"v":1e-104,"d":"1.00E-104"},10,1,"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",7,314,317,7,313,314]
[null,"Q6HK31","_",0.97161,0.98089,50.32,{"v":1e-104,"d":"1.00E-104"},10,1,"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",7,314,317,7,313,314]
[null,"P00344","IPMed?",0.9653,0.9653,49.67,{"v":2e-104,"d":"2.00E-104"},11,1,"ldh","L-lactate dehydrogenase","1.1.1.27","3D-structure, Allosteric enzyme, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","3026926, 3675869, 6618448, 6352452, 3580377, 2330370, 1731077","Geobacillus stearothermophilus","ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924 / ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924",3,308,317,4,308,317]
[null,"P14561","IPMed?",0.95283,0.95584,51.82,{"v":7e-104,"d":"7.00E-104"},12,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Allosteric enzyme, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","2334516, 3435642","Bacillus psychrosaccharolyticus","_",7,309,317,8,309,318]
[null,"P10655","IPMed?",0.95268,0.95268,50.66,{"v":1e-102,"d":"1.00E-102"},13,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","3675869, 3297694","Bacillus caldotenax","_",7,308,317,8,308,317]
[null,"D8KFT1","IPMed?",0.98107,0.99045,49.84,{"v":2e-101,"d":"2.00E-101"},14,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","12867459, 20639323","Lactococcus lactis subsp. cremoris (strain NZ9000)","NZ9000 / NZ9000",5,315,317,5,314,314]
[null,"P20619","IPMed?",0.94984,0.95584,51.16,{"v":1E-100,"d":"1.00E-100"},15,1,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",2334516,"Bacillus psychrosaccharolyticus","_",7,309,317,8,309,319]
[null,"Q5HJD7","IPMed?",0.95268,0.95268,48.34,{"v":2e-97,"d":"2.00E-97"},16,1,"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",7,308,317,8,307,317]
[null,"A6QDL6","IPMed?",0.95268,0.95268,48.34,{"v":2e-97,"d":"2.00E-97"},16,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Stress response","17951380, 18356528","Staphylococcus aureus (strain Newman)","Newman",7,308,317,8,307,317]
[null,"P56511","IPMed?",0.96562,0.97476,48.54,{"v":2E-95,"d":"2.00E-95"},17,1,"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",1,309,317,4,308,320]
[]
["CLOSTRIBL6_v1_0279","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?",0.99831,1.01025,59.59,0,1,1,"_","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",6,1184,1185,4,1170,1171]
[null,"P19543","IPMed?",1.00338,1.01364,56.52,0,2,1,"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",1,1183,1185,1,1171,1173]
[null,"P03833","IPMed?",0.99916,1.0111,56.67,0,3,1,"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","_",1,1183,1185,1,1168,1171]
[null,"P94692","IPMed?",0.9651,1.00338,56.1,0,4,1,"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",1,1183,1185,1,1167,1232]
[null,"Q94IN5","IPMed?",0.65779,1.00084,47.81,0,5,1,"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",2,1182,1185,66,1232,1803]
[null,"Q06879","IPMed?",1.01251,1.02447,47.53,0,6,1,"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",1,1185,1185,1,1199,1199]
[null,"Q3M8N0","IPMed?",1.01008,1.01435,48.5,0,7,1,"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",3,1183,1185,4,1183,1190]
[null,"P52647","IPMed?",1.01097,1.02044,47.58,0,8,1,"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",5,1183,1185,1,1165,1174]
[null,"Q968X7","IPMed?",0.64426,1.05148,46.87,0,9,1,"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",8,1184,1185,7,1242,1934]
[null,"P52965","_",0.99249,1.00422,48.24,0,10,1,"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",7,1185,1185,8,1175,1199]
[null,"Q53046","IPMed?",1.00672,1.01181,47.37,0,11,1,"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",3,1183,1185,4,1178,1191]
[]
["CLOSTRIBL6_v1_3009","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?",0.97927,0.98438,48.15,{"v":3E-52,"d":"3.00E-52"},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",3,191,193,5,189,192]
[null,"O58411","_",0.96891,1.01081,43.85,{"v":4e-45,"d":"4.00E-45"},2,1,"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",5,191,193,1,181,185]
[null,"Q9UYY9","_",0.96891,1.01081,42.78,{"v":3e-44,"d":"3.00E-44"},3,1,"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",5,191,193,1,181,185]
[null,"Q51799","IPMed?",0.96891,1.01081,41.71,{"v":1e-43,"d":"1.00E-43"},4,1,"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",5,191,193,1,181,185]
[null,"P84820","IPMed?",0.95855,1,42.7,{"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",5,189,193,1,179,185]
[null,"Q5JIK2","_",0.95855,1,42.7,{"v":7e-43,"d":"7.00E-43"},6,1,"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",5,189,193,1,179,185]
[null,"Q57717","_",0.96373,1.04494,43.55,{"v":4e-40,"d":"4.00E-40"},7,1,"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",5,190,193,1,173,178]
[null,"O27772","_",0.96891,1.03889,42.78,{"v":2e-39,"d":"2.00E-39"},8,1,"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",5,191,193,1,174,180]
[null,"P80902","IPMed?",0.96891,1.0565,41.18,{"v":7e-38,"d":"7.00E-38"},9,1,"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",5,191,193,1,174,177]
[null,"P80523","IPMed?",0.95855,1.01648,37.3,{"v":2E-35,"d":"2.00E-35"},10,1,"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,"Q8L3B3","IPMed?",0.95855,0.97368,38.38,{"v":4e-27,"d":"4.00E-27"},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?",0.49206,0.80311,30.97,3e-12,12,2,"_","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",18,152,193,28,181,315]
[null,"P80907","IPMed?",0.37657,0.93264,31.11,2e-09,13,3,"vorA","Ketoisovalerate oxidoreductase subunit VorA","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",6,184,193,297,464,478]
[null,"Q2RMD6","IPMed?",0.17336,1.05181,22.66,6e-07,14,4,"_","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",3,191,193,412,610,1171]
[null,"Q53046","IPMed?",0.16961,1.04663,22.77,1e-06,15,4,"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",4,192,193,424,622,1191]
[]
["CLOSTRIBL6_v1_3010","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?",0.83333,0.85859,50.59,{"v":5e-24,"d":"5.00E-24"},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",13,97,102,5,88,99]
[null,"O58415","_",0.88571,0.91176,48.39,{"v":2e-22,"d":"2.00E-22"},2,1,"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",10,102,102,15,105,105]
[null,"Q51803","IPMed?",0.8381,0.86275,46.59,{"v":1e-21,"d":"1.00E-21"},3,1,"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",15,102,102,19,105,105]
[null,"Q9UYZ3","_",0.88571,0.91176,46.24,{"v":5e-21,"d":"5.00E-21"},4,1,"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",10,102,102,15,105,105]
[null,"Q51800","IPMed?",0.72381,0.7451,47.37,{"v":8e-20,"d":"8.00E-20"},5,1,"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",27,102,102,31,105,105]
[null,"O58412","_",0.97143,1,46.08,{"v":2E-19,"d":"2.00E-19"},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",9679194,"Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)","ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3",4,102,102,7,105,105]
[null,"P80524","IPMed?",0.80392,0.86316,43.9,{"v":5e-19,"d":"5.00E-19"},7,1,"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",21,102,102,15,95,95]
[null,"Q9UYZ0","_",0.97143,1,46.08,{"v":6e-19,"d":"6.00E-19"},8,1,"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",4,102,102,7,105,105]
[null,"P80903","IPMed?",0.80392,1.01235,43.9,{"v":6e-17,"d":"6.00E-17"},9,1,"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",20,101,102,5,81,81]
[null,"P56815","_",0.80392,1.01235,42.68,{"v":3e-16,"d":"3.00E-16"},10,1,"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",20,101,102,5,81,81]
[null,"Q2RI40","IPMed?",0.2127,0.65686,43.28,6e-13,11,1,"_","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",34,100,102,246,310,315]
[null,"Q8L3B2","IPMed?",0.55882,0.6129,45.61,2e-10,12,1,"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",35,91,102,34,88,93]
[null,"P84626","IPMed?",0.10128,0.69608,36.62,4e-07,13,1,"hdlA","Heterodisulfide reductase subunit A-like protein","1.8.-.-","4Fe-4S, Complete proteome, Cytoplasm, Direct protein sequencing, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat","21304717, 15009189","Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18)","DSM 5631 / JCM 9629 / NBRC 100127 / Av18",31,97,102,607,677,701]
[null,"Q8TM02","IPMed?",0.08827,0.68627,37.14,4e-06,14,1,"hdrA2","Ferredoxin/F(420)H(2)-dependent CoB-CoM heterodisulfide reductase subunit A","1.8.7.3, 1.8.98.4","2Fe-2S, 4Fe-4S, Complete proteome, Cytoplasm, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Methanogenesis, Oxidoreductase, Reference proteome, Repeat","11932238, 19968794, 28174314","Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)","ATCC 35395 / DSM 2834 / JCM 12185 / C2A / ATCC 35395 / DSM 2834 / JCM 12185 / C2A / ATCC 35395 / DSM 2834 / JCM 12185 / C2A",30,97,102,559,626,793]
[null,"P16432","IPMed?",0.35556,0.62745,37.5,5e-06,15,2,"hycF","Formate hydrogenlyase subunit 6","_","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",41,100,102,32,95,180]
[]
["CLOSTRIBL6_v1_3011","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?",0.9949,0.99744,50.26,{"v":7e-118,"d":"7.00E-118"},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",4,391,391,7,392,392]
[null,"Q57715","_",0.94885,0.95373,44.47,{"v":2E-100,"d":"2.00E-100"},2,1,"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",7,373,391,10,376,389]
[null,"Q51804","IPMed?",0.9899,1.00256,43.37,{"v":4e-98,"d":"4.00E-98"},3,1,"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,"Q51801","IPMed?",0.95685,0.96419,43.24,{"v":2e-97,"d":"2.00E-97"},4,1,"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",3,378,391,6,381,394]
[null,"Q9UYZ4","_",0.99494,1.00512,43,{"v":6e-97,"d":"6.00E-97"},5,1,"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,"O73986","_",0.99494,1.00512,42.49,{"v":1e-94,"d":"1.00E-94"},6,1,"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,"O58413","_",0.98731,0.99488,40.62,{"v":6e-94,"d":"6.00E-94"},7,1,"vorA","Ketoisovalerate oxidoreductase subunit VorA","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",3,390,391,6,393,394]
[null,"Q9UYZ1","_",0.95949,0.96931,41.69,{"v":8e-94,"d":"8.00E-94"},8,1,"vorA","Ketoisovalerate oxidoreductase subunit VorA","1.2.7.7","Complete proteome, Oxidoreductase","12622808, 22057919","Pyrococcus abyssi (strain GE5 / Orsay)","GE5 / Orsay / GE5 / Orsay",3,380,391,7,384,395]
[null,"P80521","IPMed?",0.96766,0.99488,42.16,{"v":4e-93,"d":"4.00E-93"},9,1,"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",7,391,391,13,399,402]
[null,"P80900","IPMed?",0.95396,0.97389,40.75,{"v":6e-93,"d":"6.00E-93"},10,1,"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",7,377,391,6,372,383]
[null,"Q8L3B1","IPMed?",0.90168,0.96164,35.9,{"v":3e-70,"d":"3.00E-70"},11,1,"padG","NADH-dependent phenylglyoxylate dehydrogenase subunit alpha","1.2.1.58","Direct protein sequencing, NAD, Oxidoreductase",9490067,"Azoarcus evansii","KB740 / DSM 6898",9,374,391,25,400,417]
[null,"Q2RI41","IPMed?",0.99241,1.00256,34.18,{"v":1e-68,"d":"1.00E-68"},12,1,"_","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",1,387,391,1,391,395]
[null,"Q3M8N0","IPMed?",0.32101,0.97698,31.41,{"v":8e-45,"d":"8.00E-45"},13,2,"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",7,371,391,9,385,1190]
[null,"Q9APC2","IPMed?",0.94059,0.97187,30.53,{"v":1e-43,"d":"1.00E-43"},14,2,"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)","_",7,371,391,1,374,404]
[null,"Q06879","IPMed?",0.32527,0.99744,28.97,{"v":3e-41,"d":"3.00E-41"},15,2,"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",7,373,391,8,396,1199]
[]
["CLOSTRIBL6_v1_3012","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?",0.95062,0.99355,52.27,{"v":8e-102,"d":"8.00E-102"},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",5,307,310,8,314,324]
[null,"Q57714","_",0.94516,0.98322,51.54,{"v":5e-99,"d":"5.00E-99"},2,1,"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",8,298,310,5,290,298]
[null,"O27771","_",0.95806,1.03125,48.48,{"v":6e-87,"d":"6.00E-87"},3,1,"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",8,304,310,2,286,288]
[null,"P80901","IPMed?",0.95806,1.03125,48.48,{"v":6e-86,"d":"6.00E-86"},4,1,"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",8,304,310,2,286,288]
[null,"P80522","IPMed?",0.94194,0.98649,47.6,{"v":3e-85,"d":"3.00E-85"},5,1,"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",12,302,310,7,289,296]
[null,"Q51805","IPMed?",0.98187,1.04839,43.08,{"v":4e-83,"d":"4.00E-83"},6,1,"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",6,304,310,5,320,331]
[null,"O58417","_",0.98187,1.04839,43.08,{"v":8e-83,"d":"8.00E-83"},7,1,"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",6,304,310,5,320,331]
[null,"Q9UYZ5","_",0.98187,1.04839,42.46,{"v":4e-81,"d":"4.00E-81"},8,1,"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",6,304,310,5,320,331]
[null,"Q51802","IPMed?",0.94855,0.95161,41.02,{"v":2E-70,"d":"2.00E-70"},9,1,"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",12,304,310,16,303,311]
[null,"Q9UYZ2","_",0.94855,0.95161,40.34,{"v":7e-70,"d":"7.00E-70"},10,1,"vorB","Ketoisovalerate oxidoreductase subunit VorB","1.2.7.7","Complete proteome, Oxidoreductase","12622808, 22057919","Pyrococcus abyssi (strain GE5 / Orsay)","GE5 / Orsay / GE5 / Orsay",12,304,310,16,303,311]
[null,"Q2RI42","IPMed?",0.94904,0.96129,40.6,{"v":3e-69,"d":"3.00E-69"},11,1,"_","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",12,304,310,14,303,314]
[null,"Q8L3A9","IPMed?",0.67937,0.97742,37.29,{"v":3e-47,"d":"3.00E-47"},12,1,"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",4,300,310,143,432,446]
[null,"P94692","IPMed?",0.17127,0.68065,31.75,4E-14,13,3,"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",106,304,310,960,1163,1232]
[null,"Q53046","IPMed?",0.22502,0.86452,26.12,5e-14,14,3,"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",67,309,310,920,1179,1191]
[null,"Q94IN5","IPMed?",0.11703,0.68065,28.91,4e-12,15,3,"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",107,307,310,1028,1232,1803]
[]
["CLOSTRIBL6_v1_0126","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P77851","_",0.99644,1.00719,60.71,{"v":4e-110,"d":"4.00E-110"},1,1,"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)","_",2,277,278,3,280,281]
[null,"P52041","IPMed?",0.99291,1.00719,59.64,{"v":4E-109,"d":"4.00E-109"},2,1,"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",2,278,278,3,281,282]
[null,"P45364","IPMed?",1.00356,1.01439,54.61,{"v":2E-92,"d":"2.00E-92"},3,1,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase",8001771,"Clostridioides difficile","E",1,278,278,1,280,281]
[null,"Q0AVM2","IPMed?",1.00717,1.01079,51.96,{"v":7e-91,"d":"7.00E-91"},4,1,"_","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",1,277,278,1,279,279]
[null,"Q9RVG1","_",1.01079,1.01079,52.31,{"v":1e-88,"d":"1.00E-88"},5,1,"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",1,277,278,1,278,278]
[null,"P45856","IPMed?",0.97213,1.0036,49.1,{"v":1E-84,"d":"1.00E-84"},6,1,"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",2,277,278,5,282,287]
[null,"Q45223","_",0.95222,1.0036,48.39,{"v":3e-78,"d":"3.00E-78"},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",2,277,278,7,284,293]
[null,"P34439","_",0.95302,1.02158,43.66,{"v":8e-68,"d":"8.00E-68"},8,1,"_","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",3,277,278,14,296,298]
[null,"Q16836","IPMed?",0.90764,1.02518,44.56,{"v":2e-64,"d":"2.00E-64"},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","_",3,277,278,30,313,314]
[null,"P00348","IPMed?",0.90764,1.02518,43.51,{"v":3e-64,"d":"3.00E-64"},10,1,"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","_",3,277,278,30,313,314]
[null,"Q9WVK7","IPMed?",0.90764,1.02518,43.51,{"v":4e-63,"d":"4.00E-63"},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",3,277,278,30,313,314]
[null,"Q61425","IPMed?",0.90764,1.02518,43.51,{"v":7e-63,"d":"7.00E-63"},12,1,"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",3,277,278,30,313,314]
[null,"P9WNP7","IPMed?",0.98601,1.01439,41.13,{"v":1E-61,"d":"1.00E-61"},13,1,"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",2,277,278,7,286,286]
[null,"P76083","IPMed?",0.58947,1.00719,40.71,{"v":3e-53,"d":"3.00E-53"},14,1,"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",3,277,278,8,285,475]
[]
["CLOSTRIBL6_v1_0127","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P14611","IPMed?",0.98734,0.99237,60.77,{"v":2E-165,"d":"2.00E-165"},1,1,"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",5,394,395,4,391,393]
[null,"P45359","IPMed?",0.99241,1,59.69,{"v":2e-162,"d":"2.00E-162"},2,1,"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",3,394,395,2,390,392]
[null,"P45369","IPMed?",0.99747,1,58.12,{"v":1e-159,"d":"1.00E-159"},3,1,"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",1,394,395,1,392,394]
[null,"Q9I2A8","_",0.98228,0.98728,57.99,{"v":2E-155,"d":"2.00E-155"},4,1,"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",3,390,395,2,387,393]
[null,"Q9ZHI1","IPMed?",0.98987,0.99745,57.8,{"v":2e-154,"d":"2.00E-154"},5,1,"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",4,394,395,2,390,392]
[null,"P45363","IPMed?",0.99747,1,57.11,{"v":3E-153,"d":"3.00E-153"},6,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase","7763384, 1476773","Thiocystis violacea","2311 / DSM 208",1,394,395,1,392,394]
[null,"Q0AVM3","IPMed?",1.00505,1.00759,57.79,{"v":1e-149,"d":"1.00E-149"},7,1,"_","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",1,394,395,1,394,396]
[null,"Q18AR0","_",0.99241,1.00256,55.36,{"v":2e-144,"d":"2.00E-144"},8,1,"thlA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",16804543,"Peptoclostridium difficile (strain 630)",630,3,394,395,2,390,391]
[null,"Q46939","_",0.99241,0.99746,53.06,{"v":2e-141,"d":"2.00E-141"},9,1,"yqeF","Probable acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","9278503, 16738553","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",3,394,395,2,390,393]
[null,"Q5XI22","_",0.98237,0.98734,54.62,{"v":9e-141,"d":"9.00E-141"},10,1,"Acat2","Acetyl-CoA acetyltransferase, cytosolic","2.3.1.9","Acetylation, Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase",15489334,"Rattus norvegicus","_",5,394,395,8,395,397]
[null,"P54810","IPMed?",0.98987,1,54.73,{"v":3e-140,"d":"3.00E-140"},11,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase",8566717,"Paracoccus denitrificans","_",4,394,395,3,389,391]
[null,"Q8CAY6","IPMed?",0.98237,0.98734,54.36,{"v":5e-140,"d":"5.00E-140"},12,1,"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",5,394,395,8,395,397]
[null,"P50174","IPMed?",0.98734,0.99237,54.1,{"v":3e-137,"d":"3.00E-137"},13,1,"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",5,394,395,6,391,393]
[null,"Q9BWD1","IPMed?",0.98237,0.98734,53.59,{"v":3e-135,"d":"3.00E-135"},14,1,"ACAT2","Acetyl-CoA acetyltransferase, cytosolic","2.3.1.9","3D-structure, Acetylation, Acyltransferase, Alternative splicing, Complete proteome, Cytoplasm, Direct protein sequencing, Polymorphism, Reference proteome, Transferase","7911016, 14702039, 14574404, 15489334, 19413330, 19608861, 21269460, 22223895, 22814378, 24275569, 25944712, 15733928","Homo sapiens","_",5,394,395,8,395,397]
[]
["CLOSTRIBL6_v1_0555","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?",0.95987,1.01773,37.98,{"v":7e-61,"d":"7.00E-61"},1,3,"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",6,292,299,1,281,282]
[null,"P77851","_",0.95652,1.01779,37.76,{"v":6e-59,"d":"6.00E-59"},2,2,"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)","_",6,291,299,1,280,281]
[null,"Q0AVM2","IPMed?",0.94649,1.01434,34.63,{"v":1E-53,"d":"1.00E-53"},3,2,"_","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",9,291,299,3,279,279]
[null,"P45856","IPMed?",0.95987,1,35.54,{"v":6e-53,"d":"6.00E-53"},4,2,"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",5,291,299,2,282,287]
[null,"P00348","IPMed?",0.93312,0.97993,36.18,{"v":2E-52,"d":"2.00E-52"},5,2,"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","_",6,291,299,27,313,314]
[null,"Q16836","IPMed?",0.93631,0.98328,35.71,{"v":6E-51,"d":"6.00E-51"},6,2,"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","_",6,291,299,27,313,314]
[null,"Q9WVK7","IPMed?",0.93631,0.98328,36.05,{"v":9e-51,"d":"9.00E-51"},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",10064895,"Rattus norvegicus","Sprague-Dawley",6,291,299,27,313,314]
[null,"P34439","_",0.98662,0.98993,35.59,{"v":2E-50,"d":"2.00E-50"},8,2,"_","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",3,291,299,8,296,298]
[null,"Q61425","IPMed?",0.93631,0.98328,35.71,{"v":7e-50,"d":"7.00E-50"},9,2,"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",6,291,299,27,313,314]
[null,"P41938","_",0.97411,1.00669,35.22,{"v":2e-48,"d":"2.00E-48"},10,2,"_","Probable 3-hydroxyacyl-CoA dehydrogenase B0272.3","1.1.1.35","Complete proteome, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome",9851916,"Caenorhabditis elegans","Bristol N2",3,291,299,19,308,309]
[null,"P9WNP7","IPMed?",0.96656,1.01049,32.87,{"v":4e-47,"d":"4.00E-47"},11,2,"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",4,291,299,3,286,286]
[null,"P76083","IPMed?",0.60421,0.95987,37.63,{"v":4e-46,"d":"4.00E-46"},12,2,"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",6,291,299,5,285,475]
[null,"P45364","IPMed?",0.94983,1.01068,33.1,{"v":1e-45,"d":"1.00E-45"},13,3,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase",8001771,"Clostridioides difficile","E",9,292,299,3,280,281]
[]
["CLOSTRIBL6_v1_0556","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?",0.99748,1.0102,51.77,{"v":1e-131,"d":"1.00E-131"},1,2,"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",3,396,397,1,391,392]
[null,"Q0AVM3","IPMed?",1.00252,1.00505,47.74,{"v":5e-124,"d":"5.00E-124"},2,2,"_","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",6,397,397,5,396,396]
[null,"Q9I2A8","_",1,1.01018,50.38,{"v":4e-123,"d":"4.00E-123"},3,2,"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",3,396,397,1,392,393]
[null,"P76461","_",1.00756,1.01523,49.5,{"v":2E-118,"d":"2.00E-118"},4,2,"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",3,397,397,1,393,394]
[null,"P44873","_",1.00504,1.01527,47.12,{"v":2E-118,"d":"2.00E-118"},5,2,"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",3,397,397,1,393,393]
[null,"Q18AR0","_",0.99748,1.01279,47.73,{"v":2e-117,"d":"2.00E-117"},6,2,"thlA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",16804543,"Peptoclostridium difficile (strain 630)",630,3,396,397,1,391,391]
[null,"P45369","IPMed?",1,1.00761,46.1,{"v":2e-115,"d":"2.00E-115"},7,2,"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",4,397,397,3,394,394]
[null,"Q9ZHI1","IPMed?",0.99244,1.0051,48.22,{"v":3e-115,"d":"3.00E-115"},8,2,"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",6,396,397,3,391,392]
[null,"P14611","IPMed?",1,1.01018,47.61,{"v":5e-115,"d":"5.00E-115"},9,2,"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",3,396,397,1,392,393]
[null,"Q9I6R0","_",0.99002,1,46.85,{"v":8e-113,"d":"8.00E-113"},10,1,"pcaF","Beta-ketoadipyl-CoA thiolase","2.3.1.174","Acyltransferase, Aromatic hydrocarbons catabolism, Complete proteome, 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",6,397,397,5,401,401]
[null,"P07097","IPMed?",0.98489,0.99745,47.31,{"v":2e-112,"d":"2.00E-112"},11,2,"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",8,397,397,7,392,392]
[null,"P50174","IPMed?",1.00756,1.01781,47.75,{"v":1e-111,"d":"1.00E-111"},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",1,397,397,1,393,393]
[null,"Q0KBP1","IPMed?",1.00252,1.01015,46.98,{"v":4e-111,"d":"4.00E-111"},13,2,"bktB","Beta-ketothiolase BktB","2.3.1.16, 2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Direct protein sequencing, Reference proteome, Transferase","9555876, 16964242","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337",6,397,397,5,394,394]
[null,"Q43935","IPMed?",1.00249,1.01259,45.77,{"v":1e-110,"d":"1.00E-110"},14,1,"catF","Beta-ketoadipyl-CoA thiolase","2.3.1.174","Acyltransferase, Aromatic hydrocarbons catabolism, Complete proteome, Transferase","8125318, 15514110","Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)","ATCC 33305 / BD413 / ADP1",3,397,397,1,401,401]
[null,"P45363","IPMed?",1.01259,1.0203,44.28,{"v":2e-110,"d":"2.00E-110"},15,2,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase","7763384, 1476773","Thiocystis violacea","2311 / DSM 208",4,397,397,3,394,394]
[]
["CLOSTRIBL6_v1_0558","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O34893","IPMed?",0.99618,1.00385,50.96,{"v":1e-71,"d":"1.00E-71"},1,1,"yngF","Putative enoyl-CoA hydratase/isomerase YngF","_","Complete proteome, Lyase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",6,261,262,3,259,260]
[null,"P52046","IPMed?",1.01145,1.01533,46.79,{"v":4e-69,"d":"4.00E-69"},2,2,"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",3,262,262,1,261,261]
[null,"Q0AVM1","IPMed?",0.98855,0.99615,45.56,{"v":1e-67,"d":"1.00E-67"},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",5,259,262,3,257,260]
[null,"A4YI89","IPMed?",1,1.01158,41.22,{"v":2e-60,"d":"2.00E-60"},4,2,"_","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",3,262,262,1,259,259]
[null,"Q52995","IPMed?",0.99237,1.01167,41.92,{"v":1E-58,"d":"1.00E-58"},5,1,"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",3,262,262,1,257,257]
[null,"Q9JLZ3","IPMed?",0.82166,0.98473,41.47,{"v":2e-58,"d":"2.00E-58"},6,1,"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",9,261,262,57,313,314]
[null,"F1LU71","IPMed?",0.81905,0.98473,41.47,{"v":2e-58,"d":"2.00E-58"},6,1,"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",9,261,262,58,314,315]
[null,"P9WNN9","_",0.98473,1.00389,41.09,{"v":6E-57,"d":"6.00E-57"},7,2,"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",5,262,262,3,257,257]
[null,"P64017","_",0.98473,1.00389,41.09,{"v":6E-57,"d":"6.00E-57"},7,2,"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",5,262,262,3,257,257]
[null,"P9WNN8","_",0.98473,1.00389,41.09,{"v":6E-57,"d":"6.00E-57"},7,2,"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",5,262,262,3,257,257]
[null,"P14604","IPMed?",0.90345,1,40.84,{"v":2e-56,"d":"2.00E-56"},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","_",2,260,262,30,288,290]
[null,"Q1ZXF1","_",0.8556,0.90458,45.15,{"v":2e-56,"d":"2.00E-56"},9,2,"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",19,255,262,37,270,277]
[null,"Q13825","IPMed?",0.75811,0.98092,40.47,{"v":4e-56,"d":"4.00E-56"},10,1,"AUH","Methylglutaconyl-CoA hydratase, mitochondrial","4.2.1.18","3D-structure, Acetylation, Alternative splicing, Branched-chain amino acid catabolism, Complete proteome, Direct protein sequencing, Disease mutation, Lyase, Mitochondrion, Reference proteome, RNA-binding, Transit peptide","7892223, 15164053, 15489334, 12434311, 21269460, 24275569, 25944712, 29056341, 11738050, 12655555","Homo sapiens","_",9,261,262,82,338,339]
[null,"P76082","IPMed?",0.94275,0.96863,41.7,{"v":5e-55,"d":"5.00E-55"},11,1,"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",16,262,262,12,255,255]
[null,"P30084","IPMed?",0.90345,1,40.08,{"v":3e-54,"d":"3.00E-54"},12,2,"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","_",2,260,262,30,288,290]
[]
["CLOSTRIBL6_v1_0559","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q93AM1","IPMed?",0.96845,0.9975,31.83,{"v":6E-68,"d":"6.00E-68"},1,1,"fldA","Cinnamoyl-CoA:phenyllactate CoA-transferase","2.8.3.17","Direct protein sequencing, Transferase","11967068, 10849007","Clostridium sporogenes","ATCC 3584 / ATCC 3584",7,399,400,11,406,412]
[null,"Q7TNE1","_",0.77064,0.84,31.55,{"v":2e-40,"d":"2.00E-40"},2,1,"Sugct","Succinate--hydroxymethylglutarate CoA-transferase","2.8.3.13","Acetylation, Complete proteome, Mitochondrion, Reference proteome, Transferase, Transit peptide","19468303, 15489334, 21183079, 23576753","Mus musculus","C57BL/6J / FVB/N",1,333,400,36,365,436]
[null,"Q9HAC7","IPMed?",0.8809,0.98,28.57,{"v":5e-40,"d":"5.00E-40"},4,1,"SUGCT","Succinate--hydroxymethylglutarate CoA-transferase","2.8.3.13","Acetylation, Alternative splicing, Complete proteome, Disease mutation, Glutaricaciduria, Mitochondrion, Reference proteome, Transferase, Transit peptide","14702039, 12853948, 12690205, 15489334, 11829489, 23893049, 18926513","Homo sapiens","_",1,389,400,45,428,445]
[null,"Q68FU4","_",0.77064,0.84,31.25,{"v":5e-40,"d":"5.00E-40"},3,1,"Sugct","Succinate--hydroxymethylglutarate CoA-transferase","2.8.3.13","Acetylation, Complete proteome, Mitochondrion, Reference proteome, Transferase, Transit peptide","15057822, 15489334","Rattus norvegicus","Brown Norway",1,333,400,36,365,436]
[null,"O87838","_",1.0122,1.0375,27.95,{"v":5e-38,"d":"5.00E-38"},5,1,"frc","Formyl-CoA:oxalate CoA-transferase","2.8.3.16","Complete proteome, Reference proteome, Transferase",12000953,"Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)","ATCC BAA-471 / A3(2) / M145",2,396,400,4,407,410]
[null,"Q82M40","_",1.00733,1.03,27.67,{"v":2e-37,"d":"2.00E-37"},6,1,"frc","Formyl-CoA:oxalate CoA-transferase","2.8.3.16","Complete proteome, Reference proteome, Transferase","11572948, 12692562","Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)","ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680 / ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680",2,393,400,3,403,409]
[null,"A9X6P9","IPMed?",0.845,0.86889,30.77,{"v":7e-35,"d":"7.00E-35"},7,1,"uctC","Acetyl-CoA:oxalate CoA-transferase","2.8.3.19","Transferase","18502856, 23935849","Acetobacter aceti","1023 / 1023",3,334,400,12,340,389]
[null,"Q8FFE8","_",1.02404,1.065,26.76,{"v":8e-34,"d":"8.00E-34"},8,1,"frc","Formyl-CoA:oxalate CoA-transferase","2.8.3.16","Complete proteome, Transferase",12471157,"Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","CFT073 / ATCC 700928 / UPEC",3,399,400,4,416,416]
[null,"P69902","IPMed?",1.02404,1.065,26.76,{"v":1e-33,"d":"1.00E-33"},10,1,"frc","Formyl-CoA:oxalate CoA-transferase","2.8.3.16","3D-structure, Complete proteome, Reference proteome, Transferase","9205837, 9278503, 16738553, 12694615, 18245280, 23335415, 12844490, 14993676","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",3,399,400,4,416,416]
[null,"P69903","_",1.02404,1.065,26.76,{"v":1e-33,"d":"1.00E-33"},10,1,"frc","Formyl-CoA:oxalate CoA-transferase","2.8.3.16","Complete proteome, Reference proteome, Transferase","12384590, 12704152","Shigella flexneri","301 / Serotype 2a / ATCC 700930 / 2457T / Serotype 2a",3,399,400,4,416,416]
[null,"Q0T2C3","_",1.02404,1.065,26.76,{"v":1e-33,"d":"1.00E-33"},10,1,"frc","Formyl-CoA:oxalate CoA-transferase","2.8.3.16","Complete proteome, Transferase",16822325,"Shigella flexneri serotype 5b (strain 8401)",8401,3,399,400,4,416,416]
[null,"Q31Y97","_",1.02404,1.065,26.76,{"v":1e-33,"d":"1.00E-33"},10,1,"frc","Formyl-CoA:oxalate CoA-transferase","2.8.3.16","Complete proteome, Transferase",16275786,"Shigella boydii serotype 4 (strain Sb227)","Sb227",3,399,400,4,416,416]
[null,"Q1R8Z2","_",1.02404,1.065,26.76,{"v":1e-33,"d":"1.00E-33"},10,1,"frc","Formyl-CoA:oxalate CoA-transferase","2.8.3.16","Complete proteome, Transferase",16585510,"Escherichia coli (strain UTI89 / UPEC)","UTI89 / UPEC",3,399,400,4,416,416]
[null,"A9WGE3","_",0.84826,0.8525,29.33,{"v":1e-33,"d":"1.00E-33"},9,1,"_","Succinyl-CoA--D-citramalate CoA-transferase","2.8.3.20","Complete proteome, Reference proteome, Transferase",21714912,"Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)","ATCC 29366 / DSM 635 / J-10-fl",2,328,400,8,332,402]
[null,"P96877","IPMed?",0.875,0.88832,29.71,{"v":8e-33,"d":"8.00E-33"},11,1,"_","Probable fatty acyl-CoA transferase Rv3272","2.8.3.-","3D-structure, Complete proteome, Reference proteome, Transferase","9634230, 21969609, 30342240","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / H37Rv",2,336,400,8,350,394]
[null,"O06644","IPMed?",1.03037,1.1025,26.76,{"v":3E-32,"d":"3.00E-32"},12,1,"frc","Formyl-CoA:oxalate CoA-transferase","2.8.3.16","3D-structure, Cytoplasm, Direct protein sequencing, Transferase","9150242, 2361939, 12839984, 15213226, 18245280, 18162462","Oxalobacter formigenes","OxB / OxB",2,399,400,3,428,428]
[null,"Q1KLK0","IPMed?",1.00988,1.0225,28.36,{"v":2e-30,"d":"2.00E-30"},13,1,"smtB","Succinyl-CoA--L-malate CoA-transferase beta subunit","2.8.3.22","Carbon dioxide fixation, Direct protein sequencing, Transferase",16547052,"Chloroflexus aurantiacus","Ok-70-fl",3,399,400,9,405,405]
[null,"P76518","IPMed?",0.84,0.88189,27.08,{"v":5e-27,"d":"5.00E-27"},14,1,"yfdE","Acetyl-CoA:oxalate CoA-transferase","2.8.3.19","3D-structure, Complete proteome, Reference proteome, Transferase","9205837, 9278503, 16738553, 8125343, 12694615, 23335415, 23935849","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12 / MG1655 / ATCC 47076 / K12 / BW25113",3,334,400,9,336,381]
[null,"Q1KLK1","IPMed?",0.92056,0.985,26.65,{"v":1E-26,"d":"1.00E-26"},15,1,"smtA","Succinyl-CoA--L-malate CoA-transferase alpha subunit","2.8.3.22","Carbon dioxide fixation, Direct protein sequencing, Transferase",16547052,"Chloroflexus aurantiacus","DSM 636 / Ok-70-fl",3,383,400,33,411,428]
[null,"Q9KJE9","IPMed?",0.99756,1.02,25.98,{"v":4e-26,"d":"4.00E-26"},16,1,"bbsF","Succinyl-CoA:(R)-benzylsuccinate CoA-transferase subunit BbsF","2.8.3.15","Aromatic hydrocarbons catabolism, Direct protein sequencing, Transferase","10629170, 11418570","Thauera aromatica","DSM 6984 / K172 / DSM 6984 / K172",2,393,400,7,402,409]
[]
["CLOSTRIBL6_v1_0560","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q5U925","IPMed?",0.97744,0.98113,56.92,{"v":4e-99,"d":"4.00E-99"},1,1,"hadI","2-hydroxyisocaproyl-CoA dehydratase activator","3.-.-.-","3D-structure, 4Fe-4S, ATP-binding, Hydrolase, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding, Plasmid","15654892, 22827463","Clostridioides difficile","DSMZ 1296",1,260,265,1,260,266]
[null,"G3KIM5","IPMed?",0.97736,1,57.14,{"v":7e-96,"d":"7.00E-96"},2,1,"lcdC","Activator of lactoyl-CoA dehydratase","_","4Fe-4S, Iron, Iron-sulfur, Metal-binding","4055736, 1597194, 22810300","Anaerotignum propionicum","_",1,259,265,1,259,259]
[null,"Q93AM0","IPMed?",0.98113,0.98485,55.38,{"v":8E-90,"d":"8.00E-90"},3,2,"fldI","(R)-phenyllactate dehydratase activator","3.6.1.-","Hydrolase, Iron, Iron-sulfur, Metal-binding",11967068,"Clostridium sporogenes","ATCC 3584",1,260,265,4,263,264]
[null,"P11568","IPMed?",0.97736,0.99615,54.05,{"v":8e-87,"d":"8.00E-87"},4,2,"hgdC","(R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase","3.6.1.3","3D-structure, 4Fe-4S, ATP-binding, Complete proteome, Direct protein sequencing, Hydrolase, Iron, Iron-sulfur, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome","8365476, 21304687, 2659350, 7607244, 3691501, 11106419, 11243821","Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4)","ATCC 25085 / DSM 20731 / VR4 / ATCC 25085 / DSM 20731 / VR4 / ATCC 25085 / DSM 20731 / VR4 / ATCC 25085 / DSM 20731 / VR4",1,258,265,3,260,260]
[null,"P39383","_",0.96981,1.00784,40.08,{"v":5E-52,"d":"5.00E-52"},5,1,"yjiL","Uncharacterized protein YjiL","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome","7610040, 9278503, 16738553","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",2,258,265,3,254,255]
[null,"Q60315","_",0.95094,1.03704,36.11,{"v":3e-40,"d":"3.00E-40"},6,2,"_","Uncharacterized protein MJ0004","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, 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",4,251,265,3,243,243]
[null,"O87876","IPMed?",0.4589,0.75849,41.29,{"v":1e-37,"d":"1.00E-37"},7,2,"bcrA","Benzoyl-CoA reductase subunit A","1.3.7.8","4Fe-4S, Aromatic hydrocarbons catabolism, ATP-binding, Direct protein sequencing, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding, Oxidoreductase","9746358, 8575453, 11208796","Thauera aromatica","DSM 6984 / K172 / DSM 6984 / K172 / DSM 6984 / K172",59,252,265,231,431,438]
[null,"O87877","IPMed?",0.95745,1.01887,32.22,{"v":5e-31,"d":"5.00E-31"},8,2,"bcrD","Benzoyl-CoA reductase subunit D","1.3.7.8","4Fe-4S, Aromatic hydrocarbons catabolism, ATP-binding, Direct protein sequencing, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding, Oxidoreductase","9746358, 8575453, 11208796","Thauera aromatica","DSM 6984 / K172 / DSM 6984 / K172 / DSM 6984 / K172",3,261,265,4,270,282]
[]
["CLOSTRIBL6_v1_0561","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q5U924","IPMed?",0.94884,1,46.32,{"v":7e-122,"d":"7.00E-122"},1,2,"hadB","(R)-2-hydroxyisocaproyl-CoA dehydratase alpha subunit","4.2.1.157","3D-structure, 4Fe-4S, Direct protein sequencing, Iron, Iron-sulfur, Lyase, Metal-binding, Plasmid","15654892, 21366233","Clostridioides difficile","_",21,425,430,4,402,408]
[null,"Q93AL9","IPMed?",0.94651,1,45.45,{"v":3e-118,"d":"3.00E-118"},2,2,"fldB","(R)-phenyllactyl-CoA dehydratase alpha subunit","4.2.1.-","4Fe-4S, Direct protein sequencing, Iron, Iron-sulfur, Lyase, Metal-binding","11967068, 10849007","Clostridium sporogenes","ATCC 3584 / ATCC 3584",23,427,430,12,407,407]
[null,"P11569","IPMed?",0.97904,1.08605,38.12,{"v":1e-104,"d":"1.00E-104"},3,2,"hgdA","(R)-2-hydroxyglutaryl-CoA dehydratase, subunit alpha","4.2.1.167","4Fe-4S, Complete proteome, Cytoplasm, Direct protein sequencing, Flavoprotein, FMN, Iron, Iron-sulfur, Lyase, Magnesium, Metal-binding, Reference proteome","2659350, 21304687, 8365476, 3691501, 7398622, 7607244, 11106419","Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4)","ATCC 25085 / DSM 20731 / VR4 / ATCC 25085 / DSM 20731 / VR4 / ATCC 25085 / DSM 20731 / VR4 / ATCC 25085 / DSM 20731 / VR4 / ATCC 25085 / DSM 20731 / VR4",28,428,430,12,476,477]
[null,"G3KIM4","IPMed?",0.94186,0.95972,36.79,{"v":5e-81,"d":"5.00E-81"},4,2,"lcdA","Lactoyl-CoA dehydratase subunit alpha","4.2.1.54","4Fe-4S, Flavoprotein, FMN, Iron, Iron-sulfur, Lyase, Metal-binding","4055736, 1597194, 22810300","Anaerotignum propionicum","_",38,426,430,23,420,422]
[null,"O87875","IPMed?",0.99306,0.99767,24.01,{"v":3E-24,"d":"3.00E-24"},5,2,"bcrB","Benzoyl-CoA reductase subunit B","1.3.7.8","Aromatic hydrocarbons catabolism, ATP-binding, Direct protein sequencing, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding, Oxidoreductase","9746358, 8575453, 11208796","Thauera aromatica","DSM 6984 / K172 / DSM 6984 / K172",17,424,430,7,424,432]
[]
["CLOSTRIBL6_v1_0562","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q5U923","IPMed?",0.98138,0.984,49.86,{"v":9e-127,"d":"9.00E-127"},1,1,"hadC","(R)-2-hydroxyisocaproyl-CoA dehydratase beta subunit","4.2.1.157","3D-structure, 4Fe-4S, Direct protein sequencing, Iron, Iron-sulfur, Lyase, Metal-binding, Plasmid","15654892, 21366233","Clostridioides difficile","DSMZ 1296",8,375,376,5,372,375]
[null,"G3KIM3","IPMed?",1.00532,1.0107,45.24,{"v":4E-109,"d":"4.00E-109"},2,1,"lcdB","Lactoyl-CoA dehydratase subunit beta","4.2.1.54","4Fe-4S, Flavoprotein, FMN, Iron, Iron-sulfur, Lyase, Metal-binding","4055736, 1597194, 22810300","Anaerotignum propionicum","_",1,375,376,1,374,374]
[null,"Q93AL8","IPMed?",1,1.00535,41.22,{"v":5e-100,"d":"5.00E-100"},3,1,"fldC","(R)-phenyllactyl-CoA dehydratase beta subunit","4.2.1.-","4Fe-4S, Direct protein sequencing, Iron, Iron-sulfur, Lyase, Metal-binding","11967068, 10849007","Clostridium sporogenes","ATCC 3584 / ATCC 3584",1,375,376,1,374,374]
[null,"P11570","IPMed?",0.98681,0.99468,35.83,{"v":4e-75,"d":"4.00E-75"},4,2,"hgdB","(R)-2-hydroxyglutaryl-CoA dehydratase, subunit beta","4.2.1.167","4Fe-4S, Complete proteome, Cytoplasm, Direct protein sequencing, Flavoprotein, FMN, Iron, Iron-sulfur, Lyase, Magnesium, Metal-binding, Reference proteome","2659350, 21304687, 3691501, 7398622, 7607244, 11106419","Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4)","ATCC 25085 / DSM 20731 / VR4 / ATCC 25085 / DSM 20731 / VR4 / ATCC 25085 / DSM 20731 / VR4",8,375,376,7,379,379]
[null,"O87874","IPMed?",0.9171,0.94149,22.6,{"v":9e-28,"d":"9.00E-28"},5,2,"bcrC","Benzoyl-CoA reductase subunit C","1.3.7.8","Aromatic hydrocarbons catabolism, ATP-binding, Direct protein sequencing, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding, Oxidoreductase","9746358, 8575453, 11208796","Thauera aromatica","DSM 6984 / K172 / DSM 6984 / K172 / DSM 6984 / K172",30,373,376,32,380,386]
[]
[]
["CLOSTRIBL6_v1_0871","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?",0.90764,1.01064,41.05,{"v":4e-61,"d":"4.00E-61"},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",6,289,314,1,281,282]
[null,"P77851","_",0.90446,1.01068,38.73,{"v":1e-57,"d":"1.00E-57"},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)","_",6,288,314,1,280,281]
[null,"Q9RVG1","_",0.89809,1.01439,39.72,{"v":3E-57,"d":"3.00E-57"},3,2,"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",8,288,314,2,278,278]
[null,"Q0AVM2","IPMed?",0.89809,1.01075,36.52,{"v":4E-52,"d":"4.00E-52"},4,3,"_","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",8,288,314,2,279,279]
[null,"P45364","IPMed?",0.90127,1.00712,36.04,{"v":8e-52,"d":"8.00E-52"},5,2,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase",8001771,"Clostridioides difficile","E",8,289,314,2,280,281]
[null,"P45856","IPMed?",0.90764,0.99303,37.54,{"v":5E-51,"d":"5.00E-51"},6,3,"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",5,288,314,2,282,287]
[null,"Q61425","IPMed?",0.92994,0.92994,35.62,{"v":4e-44,"d":"4.00E-44"},7,3,"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",6,288,314,27,313,314]
[null,"P9WNP7","IPMed?",0.9172,1.00699,31.6,{"v":4e-44,"d":"4.00E-44"},8,3,"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",3,288,314,2,286,286]
[null,"P9WNP6","_",0.9172,1.00699,31.6,{"v":4e-44,"d":"4.00E-44"},8,3,"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",3,288,314,2,286,286]
[null,"Q9WVK7","IPMed?",0.92994,0.92994,35.27,{"v":5e-44,"d":"5.00E-44"},9,3,"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",6,288,314,27,313,314]
[null,"Q16836","IPMed?",0.92675,0.92675,35.05,{"v":7e-44,"d":"7.00E-44"},10,3,"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","_",6,288,314,27,313,314]
[null,"P00348","IPMed?",0.92675,0.92675,33.33,{"v":3E-43,"d":"3.00E-43"},11,3,"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","_",6,288,314,27,313,314]
[null,"Q9AHY3","IPMed?",0.40559,0.92357,32.41,{"v":5e-35,"d":"5.00E-35"},12,3,"fadB","Enoyl-CoA hydratase/Delta(3)-cis-Delta(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","Fatty acid metabolism, Isomerase, Lipid degradation, Lipid metabolism, Lyase, Multifunctional enzyme, NAD, Oxidoreductase",11251808,"Pseudomonas putida","U",3,288,314,311,592,715]
[]
["CLOSTRIBL6_v1_2953","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O59028","_",0.96667,1.00578,38.79,{"v":7e-70,"d":"7.00E-70"},1,1,"mdh","Malate dehydrogenase","1.1.1.37","3D-structure, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Tricarboxylic acid cycle",9679194,"Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)","ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3",3,342,346,13,357,360]
[null,"Q9V0D5","_",0.96133,1.00578,39.08,{"v":1e-68,"d":"1.00E-68"},2,1,"mdh","Malate dehydrogenase","1.1.1.37","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Tricarboxylic acid cycle","12622808, 22057919","Pyrococcus abyssi (strain GE5 / Orsay)","GE5 / Orsay / GE5 / Orsay",3,342,346,13,357,362]
[null,"Q58820","IPMed?",0.95376,0.9593,39.39,{"v":2E-66,"d":"2.00E-66"},3,2,"comC","L-sulfolactate dehydrogenase","1.1.1.337","3D-structure, Coenzyme M biosynthesis, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Reference proteome","8688087, 10850983","Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440",4,333,346,3,328,344]
[null,"P16142","IPMed?",0.95376,0.97345,36.67,{"v":3e-66,"d":"3.00E-66"},4,1,"mdh","Malate/(S)-sulfolactate dehydrogenase","1.1.1.310, 1.1.1.37, 1.1.1.82","Complete proteome, Cytoplasm, Direct protein sequencing, NAD, NADP, Oxidoreductase, Reference proteome, Tricarboxylic acid cycle","2110059, 21304736, 10850983","Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)","ATCC 43054 / DSM 2088 / JCM 10308 / V24 S / ATCC 43054 / DSM 2088 / JCM 10308 / V24 S",4,333,346,3,326,339]
[null,"O34736","IPMed?",0.91908,0.94362,36.79,{"v":1e-65,"d":"1.00E-65"},5,1,"yjmC","Uncharacterized oxidoreductase YjmC","1.1.1.-","Complete proteome, Cytoplasm, Oxidoreductase, Reference proteome","9579062, 9384377, 9882655","Bacillus subtilis (strain 168)","168 / 168 / 168 / MB24",17,333,346,19,334,337]
[null,"P58408","_",0.95702,0.96532,34.43,{"v":3e-62,"d":"3.00E-62"},7,1,"allD","Ureidoglycolate dehydrogenase (NAD(+))","1.1.1.350","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Purine metabolism, Reference proteome","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",3,335,346,2,333,349]
[null,"P77555","IPMed?",0.95702,0.96532,34.73,{"v":3e-62,"d":"3.00E-62"},6,1,"allD","Ureidoglycolate dehydrogenase (NAD(+))","1.1.1.350","3D-structure, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Purine metabolism, Reference proteome","10601204, 9278503, 16738553, 23284870","Escherichia coli (strain K12)","K12 / ECL1 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",3,335,346,2,333,349]
[null,"O27273","_",0.97977,0.99413,35.4,{"v":2e-61,"d":"2.00E-61"},8,1,"comC","L-sulfolactate dehydrogenase","1.1.1.337","Coenzyme M biosynthesis, Complete proteome, Cytoplasm, NAD, 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",3,338,346,2,330,341]
[null,"Q1QWN5","IPMed?",0.9711,1.00901,35.42,{"v":7e-57,"d":"7.00E-57"},9,1,"comC","(2R)-3-sulfolactate dehydrogenase (NADP(+))","1.1.1.338","Complete proteome, NAD, NADP, Oxidoreductase","22675587, 20007648","Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768)","DSM 3043 / ATCC BAA-138 / NCIMB 13768 / DSM 3043 / ATCC BAA-138 / NCIMB 13768",2,336,346,3,328,333]
[null,"Q5FB93","IPMed?",0.94509,0.95894,32.42,{"v":4E-41,"d":"4.00E-41"},10,2,"dpkA","Delta(1)-pyrroline-2-carboxylate/Delta(1)-piperideine-2-carboxylate reductase","1.5.1.21","Direct protein sequencing, NADP, Oxidoreductase","15720386, 15561717","Pseudomonas putida","ATCC 12633 / DSM 291 / JCM 13063 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90 / ATCC 12633 / DSM 291 / JCM 13063 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90",9,333,346,17,336,341]
[null,"P30178","IPMed?",0.95014,0.99133,31.49,{"v":4e-39,"d":"4.00E-39"},11,1,"hcxB","Hydroxycarboxylate dehydrogenase B","1.1.1.-","3D-structure, Complete proteome, NAD, NADP, Oxidoreductase, Reference proteome","8037924, 8905232, 9278503, 16738553, 27941785","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",7,342,346,10,347,361]
[null,"Q9I492","IPMed?",0.97399,1.00898,28.19,{"v":2e-38,"d":"2.00E-38"},12,1,"lhpD","Delta(1)-pyrroline-2-carboxylate/Delta(1)-piperideine-2-carboxylate reductase","1.5.1.21","Complete proteome, NADP, Oxidoreductase, Reference proteome","10984043, 24649405, 24980702","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 / 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",7,335,346,7,331,334]
[null,"Q4U331","IPMed?",0.93353,0.94169,30.96,{"v":5e-37,"d":"5.00E-37"},13,2,"dpkA","Delta(1)-pyrroline-2-carboxylate/Delta(1)-piperideine-2-carboxylate reductase","1.5.1.21","3D-structure, NADP, Nucleotide-binding, Oxidoreductase",16192274,"Pseudomonas syringae pv. tomato","DSM 50315",20,336,346,29,343,343]
[null,"Q07251","IPMed?",1.03725,1.04624,27.62,{"v":5e-35,"d":"5.00E-35"},14,3,"ldh","L-lactate dehydrogenase","1.1.1.27","Complete proteome, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Reference proteome","8405966, 16964242","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337",3,345,346,2,347,349]
[]
["CLOSTRIBL6_v1_0031","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O34893","IPMed?",0.87361,0.90385,36.17,{"v":2e-36,"d":"2.00E-36"},1,3,"yngF","Putative enoyl-CoA hydratase/isomerase YngF","_","Complete proteome, Lyase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",4,236,269,5,226,260]
[null,"A4YI89","IPMed?",0.92193,0.95753,31.85,{"v":9e-36,"d":"9.00E-36"},2,3,"_","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",15,262,269,17,251,259]
[null,"P77467","IPMed?",0.99257,1.01908,32.58,{"v":5e-34,"d":"5.00E-34"},3,2,"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",1,262,269,2,255,262]
[null,"P9WNN8","_",0.86617,0.90661,32.19,{"v":2e-33,"d":"2.00E-33"},5,3,"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",4,236,269,6,223,257]
[null,"P24162","IPMed?",0.95911,1.00389,32.95,{"v":2e-33,"d":"2.00E-33"},4,1,"fadB1","Probable enoyl-CoA hydratase","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","1743516, 20418398","Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)","ATCC BAA-309 / NBRC 16581 / SB1003 / ATCC BAA-309 / NBRC 16581 / SB1003",6,262,269,8,249,257]
[null,"P9WNN9","_",0.86617,0.90661,32.19,{"v":2e-33,"d":"2.00E-33"},5,3,"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",4,236,269,6,223,257]
[null,"P64017","_",0.86617,0.90661,32.19,{"v":2e-33,"d":"2.00E-33"},5,3,"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",4,236,269,6,223,257]
[null,"Q0AVM1","IPMed?",0.97026,1.00385,29.5,{"v":2e-32,"d":"2.00E-32"},6,3,"_","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",3,262,269,5,252,260]
[null,"P52046","IPMed?",0.97026,1,31.03,{"v":7e-32,"d":"7.00E-32"},7,3,"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",3,262,269,5,252,261]
[null,"O07137","_",0.82528,0.86381,32.88,{"v":6e-31,"d":"6.00E-31"},8,3,"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",15,236,269,17,223,257]
[null,"Q7U004","_",0.92632,0.98141,32.2,{"v":1e-30,"d":"1.00E-30"},9,1,"echA12","Probable enoyl-CoA hydratase echA12","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",4,262,269,21,276,285]
[null,"Q52995","IPMed?",0.99257,1.03891,31.09,{"v":1e-30,"d":"1.00E-30"},10,3,"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",4,269,269,6,257,257]
[null,"P76082","IPMed?",0.97398,1.02745,27.48,{"v":3e-29,"d":"3.00E-29"},11,3,"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",1,262,269,1,247,255]
[null,"P23966","IPMed?",0.98893,0.99628,30.6,{"v":4e-29,"d":"4.00E-29"},12,2,"menB","1,4-dihydroxy-2-naphthoyl-CoA synthase","4.1.3.36","Complete proteome, Lyase, Menaquinone biosynthesis, Reference proteome","1629163, 8566759, 9387221, 9384377, 20643650","Bacillus subtilis (strain 168)","168 / RB1 / 168 / RB1 / 168 / 168",3,269,269,12,260,271]
[null,"Q8GYN9","IPMed?",0.67062,0.84015,32.3,{"v":6e-29,"d":"6.00E-29"},13,3,"MENB","1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal","4.1.3.36","Complete proteome, Isomerase, Lyase, Peroxisome, Reference proteome","11130712, 27862469, 11910074, 17951448, 20150517","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia",3,225,269,76,289,337]
[]
["CLOSTRIBL6_v1_1904","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?",0.59746,0.99472,58.36,{"v":3e-144,"d":"3.00E-144"},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",1,377,631,1,377,379]
[null,"P45857","IPMed?",0.59271,0.98681,53.74,{"v":2E-137,"d":"2.00E-137"},3,3,"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",6,379,631,4,377,379]
[null,"P45867","IPMed?",0.59271,0.98681,57.22,{"v":2E-137,"d":"2.00E-137"},2,4,"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",1,374,631,1,374,379]
[null,"Q06319","IPMed?",0.60539,0.99739,51.31,{"v":2e-123,"d":"2.00E-123"},4,4,"_","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","_",1,378,631,1,382,383]
[null,"Q3ZBF6","IPMed?",0.58954,0.90291,52.15,{"v":1e-120,"d":"1.00E-120"},5,3,"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","_",7,378,631,36,407,412]
[null,"Q5RAS0","_",0.58954,0.90291,52.69,{"v":3e-120,"d":"3.00E-120"},6,3,"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","_",7,378,631,36,407,412]
[null,"O34421","IPMed?",0.60063,0.99737,50.92,{"v":3e-120,"d":"3.00E-120"},7,3,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,378,631,1,379,380]
[null,"P15651","IPMed?",0.58954,0.90291,52.42,{"v":8e-120,"d":"8.00E-120"},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","_",7,378,631,36,407,412]
[null,"Q07417","IPMed?",0.58954,0.90291,52.15,{"v":2E-119,"d":"2.00E-119"},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","8276399, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / FVB/N",7,378,631,36,407,412]
[null,"P16219","IPMed?",0.58954,0.90291,52.42,{"v":2E-119,"d":"2.00E-119"},9,3,"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","_",7,378,631,36,407,412]
[null,"G3KIM8","IPMed?",0.60222,0.96447,50.53,{"v":3e-114,"d":"3.00E-114"},11,3,"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",1,378,631,14,392,394]
[]
["CLOSTRIBL6_v1_3062","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?",0.66726,0.99472,56.23,{"v":3e-144,"d":"3.00E-144"},1,4,"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",1,377,565,1,377,379]
[null,"P45867","IPMed?",0.66726,0.99472,56.76,{"v":1E-139,"d":"1.00E-139"},2,3,"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",1,377,565,1,377,379]
[null,"P45857","IPMed?",0.66372,0.98945,54.67,{"v":2e-139,"d":"2.00E-139"},3,2,"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",5,379,565,3,377,379]
[null,"Q06319","IPMed?",0.67611,0.99739,52.88,{"v":9E-130,"d":"9.00E-130"},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","_",1,378,565,1,382,383]
[null,"O34421","IPMed?",0.6708,0.99737,51.19,{"v":2E-120,"d":"2.00E-120"},5,2,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,378,565,1,379,380]
[null,"G3KIM8","IPMed?",0.67257,0.96447,49.21,{"v":3e-113,"d":"3.00E-113"},6,4,"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",1,378,565,14,392,394]
[null,"H6LGM6","IPMed?",0.66549,0.99208,47.87,{"v":9e-113,"d":"9.00E-113"},7,3,"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",6,380,565,4,379,379]
[null,"Q07417","IPMed?",0.64956,0.89078,49.86,{"v":1e-112,"d":"1.00E-112"},8,4,"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",12,378,565,41,407,412]
[null,"P15651","IPMed?",0.64956,0.89078,49.86,{"v":2e-112,"d":"2.00E-112"},9,4,"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","_",12,378,565,41,407,412]
[null,"Q3ZBF6","IPMed?",0.64956,0.89078,49.32,{"v":5e-112,"d":"5.00E-112"},10,4,"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","_",12,378,565,41,407,412]
[]
["CLOSTRIBL6_v1_0135","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?",1,1,68.6,0,1,1,"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?",0.99472,0.99472,59.42,{"v":8e-154,"d":"8.00E-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",1,377,379,1,377,379]
[null,"P45857","IPMed?",0.98681,0.98681,53.48,{"v":3e-142,"d":"3.00E-142"},3,1,"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",5,378,379,3,376,379]
[null,"Q06319","IPMed?",1,1.01055,56.92,{"v":5e-142,"d":"5.00E-142"},4,1,"_","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?",0.96701,1.00528,52.76,{"v":6e-131,"d":"6.00E-131"},5,1,"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,"O34421","IPMed?",1,1.00264,51.58,{"v":2e-129,"d":"2.00E-129"},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?",0.91262,0.99208,50,{"v":3e-126,"d":"3.00E-126"},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",4,379,379,33,408,412]
[null,"P15651","IPMed?",0.91262,0.99208,50,{"v":5e-126,"d":"5.00E-126"},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","_",4,379,379,33,408,412]
[null,"H6LGM6","IPMed?",0.98945,0.98945,50.4,{"v":3E-124,"d":"3.00E-124"},9,1,"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,"Q3ZBF6","IPMed?",0.91262,0.99208,49.73,{"v":3e-123,"d":"3.00E-123"},10,2,"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","_",4,379,379,33,408,412]
[]
["CLOSTRIBL6_v1_0136","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?",0.98842,0.98842,60.94,{"v":3e-109,"d":"3.00E-109"},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",1,256,259,1,256,259]
[null,"P97089","_",1,1.00386,55,{"v":1e-93,"d":"1.00E-93"},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?",1,1.01158,55.34,{"v":2E-92,"d":"2.00E-92"},3,1,"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?",0.98889,1.03089,47.19,{"v":2e-72,"d":"2.00E-72"},4,2,"etfB","Electron transfer flavoprotein subunit beta","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,258,259,1,265,270]
[null,"G3KIM7","IPMed?",1,1.03089,47.19,{"v":2e-72,"d":"2.00E-72"},4,1,"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,"P26482","IPMed?",0.92171,1,43.63,{"v":1E-61,"d":"1.00E-61"},5,2,"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)","_",1,249,259,1,259,281]
[null,"P53577","IPMed?",0.89931,1,41.31,{"v":5e-59,"d":"5.00E-59"},6,2,"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",4,253,259,4,262,288]
[null,"P53576","_",0.85409,0.92664,45.83,{"v":5e-58,"d":"5.00E-58"},7,2,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",4,234,259,4,242,281]
[null,"Q53210","_",0.89474,0.98456,42.35,{"v":8e-58,"d":"8.00E-58"},8,2,"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",1,246,259,1,254,285]
[null,"P09818","IPMed?",0.80822,0.9112,44.07,{"v":1E-53,"d":"1.00E-53"},9,2,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104, 6317191","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",1,227,259,1,236,292]
[null,"Q05559","IPMed?",0.93907,1.01158,39.69,{"v":5e-50,"d":"5.00E-50"},10,2,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport",8369342,"Rhizobium leguminosarum bv. phaseoli","_",1,253,259,1,260,279]
[null,"P64098","IPMed?",0.97368,1,32.05,{"v":8e-35,"d":"8.00E-35"},11,1,"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",2,253,259,3,260,266]
[null,"Q68FU3","IPMed?",0.82625,0.83922,34.58,{"v":7e-28,"d":"7.00E-28"},12,1,"Etfb","Electron transfer flavoprotein subunit beta","_","Acetylation, Complete proteome, Electron transport, Methylation, Mitochondrion, Nucleotide-binding, Phosphoprotein, Reference proteome, Transport","15489334, 7334008","Rattus norvegicus","_",4,210,259,7,217,255]
[null,"P38117","IPMed?",0.83398,0.84706,35.19,{"v":6e-27,"d":"6.00E-27"},13,1,"ETFB","Electron transfer flavoprotein subunit beta","_","3D-structure, Acetylation, Alternative splicing, Complete proteome, Disease mutation, Electron transport, Glutaricaciduria, Methylation, Mitochondrion, Phosphoprotein, Polymorphism, Reference proteome, Transport","8504797, 12815589, 15498874, 14702039, 15489334, 7912128, 17941859, 21269460, 25023281, 24275569, 24129315, 25416781, 25944712, 27499296, 8962055, 15159392, 15975918, 10356313","Homo sapiens","_",1,210,259,4,217,255]
[]
["CLOSTRIBL6_v1_0137","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","_",0.94509,0.99091,57.49,{"v":3E-132,"d":"3.00E-132"},1,1,"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)","_",12,338,346,3,328,330]
[null,"P52039","IPMed?",0.95954,0.9881,58.43,{"v":6e-131,"d":"6.00E-131"},2,1,"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",8,337,346,1,332,336]
[null,"P53578","IPMed?",0.95665,0.99102,55.59,{"v":2e-126,"d":"2.00E-126"},3,1,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Transport",7875566,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",8,338,346,1,329,334]
[null,"H6LGM8","IPMed?",0.84848,0.9711,53.87,{"v":3E-124,"d":"3.00E-124"},4,1,"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",3,338,346,60,393,396]
[null,"O85692","IPMed?",0.97399,0.99704,51.63,{"v":2e-111,"d":"2.00E-111"},5,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",8,340,346,1,335,338]
[null,"G3KIM6","IPMed?",1.00272,1.06358,47.01,{"v":3e-104,"d":"3.00E-104"},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",13,346,346,11,367,367]
[null,"P26483","IPMed?",0.88347,0.9422,44.48,{"v":6e-86,"d":"6.00E-86"},7,1,"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)","_",13,334,346,29,353,369]
[null,"P94551","_",0.9422,1.00308,40.8,{"v":2e-83,"d":"2.00E-83"},8,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8969504, 9384377","Bacillus subtilis (strain 168)","168 / 168",14,338,346,3,320,325]
[null,"Q53209","_",0.90515,0.96532,42.22,{"v":6e-82,"d":"6.00E-82"},9,1,"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",12,341,346,28,360,369]
[null,"P53574","_",0.94444,0.98266,41.47,{"v":4e-81,"d":"4.00E-81"},10,1,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",12,346,346,21,359,360]
[null,"P09819","IPMed?",0.94334,0.96243,41.74,{"v":3e-80,"d":"3.00E-80"},11,1,"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",11,338,346,10,341,353]
[null,"P10449","IPMed?",0.88618,0.94509,42.2,{"v":7e-80,"d":"7.00E-80"},12,2,"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",11,333,346,27,352,369]
[null,"Q0AZ33","IPMed?",0.93642,1.02208,40.12,{"v":5e-76,"d":"5.00E-76"},13,1,"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",15,338,346,3,317,317]
[null,"P13803","IPMed?",0.9422,0.97898,36.81,{"v":2e-57,"d":"2.00E-57"},14,1,"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","_",13,338,346,19,332,333]
[]
["CLOSTRIBL6_v1_3216","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?",0.98684,0.98945,57.87,{"v":1E-146,"d":"1.00E-146"},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",1,375,380,1,375,379]
[null,"P45867","IPMed?",0.98421,0.98681,55.88,{"v":3e-146,"d":"3.00E-146"},2,2,"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",1,374,380,1,374,379]
[null,"Q06319","IPMed?",0.98956,0.99737,53.03,{"v":5e-129,"d":"5.00E-129"},3,3,"_","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","_",1,375,380,1,379,383]
[null,"P15651","IPMed?",0.86893,0.94211,51.96,{"v":7E-126,"d":"7.00E-126"},4,2,"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","_",18,375,380,47,404,412]
[null,"Q3ZBF6","IPMed?",0.86893,0.94211,52.79,{"v":1E-125,"d":"1.00E-125"},5,1,"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","_",18,375,380,47,404,412]
[null,"Q07417","IPMed?",0.86893,0.94211,51.96,{"v":2E-125,"d":"2.00E-125"},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","8276399, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / FVB/N",18,375,380,47,404,412]
[null,"Q5RAS0","_",0.88835,0.96316,51.09,{"v":2e-124,"d":"2.00E-124"},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","_","Pongo abelii","_",10,375,380,39,404,412]
[null,"P16219","IPMed?",0.88835,0.96316,50.82,{"v":1e-123,"d":"1.00E-123"},8,1,"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","_",10,375,380,39,404,412]
[null,"P79273","_",0.86925,0.94474,51.81,{"v":2E-121,"d":"2.00E-121"},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","_","Sus scrofa","_",18,375,380,47,405,413]
[null,"P45857","IPMed?",0.97895,0.98153,47.85,{"v":2E-118,"d":"2.00E-118"},10,4,"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",6,377,380,4,375,379]
[null,"G3KIM8","IPMed?",0.95431,0.98947,47.61,{"v":7e-116,"d":"7.00E-116"},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",1,374,380,14,388,394]
[null,"O34421","IPMed?",0.98684,0.98684,47.73,{"v":6e-114,"d":"6.00E-114"},12,4,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,374,380,1,375,380]
[]
["CLOSTRIBL6_v1_3217","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","_",0.99102,1.00303,58.01,{"v":3e-120,"d":"3.00E-120"},1,2,"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)","_",6,333,334,5,330,330]
[null,"P53578","IPMed?",0.97605,0.97605,52.45,{"v":2e-114,"d":"2.00E-114"},2,2,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Transport",7875566,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",6,331,334,7,329,334]
[null,"O85692","IPMed?",0.97929,0.99102,50.45,{"v":8e-104,"d":"8.00E-104"},3,2,"etfA","Electron transfer flavoprotein subunit alpha","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",6,333,334,7,335,338]
[null,"H6LGM8","IPMed?",0.82828,0.98204,49.7,{"v":1e-103,"d":"1.00E-103"},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",6,331,334,69,393,396]
[null,"P52039","IPMed?",0.98214,0.98802,48.79,{"v":2e-103,"d":"2.00E-103"},5,2,"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",6,332,334,7,334,336]
[null,"G3KIM6","IPMed?",0.97003,1.06587,47.19,{"v":5e-99,"d":"5.00E-99"},6,2,"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",6,333,334,12,365,367]
[null,"P10449","IPMed?",0.8916,0.98503,44.38,{"v":3e-82,"d":"3.00E-82"},7,1,"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",6,330,334,30,356,369]
[null,"P26483","IPMed?",0.88347,0.97605,44.79,{"v":7e-80,"d":"7.00E-80"},8,2,"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)","_",6,326,334,30,352,369]
[null,"P94551","_",0.94611,0.97231,43.35,{"v":2E-78,"d":"2.00E-78"},9,2,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8969504, 9384377","Bacillus subtilis (strain 168)","168 / 168",17,331,334,13,320,325]
[null,"P09819","IPMed?",0.94051,0.99401,42.47,{"v":2e-77,"d":"2.00E-77"},10,2,"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",6,331,334,13,341,353]
[null,"Q0AZ33","IPMed?",0.96707,1.01893,40.87,{"v":2E-73,"d":"2.00E-73"},11,2,"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",9,331,334,5,317,317]
[null,"P13803","IPMed?",0.89222,0.89489,37.58,{"v":7e-51,"d":"7.00E-51"},12,2,"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","_",35,331,334,44,332,333]
[]
["CLOSTRIBL6_v1_3218","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O85691","IPMed?",0.92593,0.93284,53.2,{"v":1e-82,"d":"1.00E-82"},1,1,"etfB","Electron transfer flavoprotein subunit beta","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,249,268,1,249,270]
[null,"P97089","_",1,1.03077,51.87,{"v":6e-78,"d":"6.00E-78"},2,2,"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)","_",1,268,268,1,260,260]
[null,"H6LGM7","IPMed?",1,1.0229,48.51,{"v":5e-75,"d":"5.00E-75"},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",1,268,268,1,262,262]
[null,"P52040","IPMed?",0.97388,1.00772,48.66,{"v":3e-74,"d":"3.00E-74"},4,2,"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",1,261,268,1,253,259]
[null,"P26482","IPMed?",0.92527,0.97015,44.23,{"v":1e-63,"d":"1.00E-63"},5,1,"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)","_",1,255,268,1,258,281]
[null,"Q53210","_",0.89825,0.95522,45.7,{"v":2e-63,"d":"2.00E-63"},6,1,"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",1,252,268,1,252,285]
[null,"P53577","IPMed?",0.92361,0.99254,43.98,{"v":7e-63,"d":"7.00E-63"},7,1,"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",1,262,268,1,262,288]
[null,"Q05559","IPMed?",0.94982,0.98881,43.4,{"v":1e-60,"d":"1.00E-60"},8,1,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport",8369342,"Rhizobium leguminosarum bv. phaseoli","_",1,262,268,1,260,279]
[null,"P09818","IPMed?",0.83562,0.91045,45.49,{"v":2e-60,"d":"2.00E-60"},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",1,241,268,1,242,292]
[null,"P53576","_",0.96441,1.01119,41.7,{"v":4e-59,"d":"4.00E-59"},10,1,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",1,259,268,1,266,281]
[null,"G3KIM7","IPMed?",1,1.00375,42.91,{"v":1e-55,"d":"1.00E-55"},11,2,"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",1,260,268,1,263,267]
[null,"P64098","IPMed?",0.94403,0.95113,31.62,{"v":4e-31,"d":"4.00E-31"},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",2,249,268,3,249,266]
[null,"Q0AZ34","IPMed?",0.98507,1.04762,31.06,{"v":2e-29,"d":"2.00E-29"},13,1,"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",1,264,268,3,245,252]
[]
["CLOSTRIBL6_v1_3220","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P94535","_",0.92632,0.93617,40.68,{"v":8e-101,"d":"8.00E-101"},1,1,"glcD","Glycolate oxidase subunit GlcD","_","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","8969504, 9384377","Bacillus subtilis (strain 168)","168 / 168",33,469,475,29,457,470]
[null,"O29853","IPMed?",0.90316,0.9684,41.03,{"v":1E-87,"d":"1.00E-87"},2,3,"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",48,473,475,38,443,443]
[null,"P9WIT1","_",0.96632,1,38.78,{"v":3e-85,"d":"3.00E-85"},3,2,"_","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",22,469,475,16,455,459]
[null,"P9WIT0","_",0.96632,1,38.78,{"v":3e-85,"d":"3.00E-85"},3,2,"_","Uncharacterized FAD-linked oxidoreductase MT2338","1.-.-.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",22,469,475,16,455,459]
[null,"Q7TNG8","IPMed?",0.95661,0.97474,33.26,{"v":2e-69,"d":"2.00E-69"},4,1,"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",14,469,475,33,483,484]
[null,"Q86WU2","IPMed?",0.95858,1.02316,32.72,{"v":1e-66,"d":"1.00E-66"},5,1,"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","_",14,469,475,33,506,507]
[null,"P0AEQ0","_",0.92385,0.97053,32.1,{"v":4e-61,"d":"4.00E-61"},6,2,"glcD","Glycolate oxidase subunit GlcD","_","Complete proteome, FAD, Flavoprotein, Oxidoreductase",12471157,"Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","CFT073 / ATCC 700928 / UPEC",11,468,475,21,470,499]
[null,"P0AEP9","IPMed?",0.92385,0.97053,32.1,{"v":4e-61,"d":"4.00E-61"},6,2,"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",11,468,475,21,470,499]
[null,"Q94AX4","IPMed?",0.83422,0.99579,28.54,{"v":6e-56,"d":"6.00E-56"},7,2,"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",4,469,475,103,560,567]
[null,"P46681","IPMed?",0.82264,0.91789,30.96,{"v":4e-54,"d":"4.00E-54"},8,1,"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",53,468,475,109,528,530]
[null,"P84850","_",0.9028,1.01684,30.64,{"v":2e-53,"d":"2.00E-53"},9,1,"D2hgdh","D-2-hydroxyglutarate dehydrogenase, mitochondrial","1.1.99.-","Complete proteome, FAD, Flavoprotein, Mitochondrion, Oxidoreductase, Reference proteome, Transit peptide",15057822,"Rattus norvegicus","Brown Norway",4,468,475,73,529,535]
[null,"A1L258","_",0.89118,1,29.89,{"v":2e-53,"d":"2.00E-53"},10,1,"d2hgdh","D-2-hydroxyglutarate dehydrogenase, mitochondrial","1.1.99.-","Complete proteome, FAD, Flavoprotein, Mitochondrion, Oxidoreductase, Reference proteome, Transit peptide","_","Danio rerio","_",4,468,475,70,526,533]
[null,"P32891","IPMed?",0.74617,0.92211,30.37,{"v":5E-52,"d":"5.00E-52"},11,1,"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",46,469,475,151,574,587]
[null,"Q8N465","IPMed?",0.91363,1.00211,30.88,{"v":4E-50,"d":"4.00E-50"},12,1,"D2HGDH","D-2-hydroxyglutarate dehydrogenase, mitochondrial","1.1.99.-","Alternative splicing, Complete proteome, Disease mutation, FAD, Flavoprotein, Mitochondrion, Oxidoreductase, Polymorphism, Reference proteome, Transit peptide","14702039, 15815621, 15489334, 15070399, 15609246, 16037974, 16081310, 16442322","Homo sapiens","_",4,468,475,59,515,521]
[null,"O23240","IPMed?",0.75313,0.88632,31.12,{"v":2e-48,"d":"2.00E-48"},13,1,"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",53,469,475,141,551,559]
[null,"Q12627","IPMed?",0.75694,0.91789,28.67,{"v":3e-47,"d":"3.00E-47"},14,1,"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",46,469,475,144,566,576]
[]
["CLOSTRIBL6_v1_2270","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P49851","IPMed?",0.91279,0.98742,36.94,{"v":2e-23,"d":"2.00E-23"},1,1,"ykhA","Uncharacterized acyl-CoA thioester hydrolase YkhA","3.1.2.-","Complete proteome, Hydrolase, Reference proteome","8682784, 9384377, 10568751","Bacillus subtilis (strain 168)","168 / 168",1,151,159,1,157,172]
[null,"Q91V12","IPMed?",0.39633,0.94969,34.44,{"v":1e-17,"d":"1.00E-17"},2,1,"Acot7","Cytosolic acyl coenzyme A thioester hydrolase","3.1.2.2","3D-structure, Acetylation, Alternative splicing, Complete proteome, Cytoplasm, Direct protein sequencing, Fatty acid metabolism, Hydrolase, Lipid metabolism, Reference proteome, Repeat, Serine esterase","12435388, 11834298, 15288813, 16141072, 19468303, 15489334, 14729242, 21183079, 17563367","Mus musculus","ICR / ICR / ICR / C57BL/6J / C57BL/6J",9,155,159,224,373,381]
[null,"Q64559","IPMed?",0.39633,0.94969,34.44,{"v":1e-17,"d":"1.00E-17"},2,1,"Acot7","Cytosolic acyl coenzyme A thioester hydrolase","3.1.2.2","Acetylation, Alternative splicing, Complete proteome, Cytoplasm, Direct protein sequencing, Fatty acid metabolism, Hydrolase, Lipid metabolism, Reference proteome, Repeat, Serine esterase","8631842, 9125130, 9163348, 15489334, 7906114, 22673903, 11755680","Rattus norvegicus","Sprague-Dawley",9,155,159,224,373,381]
[null,"O84540","_",0.91875,0.92453,32.65,{"v":1e-16,"d":"1.00E-16"},3,1,"_","Uncharacterized acyl-CoA thioester hydrolase CT_535","3.1.2.-","Complete proteome, Hydrolase, Reference proteome",9784136,"Chlamydia trachomatis (strain D/UW-3/Cx)","D/UW-3/Cx",7,151,159,11,157,160]
[null,"Q9Z7Q0","_",0.92453,0.94839,31.97,{"v":2E-16,"d":"2.00E-16"},4,1,"_","Uncharacterized acyl-CoA thioester hydrolase CPn_0654/CP_0093/CPj0654/CpB0680","3.1.2.-","Complete proteome, Hydrolase","10192388, 10684935, 10871362","Chlamydia pneumoniae","CWL029 / AR39 / J138",7,151,159,5,151,155]
[null,"O00154","IPMed?",0.39737,0.94969,33.11,{"v":7e-16,"d":"7.00E-16"},5,1,"ACOT7","Cytosolic acyl coenzyme A thioester hydrolase","3.1.2.2","3D-structure, Acetylation, Alternative splicing, Complete proteome, Cytoplasm, Direct protein sequencing, Fatty acid metabolism, Hydrolase, Lipid metabolism, Mitochondrion, Reference proteome, Repeat, Serine esterase","10578051, 12435388, 14702039, 16710414, 15489334, 19608861, 21269460","Homo sapiens","_",9,155,159,223,372,380]
[null,"Q8VHQ9","IPMed?",0.24579,0.91824,27.4,3e-15,6,1,"Acot11","Acyl-coenzyme A thioesterase 11","3.1.2.-","Complete proteome, Cytoplasm, Fatty acid metabolism, Hydrolase, Lipid metabolism, Mitochondrion, Phosphoprotein, Reference proteome, Repeat, Serine esterase, Transit peptide","11696000, 15489334, 21183079","Mus musculus","FVB/N / FVB/N",12,155,159,219,364,594]
[null,"Q9PJK7","_",0.92453,0.92453,30.61,3e-15,7,1,"_","Uncharacterized acyl-CoA thioester hydrolase TC_0822","3.1.2.-","Complete proteome, Hydrolase",10684935,"Chlamydia muridarum (strain MoPn / Nigg)","MoPn / Nigg",7,151,159,10,156,159]
[null,"Q8WYK0","IPMed?",0.25586,0.89308,28.87,1E-14,8,1,"ACOT12","Acetyl-coenzyme A thioesterase","3.1.2.1","3D-structure, Alternative splicing, Complete proteome, Cytoplasm, Fatty acid metabolism, Hydrolase, Lipid metabolism, Polymorphism, Reference proteome, Repeat, Serine esterase","16951743, 14702039, 15372022, 15489334, 24275569, 21248752","Homo sapiens","_",13,153,159,8,149,555]
[null,"Q9DBK0","IPMed?",0.26259,0.91824,26.03,1E-13,9,1,"Acot12","Acetyl-coenzyme A thioesterase","3.1.2.1","Complete proteome, Cytoplasm, Fatty acid metabolism, Hydrolase, Lipid metabolism, Reference proteome, Repeat, Serine esterase","12545200, 16141072, 15489334, 21183079, 23806337","Mus musculus","C57BL/6J / C57BL/6J",9,153,159,5,150,556]
[null,"O66120","IPMed?",0.7044,0.75168,33.04,2e-13,10,1,"_","Uncharacterized acyl-CoA thioester hydrolase ZMO0511","3.1.2.-","Complete proteome, Hydrolase, Reference proteome","9515924, 15592456","Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)","ATCC 29191 / DSM 3580 / NBRC 13756 / NCIMB 11199 / NRRL B-4490 / ZM6 / ATCC 31821 / ZM4 / CP4",19,128,159,25,135,149]
[null,"Q99NB7","IPMed?",0.26259,0.91824,25.34,5e-13,11,1,"Acot12","Acetyl-coenzyme A thioesterase","3.1.2.1","Allosteric enzyme, Complete proteome, Cytoplasm, Direct protein sequencing, Fatty acid metabolism, Hydrolase, Lipid metabolism, Reference proteome, Repeat, Serine esterase","11322891, 6136404","Rattus norvegicus","Donryu",9,153,159,5,150,556]
[null,"P0A0Q7","IPMed?",0.77586,0.84906,31.85,7e-13,12,1,"vdlD","Protein VdlD","_","Complete proteome, Hydrolase, Reference proteome","9139899, 9252185","Helicobacter pylori (strain ATCC 700392 / 26695)","ATCC 49503 / 60190 / ATCC 700392 / 26695",19,151,159,29,161,174]
[null,"Q8WXI4","IPMed?",0.24053,0.91824,26.03,9E-13,13,1,"ACOT11","Acyl-coenzyme A thioesterase 11","3.1.2.-","3D-structure, Alternative splicing, Complete proteome, Cytoplasm, Fatty acid metabolism, Hydrolase, Lipid metabolism, Mitochondrion, Phosphoprotein, Polymorphism, Reference proteome, Repeat, Serine esterase, Transit peptide","11696000, 9734811, 14702039, 16710414, 15489334, 22897136, 21738568","Homo sapiens","_",12,155,159,218,363,607]
[]
["CLOSTRIBL6_v1_2820","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","_",0.99091,0.99695,43.12,{"v":4e-77,"d":"4.00E-77"},1,3,"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)","_",6,326,328,5,330,330]
[null,"P53578","IPMed?",0.95509,0.97256,42.32,{"v":2e-68,"d":"2.00E-68"},2,3,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Transport",7875566,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",6,319,328,7,324,334]
[null,"H6LGM8","IPMed?",0.83081,1.00305,41.03,{"v":3E-68,"d":"3.00E-68"},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",6,322,328,69,391,396]
[null,"P52039","IPMed?",0.99702,1.02134,40.3,{"v":3E-68,"d":"3.00E-68"},4,3,"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",6,325,328,7,334,336]
[null,"O85692","IPMed?",0.97633,1.0061,43.03,{"v":6e-67,"d":"6.00E-67"},5,3,"etfA","Electron transfer flavoprotein subunit alpha","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",6,326,328,7,335,338]
[null,"Q53209","_",0.87534,0.98476,36.53,{"v":2e-58,"d":"2.00E-58"},6,3,"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",8,318,328,32,351,369]
[null,"P26483","IPMed?",0.90515,1.01829,35.63,{"v":3e-58,"d":"3.00E-58"},7,3,"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)","_",3,324,328,27,357,369]
[null,"P09819","IPMed?",0.92351,0.9939,36.5,{"v":4E-55,"d":"4.00E-55"},8,3,"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",6,318,328,13,335,353]
[null,"P10449","IPMed?",0.89702,1.00915,35.35,{"v":6e-53,"d":"6.00E-53"},9,3,"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",6,324,328,30,357,369]
[null,"P94551","_",0.96646,0.97538,36.28,{"v":5E-52,"d":"5.00E-52"},10,3,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8969504, 9384377","Bacillus subtilis (strain 168)","168 / 168",4,318,328,1,314,325]
[null,"G3KIM6","IPMed?",0.97275,1.08841,36.69,{"v":7e-49,"d":"7.00E-49"},11,3,"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",6,326,328,12,365,367]
[null,"Q0AZ33","IPMed?",0.98171,1.01577,34.47,{"v":1e-47,"d":"1.00E-47"},12,3,"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",7,322,328,3,315,317]
[null,"Q9C6I6","IPMed?",0.90909,1.0061,31.52,{"v":4E-41,"d":"4.00E-41"},13,3,"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",9,326,328,38,363,363]
[]
["CLOSTRIBL6_v1_2821","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O85691","IPMed?",1.01111,1.02632,39.56,{"v":5E-56,"d":"5.00E-56"},1,3,"etfB","Electron transfer flavoprotein subunit beta","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,266,266,1,270,270]
[null,"P52040","IPMed?",0.86466,0.88803,44.35,{"v":2e-53,"d":"2.00E-53"},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",1,230,266,1,225,259]
[null,"P97089","_",1.00376,1.02692,37.83,{"v":1E-46,"d":"1.00E-46"},3,3,"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)","_",1,266,266,1,260,260]
[null,"H6LGM7","IPMed?",1,1.01527,36.09,{"v":3e-46,"d":"3.00E-46"},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",1,266,266,1,262,262]
[null,"G3KIM7","IPMed?",0.89888,0.90226,37.5,{"v":1E-41,"d":"1.00E-41"},5,3,"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",1,235,266,1,238,267]
[null,"P53577","IPMed?",0.92708,1.00376,35.96,{"v":3e-41,"d":"3.00E-41"},6,3,"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",1,260,266,1,262,288]
[null,"P53576","_",0.92527,0.97744,35.38,{"v":8E-41,"d":"8.00E-41"},7,3,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",1,250,266,1,253,281]
[null,"P26482","IPMed?",0.97865,1.03383,35.27,{"v":2e-40,"d":"2.00E-40"},8,3,"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)","_",1,264,266,1,267,281]
[null,"Q53210","_",0.84561,0.90602,36.51,{"v":2e-37,"d":"2.00E-37"},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",1,234,266,1,238,285]
[null,"P09818","IPMed?",0.92808,1.0188,34.69,{"v":2e-34,"d":"2.00E-34"},10,3,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104, 6317191","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",1,260,266,1,266,292]
[null,"Q05559","IPMed?",0.88172,0.92481,34.55,{"v":2e-32,"d":"2.00E-32"},11,3,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport",8369342,"Rhizobium leguminosarum bv. phaseoli","_",1,235,266,1,237,279]
[null,"P64098","IPMed?",0.96241,0.96241,34.77,{"v":5e-31,"d":"5.00E-31"},12,3,"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",2,252,266,3,253,266]
[null,"P60566","IPMed?",0.81203,0.84375,32.41,{"v":6e-30,"d":"6.00E-30"},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",1,209,266,1,215,256]
[]
["CLOSTRIBL6_v1_0258","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P07598","IPMed?",0.69739,0.95249,25.69,{"v":9e-21,"d":"9.00E-21"},1,4,"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",5,328,575,28,418,421]
[null,"P29166","IPMed?",0.64174,0.64286,24.39,{"v":6e-18,"d":"6.00E-18"},2,4,"_","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",5,298,575,140,506,574]
[null,"P13629","IPMed?",0.68174,0.93112,26.02,3e-15,3,4,"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)","_",5,328,575,28,418,421]
[null,"Q46508","IPMed?",0.5641,0.57391,24.55,1e-12,4,4,"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","_",33,298,575,188,517,585]
[null,"Q57661","IPMed?",0.08522,0.19919,44.9,3e-07,5,1,"dmrX","Dihydromethanopterin reductase (acceptor)","1.5.99.15","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","8688087, 23995635","Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440",7,55,575,154,202,246]
[null,"Q57934","_",0.0887,0.204,39.22,2e-06,6,6,"_","Uncharacterized polyferredoxin-like protein MJ0514","_","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",5,55,575,193,243,250]
[null,"P81292","_",0.09739,0.34356,41.07,3e-06,7,6,"_","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",2,55,575,31,84,163]
[null,"P00196","IPMed?",0.07826,0.81818,44.44,1e-05,8,2,"_","Ferredoxin","_","4Fe-4S, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",5227671,"Clostridium butyricum","_",11,55,575,7,51,55]
[null,"C5BDE6","_",0.08174,0.24607,42.55,2e-05,9,1,"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","_","Edwardsiella ictaluri (strain 93-146)","_",7,52,575,111,157,191]
[null,"P22846","_",0.07652,0.78571,45.45,2e-05,10,2,"fer","Ferredoxin","_","4Fe-4S, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport",11792842,"Clostridium perfringens (strain 13 / Type A)","13 / Type A",12,55,575,9,52,56]
[null,"Q01700","IPMed?",0.09739,0.96552,35.71,3e-05,11,2,"_","Probable ferredoxin","_","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",1379583,"Methanosarcina thermophila","ATCC 43570 / DSM 1825 / OCM 12 / TM-1",4,58,575,2,57,58]
[null,"Q00388","IPMed?",0.12348,0.17839,38.03,5e-05,12,5,"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",2,71,575,123,192,398]
[null,"P00195","IPMed?",0.07826,0.80357,42.22,7e-05,13,3,"_","Ferredoxin","_","3D-structure, 4Fe-4S, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport","3856844, 5335811, 7556151","Clostridium pasteurianum","_",11,55,575,8,52,56]
[null,"H6LGM8","IPMed?",0.0887,0.12879,39.22,1E-4,14,7,"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",5,55,575,3,52,396]
[]
["CLOSTRIBL6_v1_0260","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?",0.75261,0.9172,25.23,{"v":1E-26,"d":"1.00E-26"},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",75,440,471,90,508,574]
[null,"P07598","IPMed?",0.81316,0.90974,26.89,{"v":8e-25,"d":"8.00E-25"},2,3,"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",119,440,471,26,387,421]
[null,"P13629","IPMed?",0.80467,0.90024,27.18,{"v":2e-24,"d":"2.00E-24"},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)","_",123,440,471,30,387,421]
[null,"Q46508","IPMed?",0.55556,0.69002,28.31,{"v":6e-23,"d":"6.00E-23"},4,2,"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","_",174,440,471,196,519,585]
[null,"Q58593","_",0.26752,0.3198,31.75,6e-13,5,1,"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",87,189,471,132,255,394]
[null,"Q00388","IPMed?",0.34395,0.40704,29.63,1e-11,6,1,"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",50,189,471,91,244,398]
[null,"Q6GP25","_",0.72824,0.75219,22.74,3E-9,7,1,"narf","Nuclear prelamin A recognition factor","_","Nucleus","_","Xenopus laevis","_",166,440,471,43,383,456]
[null,"P81292","_",0.20594,0.59509,35.05,3E-9,8,2,"_","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",95,189,471,37,131,163]
[null,"A8PGQ3","_",0.75796,0.79688,22.41,6E-9,9,1,"_","Probable cytosolic Fe-S cluster assembly factor Bm1_25010","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome",17885136,"Brugia malayi","_",155,455,471,47,394,448]
[null,"P60232","IPMed?",0.22718,0.25971,33.64,1E-8,10,1,"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",89,193,471,139,235,412]
[null,"Q49180","IPMed?",0.22718,0.25971,33.64,3e-08,11,2,"mvhB","Polyferredoxin protein MvhB","_","4Fe-4S, Iron, Iron-sulfur, Metal-binding, Repeat",2115877,"Methanothermus fervidus","_",91,195,471,141,237,412]
[null,"Q9UHQ1","IPMed?",0.77495,0.80044,21.64,6e-08,12,1,"NARF","Nuclear prelamin A recognition factor","_","Alternative splicing, Complete proteome, Nucleus, Phosphoprotein, Reference proteome","10514485, 14702039, 16625196, 15489334, 23186163","Homo sapiens","_",167,465,471,46,408,456]
[null,"H6LC27","IPMed?",0.25478,0.36036,31.67,1e-07,13,3,"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",73,189,471,191,294,333]
[null,"P0AAL6","IPMed?",0.21231,0.48077,29,3e-07,14,2,"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",92,189,471,118,198,208]
[]
["CLOSTRIBL6_v1_1906","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P07598","IPMed?",0.89885,0.92874,28.13,{"v":5e-28,"d":"5.00E-28"},1,1,"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",46,383,435,6,392,421]
[null,"P13629","IPMed?",0.90575,0.93587,27.66,{"v":8e-24,"d":"8.00E-24"},2,3,"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)","_",42,383,435,5,392,421]
[null,"P29166","IPMed?",0.60453,0.7977,25.36,{"v":4e-21,"d":"4.00E-21"},3,3,"_","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",104,400,435,186,531,574]
[null,"Q46508","IPMed?",0.62906,0.84598,23.91,{"v":8e-19,"d":"8.00E-19"},4,3,"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","_",108,415,435,196,561,585]
[null,"Q9UHQ1","IPMed?",0.74561,0.78161,23.53,7e-08,5,2,"NARF","Nuclear prelamin A recognition factor","_","Alternative splicing, Complete proteome, Nucleus, Phosphoprotein, Reference proteome","10514485, 14702039, 16625196, 15489334, 23186163","Homo sapiens","_",97,377,435,42,381,456]
[null,"Q9Y7N7","_",0.49442,0.61149,23.68,2e-07,6,1,"_","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",99,300,435,55,319,538]
[null,"Q94CL6","IPMed?",0.50844,0.55402,24.9,2e-06,7,1,"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",101,303,435,54,291,474]
[null,"B6K2N0","_",0.46796,0.55402,21.16,1E-4,8,1,"_","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",96,300,435,53,293,515]
[null,"H6LC27","IPMed?",0.11724,0.15315,35.29,0.0004,9,9,"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",74,124,435,138,188,333]
[null,"Q0UM75","_",0.21044,0.30575,26.32,2E-3,10,1,"NAR1","Cytosolic Fe-S cluster assembly factor NAR1","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome",18024570,"Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173)","SN15 / ATCC MYA-4574 / FGSC 10173",198,307,435,227,359,632]
[null,"Q9N392","IPMed?",0.74836,0.78621,22.22,0.062,11,3,"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",91,377,435,54,387,457]
[null,"P33389","IPMed?",0.17701,0.20811,32.47,0.074,12,1,"_","Protein DVU_0535","_","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Transmembrane, Transmembrane helix, Transport","8335628, 15077118","Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)","Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303",43,118,435,78,152,370]
[null,"P62856","IPMed?",0.12874,0.48696,37.5,0.088,13,1,"Rps26","40S ribosomal protein S26","_","Complete proteome, Cytoplasm, Endoplasmic reticulum, Phosphoprotein, Reference proteome, Ribonucleoprotein, Ribosomal protein","2993263, 15489334","Rattus norvegicus","_",95,149,435,10,65,115]
[null,"P30742","IPMed?",0.12874,0.48696,37.5,0.088,13,1,"RPS26","40S ribosomal protein S26","_","Cytoplasm, Endoplasmic reticulum, Phosphoprotein, Ribonucleoprotein, Ribosomal protein",8464749,"Cricetus cricetus","_",95,149,435,10,65,115]
[null,"P62854","IPMed?",0.12874,0.48696,37.5,0.088,13,1,"RPS26","40S ribosomal protein S26","_","3D-structure, Complete proteome, Cytoplasm, Diamond-Blackfan anemia, Direct protein sequencing, Disease mutation, Endoplasmic reticulum, Phosphoprotein, Reference proteome, Ribonucleoprotein, Ribosomal protein","8464749, 7945460, 9602156, 15489334, 8706699, 19608861, 21269460, 23186163, 24524803, 24275569, 25944712, 23636399, 25957688, 25901680, 20116044, 24942156","Homo sapiens","_",95,149,435,10,65,115]
[]
["CLOSTRIBL6_v1_2017","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?",0.64634,0.77131,29.11,{"v":2e-33,"d":"2.00E-33"},1,1,"_","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",124,438,481,142,508,574]
[null,"P07598","IPMed?",0.842,0.962,28.89,{"v":9e-27,"d":"9.00E-27"},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",124,460,481,30,412,421]
[null,"P13629","IPMed?",0.83784,0.95724,28.54,{"v":2e-26,"d":"2.00E-26"},3,1,"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)","_",124,463,481,30,404,421]
[null,"Q46508","IPMed?",0.69231,0.842,27.16,{"v":1e-24,"d":"1.00E-24"},4,1,"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","_",125,458,481,149,541,585]
[null,"H6LC27","IPMed?",0.3264,0.47147,32.48,4e-13,5,1,"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",64,193,481,174,328,333]
[null,"P81292","_",0.29106,0.8589,33.57,6e-12,6,1,"_","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",91,214,481,22,159,163]
[null,"Q9N392","IPMed?",0.69439,0.73085,22.46,1e-09,7,1,"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",163,440,481,59,391,457]
[null,"P20925","IPMed?",0.23909,0.73248,32.17,8e-09,8,1,"_","Frd operon probable iron-sulfur subunit A","_","4Fe-4S, Iron, Iron-sulfur, Metal-binding, Repeat",3308458,"Proteus vulgaris","_",98,204,481,34,144,157]
[null,"Q00388","IPMed?",0.2973,0.3593,29.37,1E-8,9,2,"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",88,224,481,122,253,398]
[null,"P44101","_",0.24532,0.71084,35.59,2E-8,10,1,"_","Uncharacterized protein HI_1043","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",98,191,481,53,164,166]
[null,"Q49180","IPMed?",0.26195,0.30583,30.16,4e-08,11,3,"mvhB","Polyferredoxin protein MvhB","_","4Fe-4S, Iron, Iron-sulfur, Metal-binding, Repeat",2115877,"Methanothermus fervidus","_",106,224,481,152,269,412]
[null,"Q50784","IPMed?",0.26403,0.30825,31.5,7e-08,12,2,"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",106,224,481,152,270,412]
[]
["CLOSTRIBL6_v1_2260","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q9WYB1","IPMed?",0.99752,1.00249,59.95,{"v":7e-169,"d":"7.00E-169"},1,1,"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",1,401,401,1,401,403]
[null,"A5IKE7","_",0.99752,1.00249,58.96,{"v":4E-165,"d":"4.00E-165"},2,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase","_","Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)","_",1,401,401,1,401,403]
[null,"B1L9M9","_",0.99752,1.00249,58.71,{"v":1e-164,"d":"1.00E-164"},3,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase","_","Thermotoga sp. (strain RQ2)","_",1,401,401,1,401,403]
[null,"Q8R9V4","_",1.00499,1.00499,58.06,{"v":5e-161,"d":"5.00E-161"},4,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, 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",1,401,401,1,400,401]
[null,"B0K9Y6","_",1.00499,1.00499,57.07,{"v":1e-159,"d":"1.00E-159"},5,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","_","Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E)","_",1,401,401,1,400,401]
[null,"B8FRT2","_",0.99501,1,54.89,{"v":3E-158,"d":"3.00E-158"},6,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase",22316246,"Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)","DCB-2 / DSM 10664",1,399,401,1,397,399]
[null,"Q24U35","_",0.99501,1,54.89,{"v":5e-158,"d":"5.00E-158"},7,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase",16513756,"Desulfitobacterium hafniense (strain Y51)","Y51",1,399,401,1,397,399]
[null,"Q59331","_",1.00249,1.005,56.72,{"v":4e-157,"d":"4.00E-157"},8,1,"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)","_",1,401,401,1,399,400]
[null,"B8CWV8","_",0.99751,1.00503,55.25,{"v":5e-157,"d":"5.00E-157"},9,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase",19145256,"Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562)","H 168 / OCM 544 / DSM 9562",1,400,401,1,398,398]
[null,"Q3AC47","_",0.99501,1.00251,57.64,{"v":8e-157,"d":"8.00E-157"},10,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase",16311624,"Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)","ATCC BAA-161 / DSM 6008 / Z-2901",1,398,401,1,395,398]
[null,"P38502","IPMed?",0.97794,0.99501,53.38,{"v":1e-151,"d":"1.00E-151"},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",1,399,401,1,397,408]
[null,"P71104","IPMed?",1.01247,1.01247,52.46,{"v":2e-148,"d":"2.00E-148"},12,1,"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",1,401,401,1,400,401]
[null,"P37877","IPMed?",0.97756,0.99241,51.79,{"v":3e-138,"d":"3.00E-138"},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",2,393,401,3,389,395]
[null,"P74879","IPMed?",0.9802,0.98753,45.96,{"v":9e-114,"d":"9.00E-114"},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",2,397,401,4,392,404]
[null,"Q9X4M1","IPMed?",0.97756,0.99492,45.15,{"v":5e-111,"d":"5.00E-111"},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",2,393,401,3,389,394]
[null,"P77845","IPMed?",0.98005,0.98992,41.98,{"v":1e-98,"d":"1.00E-98"},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",4,392,401,5,391,397]
[null,"Q49113","IPMed?",0.99252,1.01272,39.45,{"v":8e-96,"d":"8.00E-96"},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)","_",3,399,401,2,393,393]
[null,"P0A6A3","IPMed?",0.99751,1,41,{"v":1e-94,"d":"1.00E-94"},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",3,397,401,6,398,400]
[null,"P63411","IPMed?",0.99751,1,40.5,{"v":6e-94,"d":"6.00E-94"},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",3,397,401,6,398,400]
[]
["CLOSTRIBL6_v1_1872","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P39646","_",0.94737,0.94737,54.9,{"v":1e-111,"d":"1.00E-111"},1,1,"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",15,320,323,18,319,323]
[null,"Q8CQ62","_",0.94529,0.96285,51.45,{"v":2e-98,"d":"2.00E-98"},2,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",12950922,"Staphylococcus epidermidis (strain ATCC 12228)","ATCC 12228",15,320,323,18,324,329]
[null,"Q5HRF7","_",0.94529,0.96285,50.8,{"v":5e-97,"d":"5.00E-97"},3,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",15774886,"Staphylococcus epidermidis (strain ATCC 35984 / RP62A)","ATCC 35984 / RP62A",15,320,323,18,324,329]
[null,"Q5HI88","_",0.94512,0.95975,49.35,{"v":7E-94,"d":"7.00E-94"},4,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",15774886,"Staphylococcus aureus (strain COL)","COL",15,320,323,18,323,328]
[null,"P99092","_",0.94512,0.95975,49.35,{"v":7E-94,"d":"7.00E-94"},4,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase","11418146, 15590099","Staphylococcus aureus (strain N315)","N315 / N315",15,320,323,18,323,328]
[null,"P65862","_",0.94512,0.95975,49.35,{"v":7E-94,"d":"7.00E-94"},4,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",11418146,"Staphylococcus aureus (strain Mu50 / ATCC 700699)","Mu50 / ATCC 700699",15,320,323,18,323,328]
[null,"Q6GJ80","_",0.94512,0.95975,49.03,{"v":2e-93,"d":"2.00E-93"},5,1,"pta","Phosphate acetyltransferase","2.3.1.8","3D-structure, Acyltransferase, Cytoplasm, Transferase",15213324,"Staphylococcus aureus (strain MRSA252)","MRSA252",15,320,323,18,323,328]
[null,"Q6GBP8","_",0.94512,0.95975,49.03,{"v":8e-93,"d":"8.00E-93"},6,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Cytoplasm, Transferase",15213324,"Staphylococcus aureus (strain MSSA476)","MSSA476",15,320,323,18,323,328]
[null,"Q8NXW4","_",0.94512,0.95975,49.03,{"v":8e-93,"d":"8.00E-93"},6,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",12044378,"Staphylococcus aureus (strain MW2)","MW2",15,320,323,18,323,328]
[null,"Q59330","_",0.9878,1.0031,48.15,{"v":2E-92,"d":"2.00E-92"},7,1,"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)","_",1,320,323,3,324,328]
[null,"O52593","_",0.98795,1.01548,44.21,{"v":2e-83,"d":"2.00E-83"},8,1,"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)","_",3,320,323,5,324,332]
[null,"P77844","IPMed?",0.97872,0.9969,44.41,{"v":2e-82,"d":"2.00E-82"},9,1,"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",1,320,323,5,322,329]
[null,"P71103","IPMed?",0.96997,1,41.49,{"v":3e-77,"d":"3.00E-77"},10,1,"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",1,319,323,3,325,333]
[null,"P0A9M8","IPMed?",0.43838,0.96904,42.49,{"v":3e-71,"d":"3.00E-71"},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",10,320,323,402,707,714]
[null,"Q8ZND6","IPMed?",0.43838,0.96904,42.49,{"v":4e-71,"d":"4.00E-71"},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",10,320,323,401,706,714]
[null,"Q9I5A5","IPMed?",0.4446,0.96904,43.13,{"v":2e-69,"d":"2.00E-69"},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",10,320,323,390,695,704]
[null,"P38503","IPMed?",0.96396,0.99381,40.19,{"v":1e-68,"d":"1.00E-68"},15,1,"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",3,319,323,6,324,333]
[null,"Q49112","IPMed?",0.96904,0.97205,41.53,{"v":1e-68,"d":"1.00E-68"},14,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",8844861,"Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)","_",9,319,323,13,317,322]
[null,"P41790","IPMed?",0.91124,0.95356,38.31,{"v":2e-62,"d":"2.00E-62"},16,1,"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",15,320,323,16,320,338]
[null,"P39197","IPMed?",0.97833,0.99371,39.56,{"v":5e-61,"d":"5.00E-61"},17,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Cytoplasm, Transferase",7480167,"Paracoccus denitrificans","_",10,320,323,12,314,318]
[null,"O30807","IPMed?",0.41169,0.98142,27.44,{"v":3e-31,"d":"3.00E-31"},18,2,"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",7,318,323,449,761,770]
[]
["CLOSTRIBL6_v1_0095","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?",0.98481,1.00517,32.65,{"v":3e-62,"d":"3.00E-62"},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",2,387,387,1,385,395]
[null,"A6ZTT5","_",0.92506,0.93717,31.56,{"v":8e-50,"d":"8.00E-50"},2,5,"ADH4","Alcohol dehydrogenase 4","1.1.1.1","Complete proteome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Zinc",17652520,"Saccharomyces cerevisiae (strain YJM789)","YJM789",9,361,387,9,355,382]
[null,"P10127","IPMed?",0.92506,0.93717,31.28,{"v":9e-49,"d":"9.00E-49"},3,5,"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",9,361,387,9,355,382]
[null,"P31005","IPMed?",0.97416,0.9895,28.38,{"v":3e-47,"d":"3.00E-47"},4,6,"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",6,382,387,3,376,381]
[null,"P71017","IPMed?",0.9602,0.99742,30.05,{"v":9E-46,"d":"9.00E-46"},5,4,"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",5,387,387,14,395,402]
[null,"Q09669","IPMed?",0.82938,0.90439,29.71,{"v":5e-45,"d":"5.00E-45"},6,6,"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",16,362,387,58,398,422]
[null,"P0DJA2","IPMed?",0.96899,0.97911,28,{"v":5e-45,"d":"5.00E-45"},7,6,"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",16,387,387,15,383,383]
[null,"P76553","_",0.92152,0.94057,28.3,{"v":2e-44,"d":"2.00E-44"},8,5,"eutG","Ethanolamine utilization protein EutG","1.1.-.-","Complete proteome, NAD, 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",9,372,387,26,380,395]
[null,"F8DVL8","IPMed?",0.96899,0.97911,27.73,{"v":2e-44,"d":"2.00E-44"},9,6,"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",16,387,387,15,383,383]
[null,"P41795","IPMed?",0.90127,0.9199,30.06,{"v":1e-43,"d":"1.00E-43"},10,5,"eutG","Ethanolamine utilization protein EutG","1.1.-.-","Complete proteome, NAD, Oxidoreductase, Reference proteome","7868611, 10464203, 11677609","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","ATCC 14028s / SGSG 2262 / LT2 / LT2 / SGSC1412 / ATCC 700720",28,383,387,45,391,395]
[null,"P0A9S1","IPMed?",0.96899,0.98168,29.87,{"v":2e-42,"d":"2.00E-42"},11,5,"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",16,383,387,14,378,382]
[null,"P45513","IPMed?",0.99742,0.99742,27.72,{"v":3e-41,"d":"3.00E-41"},12,6,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","Iron, NAD, Oxidoreductase",7721705,"Citrobacter freundii","ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK",5,387,387,6,387,387]
[]
["CLOSTRIBL6_v1_1804","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P45513","IPMed?",0.94359,0.9509,35.33,{"v":3E-52,"d":"3.00E-52"},1,4,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","Iron, NAD, Oxidoreductase",7721705,"Citrobacter freundii","ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK",3,361,390,5,361,387]
[null,"Q59477","_",0.94359,0.9509,34.24,{"v":4E-52,"d":"4.00E-52"},2,5,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","3D-structure, Iron, NAD, Oxidoreductase","_","Klebsiella pneumoniae","_",3,361,390,5,361,387]
[null,"Q09669","IPMed?",0.67062,0.72564,39.58,{"v":3e-50,"d":"3.00E-50"},3,5,"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",6,284,390,49,321,422]
[null,"A6ZTT5","_",0.99231,1.01309,31.52,{"v":9e-49,"d":"9.00E-49"},5,6,"ADH4","Alcohol dehydrogenase 4","1.1.1.1","Complete proteome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Zinc",17652520,"Saccharomyces cerevisiae (strain YJM789)","YJM789",6,389,390,7,380,382]
[null,"P31005","IPMed?",1.01538,1.03937,31.57,{"v":9e-49,"d":"9.00E-49"},4,5,"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",5,388,390,3,380,381]
[null,"P10127","IPMed?",0.99231,1.01309,31.27,{"v":9e-48,"d":"9.00E-48"},6,6,"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",6,389,390,7,380,382]
[null,"P0DJA2","IPMed?",0.94615,0.96345,33.33,{"v":2E-45,"d":"2.00E-45"},7,5,"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",6,368,390,6,364,383]
[null,"F8DVL8","IPMed?",0.94615,0.96345,33.33,{"v":2E-45,"d":"2.00E-45"},7,5,"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",6,368,390,6,364,383]
[null,"O05239","_",1.02051,1.02842,29.65,{"v":3e-44,"d":"3.00E-44"},8,2,"yugJ","Probable NADH-dependent butanol dehydrogenase 1","1.1.1.-","Complete proteome, NAD, Oxidoreductase, Reference proteome","9274030, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,388,390,1,386,387]
[null,"P37686","IPMed?",0.92051,0.93734,31.2,{"v":7e-43,"d":"7.00E-43"},9,5,"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",6,361,390,6,357,383]
[null,"P71017","IPMed?",0.77363,0.79744,34.73,{"v":2e-42,"d":"2.00E-42"},10,5,"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",8,316,390,18,321,402]
[null,"A4ISB9","IPMed?",1.02051,1.02842,29.65,{"v":7e-41,"d":"7.00E-41"},11,2,"adh2","Long-chain-alcohol dehydrogenase 2","1.1.1.192","Complete proteome, NAD, Oxidoreductase","17372208, 19383697","Geobacillus thermodenitrificans (strain NG80-2)","NG80-2 / NG80-2",1,388,390,1,386,387]
[null,"A4IP64","IPMed?",0.93165,0.94359,31.25,{"v":3e-39,"d":"3.00E-39"},12,6,"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",29,389,390,30,385,395]
[null,"Q04945","IPMed?",0.75897,0.75897,33.11,{"v":3e-35,"d":"3.00E-35"},13,2,"bdhB","NADH-dependent butanol dehydrogenase B","1.1.1.-","Complete proteome, Direct protein sequencing, NAD, Oxidoreductase, Reference proteome","1385386, 11466286, 1809209","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",1,291,390,1,289,390]
[]
["CLOSTRIBL6_v1_2186","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q24803","IPMed?",0.9908,0.99309,54.99,0,1,1,"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",14,866,868,8,867,870]
[null,"P0A9Q7","IPMed?",0.9697,0.99539,50.93,0,2,1,"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",18,868,868,8,865,891]
[null,"P0A9Q8","_",0.9697,0.99539,50.93,0,2,1,"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",18,868,868,8,865,891]
[null,"P33744","IPMed?",0.99424,1.00116,47.05,0,3,1,"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",14,865,868,4,858,862]
[null,"P13604","IPMed?",0.4712,1.05412,44.01,{"v":1e-109,"d":"1.00E-109"},4,2,"adh1","NADPH-dependent butanol dehydrogenase","1.1.1.-","NADP, Oxidoreductase",2673928,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",459,867,868,1,383,388]
[null,"P38947","IPMed?",0.50115,0.96026,38.39,{"v":2e-86,"d":"2.00E-86"},5,1,"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",19,452,868,7,436,453]
[null,"Q0K845","IPMed?",0.52304,0.92089,31.94,{"v":4e-59,"d":"4.00E-59"},6,1,"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",4,452,868,20,469,493]
[null,"P0DJA2","IPMed?",0.4424,1.00261,36.46,{"v":2e-58,"d":"2.00E-58"},7,4,"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",486,865,868,33,383,383]
[null,"F8DVL8","IPMed?",0.4424,1.00261,36.46,{"v":2e-58,"d":"2.00E-58"},7,4,"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",486,865,868,33,383,383]
[null,"P37686","IPMed?",0.44009,0.99739,36.13,{"v":6e-58,"d":"6.00E-58"},8,4,"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",485,861,868,32,379,383]
[null,"Q09669","IPMed?",0.5,1.02844,32.26,{"v":2e-57,"d":"2.00E-57"},9,4,"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",437,864,868,24,421,422]
[null,"P10127","IPMed?",0.45622,1.03665,33.33,{"v":2e-57,"d":"2.00E-57"},10,4,"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",462,849,868,7,364,382]
[null,"A6ZTT5","_",0.45622,1.03665,33.33,{"v":2e-57,"d":"2.00E-57"},10,4,"ADH4","Alcohol dehydrogenase 4","1.1.1.1","Complete proteome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Zinc",17652520,"Saccharomyces cerevisiae (strain YJM789)","YJM789",462,849,868,7,364,382]
[]
["CLOSTRIBL6_v1_2879","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"F8DVL8","IPMed?",0.95939,0.98695,44.97,{"v":6E-103,"d":"6.00E-103"},1,1,"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",9,377,394,6,383,383]
[null,"P0DJA2","IPMed?",0.95939,0.98695,44.71,{"v":4e-102,"d":"4.00E-102"},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",9,377,394,6,383,383]
[null,"P37686","IPMed?",0.95685,0.98433,41.91,{"v":1e-95,"d":"1.00E-95"},3,1,"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",9,376,394,6,382,383]
[null,"P31005","IPMed?",0.95685,0.9895,41.11,{"v":5e-95,"d":"5.00E-95"},4,1,"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",9,376,394,4,380,381]
[null,"Q09669","IPMed?",0.8981,0.96193,43.01,{"v":6e-92,"d":"6.00E-92"},5,1,"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",9,376,394,49,421,422]
[null,"A6ZTT5","_",0.96447,0.99476,42.63,{"v":6e-91,"d":"6.00E-91"},6,1,"ADH4","Alcohol dehydrogenase 4","1.1.1.1","Complete proteome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Zinc",17652520,"Saccharomyces cerevisiae (strain YJM789)","YJM789",9,377,394,7,380,382]
[null,"P10127","IPMed?",0.96447,0.99476,42.37,{"v":6e-90,"d":"6.00E-90"},7,1,"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",9,377,394,7,380,382]
[null,"Q59477","_",0.96954,0.98708,40.31,{"v":2e-88,"d":"2.00E-88"},8,1,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","3D-structure, Iron, NAD, Oxidoreductase","_","Klebsiella pneumoniae","_",7,377,394,6,387,387]
[null,"P45513","IPMed?",0.96954,0.98708,40.84,{"v":7e-88,"d":"7.00E-88"},9,1,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","Iron, NAD, Oxidoreductase",7721705,"Citrobacter freundii","ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK",7,377,394,6,387,387]
[null,"P0A9S1","IPMed?",0.94162,0.9712,38.27,{"v":1e-75,"d":"1.00E-75"},10,2,"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",18,377,394,14,382,382]
[null,"P0A9S2","_",0.94162,0.9712,38.27,{"v":1e-75,"d":"1.00E-75"},10,2,"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",18,377,394,14,382,382]
[null,"P13604","IPMed?",0.98731,1.00258,37.79,{"v":1e-71,"d":"1.00E-71"},11,3,"adh1","NADPH-dependent butanol dehydrogenase","1.1.1.-","NADP, Oxidoreductase",2673928,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",8,379,394,3,383,388]
[null,"P71017","IPMed?",0.91294,0.93147,35.42,{"v":2e-62,"d":"2.00E-62"},12,2,"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",7,361,394,14,379,402]
[]
["CLOSTRIBL6_v1_3434","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q04944","IPMed?",0.99491,1.00514,38.36,{"v":2E-85,"d":"2.00E-85"},1,1,"bdhA","NADH-dependent butanol dehydrogenase A","1.1.1.-","Complete proteome, Direct protein sequencing, NAD, Oxidoreductase, Reference proteome","1385386, 11466286, 1809209","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",1,389,393,1,386,389]
[null,"O05239","_",0.99491,1.01034,36.57,{"v":9e-77,"d":"9.00E-77"},2,1,"yugJ","Probable NADH-dependent butanol dehydrogenase 1","1.1.1.-","Complete proteome, NAD, Oxidoreductase, Reference proteome","9274030, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,389,393,1,384,387]
[null,"O05240","_",1.00254,1.01026,35.53,{"v":1E-73,"d":"1.00E-73"},3,1,"yugK","Probable NADH-dependent butanol dehydrogenase 2","1.1.1.-","Complete proteome, NAD, Oxidoreductase, Reference proteome","9274030, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,389,393,1,387,390]
[null,"Q04945","IPMed?",0.99746,1.00513,35.71,{"v":1e-71,"d":"1.00E-71"},4,1,"bdhB","NADH-dependent butanol dehydrogenase B","1.1.1.-","Complete proteome, Direct protein sequencing, NAD, Oxidoreductase, Reference proteome","1385386, 11466286, 1809209","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",1,389,393,1,387,390]
[null,"Q46856","IPMed?",0.89567,0.90956,36.65,{"v":3e-71,"d":"3.00E-71"},5,1,"yqhD","Alcohol dehydrogenase YqhD","1.1.1.-","3D-structure, Complete proteome, Metal-binding, NADP, Oxidoreductase, Reference proteome, Zinc","9278503, 16738553, 15327949","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",1,350,393,1,348,387]
[null,"A4ISB9","IPMed?",1.00254,1.01809,34.26,{"v":1E-70,"d":"1.00E-70"},6,1,"adh2","Long-chain-alcohol dehydrogenase 2","1.1.1.192","Complete proteome, NAD, Oxidoreductase","17372208, 19383697","Geobacillus thermodenitrificans (strain NG80-2)","NG80-2 / NG80-2",1,389,393,1,384,387]
[null,"Q24857","IPMed?",0.9443,0.94911,30.56,{"v":5e-44,"d":"5.00E-44"},7,1,"ADH3","Alcohol dehydrogenase 3","1.1.1.2","NADP, Oxidoreductase","8705667, 8611619","Entamoeba histolytica","ATCC 30459 / HM-1:IMSS / ATCC 30459 / HM-1:IMSS",1,358,393,3,367,395]
[null,"Q59477","_",0.87023,0.88372,27.78,{"v":2e-29,"d":"2.00E-29"},8,7,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","3D-structure, Iron, NAD, Oxidoreductase","_","Klebsiella pneumoniae","_",14,350,393,16,349,387]
[null,"P71017","IPMed?",0.9801,1.00254,26.65,{"v":3e-27,"d":"3.00E-27"},9,7,"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",1,389,393,10,392,402]
[null,"P45513","IPMed?",0.87023,0.88372,26.9,{"v":2e-26,"d":"2.00E-26"},10,7,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","Iron, NAD, Oxidoreductase",7721705,"Citrobacter freundii","ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK",14,350,393,16,349,387]
[null,"P31005","IPMed?",0.98473,1.01575,26.36,{"v":9e-26,"d":"9.00E-26"},11,7,"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",13,391,393,11,380,381]
[null,"P37686","IPMed?",0.88295,0.90601,25.07,{"v":3E-24,"d":"3.00E-24"},12,7,"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",29,369,393,29,366,383]
[null,"P10127","IPMed?",0.90076,0.9267,23.73,{"v":4e-22,"d":"4.00E-22"},13,7,"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",14,362,393,15,354,382]
[]
["CLOSTRIBL6_v1_1351","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q9I6M5","IPMed?",0.9591,0.97101,39.02,{"v":1E-97,"d":"1.00E-97"},1,1,"davD","Glutarate-semialdehyde dehydrogenase","1.2.1.-","Complete proteome, NADP, Oxidoreductase, Reference proteome","10984043, 17388807","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 / ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1",20,482,489,14,476,483]
[null,"E1V7V8","_",0.96146,0.96933,36.71,{"v":7e-96,"d":"7.00E-96"},2,1,"doeC","Aspartate-semialdehyde dehydrogenase (Non-phosphorylating)","1.2.1.-","Complete proteome, Cytoplasm, NAD, NADP, Oxidoreductase, Reference proteome",20849449,"Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)","ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9",20,483,489,18,485,493]
[null,"P25526","IPMed?",0.96933,0.9834,37.13,{"v":2e-94,"d":"2.00E-94"},4,1,"gabD","Succinate-semialdehyde dehydrogenase [NADP(+)] GabD","1.2.1.79","3D-structure, Complete proteome, NADP, Oxidoreductase, Reference proteome","8297211, 9205837, 9278503, 16738553, 7011797, 14731280, 30498244, 20174634","Escherichia coli (strain K12)","K12 / JM103 / ATCC 39403 / DSM 2829 / NCIMB 12044 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / BW25113 / K12",21,488,489,15,482,482]
[null,"Q88RC0","IPMed?",0.9591,0.97708,37.31,{"v":2e-94,"d":"2.00E-94"},3,1,"davD","Glutarate-semialdehyde dehydrogenase","1.2.1.-","Complete proteome, NADP, Oxidoreductase, Reference proteome","12534463, 11679348","Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)","ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440 / ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440",20,482,489,14,474,480]
[null,"B9F3B6","_",0.86338,0.93047,35.82,{"v":1e-93,"d":"1.00E-93"},5,1,"ALDH5F1","Succinate-semialdehyde dehydrogenase, mitochondrial","1.2.1.24","Complete proteome, Disulfide bond, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide","16100779, 18089549, 24280374, 15685292","Oryza sativa subsp. japonica","cv. Nipponbare / cv. Nipponbare / cv. Nipponbare / cv. Nipponbare",30,482,489,68,519,527]
[null,"P55653","_",0.93686,0.9407,38.91,{"v":9e-92,"d":"9.00E-92"},6,1,"gabD","Probable succinate-semialdehyde dehydrogenase [NADP(+)]","1.2.1.79","Complete proteome, NADP, Oxidoreductase, Plasmid","9163424, 19376903","Sinorhizobium fredii (strain NBRC 101917 / NGR234)","NBRC 101917 / NGR234 / NBRC 101917 / NGR234",26,482,489,28,484,491]
[null,"P94428","IPMed?",0.93865,0.99351,36.38,{"v":2E-90,"d":"2.00E-90"},7,1,"gabD","Succinate-semialdehyde dehydrogenase [NADP(+)]","1.2.1.79","Complete proteome, NADP, Oxidoreductase, Reference proteome","8969502, 9384377, 12123465, 19114526, 26658822","Bacillus subtilis (strain 168)","168 / 168 / 168 / SMY / 168 / JH642 / 168 / 3NA",33,488,489,5,462,462]
[null,"H2IFE7","IPMed?",0.98364,1.00208,35.97,{"v":2E-87,"d":"2.00E-87"},8,1,"Vejahgd","3,6-anhydro-alpha-L-galactose dehydrogenase","1.2.1.92","Carbohydrate metabolism, NAD, NADP, Oxidoreductase","22535948, 25156229","Vibrio sp. (strain EJY3)","EJY3 / EJY3",15,489,489,2,480,480]
[null,"Q9UTM8","_",0.94726,0.95501,34.9,{"v":7e-87,"d":"7.00E-87"},9,1,"_","Putative succinate-semialdehyde dehydrogenase C139.05 [NADP(+)]","1.2.1.16","Complete proteome, Cytoplasm, NADP, Oxidoreductase, Reference proteome","11859360, 16823372","Schizosaccharomyces pombe (strain 972 / ATCC 24843)","972 / ATCC 24843",20,482,489,21,486,493]
[null,"P0DOV9","IPMed?",0.95297,0.95885,34.76,{"v":2e-86,"d":"2.00E-86"},10,1,"_","3-sulfolactaldehyde dehydrogenase","1.2.1.97","NAD, NADP, Oxidoreductase","27408681, 26195800","Pseudomonas putida","SQ1 / SQ1",20,482,489,15,477,486]
[null,"P25553","IPMed?",0.94683,0.9666,35.42,{"v":8e-86,"d":"8.00E-86"},11,1,"aldA","Lactaldehyde dehydrogenase","1.2.1.22","3D-structure, Complete proteome, Direct protein sequencing, NAD, Oxidoreductase, Reference proteome","1917845, 9097039, 9278503, 16738553, 9298646, 6345530, 3308886","Escherichia coli (strain K12)","K12 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / EMG2",20,478,489,10,469,479]
[null,"P51650","IPMed?",0.90249,0.96524,36.65,{"v":2e-84,"d":"2.00E-84"},12,1,"Aldh5a1","Succinate-semialdehyde dehydrogenase, mitochondrial","1.2.1.24","Acetylation, Alternative splicing, Complete proteome, Direct protein sequencing, Disulfide bond, Mitochondrion, NAD, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","15057822, 7814412","Rattus norvegicus","Brown Norway / Sprague-Dawley",20,482,489,52,516,523]
[null,"Q9SAK4","IPMed?",0.85985,0.92843,35.24,{"v":1E-83,"d":"1.00E-83"},13,1,"ALDH5F1","Succinate-semialdehyde dehydrogenase, mitochondrial","1.2.1.24","Complete proteome, Disulfide bond, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide","10517851, 11130712, 27862469, 14593172, 12740438, 15358267, 15642352, 17461790, 18846220, 20122158, 22639603, 21690177, 25840087","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia",31,482,489,68,518,528]
[null,"P77674","IPMed?",0.95297,0.98312,36.27,{"v":5e-81,"d":"5.00E-81"},14,1,"prr","Gamma-aminobutyraldehyde dehydrogenase","1.2.1.19","3D-structure, Complete proteome, NAD, Oxidoreductase, Reference proteome","9097039, 9278503, 16738553, 16023116, 15381418","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",21,482,489,7,468,474]
[]
["CLOSTRIBL6_v1_2699","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q49W91","_",0.5528,0.70079,33.48,{"v":8e-57,"d":"8.00E-57"},1,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Complete proteome, Hydrogen ion transport, Ion transport, Membrane, Reference proteome, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport",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",119,529,635,73,509,805]
[null,"Q4L4W7","_",0.72976,0.92283,29.18,{"v":7e-55,"d":"7.00E-55"},2,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Complete proteome, Hydrogen ion transport, Ion transport, Membrane, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport",16237012,"Staphylococcus haemolyticus (strain JCSC1435)","JCSC1435",91,629,635,44,606,803]
[null,"P60675","_",0.55805,0.70394,32.89,{"v":2e-54,"d":"2.00E-54"},3,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Complete proteome, Hydrogen ion transport, Ion transport, Membrane, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport",11418146,"Staphylococcus aureus (strain N315)","N315",123,535,635,77,515,801]
[null,"P60674","_",0.55805,0.70394,32.89,{"v":2e-54,"d":"2.00E-54"},3,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Complete proteome, Hydrogen ion transport, Ion transport, Membrane, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport",11418146,"Staphylococcus aureus (strain Mu50 / ATCC 700699)","Mu50 / ATCC 700699",123,535,635,77,515,801]
[null,"A6U059","_",0.55805,0.70394,32.89,{"v":2e-54,"d":"2.00E-54"},3,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Hydrogen ion transport, Ion transport, Membrane, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport","_","Staphylococcus aureus (strain JH1)","_",123,535,635,77,515,801]
[null,"A5IRD0","_",0.55805,0.70394,32.89,{"v":2e-54,"d":"2.00E-54"},3,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Hydrogen ion transport, Ion transport, Membrane, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport","_","Staphylococcus aureus (strain JH9)","_",123,535,635,77,515,801]
[null,"A7X0G4","_",0.55805,0.70394,32.89,{"v":2e-54,"d":"2.00E-54"},3,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Hydrogen ion transport, Ion transport, Membrane, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport",17954695,"Staphylococcus aureus (strain Mu3 / ATCC 700698)","Mu3 / ATCC 700698",123,535,635,77,515,801]
[null,"Q6GID6","_",0.55805,0.70394,32.66,{"v":6e-54,"d":"6.00E-54"},4,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Hydrogen ion transport, Ion transport, Membrane, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport",15213324,"Staphylococcus aureus (strain MRSA252)","MRSA252",123,535,635,77,515,801]
[null,"Q9ZNG6","IPMed?",0.64669,0.81575,30.89,{"v":6e-54,"d":"6.00E-54"},5,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Hydrogen ion transport, Ion transport, Membrane, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport","9852009, 17293423","Staphylococcus aureus","ATCC 21027 / 209-P / RF4220",68,535,635,7,515,801]
[null,"Q2YWT4","_",0.55805,0.70394,32.66,{"v":6e-54,"d":"6.00E-54"},4,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Hydrogen ion transport, Ion transport, Membrane, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport",17971880,"Staphylococcus aureus (strain bovine RF122 / ET3-1)","bovine RF122 / ET3-1",123,535,635,77,515,801]
[null,"A8Z059","_",0.55805,0.70394,32.66,{"v":7e-54,"d":"7.00E-54"},6,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Hydrogen ion transport, Ion transport, Membrane, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport",17986343,"Staphylococcus aureus (strain USA300 / TCH1516)","USA300 / TCH1516",123,535,635,77,515,801]
[null,"Q6GAX4","_",0.55805,0.70394,32.66,{"v":7e-54,"d":"7.00E-54"},6,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Hydrogen ion transport, Ion transport, Membrane, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport",15213324,"Staphylococcus aureus (strain MSSA476)","MSSA476",123,535,635,77,515,801]
[null,"A6QFG2","_",0.55805,0.70394,32.66,{"v":7e-54,"d":"7.00E-54"},6,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Complete proteome, Hydrogen ion transport, Ion transport, Membrane, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport",17951380,"Staphylococcus aureus (strain Newman)","Newman",123,535,635,77,515,801]
[null,"Q5HHD3","_",0.55805,0.70394,32.66,{"v":7e-54,"d":"7.00E-54"},6,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Complete proteome, Hydrogen ion transport, Ion transport, Membrane, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport",15774886,"Staphylococcus aureus (strain COL)","COL",123,535,635,77,515,801]
[null,"Q8NXF6","_",0.55805,0.70394,32.66,{"v":7e-54,"d":"7.00E-54"},6,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Complete proteome, Hydrogen ion transport, Ion transport, Membrane, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport",12044378,"Staphylococcus aureus (strain MW2)","MW2",123,535,635,77,515,801]
[null,"Q8CPU8","_",0.58427,0.73701,31.2,{"v":4e-53,"d":"4.00E-53"},8,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Complete proteome, Hydrogen ion transport, Ion transport, Membrane, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport",12950922,"Staphylococcus epidermidis (strain ATCC 12228)","ATCC 12228",91,524,635,44,500,801]
[null,"Q9K2S2","IPMed?",0.55306,0.69764,34.54,{"v":4e-53,"d":"4.00E-53"},7,1,"mrpA","Na(+)/H(+) antiporter subunit A","_","Antiport, Cell membrane, Complete proteome, Hydrogen ion transport, Ion transport, Membrane, Reference proteome, Sodium, Sodium transport, Sporulation, Transmembrane, Transmembrane helix, Transport","9274030, 9384377, 9878723, 10198001, 10648512, 11356194, 17293423, 17693497","Bacillus subtilis (strain 168)","168 / 168 / 168 / 168 / 168 / Marburg / UOT1285",120,528,635,74,507,801]
[null,"Q5HQL0","_",0.58427,0.73701,31.2,{"v":4e-53,"d":"4.00E-53"},8,1,"mnhA1","Na(+)/H(+) antiporter subunit A1","_","Antiport, Cell membrane, Complete proteome, Hydrogen ion transport, Ion transport, Membrane, Reference proteome, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport",15774886,"Staphylococcus epidermidis (strain ATCC 35984 / RP62A)","ATCC 35984 / RP62A",91,524,635,44,500,801]
[null,"Q9RGZ5","IPMed?",0.61242,0.77638,31.44,{"v":2E-52,"d":"2.00E-52"},9,1,"mrpA","Na(+)/H(+) antiporter subunit A","_","Antiport, Cell membrane, Complete proteome, Hydrogen ion transport, Ion transport, Membrane, Reference proteome, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport","11356194, 21951522, 17293423","Bacillus pseudofirmus (strain OF4)","OF4",91,541,635,44,519,805]
[null,"Q52978","IPMed?",0.31732,0.49921,37.54,{"v":4e-48,"d":"4.00E-48"},10,1,"phaAB","Probable K(+)/H(+) antiporter subunit A/B","_","Antiport, Cell membrane, Complete proteome, Hydrogen ion transport, Ion transport, Membrane, Potassium, Potassium transport, Reference proteome, Transmembrane, Transmembrane helix, Transport","9680201, 11481430, 11474104","Rhizobium meliloti (strain 1021)","41 / 1021 / 1021",123,432,635,104,412,999]
[null,"P33607","IPMed?",0.8378,0.86786,31.39,{"v":1E-46,"d":"1.00E-46"},11,1,"nuoL","NADH-quinone oxidoreductase subunit L","7.1.1.-","Cell inner membrane, Cell membrane, Complete proteome, Membrane, NAD, Quinone, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Ubiquinone","7690854, 9205837, 9278503, 16738553, 15919996","Escherichia coli (strain K12)","K12 / AN387 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",39,558,635,8,507,613]
[null,"Q56227","IPMed?",0.72283,0.75743,30.94,{"v":7e-46,"d":"7.00E-46"},12,1,"nqo12","NADH-quinone oxidoreductase subunit 12","7.1.1.-","3D-structure, Cell inner membrane, Cell membrane, Complete proteome, Membrane, NAD, Quinone, Reference proteome, Translocase, Transmembrane, Transmembrane helix",9020134,"Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","HB8 / ATCC 27634 / DSM 579",120,554,635,67,503,606]
[null,"P50939","IPMed?",0.58848,0.65984,32.22,{"v":1e-43,"d":"1.00E-43"},13,1,"nuoL","NADH-quinone oxidoreductase subunit L","7.1.1.-","Membrane, NAD, Quinone, Translocase, Transmembrane, Transmembrane helix, Ubiquinone","8566820, 9632256","Rhodobacter capsulatus","ATCC 33303 / B10 / ATCC 33303 / B10 / ATCC 33303 / B10",120,506,635,74,486,712]
[null,"P77416","IPMed?",0.67559,0.89562,28.9,{"v":1E-41,"d":"1.00E-41"},14,1,"hyfD","Hydrogenase-4 component D","1.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Oxidoreductase, Reference proteome, Transmembrane, Transmembrane helix","9387241, 9205837, 9278503, 16738553, 15919996","Escherichia coli (strain K12)","K12 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",120,524,635,72,478,479]
[null,"P31971","IPMed?",0.70331,0.73543,28.69,{"v":3e-40,"d":"3.00E-40"},15,1,"ndhF","NAD(P)H-quinone oxidoreductase chain 5","7.1.1.-","Cell membrane, Complete proteome, Membrane, NAD, NADP, Plastoquinone, Quinone, Translocase, Transmembrane, Transmembrane helix","8501038, 1554697","Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6)","_",66,486,635,11,464,664]
[null,"Q35099","IPMed?",0.7874,0.83333,27.8,{"v":3e-39,"d":"3.00E-39"},16,1,"ND5","NADH-ubiquinone oxidoreductase chain 5","7.1.1.2","Electron transport, Membrane, Mitochondrion, Mitochondrion inner membrane, NAD, Respiratory chain, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",8643626,"Metridium senile","White morph",80,564,635,36,502,600]
[]
["CLOSTRIBL6_v1_2700","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P77858","IPMed?",0.92698,1.01389,27.05,{"v":2e-24,"d":"2.00E-24"},1,1,"hyfC","Hydrogenase-4 component C","1.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Membrane, NAD, Oxidoreductase, Reference proteome, Transmembrane, Transmembrane helix","9387241, 9205837, 9278503, 16738553, 15919996","Escherichia coli (strain K12)","K12 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",6,271,288,12,299,315]
[null,"P16430","IPMed?",0.96417,1.02778,25.68,{"v":7e-19,"d":"7.00E-19"},2,1,"hycD","Formate hydrogenlyase subunit 4","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Oxidoreductase, Reference proteome, Transmembrane, Transmembrane helix","2187144, 9278503, 16738553, 15919996","Escherichia coli (strain K12)","K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",4,270,288,2,291,307]
[null,"C1DL20","_",0.92705,1.05903,26.23,{"v":2E-16,"d":"2.00E-16"},3,1,"nuoH","NADH-quinone oxidoreductase subunit H","7.1.1.-","Cell inner membrane, Cell membrane, Complete proteome, Membrane, NAD, Quinone, Translocase, Transmembrane, Transmembrane helix, Ubiquinone",19429624,"Azotobacter vinelandii (strain DJ / ATCC BAA-1303)","DJ / ATCC BAA-1303",9,283,288,19,320,329]
[null,"A4SLN8","_",0.91304,1.02083,25.85,{"v":2E-16,"d":"2.00E-16"},4,1,"nuoH","NADH-quinone oxidoreductase subunit H","7.1.1.-","Cell inner membrane, Cell membrane, Complete proteome, Membrane, NAD, Quinone, Translocase, Transmembrane, Transmembrane helix, Ubiquinone",18801193,"Aeromonas salmonicida (strain A449)","A449",19,283,288,26,312,322]
[null,"Q4FU58","_",0.89625,1.07986,24.12,{"v":3e-16,"d":"3.00E-16"},5,1,"nuoH","NADH-quinone oxidoreductase subunit H","7.1.1.-","Cell inner membrane, Cell membrane, Complete proteome, Membrane, NAD, Quinone, Translocase, Transmembrane, Transmembrane helix, Ubiquinone",20154119,"Psychrobacter arcticus (strain DSM 17307 / 273-4)","DSM 17307 / 273-4",8,287,288,33,339,347]
[null,"Q8EI35","_",0.92547,1.03472,25.5,{"v":3e-16,"d":"3.00E-16"},6,1,"nuoH","NADH-quinone oxidoreductase subunit H","7.1.1.-","Cell inner membrane, Cell membrane, Complete proteome, Membrane, NAD, Quinone, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Ubiquinone",12368813,"Shewanella oneidensis (strain MR-1)","MR-1",19,287,288,26,316,322]
[null,"A6H1Q6","_",0.9621,1.14583,24.24,{"v":4e-16,"d":"4.00E-16"},7,1,"nuoH","NADH-quinone oxidoreductase subunit H","7.1.1.-","Cell inner membrane, Cell membrane, Complete proteome, Membrane, NAD, Quinone, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Ubiquinone",17592475,"Flavobacterium psychrophilum (strain JIP02/86 / ATCC 49511)","JIP02/86 / ATCC 49511",3,283,288,8,334,343]
[null,"Q1QD91","_",0.89625,1.07986,23.79,{"v":4e-16,"d":"4.00E-16"},8,1,"nuoH","NADH-quinone oxidoreductase subunit H","7.1.1.-","Cell inner membrane, Cell membrane, Complete proteome, Membrane, NAD, Quinone, Translocase, Transmembrane, Transmembrane helix, Ubiquinone","_","Psychrobacter cryohalolentis (strain K5)","_",8,287,288,33,339,347]
[null,"A0KJ61","_",0.91304,1.02083,25.51,{"v":4e-16,"d":"4.00E-16"},9,1,"nuoH","NADH-quinone oxidoreductase subunit H","7.1.1.-","Cell inner membrane, Cell membrane, Complete proteome, Membrane, NAD, Quinone, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Ubiquinone",16980456,"Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240)","ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240",19,283,288,26,312,322]
[null,"P12772","IPMed?",0.93189,1.04514,28.24,{"v":6e-16,"d":"6.00E-16"},10,1,"ND1","NADH-ubiquinone oxidoreductase chain 1","7.1.1.2","Electron transport, Membrane, Mitochondrion, Mitochondrion inner membrane, NAD, Respiratory chain, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","2544576, 2834108","Paracentrotus lividus","_",4,270,288,2,295,323]
[null,"Q96186","IPMed?",0.79096,0.97222,24.64,3e-15,11,1,"ND1","NADH-ubiquinone oxidoreductase chain 1","7.1.1.2","Electron transport, Membrane, Mitochondrion, Mitochondrion inner membrane, NAD, Respiratory chain, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",7666448,"Pecten maximus","_",26,270,288,64,336,354]
[null,"Q8PU59","IPMed?",0.71714,0.87153,31.08,2E-14,12,1,"fpoH","F(420)H(2) dehydrogenase subunit H","1.12.98.3","Cell membrane, Complete proteome, Electron transport, Membrane, Methanogenesis, Methanol utilization, Oxidoreductase, Transmembrane, Transmembrane helix, Transport","10751389, 12125824","Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)","ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88 / ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88 / ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88",10,229,288,25,272,350]
[null,"Q01148","IPMed?",0.75077,0.84722,30.33,2E-14,13,1,"ND1","NADH-ubiquinone oxidoreductase chain 1","7.1.1.2","Electron transport, Membrane, Mitochondrion, Mitochondrion inner membrane, NAD, Respiratory chain, RNA editing, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",1902143,"Triticum aestivum","cv. Thatcher",9,229,288,9,248,325]
[null,"P69235","IPMed?",0.96166,1.04514,26.25,3e-14,14,1,"ND1","NADH-ubiquinone oxidoreductase chain 1","7.1.1.2","Electron transport, Membrane, Mitochondrion, Mitochondrion inner membrane, NAD, Respiratory chain, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","9254918, 9628930","Branchiostoma lanceolatum","_",4,283,288,4,298,313]
[null,"P69234","IPMed?",0.96166,1.04514,26.25,3e-14,14,1,"ND1","NADH-ubiquinone oxidoreductase chain 1","7.1.1.2","Complete proteome, Electron transport, Membrane, Mitochondrion, Mitochondrion inner membrane, NAD, Reference proteome, Respiratory chain, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",10331267,"Branchiostoma floridae","S238N-H82",4,283,288,4,298,313]
[null,"P33502","IPMed?",0.89809,0.97917,25.53,3e-14,15,1,"ND1","NADH-ubiquinone oxidoreductase chain 1","7.1.1.2","Electron transport, Membrane, Mitochondrion, Mitochondrion inner membrane, NAD, Respiratory chain, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",2134168,"Anopheles quadrimaculatus","Orlando",10,270,288,12,288,314]
[null,"P23650","IPMed?",0.89264,1.01042,26.12,4E-14,16,1,"ND1","NADH-ubiquinone oxidoreductase chain 1","7.1.1.2","Electron transport, Membrane, Mitochondrion, Mitochondrion inner membrane, NAD, Respiratory chain, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7672576, 2766382","Patiria pectinifera","_",9,270,288,11,295,326]
[null,"P92690","IPMed?",0.92453,1.02083,27.55,5e-14,17,1,"MT-ND1","NADH-ubiquinone oxidoreductase chain 1","7.1.1.2","Complete proteome, Electron transport, Membrane, Mitochondrion, Mitochondrion inner membrane, NAD, Reference proteome, Respiratory chain, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",8875856,"Pongo abelii","_",6,270,288,7,290,318]
[]
["CLOSTRIBL6_v1_2701","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q8U0Z8","IPMed?",0.8982,0.97403,47.33,{"v":2e-43,"d":"2.00E-43"},1,1,"mbhJ","Probable membrane-bound hydrogenase subunit mbhJ","1.12.7.2","3D-structure, 4Fe-4S, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, Oxidoreductase, Reference proteome","10430560, 11054105, 10852873, 12792025","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 / ATCC 43587 / DSM 3638 / JCM 8422 / Vc1",4,152,154,21,163,167]
[null,"Q57936","_",0.83766,0.87162,48.84,{"v":6e-39,"d":"6.00E-39"},2,1,"_","Uncharacterized protein MJ0516","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, 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",18,145,154,21,148,148]
[null,"P16433","IPMed?",0.53333,0.88312,39.71,{"v":3e-35,"d":"3.00E-35"},3,1,"hycG","Formate hydrogenlyase subunit 7","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome","2187144, 9278503, 16738553","Escherichia coli (strain K12)","K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",1,136,154,31,166,255]
[null,"P77668","IPMed?",0.53968,0.88312,39.71,{"v":6e-35,"d":"6.00E-35"},4,1,"hyfI","Hydrogenase-4 component I","1.-.-.-","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome","9387241, 9205837, 9278503, 16738553","Escherichia coli (strain K12)","K12 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",1,136,154,27,162,252]
[null,"A9WFB2","_",0.78736,0.88961,48.91,{"v":5e-34,"d":"5.00E-34"},5,1,"nuoB2","NADH-quinone oxidoreductase subunit B 2","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Transport, Ubiquinone",21714912,"Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)","ATCC 29366 / DSM 635 / J-10-fl",15,148,154,35,163,174]
[null,"B9LAU1","_",0.78736,0.88961,48.91,{"v":5e-34,"d":"5.00E-34"},5,1,"nuoB2","NADH-quinone oxidoreductase subunit B 2","7.1.1.-","4Fe-4S, Cell membrane, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Translocase, Transport, Ubiquinone","_","Chloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl)","_",15,148,154,35,163,174]
[null,"B8G705","_",0.77011,0.87013,48.51,{"v":5e-34,"d":"5.00E-34"},6,1,"nuoB1","NADH-quinone oxidoreductase subunit B 1","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Translocase, Transport, Ubiquinone","_","Chloroflexus aggregans (strain MD-66 / DSM 9485)","_",15,145,154,35,161,174]
[null,"B5YKI3","_",0.71357,0.92208,44.37,{"v":7e-34,"d":"7.00E-34"},7,1,"nuoB1","NADH-quinone oxidoreductase subunit B 1","7.1.1.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Transport, Ubiquinone","_","Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)","_",7,148,154,42,168,199]
[null,"B8J1D6","_",0.67213,0.7987,43.9,{"v":3e-33,"d":"3.00E-33"},8,1,"nuoB","NADH-quinone oxidoreductase subunit B","7.1.1.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Transport, Ubiquinone","_","Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)","_",15,137,154,57,176,183]
[null,"B5YL35","_",0.71264,0.80519,47.58,{"v":1e-32,"d":"1.00E-32"},10,1,"nuoB2","NADH-quinone oxidoreductase subunit B 2","7.1.1.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Transport, Ubiquinone","_","Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)","_",5,128,154,39,158,174]
[null,"Q2RJU6","_",0.68675,0.74026,49.12,{"v":1e-32,"d":"1.00E-32"},9,1,"nuoB","NADH-quinone oxidoreductase subunit B","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Transport",18631365,"Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320",15,127,154,40,151,166]
[null,"F1SVH7","IPMed?",0.64674,0.77273,39.5,{"v":5e-30,"d":"5.00E-30"},11,1,"fpoB","F(420)H(2) dehydrogenase subunit B","1.12.98.3","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Direct protein sequencing, Electron transport, FAD, Flavoprotein, Iron, Iron-sulfur, Membrane, Metal-binding, Methanogenesis, Methanol utilization, Oxidoreductase, Transport","10751389, 12125824","Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)","ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88 / ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88 / ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88",21,139,154,62,180,184]
[null,"Q94360","IPMed?",0.66332,0.85714,40.15,{"v":1e-29,"d":"1.00E-29"},12,1,"nduf-7","Probable NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial","1.6.99.3, 7.1.1.2","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","9851916, 12853115","Caenorhabditis elegans","Bristol N2",7,138,154,64,192,199]
[null,"P42026","IPMed?",0.5787,0.81169,38.4,{"v":2e-28,"d":"2.00E-28"},13,1,"NDUFS7","NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial","1.6.99.3, 7.1.1.2","3D-structure, 4Fe-4S, Complete proteome, Direct protein sequencing, Electron transport, Hydroxylation, Iron, Iron-sulfur, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","1577158, 23836892, 10852722, 18721790","Bos taurus","_",15,139,154,88,208,216]
[null,"O75251","IPMed?",0.57746,0.7987,35.77,{"v":4e-28,"d":"4.00E-28"},14,1,"NDUFS7","NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial","1.6.99.3, 7.1.1.2","3D-structure, 4Fe-4S, Alternative splicing, Complete proteome, Disease mutation, Electron transport, Hydroxylation, Iron, Iron-sulfur, Leigh syndrome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Polymorphism, Primary mitochondrial disease, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","8938450, 14702039, 15057824, 15489334, 12611891, 21269460, 25944712, 27226634, 10360771, 10330338","Homo sapiens","_",15,137,154,85,205,213]
[null,"Q8DKZ4","IPMed?",0.51899,0.7987,43.09,{"v":6e-28,"d":"6.00E-28"},15,1,"ndhK","NAD(P)H-quinone oxidoreductase subunit K","7.1.1.-","3D-structure, 4Fe-4S, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, NADP, Plastoquinone, Quinone, Reference proteome, Thylakoid, Translocase, Transport","12240834, 15910282","Thermosynechococcus elongatus (strain BP-1)","BP-1",7,128,154,42,161,237]
[null,"P17062","IPMed?",0.52511,0.74675,44.35,{"v":8e-28,"d":"8.00E-28"},16,1,"ndhK2","NAD(P)H-quinone oxidoreductase subunit K 2","7.1.1.-","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, NADP, Plasmid, Plastoquinone, Quinone, Reference proteome, Thylakoid, Translocase, Transport","2108054, 14686584","Synechocystis sp. (strain PCC 6803 / Kazusa)","PCC 6803 / Kazusa",15,128,154,50,162,219]
[null,"A1B497","IPMed?",0.65143,0.74026,38.6,{"v":8e-28,"d":"8.00E-28"},17,1,"nuoB","NADH-quinone oxidoreductase subunit B","7.1.1.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Transport, Ubiquinone",14610094,"Paracoccus denitrificans (strain Pd 1222)","_",15,128,154,51,162,175]
[null,"P29918","IPMed?",0.65896,0.74026,38.6,{"v":8e-28,"d":"8.00E-28"},17,1,"nqo6","NADH-quinone oxidoreductase subunit 6","7.1.1.-","4Fe-4S, Cell inner membrane, Cell membrane, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Translocase, Ubiquinone",1637825,"Paracoccus denitrificans","ATCC 13543 / NRRL B-3784 / NRC 449",15,128,154,50,161,173]
[]
["CLOSTRIBL6_v1_2702","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P23710","IPMed?",0.25088,0.61739,30.99,0.053,1,1,"nuo-31","NADH-ubiquinone oxidoreductase 30.4 kDa subunit, mitochondrial","1.6.99.3, 7.1.1.2","Complete proteome, Electron transport, Membrane, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","2145832, 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",35,97,115,135,205,283]
[null,"O84971","_",0.55276,0.95652,25.45,0.17,2,1,"nuoC","NADH-quinone oxidoreductase subunit C","7.1.1.-","Cell inner membrane, Cell membrane, Membrane, NAD, Quinone, Translocase, Transport, Ubiquinone","_","Rhodobacter capsulatus","_",4,97,115,28,137,199]
[null,"Q2G5Y5","_",0.35922,0.96522,20.72,0.88,3,1,"nuoC","NADH-quinone oxidoreductase subunit C","7.1.1.-","Cell inner membrane, Cell membrane, Complete proteome, Membrane, NAD, Quinone, Reference proteome, Translocase, Transport, Ubiquinone","_","Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199)","_",2,97,115,34,143,309]
[]
["CLOSTRIBL6_v1_2703","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P31895","IPMed?",1.00277,1.00836,39.23,{"v":9e-83,"d":"9.00E-83"},1,1,"cooH","Carbon monoxide-induced hydrogenase","_","Metal-binding, Nickel, Oxidoreductase","8626276, 1644755","Rhodospirillum rubrum","UR2 / UR1",1,359,359,1,361,361]
[null,"Q57935","_",0.94737,1.00279,38.89,{"v":2e-81,"d":"2.00E-81"},2,1,"_","Uncharacterized protein MJ0515","_","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",5,359,359,6,362,380]
[null,"Q8U0Z6","IPMed?",0.8829,1.05014,38.73,{"v":2e-80,"d":"2.00E-80"},3,1,"mbhL","Membrane-bound hydrogenase subunit alpha","1.12.7.2","3D-structure, Cell membrane, Complete proteome, Direct protein sequencing, Membrane, Metal-binding, Nickel, Oxidoreductase, Reference proteome","10430560, 11054105, 10852873, 12792025","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 / ATCC 43587 / DSM 3638 / JCM 8422 / Vc1",7,359,359,10,380,427]
[null,"F1SVE4","IPMed?",0.98396,1.02507,35.05,{"v":1e-71,"d":"1.00E-71"},4,1,"fpoD","F(420)H(2) dehydrogenase subunit D","1.12.98.3","Cell inner membrane, Cell membrane, Complete proteome, Direct protein sequencing, Electron transport, Membrane, Methanogenesis, Methanol utilization, Oxidoreductase, Transport","10751389, 12125824","Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)","ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88 / ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88 / ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88",2,359,359,7,374,374]
[null,"P16431","IPMed?",0.63972,1.01393,35.99,{"v":1e-69,"d":"1.00E-69"},5,1,"hycE","Formate hydrogenlyase subunit 5","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, NAD, Nickel, Oxidoreductase, Reference proteome","2187144, 9278503, 16738553, 8125094","Escherichia coli (strain K12)","K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",5,359,359,180,537,569]
[null,"B3QUS0","_",0.85455,1.04735,34.31,{"v":9e-69,"d":"9.00E-69"},6,1,"nuoD1","NADH-quinone oxidoreductase subunit D 1","7.1.1.-","Cell inner membrane, Cell membrane, Complete proteome, Membrane, NAD, Quinone, Reference proteome, Translocase, Transport","_","Chloroherpeton thalassium (strain ATCC 35110 / GB-78)","_",6,352,359,58,433,440]
[null,"P77329","IPMed?",0.65225,1.00836,34.81,{"v":2e-65,"d":"2.00E-65"},7,1,"hyfG","Hydrogenase-4 component G","1.-.-.-","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, NAD, Oxidoreductase, Reference proteome","9387241, 9205837, 9278503, 16738553","Escherichia coli (strain K12)","K12 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",2,359,359,179,523,555]
[null,"B5YL34","_",0.95262,1.06407,33.51,{"v":2e-64,"d":"2.00E-64"},8,1,"nuoD2","NADH-quinone oxidoreductase subunit D 2","7.1.1.-","Cell inner membrane, Cell membrane, Complete proteome, Membrane, NAD, Quinone, Reference proteome, Translocase, Transport, Ubiquinone","_","Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)","_",3,351,359,12,393,401]
[null,"A6LXQ2","_",0.95946,0.98886,32.11,{"v":1e-63,"d":"1.00E-63"},9,1,"nuoD","NADH-quinone oxidoreductase subunit D","7.1.1.-","Cell membrane, Complete proteome, Membrane, NAD, Quinone, Reference proteome, Translocase, Transport","_","Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052)","_",9,359,359,16,370,370]
[null,"Q02CU0","_",0.94132,1.07242,31.17,{"v":2e-62,"d":"2.00E-62"},10,1,"nuoD1","NADH-quinone oxidoreductase subunit D 1","7.1.1.-","Cell inner membrane, Cell membrane, Complete proteome, Membrane, NAD, Quinone, Reference proteome, Translocase, Transport, Ubiquinone",19201974,"Solibacter usitatus (strain Ellin6076)","Ellin6076",4,359,359,25,409,409]
[null,"Q56220","IPMed?",0.92665,1.05571,31.4,{"v":2e-57,"d":"2.00E-57"},11,1,"nqo4","NADH-quinone oxidoreductase subunit 4","7.1.1.-","3D-structure, Cell membrane, Complete proteome, Direct protein sequencing, Membrane, NAD, Quinone, Reference proteome, Translocase, Transport","9020134, 16584177, 16469879","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","HB8 / ATCC 27634 / DSM 579 / HB8 / ATCC 27634 / DSM 579",10,359,359,31,409,409]
[null,"P12131","IPMed?",0.95408,1.04178,30.48,{"v":3e-56,"d":"3.00E-56"},12,1,"ndhH","NAD(P)H-quinone oxidoreductase subunit H, chloroplastic","7.1.1.-","Chloroplast, Membrane, NAD, NADP, Plastid, Plastoquinone, Quinone, Thylakoid, Translocase, Transport",3199437,"Marchantia polymorpha","_",6,351,359,11,384,392]
[null,"O98691","IPMed?",0.95165,1.04178,30.75,{"v":2E-52,"d":"2.00E-52"},13,1,"ndhH","NAD(P)H-quinone oxidoreductase subunit H, chloroplastic","7.1.1.-","Chloroplast, Membrane, NAD, NADP, Plastid, Plastoquinone, Quinone, Thylakoid, Translocase, Transport","10666448, 17534593","Hordeum vulgare","cv. Hassan / cv. Morex",6,351,359,12,385,393]
[null,"P25709","IPMed?",0.95165,1.04178,30.75,{"v":3E-52,"d":"3.00E-52"},14,1,"ndhH","NAD(P)H-quinone oxidoreductase subunit H, chloroplastic","7.1.1.-","Chloroplast, Complete proteome, Membrane, NAD, NADP, Plastid, Plastoquinone, Quinone, Reference proteome, Thylakoid, Translocase, Transport","2249254, 7666415","Zea mays","cv. B73",6,351,359,12,385,393]
[null,"P56753","IPMed?",0.95165,1.04178,30.48,{"v":4E-51,"d":"4.00E-51"},15,1,"ndhH","NAD(P)H-quinone oxidoreductase subunit H, chloroplastic","7.1.1.-","Chloroplast, Complete proteome, Membrane, NAD, NADP, Plastid, Plastoquinone, Quinone, Reference proteome, Thylakoid, Translocase, Transport","10574454, 21483722","Arabidopsis thaliana","cv. Columbia",6,351,359,12,385,393]
[]
["CLOSTRIBL6_v1_2704","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"A4TDB3","_",0.69082,0.81714,31.47,8e-15,1,1,"nuoI","NADH-quinone oxidoreductase subunit I","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Repeat, Translocase","_","Mycolicibacterium gilvum (strain PYR-GCK)","_",13,136,207,17,156,175]
[null,"Q744Z4","_",0.70531,0.83429,30.14,2E-14,2,1,"nuoI1","NADH-quinone oxidoreductase subunit I 1","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Repeat, Translocase",16116077,"Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)","ATCC BAA-968 / K-10",14,140,207,18,160,175]
[null,"Q2IL14","_",0.88636,1.13043,29.06,3e-14,3,1,"nuoI2","NADH-quinone oxidoreductase subunit I 2","7.1.1.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Repeat, Translocase, Ubiquinone","_","Anaeromyxobacter dehalogenans (strain 2CP-C)","_",14,198,207,30,259,264]
[null,"A1T698","_",0.68116,0.81034,31.21,3e-14,4,1,"nuoI","NADH-quinone oxidoreductase subunit I","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Repeat, Translocase","_","Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / NRRL B-24157 / PYR-1)","_",13,134,207,17,154,174]
[null,"Q5YWD4","_",0.28141,0.81159,29.76,8E-14,5,1,"nuoH/I","NADH-quinone oxidoreductase subunits H/I","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Repeat, Translocase, Transmembrane, Transmembrane helix, Ubiquinone",15466710,"Nocardia farcinica (strain IFM 10152)","IFM 10152",14,162,207,429,593,597]
[null,"Q3AGY9","_",0.75349,0.78261,30.25,1e-12,6,1,"ndhI","NAD(P)H-quinone oxidoreductase subunit I","7.1.1.-","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, NADP, Plastoquinone, Quinone, Repeat, Thylakoid, Translocase","_","Synechococcus sp. (strain CC9605)","_",17,169,207,36,195,215]
[null,"Q1BBQ1","_",0.68599,0.81609,30.99,1e-12,7,1,"nuoI","NADH-quinone oxidoreductase subunit I","7.1.1.-","4Fe-4S, Cell membrane, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Repeat, Translocase","_","Mycobacterium sp. (strain MCS)","_",14,136,207,18,156,174]
[null,"A1UD96","_",0.68599,0.81609,30.99,1e-12,7,1,"nuoI","NADH-quinone oxidoreductase subunit I","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Repeat, Translocase","_","Mycobacterium sp. (strain KMS)","_",14,136,207,18,156,174]
[null,"C1AGS0","_",0.65403,0.66667,28.99,1e-12,8,1,"nuoI","NADH-quinone oxidoreductase subunit I","7.1.1.-","4Fe-4S, Cell membrane, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Repeat, Translocase",19200449,"Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019)","BCG / Tokyo 172 / ATCC 35737 / TMC 1019",13,131,207,44,180,211]
[null,"A1KNE9","_",0.65403,0.66667,28.99,1e-12,8,1,"nuoI","NADH-quinone oxidoreductase subunit I","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Repeat, Translocase",17372194,"Mycobacterium bovis (strain BCG / Pasteur 1173P2)","BCG / Pasteur 1173P2",13,131,207,44,180,211]
[null,"Q7TX57","_",0.65403,0.66667,28.99,1e-12,8,1,"nuoI","NADH-quinone oxidoreductase subunit I","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Repeat, Translocase","12788972, 28385856","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97",13,131,207,44,180,211]
[null,"A3PWR3","_",0.68599,0.81609,30.99,1e-12,7,1,"nuoI","NADH-quinone oxidoreductase subunit I","7.1.1.-","4Fe-4S, Cell membrane, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Repeat, Translocase","_","Mycobacterium sp. (strain JLS)","_",14,136,207,18,156,174]
[null,"Q3AC82","_",0.45411,0.67143,32.98,2E-12,9,1,"nuoI","NADH-quinone oxidoreductase subunit I","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Repeat, Translocase, Ubiquinone",16311624,"Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)","ATCC BAA-161 / DSM 6008 / Z-2901",12,97,207,18,111,140]
[null,"Q46HL4","_",0.60092,0.63285,30.53,5e-12,10,1,"ndhI","NAD(P)H-quinone oxidoreductase subunit I","7.1.1.-","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, NADP, Plastoquinone, Quinone, Reference proteome, Repeat, Thylakoid, Translocase",18159947,"Prochlorococcus marinus (strain NATL2A)","NATL2A",17,138,207,36,166,218]
[null,"A2BZY6","_",0.60092,0.63285,30.53,5e-12,10,1,"ndhI","NAD(P)H-quinone oxidoreductase subunit I","7.1.1.-","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, NADP, Plastoquinone, Quinone, Repeat, Thylakoid, Translocase",18159947,"Prochlorococcus marinus (strain NATL1A)","NATL1A",17,138,207,36,166,218]
[null,"Q92954","IPMed?",0.0812,0.55072,34.21,2e-11,11,2,"PRG4","Proteoglycan 4","_","Alternative splicing, Complete proteome, Disulfide bond, Glycoprotein, Polymorphism, Proteoglycan, Reference proteome, Repeat, Secreted, Signal","14702039, 16710414, 9920774, 14976050, 8185311, 10545950, 11124536, 10743795, 16335952, 18088087, 21406692, 25187573","Homo sapiens","_",96,202,207,415,528,1404]
[null,"O98692","IPMed?",0.42995,0.49444,38.2,6E-11,12,1,"ndhI","NAD(P)H-quinone oxidoreductase subunit I, chloroplastic","7.1.1.-","4Fe-4S, Chloroplast, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, NADP, Plastid, Plastoquinone, Quinone, Repeat, Thylakoid, Translocase","10666448, 17534593","Hordeum vulgare","cv. Hassan / cv. Morex",18,97,207,37,125,180]
[null,"P05312","IPMed?",0.42995,0.49444,38.2,6E-11,12,1,"ndhI","NAD(P)H-quinone oxidoreductase subunit I, chloroplastic","7.1.1.-","4Fe-4S, Chloroplast, Complete proteome, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, NADP, Plastid, Plastoquinone, Quinone, Reference proteome, Repeat, Thylakoid, Translocase",3340530,"Triticum aestivum","cv. Mardler / cv. Chinese Spring",18,97,207,37,125,180]
[null,"P06253","IPMed?",0.42995,0.48634,37.08,1E-10,13,1,"ndhI","NAD(P)H-quinone oxidoreductase subunit I, chloroplastic","7.1.1.-","4Fe-4S, Chloroplast, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, NADP, Plastid, Plastoquinone, Quinone, Repeat, Thylakoid, Translocase",3199437,"Marchantia polymorpha","_",18,97,207,37,125,183]
[null,"P26525","IPMed?",0.43478,0.46632,36.67,1E-10,14,1,"ndhI","NAD(P)H-quinone oxidoreductase subunit I","7.1.1.-","4Fe-4S, Complete proteome, Direct protein sequencing, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, NADP, Plastoquinone, Quinone, Reference proteome, Repeat, Thylakoid, Translocase","1463844, 8590279, 8905231, 8325373","Synechocystis sp. (strain PCC 6803 / Kazusa)","ATCC 27184 / PCC 6803 / N-1 / PCC 6803 / Kazusa",17,97,207,37,126,193]
[null,"P06252","IPMed?",0.42995,0.53293,39.33,2e-10,15,1,"ndhI","NAD(P)H-quinone oxidoreductase subunit I, chloroplastic","7.1.1.-","4Fe-4S, Chloroplast, Direct protein sequencing, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, NADP, Plastid, Plastoquinone, Quinone, Repeat, Thylakoid, Translocase","16453699, 2103463","Nicotiana tabacum","cv. Bright Yellow 4",18,97,207,37,125,167]
[null,"Q62267","IPMed?",0.3913,0.52941,39.51,3E-10,16,1,"Sprr1b","Cornifin-B","_","Complete proteome, Cytoplasm, Keratinization, Reference proteome, Repeat","8601731, 9931436, 16141072, 15489334","Mus musculus","CD-1 / 129/SvJ / C57BL/6J",113,193,207,51,131,153]
[null,"Q9JM99","IPMed?",0.09393,0.47826,32.32,4e-10,17,2,"Prg4","Proteoglycan 4","_","Alternative splicing, Complete proteome, Disulfide bond, Glycoprotein, Proteoglycan, Reference proteome, Repeat, Secreted, Signal","11124536, 16141072, 15719068, 16000300","Mus musculus","C57BL/6J",96,194,207,497,595,1054]
[null,"Q8PU60","IPMed?",0.50242,0.58757,29.81,4e-10,18,1,"fpoI","F(420)H(2) dehydrogenase subunit I","1.12.98.3","4Fe-4S, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Methanogenesis, Methanol utilization, Oxidoreductase, Repeat, Transport","10751389, 12125824","Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)","ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88 / ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88 / ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88",3,97,207,43,146,177]
[null,"P0AFD6","IPMed?",0.51208,0.58889,32.08,5e-10,19,1,"nuoI","NADH-quinone oxidoreductase subunit I","7.1.1.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Direct protein sequencing, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Repeat, Translocase, Ubiquinone","7690854, 9205837, 9278503, 16738553, 9298646, 7607227","Escherichia coli (strain K12)","K12 / AN387 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / EMG2 / K12 / MG1655 / ATCC 47076",15,107,207,25,129,180]
[null,"P35324","IPMed?",0.39614,0.65079,35.37,5e-10,20,1,"_","Cornifin alpha","_","Acetylation, Complete proteome, Cytoplasm, Keratinization, Reference proteome, Repeat",1438308,"Oryctolagus cuniculus","_",113,194,207,35,116,126]
[]
["CLOSTRIBL6_v1_2705","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q55638","_",1,1.03369,37.94,{"v":5e-154,"d":"5.00E-154"},1,1,"hypF","Carbamoyltransferase HypF","6.2.-.-","Complete proteome, Ligase, Metal-binding, Reference proteome, Zinc, Zinc-finger","8590279, 8905231","Synechocystis sp. (strain PCC 6803 / Kazusa)","ATCC 27184 / PCC 6803 / N-1 / PCC 6803 / Kazusa",2,735,742,4,755,767]
[null,"P40596","IPMed?",0.98067,1.02561,38.24,{"v":1e-138,"d":"1.00E-138"},2,1,"hypF","Carbamoyltransferase HypF","6.2.-.-","Ligase, Metal-binding, Zinc, Zinc-finger",1610901,"Azotobacter vinelandii","ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW",9,737,742,15,761,776]
[null,"Q43950","IPMed?",0.98196,1.02695,37.4,{"v":5e-135,"d":"5.00E-135"},3,1,"hypF","Carbamoyltransferase HypF","6.2.-.-","Ligase, Metal-binding, Zinc, Zinc-finger",8486288,"Azotobacter chroococcum mcd 1","_",9,738,742,15,762,776]
[null,"O07451","IPMed?",0.9777,1.06334,35.99,{"v":3e-133,"d":"3.00E-133"},4,1,"hypF2","Carbamoyltransferase HypF2","6.2.-.-","Complete proteome, Ligase, Metal-binding, Plasmid, Reference proteome, Zinc, Zinc-finger","9799289, 12948488","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337",5,738,742,17,800,807]
[null,"Q58123","_",0.99608,1.0283,35.91,{"v":4e-132,"d":"4.00E-132"},5,1,"hypF","Probable carbamoyltransferase HypF","6.2.-.-","Complete proteome, Ligase, Metal-binding, Reference proteome, Zinc, Zinc-finger",8688087,"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440",1,735,742,10,756,766]
[null,"P30131","IPMed?",1.00133,1.01213,37.42,{"v":1e-129,"d":"1.00E-129"},6,1,"hypF","Carbamoyltransferase HypF","6.2.-.-","3D-structure, Complete proteome, Ligase, Metal-binding, Reference proteome, Zinc, Zinc-finger","9278503, 16738553, 8661925, 12377778, 12586941, 15291820, 18065529, 12206761","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MC4100 / ATCC 35695 / DSM 6574",5,735,742,11,734,750]
[null,"P28156","IPMed?",0.99736,1.02022,34.61,{"v":5e-118,"d":"5.00E-118"},7,1,"hypF","Carbamoyltransferase HypF","6.2.-.-","Ligase, Metal-binding, Zinc, Zinc-finger",8326860,"Rhizobium leguminosarum bv. viciae","128c53",3,735,742,16,737,759]
[null,"Q02987","IPMed?",1.02291,1.02706,38.34,{"v":9e-118,"d":"9.00E-118"},8,1,"hypF","Carbamoyltransferase HypF","6.2.-.-","Ligase, Metal-binding, Zinc, Zinc-finger","8497190, 9492269","Rhodobacter capsulatus","ATCC 33303 / B10",5,736,742,6,729,739]
[null,"P45805","IPMed?",0.48922,0.92132,33.06,{"v":9e-44,"d":"9.00E-44"},9,1,"hypF1","Carbamoyltransferase HypF homolog","_","Complete proteome, Plasmid, Reference proteome","8352644, 8631353, 12948488","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337",396,740,742,14,373,394]
[null,"Q3U5F4","IPMed?",0.19542,0.51786,30.34,7e-08,10,2,"Yrdc","YrdC domain-containing protein, mitochondrial","_","Complete proteome, Membrane, Mitochondrion, Phosphoprotein, Reference proteome, Transit peptide","16141072, 19468303, 16024787, 15489334, 21183079, 24129315","Mus musculus","C57BL/6J / C57BL/6J / C57BL/6 X CBA / FVB/N",199,338,742,69,210,280]
[null,"Q86U90","IPMed?",0.19542,0.51971,29.66,1e-06,11,2,"YRDC","YrdC domain-containing protein, mitochondrial","_","Complete proteome, Membrane, Mitochondrion, Phosphoprotein, Reference proteome, Transit peptide","12730717, 16710414, 15489334, 16024787, 14702039, 17081983, 16964243, 17924679, 18691976, 18669648, 19413330, 19690332, 20068231, 21269460, 21406692, 23186163, 24275569","Homo sapiens","_",199,338,742,68,209,279]
[null,"Q97ZL0","IPMed?",0.09434,0.69307,38.57,0.0005,12,2,"acyP","Acylphosphatase","3.6.1.7","3D-structure, Complete proteome, Hydrolase, Reference proteome","11427726, 16287076","Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)","ATCC 35092 / DSM 1617 / JCM 11322 / P2",3,71,742,16,84,101]
[]
["CLOSTRIBL6_v1_2706","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q57653","_",0.92683,1.08571,40.79,4e-08,1,1,"_","Uncharacterized hydrogenase expression/formation protein MJ0200","_","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",1,70,70,1,76,82]
[null,"P31900","IPMed?",0.77778,1,31.43,0.0003,2,1,"hypC","Hydrogenase maturation factor HypC","_","Complete proteome, Plasmid, Reference proteome","8352644, 12948488","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337",1,68,70,1,70,90]
[null,"Q7VJB9","IPMed?",0.84884,1.04286,38.36,0.0005,3,1,"hypC","Hydrogenase maturation factor HypC","_","Complete proteome, Reference proteome","12810954, 17975083","Helicobacter hepaticus (strain ATCC 51449 / 3B1)","ATCC 51449 / 3B1 / ATCC 51449 / 3B1",1,67,70,1,70,86]
[null,"P74095","_",0.96053,1.04286,34.25,0.0005,4,1,"hypC","Hydrogenase maturation factor HypC","_","Complete proteome, Reference proteome",8905231,"Synechocystis sp. (strain PCC 6803 / Kazusa)","PCC 6803 / Kazusa",1,65,70,1,73,76]
[null,"P0AAM3","IPMed?",0.75556,0.97143,30.88,0.009,5,1,"hypC","Hydrogenase maturation factor HypC","_","3D-structure, Complete proteome, Reference proteome","1849603, 9278503, 16738553, 9298644, 9485446, 10783387, 11292801, 12441107, 15504408, 23022438, 23851071, 17669368","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",1,60,70,1,68,90]
[null,"P31881","IPMed?",0.82143,0.98571,30.43,0.009,6,1,"hypC","Hydrogenase maturation factor HypC","_","_",1610901,"Azotobacter vinelandii","ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW",1,67,70,1,69,84]
[null,"Q43951","IPMed?",0.82143,0.98571,30.43,0.016,7,1,"hypC","Hydrogenase maturation factor HypC","_","_",8486288,"Azotobacter chroococcum mcd 1","_",1,67,70,1,69,84]
[null,"Q03005","IPMed?",0.50943,0.77143,35.19,0.043,8,1,"hupF","Hydrogenase expression/formation protein HupF","_","_",8497190,"Rhodobacter capsulatus","ATCC 33303 / B10",1,53,70,1,54,106]
[null,"P28157","IPMed?",0.90667,0.97143,32.35,0.074,9,1,"hypC","Hydrogenase maturation factor HypC","_","_",8326860,"Rhizobium leguminosarum bv. viciae","128c53 / B10",1,66,70,1,68,75]
[null,"P20927","IPMed?",0.64583,0.88571,32.26,0.1,10,1,"_","Frd operon uncharacterized protein C","_","_",3308458,"Proteus vulgaris","_",1,54,70,1,62,96]
[null,"P40428","IPMed?",0.8125,1.11429,21.79,0.82,11,1,"hypC","Hydrogenase maturation factor HypC","_","_",8497190,"Rhodobacter capsulatus","ATCC 33303 / B10",1,70,70,1,78,96]
[]
["CLOSTRIBL6_v1_2707","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P31882","IPMed?",0.88391,0.97384,41.19,{"v":7e-79,"d":"7.00E-79"},1,1,"hypD","Hydrogenase maturation factor HypD","_","4Fe-4S, Iron, Iron-sulfur, Metal-binding",1610901,"Azotobacter vinelandii","ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW",17,339,344,31,365,379]
[null,"P42033","IPMed?",0.88391,0.97384,40.3,{"v":2e-76,"d":"2.00E-76"},2,1,"hupD","Hydrogenase expression/formation protein HupD","_","Metal-binding",1526470,"Azotobacter chroococcum mcd 1","_",17,339,344,31,365,379]
[null,"P31903","IPMed?",0.90501,0.99709,39.94,{"v":1e-75,"d":"1.00E-75"},3,1,"hypD","Hydrogenase maturation factor HypD","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Plasmid, Reference proteome","8352644, 12948488","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337",13,339,344,27,366,379]
[null,"Q9ANP1","_",0.89474,0.98837,38.24,{"v":8e-75,"d":"8.00E-75"},4,1,"hypD1","Hydrogenase maturation factor HypD1","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome","11157954, 12597275","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","USDA 110spc4 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110",17,343,344,31,370,380]
[null,"Q58400","_",0.94134,0.97965,39.47,{"v":8e-75,"d":"8.00E-75"},5,1,"_","Putative hydrogenase expression/formation protein MJ0993","_","Complete proteome, Metal-binding, 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",16,343,344,27,357,358]
[null,"P24192","IPMed?",0.8874,0.96221,41.69,{"v":1e-74,"d":"1.00E-74"},6,1,"hypD","Hydrogenase maturation factor HypD","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome","1849603, 9278503, 16738553, 9298644, 12441107, 15504408, 16412426, 23022438, 23597401","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",15,339,344,34,364,373]
[null,"P40598","IPMed?",0.85714,0.9593,40.3,{"v":5E-74,"d":"5.00E-74"},7,1,"hypD","Hydrogenase maturation factor HypD","_","4Fe-4S, Iron, Iron-sulfur, Metal-binding",8326860,"Rhizobium leguminosarum bv. viciae","128c53",19,335,344,33,362,385]
[null,"P26411","IPMed?",0.88859,0.97384,38.51,{"v":8E-73,"d":"8.00E-73"},8,1,"hypD","Hydrogenase maturation factor HypD","_","4Fe-4S, Iron, Iron-sulfur, Metal-binding",8497190,"Rhodobacter capsulatus","ATCC 33303 / B10",15,339,344,34,368,377]
[null,"P31904","IPMed?",0.88421,0.97674,38.1,{"v":7E-72,"d":"7.00E-72"},9,1,"hypD2","Hydrogenase maturation factor HypD2","_","4Fe-4S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Reference proteome","12597275, 8510650","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110 / CB1809",15,335,344,29,362,380]
[]
["CLOSTRIBL6_v1_2708","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P40595","IPMed?",0.97654,1.01524,50.75,{"v":7e-98,"d":"7.00E-98"},1,1,"hypE","Carbamoyl dehydratase HypE","4.2.1.-","Lyase",7906310,"Azotobacter vinelandii","ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW",3,328,328,11,341,341]
[null,"P31905","IPMed?",0.94872,1.01524,49.85,{"v":7e-95,"d":"7.00E-95"},2,1,"hypE","Carbamoyl dehydratase HypE","4.2.1.-","Complete proteome, Lyase, Plasmid, Reference proteome","8352644, 12948488, 8021224","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337",2,328,328,19,351,351]
[null,"P26412","IPMed?",0.98529,1.02134,46.87,{"v":7e-95,"d":"7.00E-95"},3,1,"hypE","Carbamoyl dehydratase HypE","4.2.1.-","Lyase",8497190,"Rhodobacter capsulatus","ATCC 33303 / B10",2,328,328,7,340,340]
[null,"P42034","IPMed?",0.97654,1.01524,49.55,{"v":8e-95,"d":"8.00E-95"},4,1,"hupE","Hydrogenase expression/formation protein HupE","_","_",1526470,"Azotobacter chroococcum mcd 1","_",3,328,328,11,341,341]
[null,"P40599","IPMed?",0.95429,1.01829,48.5,{"v":1e-94,"d":"1.00E-94"},5,1,"hypE","Carbamoyl dehydratase HypE","4.2.1.-","Lyase",8326860,"Rhizobium leguminosarum bv. viciae","128c53 / B10",2,328,328,18,350,350]
[null,"P24193","IPMed?",1.00298,1.02744,47.77,{"v":1e-94,"d":"1.00E-94"},6,1,"hypE","Carbamoyl dehydratase HypE","4.2.1.-","3D-structure, Complete proteome, Direct protein sequencing, Lyase, Reference proteome","1849603, 9278503, 16738553, 15291820, 9298644, 12586941, 15504408, 16412426, 18065529","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",3,328,328,4,336,336]
[null,"P31906","IPMed?",0.95954,1.0122,49.7,{"v":1E-91,"d":"1.00E-91"},7,1,"hypE","Carbamoyl dehydratase HypE","4.2.1.-","Complete proteome, Lyase, Reference proteome","8510650, 7906310, 12597275","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","CB1809 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110",3,328,328,15,346,346]
[null,"Q58089","_",1.00597,1.02744,45.1,{"v":2e-89,"d":"2.00E-89"},8,1,"_","Putative hydrogenase expression/formation protein MJ0676","_","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",1,328,328,1,335,335]
[null,"P55881","IPMed?",0.66159,0.66769,24.88,7e-09,9,1,"thiL","Thiamine-monophosphate kinase","2.7.4.16","ATP-binding, Complete proteome, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Thiamine biosynthesis, Transferase","9188462, 11677609","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / LT2 / SGSC1412 / ATCC 700720",40,243,328,36,243,325]
[null,"O05514","IPMed?",0.78354,0.79077,22.96,7e-09,10,1,"thiL","Thiamine-monophosphate kinase","2.7.4.16","ATP-binding, Complete proteome, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Thiamine biosynthesis, Transferase","9202461, 9384377, 8419296","Bacillus subtilis (strain 168)","168 / JH642 / 168",64,308,328,61,309,325]
[null,"P0AGG0","IPMed?",0.66463,0.67077,23.85,3e-08,11,1,"thiL","Thiamine-monophosphate kinase","2.7.4.16","ATP-binding, Complete proteome, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Thiamine biosynthesis, Transferase","9278503, 16738553, 4567662, 6284709","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12",40,243,328,36,243,325]

{"sheet":"UniFIRE ","index":7,"n_rows":189,"n_cols":8,"rows_kept":189}
["CLOSTRIBL6_v1_2713","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:0004459","_","_","MF_00488","HAMAP"]
[null,"UR000103159","GO","GO:0006096","_","_","MF_00488","HAMAP"]
[null,"UR000000418","keyword","Oxidoreductase","_","_","RU003369","RuleBase"]
[null,"UR000103159","keyword","Oxidoreductase","_","_","MF_00488","HAMAP"]
[null,"UR000103159","keyword","NAD","_","_","MF_00488","HAMAP"]
[null,"UR000103159","keyword","Cytoplasm","_","_","MF_00488","HAMAP"]
[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,"UR000103159","similarity","Belongs to the LDH/MDH superfamily. LDH family","_","_","MF_00488","HAMAP"]
[null,"UR000000418","similarity","Belongs to the LDH/MDH superfamily","_","_","RU003369","RuleBase"]
[null,"UR000103159","site actif","Proton acceptor",178,178,"MF_00488","HAMAP"]
[null,"UR000103159","site binding","Substrate",91,91,"MF_00488","HAMAP"]
[null,"UR000103159","site binding","NAD or substrate",123,123,"MF_00488","HAMAP"]
[null,"UR000103159","site binding","Substrate",154,154,"MF_00488","HAMAP"]
[null,"UR000103159","site binding","Substrate",233,233,"MF_00488","HAMAP"]
[null,"UR000103159","subcellular location","Cytoplasm","_","_","MF_00488","HAMAP"]
[null,"UR000103159","subunit","Homotetramer","_","_","MF_00488","HAMAP"]
[]
["CLOSTRIBL6_v1_0279","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","Oxidoreductase","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Electron 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"]
[]
["CLOSTRIBL6_v1_0126","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"SAAS00649305","keyword","Oxidoreductase"]
[]
["CLOSTRIBL6_v1_0127","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"]
[]
["CLOSTRIBL6_v1_0555","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"SAAS00649305","keyword","Oxidoreductase"]
[]
["CLOSTRIBL6_v1_0556","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"]
[]
["CLOSTRIBL6_v1_0871","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"SAAS00649305","keyword","Oxidoreductase"]
[]
["CLOSTRIBL6_v1_2953","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"SAAS00093898","keyword","Oxidoreductase"]
[null,"SAAS00573311","similarity","Belongs to the LDH2/MDH2 oxidoreductase family"]
[]
["CLOSTRIBL6_v1_0031","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000000628","similarity","Belongs to the enoyl-CoA hydratase/isomerase family","_","_","RU003707","RuleBase"]
[]
["CLOSTRIBL6_v1_1904","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"SAAS00804701","keyword","Electron transport"]
[null,"SAAS00804703","keyword","Iron"]
[null,"SAAS00804711","keyword","Metal-binding"]
[null,"SAAS00804702","keyword","Transport"]
[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","Flavoprotein","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Oxidoreductase","_","_","RU362125","RuleBase"]
[null,"UR000170765","similarity","Belongs to the acyl-CoA dehydrogenase family","_","_","RU362125","RuleBase"]
[]
["CLOSTRIBL6_v1_3062","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","Flavoprotein","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Oxidoreductase","_","_","RU362125","RuleBase"]
[null,"UR000170765","similarity","Belongs to the acyl-CoA dehydrogenase family","_","_","RU362125","RuleBase"]
[]
["CLOSTRIBL6_v1_0135","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"]
[]
["CLOSTRIBL6_v1_3216","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","FAD","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Oxidoreductase","_","_","RU362125","RuleBase"]
[null,"UR000170765","similarity","Belongs to the acyl-CoA dehydrogenase family","_","_","RU362125","RuleBase"]
[]
["CLOSTRIBL6_v1_2270","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000414148","keyword","Hydrolase","_","_","PRU01106","ProRule"]
[]
["CLOSTRIBL6_v1_0258","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"SAAS00617120","cofactor","Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883"]
[null,"SAAS00617118","keyword","4Fe-4S"]
[null,"SAAS00617117","keyword","Iron"]
[null,"SAAS00617121","keyword","Iron-sulfur"]
[null,"SAAS00617119","keyword","Metal-binding"]
[]
["CLOSTRIBL6_v1_2260","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[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"]
[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:0008776","_","_","MF_00020","HAMAP"]
[null,"UR000037499","GO","GO:0016310","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Cytoplasm","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","ATP-binding","_","_","MF_00020","HAMAP"]
[null,"UR000000717","keyword","Transferase","_","_","RU003835","RuleBase"]
[null,"UR000037499","keyword","Kinase","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Nucleotide-binding","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Metal-binding","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Transferase","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Magnesium","_","_","MF_00020","HAMAP"]
[null,"UR000000717","keyword","Kinase","_","_","RU003835","RuleBase"]
[null,"UR000037499","metal binding","Magnesium",7,7,"MF_00020","HAMAP"]
[null,"UR000037499","metal binding","Magnesium",386,386,"MF_00020","HAMAP"]
[null,"UR000037499","nucleotide binding","ATP",208,212,"MF_00020","HAMAP"]
[null,"UR000037499","nucleotide binding","ATP",283,285,"MF_00020","HAMAP"]
[null,"UR000037499","nucleotide binding","ATP",331,335,"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,"UR000037499","similarity","Belongs to the acetokinase family","_","_","MF_00020","HAMAP"]
[null,"UR000000717","similarity","Belongs to the acetokinase family","_","_","RU003835","RuleBase"]
[null,"UR000037499","site","Transition state stabilizer",180,180,"MF_00020","HAMAP"]
[null,"UR000037499","site","Transition state stabilizer",241,241,"MF_00020","HAMAP"]
[null,"UR000037499","site actif","Proton donor/acceptor",148,148,"MF_00020","HAMAP"]
[null,"UR000037499","site binding","ATP",14,14,"MF_00020","HAMAP"]
[null,"UR000037499","site binding","Substrate",91,91,"MF_00020","HAMAP"]
[null,"UR000037499","subcellular location","Cytoplasm","_","_","MF_00020","HAMAP"]
[null,"UR000037499","subunit","Homodimer","_","_","MF_00020","HAMAP"]
[]
["CLOSTRIBL6_v1_1872","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"SAAS00923789","keyword","Acyltransferase"]
[null,"SAAS00923780","keyword","Transferase"]
[]
["CLOSTRIBL6_v1_2186","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000132767","GO","GO:0008774","_","_","PIRNR000111","PIR"]
[null,"UR000132767","GO","GO:0004022","_","_","PIRNR000111","PIR"]
[null,"UR000132767","keyword","Oxidoreductase","_","_","PIRNR000111","PIR"]
[null,"UR000132767","product name","Aldehyde-alcohol dehydrogenase","_","_","PIRNR000111","PIR"]
[null,"UR000132767","similarity","In the N-terminal section; belongs to the aldehyde dehydrogenase family","_","_","PIRNR000111","PIR"]
[null,"UR000132767","similarity","In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family","_","_","PIRNR000111","PIR"]
[]
["CLOSTRIBL6_v1_1351","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000000406","keyword","Oxidoreductase","_","_","RU003345","RuleBase"]
[null,"UR000000406","similarity","Belongs to the aldehyde dehydrogenase family","_","_","RU003345","RuleBase"]
[]
["CLOSTRIBL6_v1_2699","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000000066","keyword","Transmembrane","_","_","RU000320","RuleBase"]
[null,"UR000000066","subcellular location","Membrane; Multi-pass membrane protein","_","_","RU000320","RuleBase"]
[]
["CLOSTRIBL6_v1_2703","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000000608","keyword","Oxidoreductase","_","_","RU003685","RuleBase"]
[null,"UR000000608","keyword","NAD","_","_","RU003685","RuleBase"]
[null,"UR000000608","similarity","Belongs to the complex I 49 kDa subunit family","_","_","RU003685","RuleBase"]
[]
["CLOSTRIBL6_v1_2705","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000329322","GO","GO:0016743","_","_","PIRNR006256","PIR"]
[null,"UR000329322","GO","GO:0046944","_","_","PIRNR006256","PIR"]
[null,"UR000400738","GO","GO:0016787","_","_","PRU00520","ProRule"]
[null,"UR000400738","keyword","Hydrolase","_","_","PRU00520","ProRule"]
[null,"UR000329322","product - EC number","6.2.-.-","_","_","PIRNR006256","PIR"]
[null,"UR000400738","product - EC number","3.6.1.7","_","_","PRU00520","ProRule"]
[null,"UR000329322","product name","Carbamoyltransferase","_","_","PIRNR006256","PIR"]
[null,"UR000329322","similarity","Belongs to the carbamoyltransferase HypF family","_","_","PIRNR006256","PIR"]
[null,"UR000400738","site actif","_",17,17,"PRU00520","ProRule"]
[null,"UR000400738","site actif","_",35,35,"PRU00520","ProRule"]

{"sheet":"PRIAM EC number","index":8,"n_rows":258,"n_cols":15,"rows_kept":258}
["CLOSTRIBL6_v1_2713","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":1e-124,"d":"1.00E-124"},53,1,316,316,"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":1e-43,"d":"1.00E-43"},30,43,310,268,"Malate dehydrogenase","Malic dehydrogenase","(S)-malate + NAD(+) = oxaloacetate + NADH","_","-!- Also oxidizes some other 2-hydroxydicarboxylic acids"]
[null,"1.1.1.82","no",1,322,{"v":9e-19,"d":"9.00E-19"},20,44,283,240,"Malate dehydrogenase (NADP(+))","NADP-linked malate dehydrogenase","(S)-malate + NADP(+) = oxaloacetate + NADPH","_","-!- Activated by light"]
[]
["CLOSTRIBL6_v1_0279","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",1,1928,0,45,8,1182,1175,"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",1,1803,0,47,2,1182,1181,"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":1e-45,"d":"1.00E-45"},30,5,380,376,"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 fo"]
[null,"1.2.7.7","no",4,328,{"v":4e-26,"d":"4.00E-26"},23,6,329,324,"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. -!"]
[]
["CLOSTRIBL6_v1_3009","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":2e-48,"d":"2.00E-48"},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 fo"]
[null,"1.2.7.7","no",1,187,{"v":2e-38,"d":"2.00E-38"},40,5,191,187,"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. -!"]
[]
["CLOSTRIBL6_v1_3011","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-125,"d":"1.00E-125"},48,7,391,385,"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 fo"]
[null,"1.2.7.7","no",4,328,{"v":1E-70,"d":"1.00E-70"},39,7,323,317,"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. -!"]
[null,"1.16.1.5","no",1,1803,{"v":5e-37,"d":"5.00E-37"},29,5,371,367,"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,"1.2.1.51","no",1,1928,{"v":2e-36,"d":"2.00E-36"},27,13,358,346,"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",3,344,{"v":1e-21,"d":"1.00E-21"},25,5,309,305,"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 sp"]
[]
["CLOSTRIBL6_v1_3012","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":2e-37,"d":"2.00E-37"},36,22,227,206,"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. -!"]
[null,"1.2.1.51","no",1,1928,{"v":8e-17,"d":"8.00E-17"},27,107,307,201,"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",1,1803,8E-14,28,107,307,201,"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",2,265,5e-12,26,19,223,205,"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 sp"]
[]
["CLOSTRIBL6_v1_0126","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":6e-97,"d":"6.00E-97"},55,1,277,277,"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-77,"d":"2.00E-77"},41,2,277,276,"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":4e-62,"d":"4.00E-62"},38,2,277,276,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"1.1.1.211","no",1,763,{"v":2e-38,"d":"2.00E-38"},35,3,277,275,"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)"]
[]
["CLOSTRIBL6_v1_0127","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-150,"d":"1.00E-150"},63,6,394,389,"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 w"]
[null,"2.3.1.16","no",1,420,{"v":1e-104,"d":"1.00E-104"},40,3,394,392,"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 reactio"]
[null,"2.3.1.174","no",1,401,{"v":4e-88,"d":"4.00E-88"},44,3,394,392,"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"]
[]
["CLOSTRIBL6_v1_0555","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.1.35","high",1,301,{"v":9e-65,"d":"9.00E-65"},33,6,291,286,"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,"1.1.1.157","no",1,280,{"v":4e-62,"d":"4.00E-62"},36,9,291,283,"3-hydroxybutyryl-CoA dehydrogenase","Beta-hydroxybutyryl-CoA dehydrogenase. BHBD","(S)-3-hydroxybutanoyl-CoA + NADP(+) = 3-acetoacetyl-CoA + NADPH","_","_"]
[null,"5.1.2.3","no",1,707,{"v":6E-57,"d":"6.00E-57"},32,5,298,294,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"1.1.1.211","no",1,763,{"v":1e-33,"d":"1.00E-33"},30,4,298,295,"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)"]
[]
["CLOSTRIBL6_v1_0556","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-123,"d":"1.00E-123"},53,8,396,389,"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 w"]
[null,"2.3.1.16","no",1,420,{"v":1e-112,"d":"1.00E-112"},45,3,397,395,"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 reactio"]
[null,"2.3.1.174","no",1,401,{"v":1e-104,"d":"1.00E-104"},48,3,397,395,"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"]
[]
["CLOSTRIBL6_v1_0558","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-60,"d":"3.00E-60"},46,3,262,260,"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-56,"d":"3.00E-56"},39,8,261,254,"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":2E-55,"d":"2.00E-55"},39,15,261,247,"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":5e-40,"d":"5.00E-40"},39,12,203,192,"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 canno"]
[null,"5.1.2.3","no",1,707,{"v":2e-36,"d":"2.00E-36"},38,14,203,190,"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"},33,5,259,255,"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 coenzym"]
[null,"1.1.1.211","no",1,763,{"v":6e-25,"d":"6.00E-25"},34,7,213,207,"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":1e-21,"d":"1.00E-21"},29,6,178,173,"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-19,"d":"1.00E-19"},27,28,261,234,"Transferred entry: 7.2.4.3","_","_","_","_"]
[null,"4.2.1.100","no",1,258,{"v":2e-17,"d":"2.00E-17"},29,13,262,250,"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",43,544,8e-12,28,3,182,180,"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"]
[]
["CLOSTRIBL6_v1_0559","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.8.3.16","high",1,420,{"v":2e-40,"d":"2.00E-40"},27,2,399,398,"Formyl-CoA transferase","Formyl-CoA oxalate CoA-transferase. Formyl-coenzyme A transferase","Formyl-CoA + oxalate = formate + oxalyl-CoA","_","-!- The enzyme from Oxalobacter formigenes can also catalyze the transfer of CoA from formyl-CoA to succinate"]
[null,"5.1.99.4","no",1,382,{"v":5e-25,"d":"5.00E-25"},23,4,400,397,"Alpha-methylacyl-CoA racemase","_","(2S)-2-methylacyl-CoA = (2R)-2-methylacyl-CoA","_","-!- Alpha-methyl-branched acyl-CoA derivatives with chain lengths of more than C(10) are substrates. -!- Also active toward some aromatic compounds (e.g. ibuprofen) and bile acid intermediates, such as trihydroxycoprostanoyl-CoA. -!- Not active toward fre"]
[null,"3.1.2.26","no",1,426,2E-14,22,4,395,392,"Transferred entry: 2.8.3.25","_","_","_","_"]
[]
["CLOSTRIBL6_v1_0871","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-60,"d":"1.00E-60"},38,8,288,281,"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":5e-57,"d":"5.00E-57"},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":9e-42,"d":"9.00E-42"},30,2,290,289,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"1.1.1.211","no",1,763,{"v":4e-32,"d":"4.00E-32"},28,4,291,288,"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)"]
[]
["CLOSTRIBL6_v1_2953","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.1.37","high",7,347,{"v":8e-77,"d":"8.00E-77"},39,4,342,339,"Malate dehydrogenase","Malic dehydrogenase","(S)-malate + NAD(+) = oxaloacetate + NADH","_","-!- Also oxidizes some other 2-hydroxydicarboxylic acids"]
[null,"1.1.1.272","no",1,341,{"v":4e-67,"d":"4.00E-67"},38,4,333,330,"D-2-hydroxyacid dehydrogenase (NADP(+))","_","An (R)-2-hydroxycarboxylate + NADP(+) = a 2-oxocarboxylate + NADPH","_","-!- This enzyme, characterized from the halophilic archaeon Haloferax mediterranei and the mold Aspergillus oryzae, catalyzes a reversible stereospecific reduction of 2-oxocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids. -!- The enzyme"]
[null,"1.1.1.82","no",6,339,{"v":9E-60,"d":"9.00E-60"},36,4,333,330,"Malate dehydrogenase (NADP(+))","NADP-linked malate dehydrogenase","(S)-malate + NADP(+) = oxaloacetate + NADPH","_","-!- Activated by light"]
[null,"1.1.1.154","no",1,349,{"v":1e-55,"d":"1.00E-55"},34,3,335,333,"Ureidoglycolate dehydrogenase","_","(S)-ureidoglycolate + NAD(P)(+) = oxalurate + NAD(P)H","_","_"]
[null,"1.1.1.27","no",13,349,{"v":4e-33,"d":"4.00E-33"},30,10,309,300,"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,"1.1.1.130","no",1,332,{"v":2e-31,"d":"2.00E-31"},28,7,333,327,"3-dehydro-L-gulonate 2-dehydrogenase","2,3-diketo-L-gulonate reductase. 3-keto-L-gulonate dehydrogenase","3-dehydro-L-gulonate + NAD(P)(+) = (4R,5S)-4,5,6-trihydroxy-2,3- dioxohexanoate + NAD(P)H","_","_"]
[]
["CLOSTRIBL6_v1_0031","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":9e-35,"d":"9.00E-35"},29,9,262,254,"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,"4.1.3.36","no",1,263,{"v":5e-32,"d":"5.00E-32"},31,3,233,231,"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 coenzym"]
[null,"5.3.3.8","no",1,265,{"v":8e-31,"d":"8.00E-31"},27,8,221,214,"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 canno"]
[null,"4.2.1.55","no",1,261,{"v":1e-29,"d":"1.00E-29"},31,3,262,260,"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,"3.1.2.4","no",1,408,{"v":7e-27,"d":"7.00E-27"},31,5,199,195,"3-hydroxyisobutyryl-CoA hydrolase","_","3-hydroxy-2-methylpropanoyl-CoA + H(2)O = CoA + 3-hydroxy-2- methylpropanoate","_","-!- Also hydrolyzes 3-hydroxypropanoyl-CoA"]
[null,"5.1.2.3","no",1,707,{"v":2e-25,"d":"2.00E-25"},29,10,208,199,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"4.2.1.18","no",1,276,{"v":4e-24,"d":"4.00E-24"},27,15,236,222,"Methylglutaconyl-CoA hydratase","_","(S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA + H(2)O","_","_"]
[null,"1.1.1.211","no",1,763,{"v":5e-19,"d":"5.00E-19"},28,6,204,199,"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)"]
[]
["CLOSTRIBL6_v1_1904","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"},57,1,378,378,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":4e-85,"d":"4.00E-85"},36,7,373,367,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":1e-81,"d":"1.00E-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":1e-67,"d":"1.00E-67"},36,4,379,376,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":4e-61,"d":"4.00E-61"},36,6,381,376,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":1e-37,"d":"1.00E-37"},29,1,378,378,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":4e-27,"d":"4.00E-27"},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)"]
[]
["CLOSTRIBL6_v1_3062","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-141,"d":"1.00E-141"},54,1,378,378,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":1e-86,"d":"1.00E-86"},38,5,373,369,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":7e-80,"d":"7.00E-80"},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":4e-61,"d":"4.00E-61"},34,4,381,378,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":1e-57,"d":"1.00E-57"},35,6,378,373,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":3e-35,"d":"3.00E-35"},28,1,378,378,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":1e-28,"d":"1.00E-28"},22,14,378,365,"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)"]
[]
["CLOSTRIBL6_v1_0135","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-156,"d":"1.00E-156"},61,1,379,379,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":1E-97,"d":"1.00E-97"},41,5,379,375,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":2e-89,"d":"2.00E-89"},41,3,374,372,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":2e-62,"d":"2.00E-62"},36,6,374,369,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":5E-52,"d":"5.00E-52"},29,4,377,374,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":9e-45,"d":"9.00E-45"},32,1,378,378,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":5e-28,"d":"5.00E-28"},22,1,379,379,"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)"]
[]
["CLOSTRIBL6_v1_3216","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-147,"d":"1.00E-147"},58,1,375,375,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":1e-94,"d":"1.00E-94"},42,19,373,355,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":5e-85,"d":"5.00E-85"},39,3,374,372,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":4e-59,"d":"4.00E-59"},34,5,374,370,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":7e-53,"d":"7.00E-53"},29,4,373,370,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":4E-41,"d":"4.00E-41"},30,1,374,374,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":4e-20,"d":"4.00E-20"},20,41,374,334,"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)"]
[]
["CLOSTRIBL6_v1_3220","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":4e-76,"d":"4.00E-76"},32,33,469,437,"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":4e-28,"d":"4.00E-28"},31,44,243,200,"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,"1.17.99.1","no",1,521,2e-13,28,33,241,209,"Transferred entry: 1.17.9.1","_","_","_","_"]
[]
["CLOSTRIBL6_v1_2270","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","medium",2,549,5e-14,26,18,153,136,"Acetyl-CoA hydrolase","Acetyl-CoA acylase. Acetyl-CoA deacylase","Acetyl-CoA + H(2)O = CoA + acetate","_","_"]
[]
["CLOSTRIBL6_v1_0258","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":2e-24,"d":"2.00E-24"},23,5,298,294,"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"]
[]
["CLOSTRIBL6_v1_0260","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-31,"d":"1.00E-31"},25,123,440,318,"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"]
[]
["CLOSTRIBL6_v1_1906","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-31,"d":"5.00E-31"},26,104,377,274,"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"]
[]
["CLOSTRIBL6_v1_2017","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":7e-37,"d":"7.00E-37"},30,124,463,340,"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"]
[]
["CLOSTRIBL6_v1_2260","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,{"v":1E-172,"d":"1.00E-172"},59,2,400,399,"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-105,"d":"1.00E-105"},44,3,393,391,"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":1e-21,"d":"1.00E-21"},32,175,332,158,"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)"]
[]
["CLOSTRIBL6_v1_1872","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":8e-96,"d":"8.00E-96"},49,3,320,318,"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-11,25,5,317,313,"Phosphate butyryltransferase","Phosphotransbutyrylase","Butanoyl-CoA + phosphate = CoA + butanoylphosphate","_","_"]
[]
["CLOSTRIBL6_v1_0095","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":2e-60,"d":"2.00E-60"},33,10,387,378,"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-44,"d":"5.00E-44"},30,8,387,380,"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":2e-42,"d":"2.00E-42"},28,6,378,373,"Methanol dehydrogenase","_","Methanol + NAD(+) = formaldehyde + NADH","_","_"]
[null,"1.1.99.24","no",1,479,{"v":6e-40,"d":"6.00E-40"},25,16,383,368,"Hydroxyacid-oxoacid transhydrogenase","_","(1) (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2- hydroxyglutarate. (2) 4-hydroxybutanoate + 2-oxoglutarate = succinic semialdehyde + (R)-2- hydroxyglutarate","_","_"]
[null,"1.1.1.77","no",1,383,{"v":9e-40,"d":"9.00E-40"},30,16,383,368,"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,"1.1.1.202","no",1,387,{"v":5e-38,"d":"5.00E-38"},28,9,387,379,"1,3-propanediol dehydrogenase","1,3-propanediol oxidoreductase. 3-hydroxypropionaldehyde reductase","Propane-1,3-diol + NAD(+) = 3-hydroxypropanal + NADH","_","_"]
[null,"1.1.1.61","no",1,371,{"v":2e-37,"d":"2.00E-37"},29,72,387,316,"4-hydroxybutyrate dehydrogenase","_","4-hydroxybutanoate + NAD(+) = succinate semialdehyde + NADH","_","_"]
[null,"1.3.1.32","no",1,356,{"v":4e-26,"d":"4.00E-26"},26,78,382,305,"Maleylacetate reductase","Maleolylacetate reductase","3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H","_","_"]
[]
["CLOSTRIBL6_v1_1804","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":3e-54,"d":"3.00E-54"},35,6,284,279,"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":1e-48,"d":"1.00E-48"},34,3,361,359,"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":3e-44,"d":"3.00E-44"},32,5,388,384,"Methanol dehydrogenase","_","Methanol + NAD(+) = formaldehyde + NADH","_","_"]
[null,"1.2.1.10","no",2,875,{"v":4e-38,"d":"4.00E-38"},30,8,354,347,"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-37,"d":"8.00E-37"},28,52,316,265,"Hydroxyacid-oxoacid transhydrogenase","_","(1) (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2- hydroxyglutarate. (2) 4-hydroxybutanoate + 2-oxoglutarate = succinic semialdehyde + (R)-2- hydroxyglutarate","_","_"]
[null,"1.1.1.77","no",1,383,{"v":5e-33,"d":"5.00E-33"},34,14,284,271,"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,"1.3.1.32","no",1,356,{"v":2e-20,"d":"2.00E-20"},28,3,390,388,"Maleylacetate reductase","Maleolylacetate reductase","3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H","_","_"]
[null,"1.1.1.61","no",1,371,{"v":1e-17,"d":"1.00E-17"},23,92,389,298,"4-hydroxybutyrate dehydrogenase","_","4-hydroxybutanoate + NAD(+) = succinate semialdehyde + NADH","_","_"]
[]
["CLOSTRIBL6_v1_2186","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",2,875,0,53,14,865,852,"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,"1.1.1.1","no",9,419,{"v":1e-148,"d":"1.00E-148"},47,462,865,404,"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,"1.1.1.77","no",1,383,{"v":3E-52,"d":"3.00E-52"},33,469,865,397,"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,"1.1.1.202","no",1,387,{"v":2E-51,"d":"2.00E-51"},35,487,865,379,"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":5E-51,"d":"5.00E-51"},33,459,864,406,"Methanol dehydrogenase","_","Methanol + NAD(+) = formaldehyde + NADH","_","_"]
[null,"1.2.1.16","no",1,421,{"v":3E-37,"d":"3.00E-37"},21,18,406,389,"Succinate-semialdehyde dehydrogenase (NAD(P)(+))","_","Succinate semialdehyde + NAD(P)(+) + H(2)O = succinate + NAD(P)H","_","_"]
[null,"1.3.1.32","no",1,356,{"v":2e-29,"d":"2.00E-29"},26,530,868,339,"Maleylacetate reductase","Maleolylacetate reductase","3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H","_","_"]
[null,"1.1.99.24","no",1,479,{"v":2e-26,"d":"2.00E-26"},24,519,850,332,"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":2e-26,"d":"2.00E-26"},34,526,747,222,"4-hydroxybutyrate dehydrogenase","_","4-hydroxybutanoate + NAD(+) = succinate semialdehyde + NADH","_","_"]
[null,"1.2.1.5","no",1,407,7e-15,22,112,407,296,"Aldehyde dehydrogenase (NAD(P)(+))","_","An aldehyde + NAD(P)(+) + H(2)O = a carboxylate + NAD(P)H","_","_"]
[null,"1.2.1.3","no",1,462,4e-13,22,89,433,345,"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"]
[null,"1.2.1.22","no",1,475,4e-12,20,59,407,349,"Lactaldehyde dehydrogenase","_","(S)-lactaldehyde + NAD(+) + H(2)O = (S)-lactate + NADH","_","_"]
[null,"1.2.1.41","no",1,427,8e-11,23,136,397,262,"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","_","_"]
[]
["CLOSTRIBL6_v1_2879","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":1e-101,"d":"1.00E-101"},42,9,377,369,"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,"1.1.1.244","no",1,381,{"v":1e-82,"d":"1.00E-82"},41,9,376,368,"Methanol dehydrogenase","_","Methanol + NAD(+) = formaldehyde + NADH","_","_"]
[null,"1.1.1.202","no",1,387,{"v":1e-77,"d":"1.00E-77"},40,7,377,371,"1,3-propanediol dehydrogenase","1,3-propanediol oxidoreductase. 3-hydroxypropionaldehyde reductase","Propane-1,3-diol + NAD(+) = 3-hydroxypropanal + NADH","_","_"]
[null,"1.2.1.10","no",2,875,{"v":5e-75,"d":"5.00E-75"},35,9,377,369,"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,"1.1.1.77","no",1,383,{"v":5e-67,"d":"5.00E-67"},38,18,377,360,"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,"1.3.1.32","no",1,356,{"v":2e-39,"d":"2.00E-39"},26,10,380,371,"Maleylacetate reductase","Maleolylacetate reductase","3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H","_","_"]
[null,"1.1.99.24","no",1,479,{"v":1e-33,"d":"1.00E-33"},27,7,376,370,"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":9e-22,"d":"9.00E-22"},33,95,277,183,"4-hydroxybutyrate dehydrogenase","_","4-hydroxybutanoate + NAD(+) = succinate semialdehyde + NADH","_","_"]
[null,"1.1.1.6","no",1,365,6E-11,22,9,369,361,"Glycerol dehydrogenase","NAD-linked glycerol dehydrogenase","Glycerol + NAD(+) = glycerone + NADH","_","-!- Also acts on 1,2-propanediol"]
[]
["CLOSTRIBL6_v1_3434","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":1E-35,"d":"1.00E-35"},23,1,389,389,"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-27,"d":"5.00E-27"},25,57,350,294,"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,"1.1.1.202","no",1,387,{"v":7e-27,"d":"7.00E-27"},27,14,350,337,"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":2e-23,"d":"2.00E-23"},26,13,358,346,"Methanol dehydrogenase","_","Methanol + NAD(+) = formaldehyde + NADH","_","_"]
[null,"1.3.1.32","no",1,356,{"v":3e-16,"d":"3.00E-16"},22,1,371,371,"Maleylacetate reductase","Maleolylacetate reductase","3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H","_","_"]
[null,"1.1.1.77","no",1,383,{"v":4e-16,"d":"4.00E-16"},23,14,350,337,"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",1,479,5e-14,21,8,253,246,"Hydroxyacid-oxoacid transhydrogenase","_","(1) (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2- hydroxyglutarate. (2) 4-hydroxybutanoate + 2-oxoglutarate = succinic semialdehyde + (R)-2- hydroxyglutarate","_","_"]
[]
["CLOSTRIBL6_v1_1351","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.2.1.3","high",1,462,{"v":2e-97,"d":"2.00E-97"},36,44,486,443,"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"]
[null,"1.2.1.16","no",1,421,{"v":4e-97,"d":"4.00E-97"},38,53,465,413,"Succinate-semialdehyde dehydrogenase (NAD(P)(+))","_","Succinate semialdehyde + NAD(P)(+) + H(2)O = succinate + NAD(P)H","_","_"]
[null,"1.2.1.8","no",1,493,{"v":7e-90,"d":"7.00E-90"},34,20,482,463,"Betaine-aldehyde dehydrogenase","BADH. Betaine aldehyde dehydrogenase. Betaine aldehyde oxidase","Betaine aldehyde + NAD(+) + H(2)O = betaine + NADH","_","-!- In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. -!- This enzyme is involved in the second step and appears to be the same in plants, ani"]
[null,"1.2.1.19","no",1,481,{"v":2E-87,"d":"2.00E-87"},35,21,482,462,"Aminobutyraldehyde dehydrogenase","1-pyrroline dehydrogenase. 4-aminobutanal dehydrogenase. ABALDH. Gamma-guanidinobutyraldehyde dehydrogenase","4-aminobutanal + NAD(+) + H(2)O = 4-aminobutanoate + NADH","_","-!- The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates. -!- The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54). -!- As 1-pyrroline"]
[null,"1.2.1.22","no",1,475,{"v":1E-83,"d":"1.00E-83"},33,20,482,463,"Lactaldehyde dehydrogenase","_","(S)-lactaldehyde + NAD(+) + H(2)O = (S)-lactate + NADH","_","_"]
[null,"1.2.1.24","no",1,537,{"v":6E-79,"d":"6.00E-79"},35,20,482,463,"Succinate-semialdehyde dehydrogenase (NAD(+))","_","Succinate semialdehyde + NAD(+) + H(2)O = succinate + NADH","_","-!- This enzyme participates in the degradation of glutamate and 4-aminobutyrate. -!- It is similar to EC 1.2.1.79 and EC 1.2.1.16 but is specific for NAD(+)"]
[null,"1.2.1.21","no",1,479,{"v":8e-76,"d":"8.00E-76"},35,20,478,459,"Glycolaldehyde dehydrogenase","_","Glycolaldehyde + NAD(+) + H(2)O = glycolate + NADH","_","_"]
[null,"1.2.1.36","no",1,496,{"v":4e-67,"d":"4.00E-67"},33,30,482,453,"Retinal dehydrogenase","_","Retinal + NAD(+) + H(2)O = retinoate + NADH","FAD","-!- Acts on both the 11-trans- and 13-cis-forms of retinal"]
[null,"1.2.1.5","no",1,407,{"v":1E-62,"d":"1.00E-62"},31,150,483,334,"Aldehyde dehydrogenase (NAD(P)(+))","_","An aldehyde + NAD(P)(+) + H(2)O = a carboxylate + NAD(P)H","_","_"]
[null,"1.5.1.6","no",1,902,{"v":2e-61,"d":"2.00E-61"},30,20,482,463,"Formyltetrahydrofolate dehydrogenase","10-formyltetrahydrofolate dehydrogenase","10-formyltetrahydrofolate + NADP(+) + H(2)O = tetrahydrofolate + CO(2) + NADPH","_","_"]
[null,"1.2.1.47","no",1,494,{"v":3e-60,"d":"3.00E-60"},31,38,482,445,"4-trimethylammoniobutyraldehyde dehydrogenase","_","4-trimethylammoniobutanal + NAD(+) + H(2)O = 4-trimethylammoniobutanoate + NADH","_","_"]
[null,"1.5.1.12","no",1,531,{"v":5E-56,"d":"5.00E-56"},28,1,465,465,"Transferred entry: 1.2.1.88","_","_","_","_"]
[null,"1.2.1.9","no",1,478,{"v":2e-54,"d":"2.00E-54"},28,14,482,469,"Glyceraldehyde-3-phosphate dehydrogenase (NADP(+))","Triosephosphate dehydrogenase","D-glyceraldehyde 3-phosphate + NADP(+) + H(2)O = 3-phospho-D-glycerate + NADPH","_","_"]
[null,"1.2.1.71","no",1,476,{"v":2e-54,"d":"2.00E-54"},30,38,476,439,"Succinylglutamate-semialdehyde dehydrogenase","N-succinylglutamate 5-semialdehyde dehydrogenase. SGSD. Succinylglutamic semialdehyde dehydrogenase","N-succinyl-L-glutamate 5-semialdehyde + NAD(+) + H(2)O = N-succinyl-L- glutamate + NADH","_","-!- This is the fourth enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine. -!- This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl"]
[null,"1.2.1.27","no",1,489,{"v":6e-54,"d":"6.00E-54"},26,11,457,447,"Methylmalonate-semialdehyde dehydrogenase (CoA acylating)","Methylmalonate-semialdehyde dehydrogenase (acylating). MMSA dehydrogenase. MSDH","2-methyl-3-oxopropanoate + CoA + H(2)O + NAD(+) = propanoyl-CoA + HCO(3)(-) + NADH","_","-!- Also converts 3-oxopropanoate into acetyl-CoA. -!- The reaction occurs in two steps with the decarboxylation process preceding CoA-binding. -!- Bicarbonate rather than CO(2) is released as a final product"]
[null,"1.2.1.39","no",1,499,{"v":3E-51,"d":"3.00E-51"},28,20,469,450,"Phenylacetaldehyde dehydrogenase","_","Phenylacetaldehyde + NAD(+) + H(2)O = phenylacetate + NADH","_","_"]
[null,"1.2.1.65","no",1,483,{"v":2E-50,"d":"2.00E-50"},27,31,482,452,"Salicylaldehyde dehydrogenase","_","Salicylaldehyde + NAD(+) + H(2)O = salicylate + NADH","_","-!- Involved in the naphthalene degradation pathway in some bacteria"]
[null,"1.2.1.28","no",1,487,{"v":5e-46,"d":"5.00E-46"},29,26,478,453,"Benzaldehyde dehydrogenase (NAD(+))","_","Benzaldehyde + NAD(+) + H(2)O = benzoate + NADH","_","_"]
[null,"1.2.1.31","no",6,511,{"v":6e-42,"d":"6.00E-42"},26,28,478,451,"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,"1.2.1.18","no",1,523,{"v":2E-41,"d":"2.00E-41"},25,11,457,447,"Malonate-semialdehyde dehydrogenase (acetylating)","_","3-oxopropanoate + CoA + NAD(P)(+) = acetyl-CoA + CO(2) + NAD(P)H","_","_"]
[null,"1.2.1.68","no",1,465,{"v":3e-38,"d":"3.00E-38"},27,54,483,430,"Coniferyl-aldehyde dehydrogenase","_","Coniferyl aldehyde + H(2)O + NAD(P)(+) = ferulate + NAD(P)H","_","-!- Also oxidizes other aromatic aldehydes, but not aliphatic aldehydes"]
[null,"1.2.1.4","no",1,292,{"v":7e-22,"d":"7.00E-22"},24,35,303,269,"Aldehyde dehydrogenase (NADP(+))","_","An aldehyde + NADP(+) + H(2)O = a carboxylate + NADPH","_","_"]
[]
["CLOSTRIBL6_v1_2699","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",3,427,{"v":4e-37,"d":"4.00E-37"},23,37,424,388,"Transferred entry: 1.6.5.11","_","_","_","_"]
[]
["CLOSTRIBL6_v1_2700","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",1,349,7e-15,29,5,208,204,"Transferred entry: 1.6.5.11","_","_","_","_"]
[]
["CLOSTRIBL6_v1_2701","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",12,159,{"v":4e-32,"d":"4.00E-32"},39,15,137,123,"Transferred entry: 1.6.5.11","_","_","_","_"]
[null,"1.6.5.3","no",66,152,{"v":3E-28,"d":"3.00E-28"},36,7,137,131,"Transferred entry: 7.1.1.2","_","_","_","_"]
[null,"1.6.99.3","no",5,206,{"v":1E-27,"d":"1.00E-27"},33,7,138,132,"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"]
[]
["CLOSTRIBL6_v1_2703","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",18,410,{"v":3e-64,"d":"3.00E-64"},29,1,359,359,"Transferred entry: 1.6.5.11","_","_","_","_"]
[null,"1.6.99.3","no",2,400,{"v":3e-50,"d":"3.00E-50"},30,9,351,343,"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,"1.6.5.3","no",57,390,{"v":8e-47,"d":"8.00E-47"},29,9,351,343,"Transferred entry: 7.1.1.2","_","_","_","_"]
[null,"1.12.98.1","no",3,444,2E-14,24,21,212,192,"Coenzyme F420 hydrogenase","8-hydroxy-5-deazaflavin-reducing hydrogenase. Coenzyme F420-dependent hydrogenase. F420-reducing hydrogenase","H(2) + oxidized coenzyme F420 = reduced coenzyme F420","FAD; Fe cation; Ni(2+)","-!- The enzyme from some sources contains selenocysteine. -!- The enzyme also reduces the riboflavin analog of F420, flavins and methylviologen, but to a lesser extent. -!- The hydrogen acceptor coenzyme F420 is a deazaflavin derivative. -!- Formerly EC 1"]
[]
["CLOSTRIBL6_v1_2704","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",2,145,2E-14,27,12,107,96,"Transferred entry: 1.6.5.11","_","_","_","_"]
[]
["CLOSTRIBL6_v1_2708","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.7.4.16","high",1,336,{"v":3e-21,"d":"3.00E-21"},24,16,321,306,"Thiamine-phosphate kinase","Thiamine-monophosphate kinase","ATP + thiamine phosphate = ADP + thiamine diphosphate","_","_"]

{"sheet":"COG","index":9,"n_rows":67,"n_cols":7,"rows_kept":67}
["CDS","COG id","Score","Begin","End","Classes","Function"]
["CLOSTRIBL6_v1_3221","COG3875",246,37,282,"S","Uncharacterized conserved protein"]
["CLOSTRIBL6_v1_3223","COG1620",515,1,515,"C","L-lactate permease"]
["CLOSTRIBL6_v1_2713","COG0039",317,1,317,"C","Malate/lactate dehydrogenases"]
["CLOSTRIBL6_v1_0279","COG0674",409,1,409,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
[null,"COG1014",384,417,800,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
[null,"COG1013",381,805,1185,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
["CLOSTRIBL6_v1_3009","COG1014",192,2,193,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
["CLOSTRIBL6_v1_3010","COG1144",91,12,102,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, delta subunit"]
["CLOSTRIBL6_v1_3011","COG0674",390,2,391,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
["CLOSTRIBL6_v1_3012","COG1013",308,3,310,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
["CLOSTRIBL6_v1_0126","COG1250",278,1,278,"I","3-hydroxyacyl-CoA dehydrogenase"]
["CLOSTRIBL6_v1_0127","COG0183",395,1,395,"I","Acetyl-CoA acetyltransferase"]
["CLOSTRIBL6_v1_0555","COG1250",299,1,299,"I","3-hydroxyacyl-CoA dehydrogenase"]
["CLOSTRIBL6_v1_0556","COG0183",397,1,397,"I","Acetyl-CoA acetyltransferase"]
["CLOSTRIBL6_v1_0558","COG1024",261,2,262,"I","Enoyl-CoA hydratase/carnithine racemase"]
["CLOSTRIBL6_v1_0559","COG1804",398,2,399,"C","Predicted acyl-CoA transferases/carnitine dehydratase"]
["CLOSTRIBL6_v1_0560","COG1924",260,1,260,"I","Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain)"]
["CLOSTRIBL6_v1_0561","COG1775",383,45,427,"E","Benzoyl-CoA reductase/2-hydroxyglutaryl-CoA dehydratase subunit, BcrC/BadD/HgdB"]
["CLOSTRIBL6_v1_0562","COG1775",348,28,375,"E","Benzoyl-CoA reductase/2-hydroxyglutaryl-CoA dehydratase subunit, BcrC/BadD/HgdB"]
["CLOSTRIBL6_v1_0871","COG1250",314,1,314,"I","3-hydroxyacyl-CoA dehydrogenase"]
["CLOSTRIBL6_v1_2953","COG2055",343,3,345,"C","Malate/L-lactate dehydrogenases"]
["CLOSTRIBL6_v1_0031","COG1024",269,1,269,"I","Enoyl-CoA hydratase/carnithine racemase"]
["CLOSTRIBL6_v1_1904","COG1960",393,1,393,"I","Acyl-CoA dehydrogenases"]
[null,"COG2025",170,394,563,"C","Electron transfer flavoprotein, alpha subunit"]
[null,"COG1773",60,572,631,"C","Rubredoxin"]
["CLOSTRIBL6_v1_3062","COG1960",395,1,395,"I","Acyl-CoA dehydrogenases"]
[null,"COG2025",170,396,565,"C","Electron transfer flavoprotein, alpha subunit"]
["CLOSTRIBL6_v1_0135","COG1960",379,1,379,"I","Acyl-CoA dehydrogenases"]
["CLOSTRIBL6_v1_0136","COG2086",259,1,259,"C","Electron transfer flavoprotein, beta subunit"]
["CLOSTRIBL6_v1_0137","COG2025",339,8,346,"C","Electron transfer flavoprotein, alpha subunit"]
["CLOSTRIBL6_v1_3216","COG1960",380,1,380,"I","Acyl-CoA dehydrogenases"]
["CLOSTRIBL6_v1_3217","COG2025",331,4,334,"C","Electron transfer flavoprotein, alpha subunit"]
["CLOSTRIBL6_v1_3218","COG2086",268,1,268,"C","Electron transfer flavoprotein, beta subunit"]
["CLOSTRIBL6_v1_3220","COG0277",475,1,475,"C","FAD/FMN-containing dehydrogenases"]
["CLOSTRIBL6_v1_2270","COG1607",154,4,157,"I","Acyl-CoA hydrolase"]
["CLOSTRIBL6_v1_2820","COG2025",325,4,328,"C","Electron transfer flavoprotein, alpha subunit"]
["CLOSTRIBL6_v1_2821","COG2086",266,1,266,"C","Electron transfer flavoprotein, beta subunit"]
["CLOSTRIBL6_v1_0258","COG4624",210,32,241,"R","Iron only hydrogenase large subunit, C-terminal domain"]
[null,"COG4624",33,285,317,"R","Iron only hydrogenase large subunit, C-terminal domain"]
[null,"COG2000",32,373,404,"R","Predicted Fe-S protein"]
[null,"COG1145",31,1,31,"C","Ferredoxin"]
["CLOSTRIBL6_v1_0260","COG4624",312,143,454,"R","Iron only hydrogenase large subunit, C-terminal domain"]
[null,"COG1145",107,36,142,"C","Ferredoxin"]
["CLOSTRIBL6_v1_1906","COG4624",202,99,300,"R","Iron only hydrogenase large subunit, C-terminal domain"]
[null,"COG1145",37,62,98,"C","Ferredoxin"]
["CLOSTRIBL6_v1_2017","COG4624",304,169,472,"R","Iron only hydrogenase large subunit, C-terminal domain"]
[null,"COG1145",132,37,168,"C","Ferredoxin"]
["CLOSTRIBL6_v1_2260","COG0282",401,1,401,"C","Acetate kinase"]
["CLOSTRIBL6_v1_1872","COG0280",320,1,320,"C","Phosphotransacetylase"]
["CLOSTRIBL6_v1_0095","COG1454",384,4,387,"C","Alcohol dehydrogenase, class IV"]
["CLOSTRIBL6_v1_1804","COG1454",389,1,389,"C","Alcohol dehydrogenase, class IV"]
["CLOSTRIBL6_v1_2186","COG1012",451,7,457,"C","NAD-dependent aldehyde dehydrogenases"]
[null,"COG1454",411,458,868,"C","Alcohol dehydrogenase, class IV"]
["CLOSTRIBL6_v1_2879","COG1454",379,4,382,"C","Alcohol dehydrogenase, class IV"]
["CLOSTRIBL6_v1_3434","COG1979",393,1,393,"C","Uncharacterized oxidoreductases, Fe-dependent alcohol dehydrogenase family"]
["CLOSTRIBL6_v1_1351","COG1012",489,1,489,"C","NAD-dependent aldehyde dehydrogenases"]
["CLOSTRIBL6_v1_2699","COG1009",524,39,562,"CP","NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunit"]
["CLOSTRIBL6_v1_2700","COG0650",278,6,283,"C","Formate hydrogenlyase subunit 4"]
["CLOSTRIBL6_v1_2701","COG3260",136,10,145,"C","Ni,Fe-hydrogenase III small subunit"]
["CLOSTRIBL6_v1_2702","COG0852",79,19,97,"C","NADH:ubiquinone oxidoreductase 27 kD subunit"]
["CLOSTRIBL6_v1_2703","COG3261",355,5,359,"C","Ni,Fe-hydrogenase III large subunit"]
["CLOSTRIBL6_v1_2704","COG1143",128,3,130,"C","Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I)"]
["CLOSTRIBL6_v1_2705","COG0068",735,3,737,"O","Hydrogenase maturation factor"]
["CLOSTRIBL6_v1_2706","COG0298",70,1,70,"O","Hydrogenase maturation factor"]
["CLOSTRIBL6_v1_2707","COG0409",341,3,343,"O","Hydrogenase maturation factor"]
["CLOSTRIBL6_v1_2708","COG0309",328,1,328,"O","Hydrogenase maturation factor"]

{"sheet":"EGGNOG","index":10,"n_rows":55,"n_cols":7,"rows_kept":55}
["CDS","OG ID","Score","Eval","Class ID","OG function","KEGG map"]
["CLOSTRIBL6_v1_3221","05QUH","531.6",{"v":1.3E-148,"d":"1.30E-148"},"S","Domain of unknown function (DUF2088)","-"]
["CLOSTRIBL6_v1_3223","05DAA","465.7",{"v":1.1E-128,"d":"1.10E-128"},"C","L-lactate","-"]
["CLOSTRIBL6_v1_2713","05C80","467.2",{"v":2.2E-129,"d":"2.20E-129"},"C","Catalyzes the reversible oxidation of malate to oxaloacetate (By similarity)","00010, 00020, 00270, 00620, 00630, 00640, 00680, 00710, 00720, 01100, 01110, 01120"]
["CLOSTRIBL6_v1_0279","05D95","1997.6",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"]
["CLOSTRIBL6_v1_3009","05EJ5","332.8",{"v":4e-89,"d":"4.00E-89"},"C","oxidoreductase gamma subunit","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 01100, 01120"]
["CLOSTRIBL6_v1_3010","05WGB","173.7",{"v":1.6e-41,"d":"1.60E-41"},"C","oxidoreductase, delta subunit","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 01100, 01120"]
["CLOSTRIBL6_v1_3011","05D95","630.6",{"v":1.9e-178,"d":"1.90E-178"},"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"]
["CLOSTRIBL6_v1_3012","05DDK","573.2",{"v":2.8e-161,"d":"2.80E-161"},"C","oxidoreductase, beta subunit","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 01100, 01120"]
["CLOSTRIBL6_v1_0126","05DYT","418.7",{"v":8e-115,"d":"8.00E-115"},"I","3-hydroxyacyl-CoA dehydrogenase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00640, 00650, 00720, 00903, 00930, 01040, 01100, 01110, 01120"]
["CLOSTRIBL6_v1_0127","05CHU","552.4",{"v":6.6e-155,"d":"6.60E-155"},"I","acetyl-coa acetyltransferase","00071, 00072, 00280, 00281, 00310, 00362, 00380, 00592, 00620, 00630, 00640, 00642, 00650, 00720, 00900, 01100, 01110, 01120, 02020"]
["CLOSTRIBL6_v1_0555","05DYT","465.7",{"v":6.1e-129,"d":"6.10E-129"},"I","3-hydroxyacyl-CoA dehydrogenase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00640, 00650, 00720, 00903, 00930, 01040, 01100, 01110, 01120"]
["CLOSTRIBL6_v1_0556","05CHU","630.6",{"v":1.9e-178,"d":"1.90E-178"},"I","acetyl-coa acetyltransferase","00071, 00072, 00280, 00281, 00310, 00362, 00380, 00592, 00620, 00630, 00640, 00642, 00650, 00720, 00900, 01100, 01110, 01120, 02020"]
["CLOSTRIBL6_v1_0558","05E39","411",{"v":1.6E-112,"d":"1.60E-112"},"I","Enoyl-CoA hydratase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00627, 00630, 00640, 00650, 00720, 00903, 00930, 01100, 01110, 01120"]
["CLOSTRIBL6_v1_0559","05C04","657.5",{"v":1.5e-186,"d":"1.50E-186"},"C","l-carnitine dehydratase bile acid-inducible protein F","00120, 01100, 04146"]
["CLOSTRIBL6_v1_0560","05CIZ","390.6",{"v":2.2e-106,"d":"2.20E-106"},"I","coA-substrate-specific enzyme activase","-"]
["CLOSTRIBL6_v1_0561","05CMH","792.7",{"v":3.1e-227,"d":"3.10E-227"},"E","dehydratase","00362, 01100, 01120, 01220"]
["CLOSTRIBL6_v1_0562","07T4M","597.8",{"v":1.3E-168,"d":"1.30E-168"},"E","dehydratase","-"]
["CLOSTRIBL6_v1_0871","05DYT","333.6",{"v":3.8e-89,"d":"3.80E-89"},"I","3-hydroxyacyl-CoA dehydrogenase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00640, 00650, 00720, 00903, 00930, 01040, 01100, 01110, 01120"]
["CLOSTRIBL6_v1_2953","05DG4","301.6",{"v":1.8e-79,"d":"1.80E-79"},"C","malate L-lactate dehydrogenase","00040, 00053, 00230, 00270, 01120"]
["CLOSTRIBL6_v1_0031","05CGU","456.8",{"v":2.6E-126,"d":"2.60E-126"},"I","Enoyl-CoA hydratase","00360, 01120"]
["CLOSTRIBL6_v1_1904","05C1G","1069.3","2.5e-310","I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["CLOSTRIBL6_v1_3062","05C1G","786.6",{"v":3e-225,"d":"3.00E-225"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["CLOSTRIBL6_v1_0135","05C1G","625.2",{"v":7.6e-177,"d":"7.60E-177"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["CLOSTRIBL6_v1_0136","05BZJ","440.3",{"v":2.4E-121,"d":"2.40E-121"},"C","Electron transfer flavoprotein","00910"]
["CLOSTRIBL6_v1_0137","05C10","538.5",{"v":8.6e-151,"d":"8.60E-151"},"C","Electron transfer flavoprotein","00910"]
["CLOSTRIBL6_v1_3216","05C1G","581.3",{"v":1.3E-163,"d":"1.30E-163"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["CLOSTRIBL6_v1_3217","05C10","500",{"v":3.3E-139,"d":"3.30E-139"},"C","Electron transfer flavoprotein","00910"]
["CLOSTRIBL6_v1_3218","05BZJ","377.9",{"v":1.5E-102,"d":"1.50E-102"},"C","Electron transfer flavoprotein","00910"]
["CLOSTRIBL6_v1_3220","05CQB","669.5",{"v":4.4e-190,"d":"4.40E-190"},"C","FAD linked oxidase domain protein","00620, 00630, 01100, 01110, 01120"]
["CLOSTRIBL6_v1_2270","08S4H","241.9",{"v":7.6e-62,"d":"7.60E-62"},"I","thioesterase Superfamily protein","00903, 01040"]
["CLOSTRIBL6_v1_2820","05C10","415.6",{"v":8e-114,"d":"8.00E-114"},"C","Electron transfer flavoprotein","00910"]
["CLOSTRIBL6_v1_2821","05BZJ","337.8",{"v":1.7E-90,"d":"1.70E-90"},"C","Electron transfer flavoprotein","00910"]
["CLOSTRIBL6_v1_0258","07QXD","592",{"v":1.1e-166,"d":"1.10E-166"},"C","PAS PAC sensor protein","-"]
["CLOSTRIBL6_v1_0260","07QHI","564.7",{"v":1.5E-158,"d":"1.50E-158"},"C","hydrogenase","00190, 00910, 01100"]
["CLOSTRIBL6_v1_1906","07QHI","519.6",{"v":5.2e-145,"d":"5.20E-145"},"C","hydrogenase","00190, 00910, 01100"]
["CLOSTRIBL6_v1_2017","07QHI","622.9",{"v":4.8e-176,"d":"4.80E-176"},"C","hydrogenase","00190, 00910, 01100"]
["CLOSTRIBL6_v1_2260","05C6H","617.1",{"v":2.2e-174,"d":"2.20E-174"},"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"]
["CLOSTRIBL6_v1_1872","08IJ2","494.2",{"v":1.7e-137,"d":"1.70E-137"},"C","phosphate acetyltransferase","00430, 00620, 00640, 00680, 00720, 01100, 01120"]
["CLOSTRIBL6_v1_0095","05C0A","721.8",{"v":6.1e-206,"d":"6.10E-206"},"C","alcohol dehydrogenase","00010, 00071, 00350, 00362, 00620, 00621, 00622, 00625, 00626, 00650, 01100, 01110, 01120"]
["CLOSTRIBL6_v1_1804","08JB8","543.9",{"v":2.3e-152,"d":"2.30E-152"},"C","alcohol dehydrogenase","00010, 00071, 00350, 00625, 00626, 00830, 00980, 00982, 01100, 01110, 01120"]
["CLOSTRIBL6_v1_2186","05C0A","1298.1",0,"C","alcohol dehydrogenase","00010, 00071, 00350, 00362, 00620, 00621, 00622, 00625, 00626, 00650, 01100, 01110, 01120"]
["CLOSTRIBL6_v1_2879","05C0A","341.7",{"v":1.8E-91,"d":"1.80E-91"},"C","alcohol dehydrogenase","00010, 00071, 00350, 00362, 00620, 00621, 00622, 00625, 00626, 00650, 01100, 01110, 01120"]
["CLOSTRIBL6_v1_3434","07QW4","501.9",{"v":1E-139,"d":"1.00E-139"},"C","alcohol dehydrogenase","00051, 00363, 00591, 00625, 00650, 01100, 01120"]
["CLOSTRIBL6_v1_1351","05C26","407.1",{"v":4.2e-111,"d":"4.20E-111"},"C","Dehydrogenase","00010, 00040, 00053, 00071, 00250, 00260, 00280, 00310, 00330, 00340, 00350, 00380, 00410, 00561, 00562, 00620, 00625, 00640, 00650, 00903, 01100, 01110, 01120"]
["CLOSTRIBL6_v1_2699","05D65","842.8",{"v":3.9E-242,"d":"3.90E-242"},"C","subunit l","00190, 00910, 01100"]
["CLOSTRIBL6_v1_2700","08IE6","386.3",{"v":4.5e-105,"d":"4.50E-105"},"C","Respiratory-chain NADH dehydrogenase, subunit 1","00190, 00910, 01100"]
["CLOSTRIBL6_v1_2701","08JP9","266.5",{"v":2.8e-69,"d":"2.80E-69"},"C","NADH ubiquinone oxidoreductase, 20 kda subunit","00680"]
["CLOSTRIBL6_v1_2702","05RZ4","127.9",{"v":1.2E-27,"d":"1.20E-27"},"C","NADH dehydrogenase (Ubiquinone), 30 kDa subunit","00680"]
["CLOSTRIBL6_v1_2703","08HM5","611.3",{"v":1.1E-172,"d":"1.10E-172"},"C","NADH-ubiquinone oxidoreductase chain 49kDa","00680"]
["CLOSTRIBL6_v1_2704","05P3U","183",{"v":5.5e-44,"d":"5.50E-44"},"C","NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity)","00190, 00910, 01100"]
["CLOSTRIBL6_v1_2705","05C8H","803.1",{"v":4e-230,"d":"4.00E-230"},"O","hydrogenase maturation protein Hypf","-"]
["CLOSTRIBL6_v1_2706","05WRB","97.4",{"v":1e-18,"d":"1.00E-18"},"O","Hydrogenase assembly chaperone hypC hupF","-"]
["CLOSTRIBL6_v1_2707","05CQS","469.5",{"v":4.9e-130,"d":"4.90E-130"},"O","hydrogenase expression formation protein HypD","-"]
["CLOSTRIBL6_v1_2708","05C45","423.3",{"v":3.8e-116,"d":"3.80E-116"},"O","hydrogenase expression formation protein (HypE)","-"]

{"sheet":"FigFam","index":11,"n_rows":34,"n_cols":4,"rows_kept":34}
["CDS","FIGFAM id","FIGFAM Description","EC number"]
["CLOSTRIBL4_v1_0061","FIG000812","L-lactate dehydrogenase","1.1.1.27"]
["CLOSTRIBL6_v1_2713","FIG000812","L-lactate dehydrogenase","1.1.1.27"]
["CLOSTRIBL6_v1_0279","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["CLOSTRIBL6_v1_3009","FIG003176","Pyruvate:ferredoxin oxidoreductase, gamma subunit","1.2.7.1"]
["CLOSTRIBL6_v1_3010","FIG057987","Pyruvate:ferredoxin oxidoreductase, delta subunit","1.2.7.1"]
["CLOSTRIBL6_v1_3011","FIG002975","Pyruvate:ferredoxin oxidoreductase, alpha subunit","1.2.7.1"]
["CLOSTRIBL6_v1_3012","FIG003175","Pyruvate:ferredoxin oxidoreductase, beta subunit","1.2.7.1"]
["CLOSTRIBL6_v1_0127","FIG002604","Acetyl-CoA acetyltransferase","2.3.1.9"]
["CLOSTRIBL6_v1_0555","FIG000819","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157, 1.1.1.35"]
["CLOSTRIBL6_v1_0556","FIG002604","Acetyl-CoA acetyltransferase","2.3.1.9"]
["CLOSTRIBL6_v1_0558","FIG002255","3-hydroxybutyryl-CoA dehydratase","4.2.1.55"]
["CLOSTRIBL6_v1_0560","FIG137656","Benzoyl-CoA reductase subunit BadG","1.3.7.8"]
["CLOSTRIBL6_v1_2953","FIG127445","(R)-2-hydroxyacid dehydrogenase, similar to L-sulfolactate dehydrogenase","1.1.1.272"]
["CLOSTRIBL6_v1_0031","FIG035155","Enoyl-CoA hydratase","4.2.1.17"]
["CLOSTRIBL6_v1_1904","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["CLOSTRIBL6_v1_3062","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["CLOSTRIBL6_v1_0135","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["CLOSTRIBL6_v1_0136","FIG136866","Electron transfer flavoprotein, beta subunit","_"]
["CLOSTRIBL6_v1_0137","FIG000366","Electron transfer flavoprotein, alpha subunit","_"]
["CLOSTRIBL6_v1_3216","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["CLOSTRIBL6_v1_3217","FIG000366","Electron transfer flavoprotein, alpha subunit","_"]
["CLOSTRIBL6_v1_3218","FIG136866","Electron transfer flavoprotein, beta subunit","_"]
["CLOSTRIBL6_v1_2820","FIG000366","Electron transfer flavoprotein, alpha subunit","_"]
["CLOSTRIBL6_v1_0258","FIG133264","Periplasmic (Fe) hydrogenase","1.12.7.2"]
["CLOSTRIBL6_v1_0260","FIG133264","Periplasmic (Fe) hydrogenase","1.12.7.2"]
["CLOSTRIBL6_v1_1906","FIG133264","Periplasmic (Fe) hydrogenase","1.12.7.2"]
["CLOSTRIBL6_v1_2017","FIG133264","Periplasmic (Fe) hydrogenase","1.12.7.2"]
["CLOSTRIBL6_v1_2260","FIG134300","Acetate kinase","2.7.2.1"]
["CLOSTRIBL6_v1_1872","FIG000522","Phosphate acetyltransferase","2.3.1.8"]
["CLOSTRIBL6_v1_0095","FIG037315","Alcohol dehydrogenase","1.1.1.1"]
["CLOSTRIBL6_v1_2186","FIG138701","Alcohol dehydrogenase","1.1.1.1, 1.2.1.10"]
["CLOSTRIBL6_v1_2707","FIG001208","(NiFe) hydrogenase metallocenter assembly protein HypD","_"]
["CLOSTRIBL6_v1_2708","FIG003378","(NiFe) hydrogenase metallocenter assembly protein HypE","_"]

{"sheet":"InterProScan","index":12,"n_rows":647,"n_cols":13,"rows_kept":647}
["CLOSTRIBL6_v1_3221","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",21,211,0.446009,{"v":4.4e-58,"d":"4.40E-58"},"LarA-like_N","Domain","LarA-like, N-terminal","Molecular Function: lactate racemase activity (GO:0050043)"]
[null,"_","_","PTHR33171","_",30,422,0.920188,{"v":1e-92,"d":"1.00E-92"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.11440","_",35,267,0.544601,{"v":2.2e-141,"d":"2.20E-141"},"_","_","_","-"]
[null,"_","_","G3DSA:3.90.226.30","_",5,417,0.967136,{"v":2.2e-141,"d":"2.20E-141"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_3223","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",2,508,0.978723,{"v":9e-134,"d":"9.00E-134"},"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",4,508,0.974855,{"v":5e-128,"d":"5.00E-128"},"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",1,509,0.982592,{"v":5.4e-121,"d":"5.40E-121"},"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","_",2,508,0.978723,{"v":9e-134,"d":"9.00E-134"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_2713","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",4,145,0.444795,{"v":1.3e-50,"d":"1.30E-50"},"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR022383","PFAM","PF02866","Ldh_1_C",148,311,0.514196,{"v":2.2e-33,"d":"2.20E-33"},"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",175,181,0.0189274,"_","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",148,316,0.529968,{"v":2.9e-56,"d":"2.90E-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",146,312,0.523659,{"v":6.56e-53,"d":"6.56E-53"},"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",5,315,0.977918,43.08,"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",10,309,0.943218,{"v":6e-118,"d":"6.00E-118"},"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",2,316,0.990536,{"v":8.4e-106,"d":"8.40E-106"},"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",143,161,0.0567823,{"v":2.8E-42,"d":"2.80E-42"},"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",32,56,0.0757098,{"v":2.8E-42,"d":"2.80E-42"},"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",7,31,0.0757098,{"v":2.8E-42,"d":"2.80E-42"},"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",119,139,0.0630915,{"v":2.8E-42,"d":"2.80E-42"},"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",173,186,0.0410095,{"v":2.8E-42,"d":"2.80E-42"},"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",7,145,0.435331,{"v":7.3e-43,"d":"7.30E-43"},"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","_",2,147,0.457413,{"v":2.6E-54,"d":"2.60E-54"},"_","_","_","-"]
[null,"_","_","PTHR43128","_",4,312,0.971609,{"v":6.5e-124,"d":"6.50E-124"},"_","_","_","-"]
[null,"_","_","PTHR43128:SF4","_",4,312,0.971609,{"v":6.5e-124,"d":"6.50E-124"},"_","_","_","-"]
[null,"_","_","cd05291","_",6,311,0.962145,{"v":2.18888e-175,"d":"2.19E-175"},"_","_","_","-"]
[null,"_","_","Coil","_",290,310,0.0630915,"_","_","_","_","-"]
[null,"_","_","Coil","_",212,232,0.0630915,"_","_","_","_","-"]
[]
["CLOSTRIBL6_v1_0279","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",269,375,0.0894515,1.1E-14,"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",3,258,0.21519,2.56E-76,"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",800,1184,0.324051,{"v":2.22e-128,"d":"2.22E-128"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",426,610,0.155274,{"v":1.1e-30,"d":"1.10E-30"},"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",630,685,0.0464135,{"v":6.9e-18,"d":"6.90E-18"},"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",624,686,0.0523207,{"v":8.3e-17,"d":"8.30E-17"},"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",750,761,0.0092827,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF12838","Fer4_7",696,761,0.0548523,3.7E-8,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",687,716,0.0244726,9.189,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",741,761,0.0168776,8.197,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011895","PIRSF","PIRSF000159","NifJ",1,1185,0.999156,0,"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",5,1183,0.994093,0,"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",970,1082,0.0945148,1.2e-12,"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",259,414,0.130802,{"v":8.7e-57,"d":"8.70E-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",259,411,0.12827,{"v":2.51e-45,"d":"2.51E-45"},"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",17,247,0.194093,{"v":2.8e-77,"d":"2.80E-77"},"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",416,625,0.176371,{"v":2.5e-89,"d":"2.50E-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,"IPR002869","SSF","SSF53323","SSF53323",417,673,0.216034,1.05E-80,"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","_",673,841,0.141772,{"v":6.56e-18,"d":"6.56E-18"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",676,791,0.0970464,{"v":2e-36,"d":"2.00E-36"},"_","_","_","-"]
[null,"_","_","cd07034","_",10,173,0.137553,{"v":2.83072e-48,"d":"2.83E-48"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",2,258,0.216034,{"v":3.9e-104,"d":"3.90E-104"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",797,1185,0.327426,{"v":5.2e-165,"d":"5.20E-165"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",1,1184,0.998312,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",1,1184,0.998312,0,"_","_","_","-"]
[null,"_","_","cd03377","_",813,1183,0.312236,0,"_","_","_","-"]
[null,"_","_","Coil","_",1165,1185,0.0168776,"_","_","_","_","-"]
[]
["CLOSTRIBL6_v1_3009","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",14,187,0.896373,{"v":6.6e-39,"d":"6.60E-39"},"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",6,191,0.958549,{"v":1.4E-65,"d":"1.40E-65"},"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":1e-63,"d":"1.00E-63"},"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",5,191,0.963731,7.19E-53,"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","_",4,191,0.968912,{"v":1.3e-60,"d":"1.30E-60"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_3010","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",49,60,0.107843,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",80,91,0.107843,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF00037","Fer4",78,96,0.176471,1.3E-7,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",71,100,0.284314,10.348,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",40,69,0.284314,9.004,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011898","PANTHER","PTHR43724","PTHR43724",10,102,0.901961,{"v":1.4e-26,"d":"1.40E-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",25,101,0.745098,{"v":1.2e-28,"d":"1.20E-28"},"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","_",39,98,0.578431,5.5e-12,"_","_","_","-"]
[null,"_","_","SSF54862","_",30,101,0.696078,{"v":2.05e-18,"d":"2.05E-18"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_3011","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",260,364,0.265985,{"v":1.2E-26,"d":"1.20E-26"},"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",5,249,0.624041,9.81E-65,"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR009014","CATHGENE3D","G3DSA:3.40.50.920","G3DSA:3.40.50.920",251,391,0.358056,{"v":4.1e-44,"d":"4.10E-44"},"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",251,371,0.306905,{"v":1.96e-34,"d":"1.96E-34"},"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",16,237,0.565217,{"v":3.2e-68,"d":"3.20E-68"},"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","_",9,167,0.404092,{"v":2.30293e-55,"d":"2.30E-55"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",1,250,0.636829,{"v":4e-91,"d":"4.00E-91"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",5,373,0.941176,{"v":2.2e-108,"d":"2.20E-108"},"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",5,373,0.941176,{"v":2.2e-108,"d":"2.20E-108"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_3012","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",9,308,0.964516,1.15E-76,"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR011766","PFAM","PF02775","TPP_enzyme_C",59,218,0.512903,{"v":1e-21,"d":"1.00E-21"},"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","_",3,100,0.312903,3e-07,"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",101,309,0.670968,{"v":6.7e-67,"d":"6.70E-67"},"_","_","_","-"]
[null,"_","_","PTHR42897","_",6,306,0.967742,{"v":7.1e-125,"d":"7.10E-125"},"_","_","_","-"]
[null,"_","_","PTHR42897:SF2","_",6,306,0.967742,{"v":7.1e-125,"d":"7.10E-125"},"_","_","_","-"]
[null,"_","_","cd03376","_",15,255,0.774194,{"v":3.13843e-130,"d":"3.14E-130"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0126","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",2,178,0.633094,{"v":6.04e-51,"d":"6.04E-51"},"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR022694","PIRSF","PIRSF000105","HCDH",1,278,0.996403,{"v":2.9e-84,"d":"2.90E-84"},"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",188,273,0.305755,{"v":8.9E-35,"d":"8.90E-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",181,278,0.348921,{"v":8.42e-32,"d":"8.42E-32"},"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",178,202,0.0863309,"_","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",2,178,0.633094,{"v":1.5E-59,"d":"1.50E-59"},"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",181,277,0.345324,{"v":1.2e-35,"d":"1.20E-35"},"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","_",1,184,0.658273,{"v":7.8e-63,"d":"7.80E-63"},"_","_","_","-"]
[null,"_","_","PTHR43145","_",2,278,0.992806,{"v":5.2e-110,"d":"5.20E-110"},"_","_","_","-"]
[null,"_","_","PTHR43145:SF10","_",2,278,0.992806,{"v":5.2e-110,"d":"5.20E-110"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0127","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",274,394,0.303797,{"v":8.1e-47,"d":"8.10E-47"},"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",5,265,0.658228,{"v":2.8e-99,"d":"2.80E-99"},"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",85,103,0.0455696,"_","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",342,358,0.0405063,"_","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",377,390,0.0329114,"_","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",9,279,0.683544,{"v":3.8e-157,"d":"3.80E-157"},"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",127,393,0.673418,{"v":3.8e-157,"d":"3.80E-157"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",274,394,0.303797,1.04E-42,"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",5,273,0.678481,1.18E-88,"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002155","CDD","cd00751","thiolase",6,395,0.98481,0,"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",1,395,0.997468,{"v":1.3E-130,"d":"1.30E-130"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR002155","TIGRFAMs","TIGR01930","AcCoA-C-Actrans",9,394,0.974684,{"v":2e-143,"d":"2.00E-143"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"_","_","PTHR18919","_",2,394,0.992405,{"v":3.7e-160,"d":"3.70E-160"},"_","_","_","-"]
[null,"_","_","PTHR18919:SF107","_",2,394,0.992405,{"v":3.7e-160,"d":"3.70E-160"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0555","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",6,192,0.622074,{"v":1.79e-48,"d":"1.79E-48"},"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR022694","PIRSF","PIRSF000105","HCDH",2,299,0.993311,{"v":1.1E-88,"d":"1.10E-88"},"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",197,298,0.337793,{"v":3.8e-35,"d":"3.80E-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",195,296,0.337793,{"v":6.29e-30,"d":"6.29E-30"},"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",192,216,0.0802676,"_","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",8,191,0.61204,{"v":1.1E-54,"d":"1.10E-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",195,291,0.32107,{"v":1e-32,"d":"1.00E-32"},"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","_",1,192,0.638796,{"v":3.9e-58,"d":"3.90E-58"},"_","_","_","-"]
[null,"_","_","PTHR43145","_",3,297,0.983278,{"v":3.9E-90,"d":"3.90E-90"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0556","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",274,396,0.307305,{"v":4.8E-50,"d":"4.80E-50"},"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",6,265,0.652393,{"v":1.4e-81,"d":"1.40E-81"},"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",343,359,0.0403023,"_","Thiolase_CS","Conserved_site","Thiolase, conserved 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",8,280,0.685139,{"v":1.3E-154,"d":"1.30E-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",128,394,0.670025,{"v":1.3E-154,"d":"1.30E-154"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",275,395,0.302267,{"v":2.92e-45,"d":"2.92E-45"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",5,274,0.677582,{"v":2.34e-81,"d":"2.34E-81"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002155","CDD","cd00751","thiolase",7,396,0.979849,0,"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",1,397,0.997481,{"v":1.1E-132,"d":"1.10E-132"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR002155","TIGRFAMs","TIGR01930","AcCoA-C-Actrans",8,395,0.974811,{"v":9.2E-144,"d":"9.20E-144"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"_","_","PTHR18919","_",1,396,0.994962,{"v":1.4e-149,"d":"1.40E-149"},"_","_","_","-"]
[null,"_","_","PTHR18919:SF107","_",1,396,0.994962,{"v":1.4e-149,"d":"1.40E-149"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0558","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",4,262,0.984733,{"v":1.7e-87,"d":"1.70E-87"},"ClpP/crotonase-like_dom_sf","Homologous_superfamily","ClpP/crotonase-like domain superfamily","-"]
[null,"IPR014748","CATHGENE3D","G3DSA:1.10.12.10","G3DSA:1.10.12.10",204,262,0.221374,{"v":1e-23,"d":"1.00E-23"},"Enoyl-CoA_hydra_C","Homologous_superfamily","Enoyl-CoA hydratase, C-terminal","-"]
[null,"IPR001753","PFAM","PF00378","ECH_1",12,261,0.950382,{"v":5.8e-61,"d":"5.80E-61"},"Enoyl-CoA_hydra/iso","Family","Enoyl-CoA hydratase/isomerase","Molecular Function: catalytic activity (GO:0003824)"]
[null,"_","_","G3DSA:3.90.226.10","_",2,203,0.767176,{"v":7.1e-69,"d":"7.10E-69"},"_","_","_","-"]
[null,"_","_","cd06558","_",8,201,0.736641,{"v":2.57607e-72,"d":"2.58E-72"},"_","_","_","-"]
[null,"_","_","PTHR11941","_",13,260,0.942748,{"v":1.2e-76,"d":"1.20E-76"},"_","_","_","-"]
[null,"_","_","PTHR11941:SF140","_",13,260,0.942748,{"v":1.2e-76,"d":"1.20E-76"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0559","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR023606","CATHGENE3D","G3DSA:3.40.50.10540","G3DSA:3.40.50.10540",3,392,0.9725,{"v":2.2e-96,"d":"2.20E-96"},"CoA-Trfase_III_dom_sf","Homologous_superfamily","CoA-transferase family III domain superfamily","-"]
[null,"IPR023606","SSF","SSF89796","SSF89796",1,397,0.99,{"v":8.11e-100,"d":"8.11E-100"},"CoA-Trfase_III_dom_sf","Homologous_superfamily","CoA-transferase family III domain superfamily","-"]
[null,"IPR003673","PFAM","PF02515","CoA_transf_3",5,359,0.885,{"v":2.4e-85,"d":"2.40E-85"},"CoA-Trfase_fam_III","Family","CoA-transferase family III","Molecular Function: catalytic activity (GO:0003824)"]
[null,"_","_","G3DSA:3.30.1540.10","_",229,326,0.2425,{"v":2.2e-96,"d":"2.20E-96"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0560","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR008275","TIGRFAMs","TIGR00241","CoA_E_activ",2,251,0.939623,{"v":1.1e-79,"d":"1.10E-79"},"CoA_E_activase","Domain","CoA enzyme activase","-"]
[null,"IPR002731","PFAM","PF01869","BcrAD_BadFG",4,252,0.935849,{"v":1.1E-64,"d":"1.10E-64"},"ATPase_BadF","Domain","ATPase, BadF/BadG/BcrA/BcrD type","-"]
[null,"_","_","SSF53067","_",1,255,0.958491,{"v":1.76e-39,"d":"1.76E-39"},"_","_","_","-"]
[null,"_","_","PTHR32329","_",2,259,0.969811,{"v":1.9e-80,"d":"1.90E-80"},"_","_","_","-"]
[null,"_","_","PTHR32329:SF2","_",2,259,0.969811,{"v":1.9e-80,"d":"1.90E-80"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",95,237,0.535849,{"v":4.6e-83,"d":"4.60E-83"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",4,252,0.935849,{"v":4.6e-83,"d":"4.60E-83"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0561","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR010327","PFAM","PF06050","HGD-D",56,419,0.844186,{"v":1.5e-66,"d":"1.50E-66"},"FldB/FldC_alpha/beta","Family","FldB/FldC dehydratase alpha/beta subunit","-"]
[null,"_","_","G3DSA:3.40.50.11900","_",310,428,0.274419,2.4E-8,"_","_","_","-"]
[null,"_","_","G3DSA:1.20.1270.370","_",199,264,0.151163,1.1e-09,"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.11890","_",136,198,0.144186,1.1e-09,"_","_","_","-"]
[null,"_","_","PTHR30548","_",21,427,0.944186,{"v":3.6E-145,"d":"3.60E-145"},"_","_","_","-"]
[null,"_","_","PTHR30548:SF4","_",21,427,0.944186,{"v":3.6E-145,"d":"3.60E-145"},"_","_","_","-"]
[null,"_","_","Coil","_",251,271,0.0465116,"_","_","_","_","-"]
[]
["CLOSTRIBL6_v1_0562","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR010327","PFAM","PF06050","HGD-D",38,374,0.893617,{"v":7.8e-51,"d":"7.80E-51"},"FldB/FldC_alpha/beta","Family","FldB/FldC dehydratase alpha/beta subunit","-"]
[null,"_","_","G3DSA:3.40.50.11900","_",232,376,0.382979,{"v":2.5e-40,"d":"2.50E-40"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.1270.370","_",12,220,0.553191,{"v":3.3e-72,"d":"3.30E-72"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.11890","_",30,155,0.332447,{"v":3.3e-72,"d":"3.30E-72"},"_","_","_","-"]
[null,"_","_","PTHR30548","_",1,374,0.992021,{"v":4.6e-126,"d":"4.60E-126"},"_","_","_","-"]
[null,"_","_","PTHR30548:SF5","_",1,374,0.992021,{"v":4.6e-126,"d":"4.60E-126"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0871","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",5,186,0.576433,{"v":4.03e-49,"d":"4.03E-49"},"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR022694","PIRSF","PIRSF000105","HCDH",1,314,0.996815,{"v":5.7e-90,"d":"5.70E-90"},"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",192,314,0.388535,{"v":1.5e-41,"d":"1.50E-41"},"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",190,288,0.312102,{"v":1.87e-26,"d":"1.87E-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",187,211,0.0764331,"_","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",9,187,0.566879,{"v":1.2E-56,"d":"1.20E-56"},"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",190,288,0.312102,{"v":2.8e-25,"d":"2.80E-25"},"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","_",1,187,0.592357,{"v":7e-61,"d":"7.00E-61"},"_","_","_","-"]
[null,"_","_","PTHR43145","_",3,299,0.942675,{"v":1.3e-91,"d":"1.30E-91"},"_","_","_","-"]
[null,"_","_","PTHR43145:SF4","_",3,299,0.942675,{"v":1.3e-91,"d":"1.30E-91"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_2953","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036111","SSF","SSF89733","SSF89733",3,342,0.979769,{"v":1.07e-112,"d":"1.07E-112"},"Mal/L-sulfo/L-lacto_DH-like_sf","Homologous_superfamily","Malate/L-sulfolactate/L-lactate dehydrogenase-like superfamily","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR003767","PANTHER","PTHR11091","PTHR11091",2,343,0.985549,{"v":1.5E-105,"d":"1.50E-105"},"Malate/L-lactate_DH-like","Family","Malate/L-lactate dehydrogenase-like","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR003767","PFAM","PF02615","Ldh_2",5,333,0.947977,{"v":1.2E-123,"d":"1.20E-123"},"Malate/L-lactate_DH-like","Family","Malate/L-lactate dehydrogenase-like","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","G3DSA:1.10.1530.10","_",10,335,0.939306,{"v":1.3E-125,"d":"1.30E-125"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.1370.60","_",68,316,0.716763,{"v":1.3E-125,"d":"1.30E-125"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0031","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",3,262,0.962825,{"v":4.79e-73,"d":"4.79E-73"},"ClpP/crotonase-like_dom_sf","Homologous_superfamily","ClpP/crotonase-like domain superfamily","-"]
[null,"IPR018376","PROSITE","PS00166","ENOYL_COA_HYDRATASE",111,131,0.0743494,"_","Enoyl-CoA_hyd/isom_CS","Conserved_site","Enoyl-CoA hydratase/isomerase, conserved site","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR001753","PFAM","PF00378","ECH_1",9,251,0.899628,{"v":8.3e-49,"d":"8.30E-49"},"Enoyl-CoA_hydra/iso","Family","Enoyl-CoA hydratase/isomerase","Molecular Function: catalytic activity (GO:0003824)"]
[null,"_","_","cd06558","_",4,209,0.762082,{"v":7.64837e-56,"d":"7.65E-56"},"_","_","_","-"]
[null,"_","_","PTHR11941","_",3,262,0.962825,{"v":3.4E-66,"d":"3.40E-66"},"_","_","_","-"]
[null,"_","_","PTHR11941:SF133","_",3,262,0.962825,{"v":3.4E-66,"d":"3.40E-66"},"_","_","_","-"]
[null,"_","_","G3DSA:3.90.226.10","_",1,269,0.996283,{"v":3.8e-74,"d":"3.80E-74"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_1904","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",1,120,0.18859,{"v":2.8E-44,"d":"2.80E-44"},"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",227,381,0.244057,{"v":1.3E-56,"d":"1.30E-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,"IPR029035","SSF","SSF52467","SSF52467",433,553,0.190174,{"v":8.72e-38,"d":"8.72E-38"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR024935","CDD","cd00730","rubredoxin",583,630,0.0744849,{"v":8.09809e-20,"d":"8.10E-20"},"Rubredoxin_dom","Domain","Rubredoxin domain","Molecular Function: iron ion binding (GO:0005506)"]
[null,"IPR024935","PFAM","PF00301","Rubredoxin",583,628,0.0713154,{"v":2E-19,"d":"2.00E-19"},"Rubredoxin_dom","Domain","Rubredoxin domain","Molecular Function: iron ion binding (GO:0005506)"]
[null,"IPR024935","PRINTS","PR00163","RUBREDOXIN",582,598,0.0253566,1.8e-08,"Rubredoxin_dom","Domain","Rubredoxin domain","Molecular Function: iron ion binding (GO:0005506)"]
[null,"IPR024935","PRINTS","PR00163","RUBREDOXIN",612,628,0.0253566,1.8e-08,"Rubredoxin_dom","Domain","Rubredoxin domain","Molecular Function: iron ion binding (GO:0005506)"]
[null,"IPR024934","PROFILE","PS50903","RUBREDOXIN_LIKE",580,631,0.0808241,13.066,"Rubredoxin-like_dom","Domain","Rubredoxin-like domain","Molecular Function: iron ion binding (GO:0005506)"]
[null,"IPR018527","PROSITE","PS00202","RUBREDOXIN",612,622,0.0158479,"_","Rubredoxin_Fe_BS","Binding_site","Rubredoxin, iron-binding site","Molecular Function: metal ion binding (GO:0046872)"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",435,517,0.129952,{"v":1.5e-25,"d":"1.50E-25"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR013786","PFAM","PF02771","Acyl-CoA_dh_N",6,118,0.177496,{"v":3.5e-40,"d":"3.50E-40"},"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",3,242,0.378764,{"v":1.83e-91,"d":"1.83E-91"},"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",229,377,0.234548,{"v":9.6e-51,"d":"9.60E-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",122,217,0.150555,{"v":2.5e-27,"d":"2.50E-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",124,136,0.0190174,"_","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","_",581,630,0.0776545,{"v":6.39e-18,"d":"6.39E-18"},"_","_","_","-"]
[null,"_","_","G3DSA:2.20.28.10","_",579,631,0.0824089,{"v":2.4e-20,"d":"2.40E-20"},"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",121,234,0.179081,{"v":1.6e-43,"d":"1.60E-43"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1220","_",429,562,0.210777,{"v":1.3e-44,"d":"1.30E-44"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",235,383,0.234548,{"v":7.1e-54,"d":"7.10E-54"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",2,558,0.881141,{"v":2.7E-227,"d":"2.70E-227"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF25","_",2,558,0.881141,{"v":2.7E-227,"d":"2.70E-227"},"_","_","_","-"]
[null,"_","_","cd01158","_",7,379,0.58954,0,"_","_","_","-"]
[]
["CLOSTRIBL6_v1_3062","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",1,120,0.210619,{"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",227,384,0.277876,1.77E-59,"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",443,563,0.212389,{"v":1.42e-38,"d":"1.42E-38"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",444,525,0.143363,{"v":3.5e-25,"d":"3.50E-25"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR013786","PFAM","PF02771","Acyl-CoA_dh_N",7,117,0.19469,{"v":5.3e-36,"d":"5.30E-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",1,242,0.426549,{"v":6.28e-87,"d":"6.28E-87"},"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",229,376,0.260177,{"v":1.5E-50,"d":"1.50E-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",122,217,0.168142,{"v":2.2e-26,"d":"2.20E-26"},"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",124,136,0.0212389,"_","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,"_","_","G3DSA:2.40.110.10","_",121,234,0.2,{"v":8.3e-43,"d":"8.30E-43"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1220","_",439,565,0.223009,{"v":1.2E-44,"d":"1.20E-44"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",235,389,0.272566,{"v":2.6E-56,"d":"2.60E-56"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",3,547,0.962832,{"v":4.7e-203,"d":"4.70E-203"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF25","_",3,547,0.962832,{"v":4.7e-203,"d":"4.70E-203"},"_","_","_","-"]
[null,"_","_","cd01158","_",8,379,0.656637,0,"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0135","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":3.6e-43,"d":"3.60E-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",227,379,0.401055,{"v":9.18e-60,"d":"9.18E-60"},"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",7,118,0.292876,{"v":7.1e-37,"d":"7.10E-37"},"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":8.9e-89,"d":"8.90E-89"},"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",229,377,0.390501,{"v":1.1E-52,"d":"1.10E-52"},"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":1.5e-26,"d":"1.50E-26"},"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","_",3,99,0.253298,3.6E-10,"_","_","_","-"]
[null,"_","_","PIRSF016578","_",130,379,0.656992,{"v":1.6e-20,"d":"1.60E-20"},"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",121,234,0.298153,{"v":2.3e-45,"d":"2.30E-45"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",235,379,0.379947,{"v":3.4e-56,"d":"3.40E-56"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",2,378,0.992084,{"v":1.3e-159,"d":"1.30E-159"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",2,378,0.992084,{"v":1.3e-159,"d":"1.30E-159"},"_","_","_","-"]
[null,"_","_","cd01158","_",8,379,0.978892,{"v":0,"d":"0.00E+00"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0136","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":2.04407E-94,"d":"2.04E-94"},"ETF_beta_N","Domain","Electron transfer flavoprotein, beta subunit, N-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",23,206,0.706564,{"v":5e-50,"d":"5.00E-50"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",22,211,0.72973,{"v":5.8e-61,"d":"5.80E-61"},"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",1,257,0.988417,{"v":2.5e-92,"d":"2.50E-92"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR012255","PANTHER","PTHR21294","PTHR21294",2,256,0.980695,{"v":3.5e-95,"d":"3.50E-95"},"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":4.6e-90,"d":"4.60E-90"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"_","_","SSF52402","_",2,255,0.976834,{"v":1.26e-78,"d":"1.26E-78"},"_","_","_","-"]
[null,"_","_","PTHR21294:SF17","_",2,256,0.980695,{"v":3.5e-95,"d":"3.50E-95"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0137","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",15,176,0.465318,{"v":9.01797e-52,"d":"9.02E-52"},"ETF_alpha_N","Domain","Electron transfer flavoprotein, alpha subunit, N-terminal","-"]
[null,"IPR029035","SSF","SSF52467","SSF52467",216,335,0.343931,{"v":3.33e-48,"d":"3.33E-48"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR018206","PROSITE","PS00696","ETF_ALPHA",280,306,0.0751445,"_","ETF_asu_C_CS","Conserved_site","Electron transfer flavoprotein subunit alpha, conserved site","-"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",216,299,0.239884,{"v":3.6e-36,"d":"3.60E-36"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",17,196,0.517341,{"v":2.4E-50,"d":"2.40E-50"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",16,205,0.546243,{"v":1.5E-48,"d":"1.50E-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",3,206,0.586705,{"v":2.3E-77,"d":"2.30E-77"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR001308","PIRSF","PIRSF000089","Electra_flavoP_a",12,341,0.950867,{"v":1.6E-118,"d":"1.60E-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,"_","_","G3DSA:3.40.50.1220","_",211,346,0.390173,{"v":1.3e-57,"d":"1.30E-57"},"_","_","_","-"]
[null,"_","_","SSF52402","_",14,209,0.563584,{"v":5.02e-58,"d":"5.02E-58"},"_","_","_","-"]
[null,"_","_","PTHR43153","_",8,341,0.962428,{"v":1.5e-143,"d":"1.50E-143"},"_","_","_","-"]
[null,"_","_","PTHR43153:SF9","_",8,341,0.962428,{"v":1.5e-143,"d":"1.50E-143"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_3216","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",1,120,0.313158,{"v":4.3e-44,"d":"4.30E-44"},"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",227,377,0.394737,{"v":2.42e-56,"d":"2.42E-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",7,118,0.292105,{"v":6.9e-38,"d":"6.90E-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",1,242,0.634211,{"v":2.88e-89,"d":"2.88E-89"},"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",229,374,0.381579,{"v":8.3e-49,"d":"8.30E-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",122,217,0.25,{"v":4.7e-29,"d":"4.70E-29"},"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","PS00073","ACYL_COA_DH_2",336,355,0.05,"_","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","_",6,378,0.978947,{"v":8.4e-24,"d":"8.40E-24"},"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",121,234,0.297368,{"v":2.5e-45,"d":"2.50E-45"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",235,379,0.378947,{"v":4.4e-54,"d":"4.40E-54"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",3,375,0.978947,{"v":3e-159,"d":"3.00E-159"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",3,375,0.978947,{"v":3e-159,"d":"3.00E-159"},"_","_","_","-"]
[null,"_","_","cd01158","_",8,375,0.965789,0,"_","_","_","-"]
[]
["CLOSTRIBL6_v1_3217","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",9,181,0.51497,{"v":2.87232e-46,"d":"2.87E-46"},"ETF_alpha_N","Domain","Electron transfer flavoprotein, alpha subunit, N-terminal","-"]
[null,"IPR029035","SSF","SSF52467","SSF52467",209,328,0.356287,{"v":4.67e-48,"d":"4.67E-48"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR018206","PROSITE","PS00696","ETF_ALPHA",273,299,0.0778443,"_","ETF_asu_C_CS","Conserved_site","Electron transfer flavoprotein subunit alpha, conserved site","-"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",209,292,0.248503,{"v":2e-37,"d":"2.00E-37"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",9,184,0.523952,{"v":9.4e-45,"d":"9.40E-45"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",8,205,0.58982,{"v":1.5e-42,"d":"1.50E-42"},"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",4,205,0.601796,{"v":1.6e-68,"d":"1.60E-68"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR001308","PIRSF","PIRSF000089","Electra_flavoP_a",4,334,0.988024,{"v":4.6E-116,"d":"4.60E-116"},"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","_",7,201,0.580838,2.16E-48,"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1220","_",206,334,0.383234,{"v":1.4E-57,"d":"1.40E-57"},"_","_","_","-"]
[null,"_","_","PTHR43153","_",4,333,0.98503,{"v":9.5e-130,"d":"9.50E-130"},"_","_","_","-"]
[null,"_","_","PTHR43153:SF9","_",4,333,0.98503,{"v":9.5e-130,"d":"9.50E-130"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_3218","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",2,206,0.761194,{"v":1.81327e-82,"d":"1.81E-82"},"ETF_beta_N","Domain","Electron transfer flavoprotein, beta subunit, N-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",23,213,0.708955,{"v":4e-45,"d":"4.00E-45"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",22,218,0.731343,{"v":2.9e-51,"d":"2.90E-51"},"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",1,268,0.996269,{"v":2.5e-90,"d":"2.50E-90"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR012255","PANTHER","PTHR21294","PTHR21294",1,266,0.988806,{"v":3.4E-86,"d":"3.40E-86"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"IPR012255","PIRSF","PIRSF000090","Beta-ETF",1,268,0.996269,{"v":1.1E-85,"d":"1.10E-85"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"IPR000049","PROSITE","PS01065","ETF_BETA",162,182,0.0746269,"_","ET-Flavoprotein_bsu_CS","Conserved_site","Electron transfer flavoprotein, beta-subunit, conserved site","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"_","_","SSF52402","_",1,263,0.977612,{"v":6.98e-74,"d":"6.98E-74"},"_","_","_","-"]
[null,"_","_","PTHR21294:SF17","_",1,266,0.988806,{"v":3.4E-86,"d":"3.40E-86"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_3220","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",6,221,0.452632,2.43E-67,"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",430,470,0.0842105,1.3E-13,"Vanillyl_alc_oxidase_C-sub2","Homologous_superfamily","Vanillyl-alcohol oxidase, C-terminal subdomain 2","-"]
[null,"IPR016166","PROFILE","PS51387","FAD_PCMH",42,220,0.374737,26.655,"FAD-bd_PCMH","Domain","FAD-binding domain, PCMH-type","Molecular Function: FAD binding (GO:0071949)"]
[null,"IPR016164","SSF","SSF55103","SSF55103",224,471,0.52,{"v":2.45e-49,"d":"2.45E-49"},"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",46,183,0.288421,{"v":1.2e-39,"d":"1.20E-39"},"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",221,469,0.522105,{"v":2.6E-53,"d":"2.60E-53"},"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","_",349,429,0.168421,7.4e-15,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.465.40","_",21,236,0.452632,{"v":2e-72,"d":"2.00E-72"},"_","_","_","-"]
[null,"_","_","PTHR42934","_",7,471,0.976842,{"v":1.4E-153,"d":"1.40E-153"},"_","_","_","-"]
[null,"_","_","PTHR42934:SF2","_",7,471,0.976842,{"v":1.4E-153,"d":"1.40E-153"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_2270","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR040170","PANTHER","PTHR11049","PTHR11049",6,154,0.930818,{"v":2.3E-40,"d":"2.30E-40"},"Cytosol_ACT","Family","Cytosolic acyl coenzyme A thioester hydrolase","Molecular Function: thiolester hydrolase activity (GO:0016790)"]
[null,"IPR033120","PROFILE","PS51770","HOTDOG_ACOT",10,121,0.698113,30.342,"HOTDOG_ACOT","Domain","Hotdog acyl-CoA thioesterase (ACOT)-type domain","-"]
[null,"IPR029069","SSF","SSF54637","SSF54637",5,155,0.943396,{"v":3.28e-42,"d":"3.28E-42"},"HotDog_dom_sf","Homologous_superfamily","HotDog domain superfamily","-"]
[null,"IPR006683","PFAM","PF03061","4HBT",29,95,0.415094,2.7E-11,"Thioestr_dom","Domain","Thioesterase domain","-"]
[null,"_","_","cd03442","_",7,128,0.761006,{"v":8.30377e-42,"d":"8.30E-42"},"_","_","_","-"]
[null,"_","_","G3DSA:3.10.129.10","_",2,159,0.987421,{"v":5E-53,"d":"5.00E-53"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_2820","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",7,174,0.509146,{"v":1.99055e-37,"d":"1.99E-37"},"ETF_alpha_N","Domain","Electron transfer flavoprotein, alpha subunit, N-terminal","-"]
[null,"IPR029035","SSF","SSF52467","SSF52467",202,322,0.365854,{"v":2.07e-43,"d":"2.07E-43"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",203,285,0.25,{"v":7.6e-33,"d":"7.60E-33"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",9,185,0.536585,{"v":8.6e-39,"d":"8.60E-39"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",8,197,0.576219,{"v":4.2e-37,"d":"4.20E-37"},"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",5,199,0.591463,{"v":2.7e-54,"d":"2.70E-54"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR001308","PIRSF","PIRSF000089","Electra_flavoP_a",5,327,0.981707,{"v":4.4e-96,"d":"4.40E-96"},"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","_",6,190,0.560976,{"v":1.81e-41,"d":"1.81E-41"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1220","_",200,328,0.390244,{"v":1.9E-50,"d":"1.90E-50"},"_","_","_","-"]
[null,"_","_","PTHR43153","_",3,326,0.984756,{"v":1.6e-101,"d":"1.60E-101"},"_","_","_","-"]
[null,"_","_","PTHR43153:SF9","_",3,326,0.984756,{"v":1.6e-101,"d":"1.60E-101"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_2821","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",2,205,0.763158,{"v":4.71202e-77,"d":"4.71E-77"},"ETF_beta_N","Domain","Electron transfer flavoprotein, beta subunit, N-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",23,207,0.691729,{"v":8.6e-44,"d":"8.60E-44"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",22,214,0.721804,{"v":9.2e-47,"d":"9.20E-47"},"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",1,266,0.996241,{"v":9.2e-82,"d":"9.20E-82"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR012255","PANTHER","PTHR21294","PTHR21294",1,260,0.973684,{"v":6.5e-74,"d":"6.50E-74"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"IPR012255","PIRSF","PIRSF000090","Beta-ETF",1,266,0.996241,{"v":7.3e-78,"d":"7.30E-78"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"_","_","SSF52402","_",1,262,0.981203,1.12E-66,"_","_","_","-"]
[null,"_","_","PTHR21294:SF17","_",1,260,0.973684,{"v":6.5e-74,"d":"6.50E-74"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0258","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR035965","SSF","SSF55785","SSF55785",407,479,0.125217,2.3e-07,"PAS-like_dom_sf","Homologous_superfamily","PAS domain superfamily","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",41,52,0.0191304,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF13237","Fer4_10",5,52,0.0817391,1.9E-6,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",32,61,0.0504348,9.491,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",3,31,0.0486957,8.046,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR013767","PFAM","PF00989","PAS",412,481,0.12,2.8E-5,"PAS_fold","Domain","PAS fold","Biological Process: regulation of transcription, DNA-templated (GO:0006355)"]
[null,"IPR011005","CATHGENE3D","G3DSA:3.20.20.20","G3DSA:3.20.20.20",351,416,0.113043,5.3e-06,"Dihydropteroate_synth-like","Homologous_superfamily","Dihydropteroate synthase-like","Biological Process: cellular metabolic process (GO:0044237)"]
[null,"IPR009016","SSF","SSF53920","SSF53920",40,318,0.483478,{"v":7.98e-55,"d":"7.98E-55"},"Fe_hydrogenase","Homologous_superfamily","Iron hydrogenase","-"]
[null,"IPR007202","PFAM","PF04060","FeS",372,401,0.0504348,4.5e-08,"4Fe-4S_dom","Domain","4Fe-4S domain","Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"IPR007202","PROFILE","PS51656","4FE4S",354,416,0.107826,26.227,"4Fe-4S_dom","Domain","4Fe-4S domain","Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"IPR004108","PFAM","PF02906","Fe_hyd_lg_C",74,299,0.391304,{"v":3.9E-43,"d":"3.90E-43"},"Fe_hydrogenase_lsu_C","Domain","Iron hydrogenase, large subunit, C-terminal","-"]
[null,"IPR000014","CDD","cd00130","PAS",418,466,0.0834783,0.000148654,"PAS","Domain","PAS domain","-"]
[null,"IPR000014","SMART","SM00091","PAS",409,474,0.113043,2.3E-5,"PAS","Domain","PAS domain","-"]
[null,"_","_","G3DSA:3.30.450.20","_",417,507,0.156522,2.2e-09,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",7,86,0.137391,2.1e-11,"_","_","_","-"]
[null,"_","_","SSF54862","_",7,81,0.128696,{"v":4.01e-16,"d":"4.01E-16"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.950.20","_",104,318,0.372174,{"v":2.4E-22,"d":"2.40E-22"},"_","_","_","-"]
[null,"_","_","PTHR11615","_",1,561,0.973913,{"v":8.8e-123,"d":"8.80E-123"},"_","_","_","-"]
[null,"_","_","PTHR11615:SF231","_",1,561,0.973913,{"v":8.8e-123,"d":"8.80E-123"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0260","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",4,443,0.932059,{"v":3.1e-172,"d":"3.10E-172"},"FeFe_hydrog_B1","Family","[FeFe] hydrogenase, group B1/B3","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",174,185,0.0233546,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF00037","Fer4",122,143,0.044586,2.8e-07,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PFAM","PF00037","Fer4",168,189,0.044586,2.6e-09,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",165,194,0.0615711,11.146,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",119,148,0.0615711,10.692,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",89,118,0.0615711,7.71,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR009016","SSF","SSF53920","SSF53920",173,453,0.59448,{"v":4.84e-66,"d":"4.84E-66"},"Fe_hydrogenase","Homologous_superfamily","Iron hydrogenase","-"]
[null,"IPR004108","PFAM","PF02906","Fe_hyd_lg_C",213,439,0.47983,{"v":2.8e-56,"d":"2.80E-56"},"Fe_hydrogenase_lsu_C","Domain","Iron hydrogenase, large subunit, C-terminal","-"]
[null,"_","_","G3DSA:3.30.70.20","_",147,204,0.121019,2.5e-12,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",90,146,0.118896,6e-14,"_","_","_","-"]
[null,"_","_","cd10549","_",84,190,0.225053,{"v":6.65937E-19,"d":"6.66E-19"},"_","_","_","-"]
[null,"_","_","SSF54862","_",86,194,0.229299,4.05E-27,"_","_","_","-"]
[null,"_","_","PTHR11615","_",150,461,0.660297,{"v":4.3E-28,"d":"4.30E-28"},"_","_","_","-"]
[null,"_","_","PTHR11615:SF231","_",150,461,0.660297,{"v":4.3E-28,"d":"4.30E-28"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.950.20","_",243,463,0.467091,{"v":1.3E-35,"d":"1.30E-35"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_1906","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",101,118,0.0390805,0.00016,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",99,128,0.0666667,9.466,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR009016","SSF","SSF53920","SSF53920",107,421,0.721839,{"v":6.15e-69,"d":"6.15E-69"},"Fe_hydrogenase","Homologous_superfamily","Iron hydrogenase","-"]
[null,"IPR004108","PFAM","PF02906","Fe_hyd_lg_C",142,378,0.542529,{"v":1.3E-54,"d":"1.30E-54"},"Fe_hydrogenase_lsu_C","Domain","Iron hydrogenase, large subunit, C-terminal","-"]
[null,"_","_","G3DSA:3.30.70.20","_",83,128,0.103448,1.8e-08,"_","_","_","-"]
[null,"_","_","SSF54862","_",61,126,0.149425,2.69E-9,"_","_","_","-"]
[null,"_","_","PTHR11615","_",87,356,0.618391,{"v":2.9e-17,"d":"2.90E-17"},"_","_","_","-"]
[null,"_","_","PTHR11615:SF231","_",87,356,0.618391,{"v":2.9e-17,"d":"2.90E-17"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.950.20","_",182,394,0.487356,{"v":1.6e-30,"d":"1.60E-30"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_2017","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",4,440,0.906445,{"v":1.1E-175,"d":"1.10E-175"},"FeFe_hydrog_B1","Family","[FeFe] hydrogenase, group B1/B3","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",175,186,0.022869,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",129,140,0.022869,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF12838","Fer4_7",151,189,0.0790021,1.2e-07,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PFAM","PF00037","Fer4",123,145,0.045738,1.3e-08,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",166,195,0.0602911,10.793,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",120,149,0.0602911,10.608,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",88,119,0.0644491,7.492,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR009016","SSF","SSF53920","SSF53920",174,451,0.575884,{"v":4.32e-65,"d":"4.32E-65"},"Fe_hydrogenase","Homologous_superfamily","Iron hydrogenase","-"]
[null,"IPR004108","PFAM","PF02906","Fe_hyd_lg_C",207,437,0.47817,{"v":1.2E-58,"d":"1.20E-58"},"Fe_hydrogenase_lsu_C","Domain","Iron hydrogenase, large subunit, C-terminal","-"]
[null,"_","_","G3DSA:3.30.70.20","_",148,208,0.12474,4.1e-13,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",92,147,0.114345,2E-14,"_","_","_","-"]
[null,"_","_","SSF54862","_",122,194,0.149688,1.81E-18,"_","_","_","-"]
[null,"_","_","cd10549","_",106,190,0.174636,{"v":3.51042e-21,"d":"3.51E-21"},"_","_","_","-"]
[null,"_","_","PTHR11615","_",96,146,0.10395,{"v":3.5e-37,"d":"3.50E-37"},"_","_","_","-"]
[null,"_","_","PTHR11615","_",151,409,0.536383,{"v":3.5e-37,"d":"3.50E-37"},"_","_","_","-"]
[null,"_","_","PTHR11615:SF231","_",151,409,0.536383,{"v":3.5e-37,"d":"3.50E-37"},"_","_","_","-"]
[null,"_","_","PTHR11615:SF231","_",96,146,0.10395,{"v":3.5e-37,"d":"3.50E-37"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.950.20","_",246,458,0.440748,{"v":1.4e-41,"d":"1.40E-41"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_2260","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",3,14,0.0274314,"_","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",204,221,0.042394,"_","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",1,401,0.997506,183.893,"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",1,401,0.997506,{"v":3.8e-151,"d":"3.80E-151"},"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",1,396,0.985037,{"v":7.3E-153,"d":"7.30E-153"},"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",1,399,0.992519,{"v":1.9E-159,"d":"1.90E-159"},"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",2,392,0.972569,{"v":1.3E-148,"d":"1.30E-148"},"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",174,187,0.032419,{"v":8e-44,"d":"8.00E-44"},"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",204,225,0.0523691,{"v":8e-44,"d":"8.00E-44"},"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",3,14,0.0274314,{"v":8e-44,"d":"8.00E-44"},"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",301,314,0.032419,{"v":8e-44,"d":"8.00E-44"},"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",323,339,0.0399003,{"v":8e-44,"d":"8.00E-44"},"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",379,391,0.0299252,{"v":8e-44,"d":"8.00E-44"},"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","_",1,197,0.488778,{"v":1.88e-68,"d":"1.88E-68"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",1,196,0.486284,{"v":1.5e-77,"d":"1.50E-77"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",197,401,0.508728,{"v":1.1e-80,"d":"1.10E-80"},"_","_","_","-"]
[null,"_","_","SSF53067","_",158,397,0.59601,{"v":2.89e-90,"d":"2.89E-90"},"_","_","_","-"]
[null,"_","_","PTHR21060:SF15","_",1,399,0.992519,{"v":1.9E-159,"d":"1.90E-159"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_1872","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",16,320,0.941176,{"v":2.2e-121,"d":"2.20E-121"},"P_AcTrfase_dom1","Homologous_superfamily","Phosphate acetyltransferase, domain 1","-"]
[null,"IPR042112","CATHGENE3D","G3DSA:3.40.50.10750","G3DSA:3.40.50.10750",139,296,0.486068,{"v":2.2e-121,"d":"2.20E-121"},"P_AcTrfase_dom2","Homologous_superfamily","Phosphate acetyltransferase, domain 2","-"]
[null,"IPR012147","PIRSF","PIRSF000428","P_Ac_trans",1,322,0.993808,{"v":1.3e-101,"d":"1.30E-101"},"P_Ac_Bu_trans","Family","Phosphate acetyl/butyryltransferase","Molecular Function: transferase activity, transferring acyl groups (GO:0016746)"]
[null,"IPR004614","TIGRFAMs","TIGR00651","pta",16,320,0.941176,{"v":2.9E-106,"d":"2.90E-106"},"P_AcTrfase","Domain","Phosphate acetyltransferase","Molecular Function: acetyltransferase activity (GO:0016407)"]
[null,"IPR002505","PFAM","PF01515","PTA_PTB",3,320,0.981424,{"v":6.7e-114,"d":"6.70E-114"},"PTA_PTB","Domain","Phosphate acetyl/butaryl transferase","Molecular Function: transferase activity, transferring acyl groups (GO:0016746)"]
[null,"_","_","SSF53659","_",2,320,0.98452,4.52E-88,"_","_","_","-"]
[null,"_","_","PTHR43356","_",2,320,0.98452,{"v":3e-133,"d":"3.00E-133"},"_","_","_","-"]
[null,"_","_","PTHR43356:SF3","_",2,320,0.98452,{"v":3e-133,"d":"3.00E-133"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_0095","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",3,386,0.989664,{"v":1.5e-101,"d":"1.50E-101"},"Alcohol_dehydrogenase_Fe","Family","Iron-type alcohol dehydrogenase-like","-"]
[null,"IPR018211","PROSITE","PS00913","ADH_IRON_1",174,202,0.0723514,"_","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",10,377,0.94832,{"v":2.9E-105,"d":"2.90E-105"},"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","_",1,185,0.475452,{"v":1.7E-46,"d":"1.70E-46"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.1090.10","_",186,385,0.514212,{"v":2.8e-60,"d":"2.80E-60"},"_","_","_","-"]
[null,"_","_","SSF56796","_",5,385,0.981912,{"v":1.7E-105,"d":"1.70E-105"},"_","_","_","-"]
[null,"_","_","cd08193","_",7,383,0.971576,{"v":8.69701e-168,"d":"8.70E-168"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_1804","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",6,389,0.982051,{"v":1e-85,"d":"1.00E-85"},"Alcohol_dehydrogenase_Fe","Family","Iron-type alcohol dehydrogenase-like","-"]
[null,"IPR001670","PFAM","PF00465","Fe-ADH",9,379,0.948718,{"v":2.1e-100,"d":"2.10E-100"},"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:1.20.1090.10","_",191,390,0.510256,{"v":1.3e-38,"d":"1.30E-38"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1970","_",2,189,0.479487,{"v":1.6E-53,"d":"1.60E-53"},"_","_","_","-"]
[null,"_","_","SSF56796","_",3,389,0.989744,{"v":1.7e-97,"d":"1.70E-97"},"_","_","_","-"]
[null,"_","_","cd08185","_",6,386,0.974359,0,"_","_","_","-"]
[]
["CLOSTRIBL6_v1_2186","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",282,868,0.675115,{"v":6e-276,"d":"6.00E-276"},"Alcohol_dehydrogenase_Fe","Family","Iron-type alcohol dehydrogenase-like","-"]
[null,"IPR034789","CDD","cd08178","AAD_C",465,862,0.457373,0,"AAD_C","Domain","Bifunctional aldehyde-alcohol dehydrogenase, C-terminal domain","Molecular Function: alcohol dehydrogenase (NAD) activity (GO:0004022)"]
[null,"IPR018211","PROSITE","PS00913","ADH_IRON_1",640,668,0.0322581,"_","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,"IPR016163","CATHGENE3D","G3DSA:3.40.309.10","G3DSA:3.40.309.10",228,413,0.213134,{"v":3.2E-174,"d":"3.20E-174"},"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",20,451,0.496544,{"v":3.2E-174,"d":"3.20E-174"},"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",17,461,0.511521,{"v":1.23e-75,"d":"1.23E-75"},"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",15,410,0.455069,{"v":5.1e-22,"d":"5.10E-22"},"Aldehyde_DH_dom","Domain","Aldehyde dehydrogenase domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR012079","PIRSF","PIRSF000111","ALDH_ADH",2,868,0.997696,0,"Bifunc_Ald-ADH","Family","Bifunctional aldehyde-alcohol dehydrogenase","Molecular Function: alcohol dehydrogenase (NAD) activity (GO:0004022); Biological Process: alcohol metabolic process (GO:0006066); Molecular Function: acetaldehyde dehydrogenase (acetylating) activity (GO:0008774); Biological Process: carbon utilization (GO:0015976); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001670","PFAM","PF00465","Fe-ADH",465,853,0.447005,{"v":1.1e-112,"d":"1.10E-112"},"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","_",458,651,0.22235,{"v":6.4e-60,"d":"6.40E-60"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.1090.10","_",652,868,0.248848,{"v":9.3e-68,"d":"9.30E-68"},"_","_","_","-"]
[null,"_","_","SSF56796","_",456,867,0.473502,{"v":2.09e-115,"d":"2.09E-115"},"_","_","_","-"]
[null,"_","_","PTHR11496:SF91","_",282,868,0.675115,{"v":6e-276,"d":"6.00E-276"},"_","_","_","-"]
[null,"_","_","cd07122","_",19,455,0.502304,0,"_","_","_","-"]
[]
["CLOSTRIBL6_v1_2879","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",8,376,0.93401,{"v":1.4e-123,"d":"1.40E-123"},"Alcohol_dehydrogenase_Fe","Family","Iron-type alcohol dehydrogenase-like","-"]
[null,"IPR018211","PROSITE","PS00060","ADH_IRON_2",254,274,0.0507614,"_","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,"IPR018211","PROSITE","PS00913","ADH_IRON_1",167,195,0.071066,"_","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",13,369,0.903553,{"v":8.1e-115,"d":"8.10E-115"},"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","_",2,178,0.446701,{"v":1.2E-49,"d":"1.20E-49"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.1090.10","_",180,380,0.507614,{"v":1.6E-65,"d":"1.60E-65"},"_","_","_","-"]
[null,"_","_","SSF56796","_",4,380,0.954315,{"v":4.71e-117,"d":"4.71E-117"},"_","_","_","-"]
[null,"_","_","PTHR11496:SF92","_",8,376,0.93401,{"v":1.4e-123,"d":"1.40E-123"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_3434","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR001670","PFAM","PF00465","Fe-ADH",10,368,0.910941,{"v":9.1e-87,"d":"9.10E-87"},"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:1.20.1090.10","_",187,392,0.521628,{"v":1.3E-39,"d":"1.30E-39"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1970","_",1,186,0.470738,{"v":6.6e-51,"d":"6.60E-51"},"_","_","_","-"]
[null,"_","_","SSF56796","_",2,389,0.984733,{"v":9.29e-94,"d":"9.29E-94"},"_","_","_","-"]
[null,"_","_","PTHR43633","_",1,391,0.992366,{"v":1.8e-104,"d":"1.80E-104"},"_","_","_","-"]
[null,"_","_","cd08187","_",3,389,0.982188,0,"_","_","_","-"]
[null,"Genomic Object Editor: "]
[]
["CLOSTRIBL6_v1_1351","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR029510","PROSITE","PS00687","ALDEHYDE_DEHYDR_GLU",260,267,0.0143149,"_","Ald_DH_CS_GLU","Conserved_site","Aldehyde dehydrogenase, glutamic acid active site","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR016163","CATHGENE3D","G3DSA:3.40.309.10","G3DSA:3.40.309.10",265,454,0.386503,{"v":3.3e-143,"d":"3.30E-143"},"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",21,482,0.94274,{"v":3.3e-143,"d":"3.30E-143"},"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",14,482,0.957055,3.93E-140,"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",28,482,0.928425,{"v":6.8E-139,"d":"6.80E-139"},"Aldehyde_DH_dom","Domain","Aldehyde dehydrogenase domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PTHR43353","_",19,482,0.94683,{"v":7.5e-137,"d":"7.50E-137"},"_","_","_","-"]
[null,"_","_","PTHR43353:SF12","_",19,482,0.94683,{"v":7.5e-137,"d":"7.50E-137"},"_","_","_","-"]
[null,"_","_","Coil","_",45,65,0.0408998,"_","_","_","_","-"]
[]
["CLOSTRIBL6_v1_2699","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR001750","PFAM","PF00361","Proton_antipo_M",182,460,0.437795,{"v":1.9e-49,"d":"1.90E-49"},"ND/Mrp_mem","Domain","NADH:quinone oxidoreductase/Mrp antiporter, membrane subunit","-"]
[null,"IPR001516","PFAM","PF00662","Proton_antipo_N",104,166,0.0976378,4.1e-11,"Proton_antipo_N","Domain","NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal","-"]
[null,"_","_","PR01434","_",266,287,0.0330709,{"v":5.8e-26,"d":"5.80E-26"},"_","_","_","-"]
[null,"_","_","PR01434","_",123,148,0.0393701,{"v":5.8e-26,"d":"5.80E-26"},"_","_","_","-"]
[null,"_","_","PR01434","_",288,314,0.0409449,{"v":5.8e-26,"d":"5.80E-26"},"_","_","_","-"]
[null,"_","_","PR01434","_",355,367,0.0188976,{"v":5.8e-26,"d":"5.80E-26"},"_","_","_","-"]
[null,"_","_","PTHR43373","_",122,560,0.689764,{"v":9.8e-87,"d":"9.80E-87"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_2700","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR001694","PFAM","PF00146","NADHdh",10,284,0.951389,{"v":2.4E-42,"d":"2.40E-42"},"NADH_UbQ_OxRdtase_su1/FPO","Family","NADH:ubiquinone oxidoreductase, subunit 1/F420H2 oxidoreductase subunit H","Cellular Component: membrane (GO:0016020); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PTHR43359","_",3,285,0.979167,{"v":2.9E-47,"d":"2.90E-47"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_2701","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR006137","PFAM","PF01058","Oxidored_q6",18,128,0.714286,{"v":2.8E-27,"d":"2.80E-27"},"NADH_UbQ_OxRdtase-like_20kDa","Domain","NADH:ubiquinone oxidoreductase-like, 20kDa subunit","Molecular Function: iron-sulfur cluster binding (GO:0051536); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","G3DSA:3.40.50.12280","_",2,151,0.967532,{"v":1.3e-50,"d":"1.30E-50"},"_","_","_","-"]
[null,"_","_","PTHR42989","_",3,142,0.902597,{"v":6.6e-51,"d":"6.60E-51"},"_","_","_","-"]
[null,"_","_","SSF56770","_",6,137,0.850649,{"v":2.62e-52,"d":"2.62E-52"},"_","_","_","-"]
[null,"_","_","Coil","_",123,143,0.12987,"_","_","_","_","-"]
[]
["CLOSTRIBL6_v1_2702","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037232","SSF","SSF143243","SSF143243",4,91,0.756522,1.14E-12,"NADH_quin_OxRdtase_su_C/D-like","Homologous_superfamily","NADH:ubiquinone oxidoreductase, 30kDa subunit superfamily","-"]
[null,"IPR001268","PFAM","PF00329","Complex1_30kDa",8,91,0.721739,4.7e-08,"NADH_UbQ_OxRdtase_30kDa_su","Domain","NADH:ubiquinone oxidoreductase, 30kDa subunit","Molecular Function: NADH dehydrogenase (ubiquinone) activity (GO:0008137); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","Coil","_",112,115,0.026087,"_","_","_","_","-"]
[]
["CLOSTRIBL6_v1_2703","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR038290","CATHGENE3D","G3DSA:1.10.645.20","G3DSA:1.10.645.20",6,359,0.983287,{"v":1.6E-126,"d":"1.60E-126"},"NADH_Q_OxRdtase_suD_sf","Homologous_superfamily","NADH-quinone oxidoreductase, subunit D superfamily","-"]
[null,"IPR029014","SSF","SSF56762","SSF56762",15,359,0.958217,{"v":8.5e-111,"d":"8.50E-111"},"NiFe-Hase_large","Homologous_superfamily","[NiFe]-hydrogenase, large subunit","-"]
[null,"IPR018194","PROSITE","PS00507","NI_HGENASE_L_1",43,68,0.0696379,"_","Ni-dep_hyd_lsu_Ni_BS","Binding_site","Nickel-dependent hydrogenase, large subunit, nickel binding site","Molecular Function: ferredoxin hydrogenase activity (GO:0008901); Molecular Function: nickel cation binding (GO:0016151); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR014029","PROSITE","PS00535","COMPLEX1_49K",41,52,0.0306407,"_","NADH_UbQ_OxRdtase_49kDa_CS","Conserved_site","NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site","Molecular Function: oxidoreductase activity, acting on NAD(P)H (GO:0016651); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001501","PFAM","PF00374","NiFeSe_Hases",43,112,0.192201,3.7E-14,"Ni-dep_hyd_lsu","Family","Nickel-dependent hydrogenase, large subunit","Molecular Function: nickel cation binding (GO:0016151)"]
[null,"IPR001135","PFAM","PF00346","Complex1_49kDa",287,359,0.200557,1.1e-15,"NADH_Q_OxRdtase_suD","Domain","NADH-quinone oxidoreductase, subunit D","Molecular Function: oxidoreductase activity, acting on NAD(P)H (GO:0016651); Molecular Function: quinone binding (GO:0048038); Molecular Function: NAD binding (GO:0051287); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001135","PFAM","PF00346","Complex1_49kDa",120,282,0.451253,{"v":8e-46,"d":"8.00E-46"},"NADH_Q_OxRdtase_suD","Domain","NADH-quinone oxidoreductase, subunit D","Molecular Function: oxidoreductase activity, acting on NAD(P)H (GO:0016651); Molecular Function: quinone binding (GO:0048038); Molecular Function: NAD binding (GO:0051287); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PTHR43485","_",5,359,0.986072,{"v":1e-116,"d":"1.00E-116"},"_","_","_","-"]
[null,"_","_","Coil","_",166,186,0.0557103,"_","_","_","_","-"]
[]
["CLOSTRIBL6_v1_2704","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",76,87,0.0531401,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",45,56,0.0531401,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF13237","Fer4_10",37,87,0.241546,4.1e-09,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",36,65,0.140097,11.264,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",67,96,0.140097,9.34,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR010226","PANTHER","PTHR10849","PTHR10849",7,104,0.468599,{"v":1.1E-22,"d":"1.10E-22"},"NADH_quinone_OxRdtase_chainI","Family","NADH-quinone oxidoreductase, chain I","Cellular Component: membrane (GO:0016020); Molecular Function: oxidoreductase activity, acting on NAD(P)H (GO:0016651); Molecular Function: 4 iron, 4 sulfur cluster binding (GO:0051539); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","G3DSA:3.30.70.20","_",19,54,0.169082,3.8E-6,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",55,91,0.173913,1.6e-08,"_","_","_","-"]
[null,"_","_","SSF54862","_",23,99,0.36715,{"v":3.93e-18,"d":"3.93E-18"},"_","_","_","-"]
[null,"_","_","PTHR10849:SF24","_",7,104,0.468599,{"v":1.1E-22,"d":"1.10E-22"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_2705","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR041440","PFAM","PF17788","HypF_C",394,489,0.128032,{"v":9.8e-31,"d":"9.80E-31"},"HypF_C","Domain","HypF, Kae1-like domain","-"]
[null,"IPR036046","SSF","SSF54975","SSF54975",2,87,0.114555,{"v":8.07e-19,"d":"8.07E-19"},"Acylphosphatase-like_dom_sf","Homologous_superfamily","Acylphosphatase-like domain superfamily","-"]
[null,"IPR017945","SSF","SSF55821","SSF55821",173,386,0.287062,{"v":1.46e-41,"d":"1.46E-41"},"DHBP_synth_RibB-like_a/b_dom","Homologous_superfamily","DHBP synthase RibB-like alpha/beta domain superfamily","-"]
[null,"IPR011125","PFAM","PF07503","zf-HYPF",157,186,0.0390836,2.3e-10,"Znf_HypF","Domain","Zinc finger, HypF-type","Molecular Function: zinc ion binding (GO:0008270)"]
[null,"IPR011125","PFAM","PF07503","zf-HYPF",107,140,0.0444744,1.7E-15,"Znf_HypF","Domain","Zinc finger, HypF-type","Molecular Function: zinc ion binding (GO:0008270)"]
[null,"IPR006070","PFAM","PF01300","Sua5_yciO_yrdC",208,378,0.229111,{"v":7.4e-41,"d":"7.40E-41"},"YrdC-like_dom","Domain","YrdC-like domain","Molecular Function: double-stranded RNA binding (GO:0003725)"]
[null,"IPR006070","PROFILE","PS51163","YRDC",198,381,0.246631,17.279,"YrdC-like_dom","Domain","YrdC-like domain","Molecular Function: double-stranded RNA binding (GO:0003725)"]
[null,"IPR004421","PIRSF","PIRSF006256","CMPcnvr_hdrg_mat",1,741,0.997305,{"v":7.8e-242,"d":"7.80E-242"},"Carbamoyltransferase_HypF","Family","Carbamoyltransferase, HypF-type","Molecular Function: carboxyl- or carbamoyltransferase activity (GO:0016743); Molecular Function: metal ion binding (GO:0046872); Biological Process: protein carbamoylation (GO:0046944)"]
[null,"IPR004421","TIGRFAMs","TIGR00143","hypF",5,737,0.986523,{"v":5.1e-214,"d":"5.10E-214"},"Carbamoyltransferase_HypF","Family","Carbamoyltransferase, HypF-type","Molecular Function: carboxyl- or carbamoyltransferase activity (GO:0016743); Molecular Function: metal ion binding (GO:0046872); Biological Process: protein carbamoylation (GO:0046944)"]
[null,"IPR001792","PFAM","PF00708","Acylphosphatase",5,86,0.109164,{"v":3.7e-17,"d":"3.70E-17"},"Acylphosphatase-like_dom","Domain","Acylphosphatase-like domain","-"]
[null,"IPR001792","PROFILE","PS51160","ACYLPHOSPHATASE_3",2,88,0.115903,26.162,"Acylphosphatase-like_dom","Domain","Acylphosphatase-like domain","-"]
[null,"_","_","G3DSA:3.30.420.350","_",478,725,0.332884,{"v":2.4e-119,"d":"2.40E-119"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.360","_",378,737,0.483828,{"v":2.4e-119,"d":"2.40E-119"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.110.120","_",250,366,0.156334,{"v":1.6E-126,"d":"1.60E-126"},"_","_","_","-"]
[null,"_","_","G3DSA:3.90.870.50","_",5,357,0.474394,{"v":1.6E-126,"d":"1.60E-126"},"_","_","_","-"]
[null,"_","_","PTHR42959","_",4,738,0.989218,{"v":1.7e-233,"d":"1.70E-233"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_2706","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037254","CATHGENE3D","G3DSA:2.40.50.970","G3DSA:2.40.50.970",1,70,0.985714,{"v":8.4e-19,"d":"8.40E-19"},"HupF/HypC_sf","Homologous_superfamily","HupF/HypC superfamily","-"]
[null,"IPR037254","SSF","SSF159127","SSF159127",1,68,0.957143,7.06e-15,"HupF/HypC_sf","Homologous_superfamily","HupF/HypC superfamily","-"]
[null,"IPR001109","PANTHER","PTHR35177","PTHR35177",1,69,0.971429,6.3e-14,"Hydrogenase_HupF/HypC","Family","Hydrogenase expression/formation protein, HupF/HypC","-"]
[null,"IPR001109","PFAM","PF01455","HupF_HypC",1,58,0.814286,{"v":3.3E-17,"d":"3.30E-17"},"Hydrogenase_HupF/HypC","Family","Hydrogenase expression/formation protein, HupF/HypC","-"]
[null,"IPR001109","TIGRFAMs","TIGR00074","hypC_hupF",1,67,0.942857,1.1E-13,"Hydrogenase_HupF/HypC","Family","Hydrogenase expression/formation protein, HupF/HypC","-"]
[null,"_","_","PTHR35177:SF2","_",1,69,0.971429,6.3e-14,"_","_","_","-"]
[]
["CLOSTRIBL6_v1_2707","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR042244","CATHGENE3D","G3DSA:3.40.50.11750","G3DSA:3.40.50.11750",10,241,0.671512,{"v":2.3E-98,"d":"2.30E-98"},"HypD_1","Homologous_superfamily","HypD, domain 1","-"]
[null,"IPR042243","CATHGENE3D","G3DSA:3.40.50.11740","G3DSA:3.40.50.11740",47,281,0.680233,{"v":2.3E-98,"d":"2.30E-98"},"HypD_2","Homologous_superfamily","HypD, domain 2","-"]
[null,"IPR002780","PANTHER","PTHR30149","PTHR30149",10,341,0.962209,{"v":3.1e-119,"d":"3.10E-119"},"Hyd_form_HypD","Family","Hydrogenase formation HypD protein","Molecular Function: metal ion binding (GO:0046872)"]
[null,"IPR002780","PFAM","PF01924","HypD",3,339,0.976744,{"v":2.7e-123,"d":"2.70E-123"},"Hyd_form_HypD","Family","Hydrogenase formation HypD protein","Molecular Function: metal ion binding (GO:0046872)"]
[null,"IPR002780","PIRSF","PIRSF005622","Hydrgn_mat_hypD",1,344,0.997093,{"v":5e-120,"d":"5.00E-120"},"Hyd_form_HypD","Family","Hydrogenase formation HypD protein","Molecular Function: metal ion binding (GO:0046872)"]
[null,"IPR002780","TIGRFAMs","TIGR00075","hypD",4,342,0.982558,{"v":9.4e-109,"d":"9.40E-109"},"Hyd_form_HypD","Family","Hydrogenase formation HypD protein","Molecular Function: metal ion binding (GO:0046872)"]
[null,"_","_","G3DSA:1.10.10.2140","_",293,343,0.145349,{"v":1.8e-21,"d":"1.80E-21"},"_","_","_","-"]
[]
["CLOSTRIBL6_v1_2708","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036921","CATHGENE3D","G3DSA:3.30.1330.10","G3DSA:3.30.1330.10",4,149,0.442073,{"v":8e-49,"d":"8.00E-49"},"PurM-like_N_sf","Homologous_superfamily","PurM-like, N-terminal domain superfamily","-"]
[null,"IPR036921","SSF","SSF55326","SSF55326",2,146,0.439024,{"v":3.14e-31,"d":"3.14E-31"},"PurM-like_N_sf","Homologous_superfamily","PurM-like, N-terminal domain superfamily","-"]
[null,"IPR036676","CATHGENE3D","G3DSA:3.90.650.10","G3DSA:3.90.650.10",150,328,0.542683,{"v":5.3e-50,"d":"5.30E-50"},"PurM-like_C_sf","Homologous_superfamily","PurM-like, C-terminal domain superfamily","-"]
[null,"IPR036676","SSF","SSF56042","SSF56042",154,322,0.512195,1.41E-37,"PurM-like_C_sf","Homologous_superfamily","PurM-like, C-terminal domain superfamily","-"]
[null,"IPR016188","PFAM","PF00586","AIRS",36,143,0.326219,{"v":8.7e-16,"d":"8.70E-16"},"PurM-like_N","Domain","PurM-like, N-terminal domain","-"]
[null,"IPR011854","CDD","cd02197","HypE",9,296,0.875,{"v":5.21638e-155,"d":"5.22E-155"},"HypE","Family","Carbamoyl dehydratase HypE","-"]
[null,"IPR011854","PANTHER","PTHR30303","PTHR30303",2,328,0.993902,{"v":4.4e-125,"d":"4.40E-125"},"HypE","Family","Carbamoyl dehydratase HypE","-"]
[null,"IPR011854","PIRSF","PIRSF005644","Hdrgns_mtr_HypE",1,328,0.996951,{"v":8.2e-116,"d":"8.20E-116"},"HypE","Family","Carbamoyl dehydratase HypE","-"]
[null,"IPR011854","TIGRFAMs","TIGR02124","hypE",2,328,0.993902,{"v":3.6e-127,"d":"3.60E-127"},"HypE","Family","Carbamoyl dehydratase HypE","-"]
[null,"IPR010918","PFAM","PF02769","AIRS_C",156,304,0.451219,{"v":1.1E-24,"d":"1.10E-24"},"PurM-like_C_dom","Domain","PurM-like, C-terminal domain","-"]
[null,"_","_","PTHR30303:SF0","_",2,328,0.993902,{"v":4.4e-125,"d":"4.40E-125"},"_","_","_","-"]

{"sheet":"PSortB","index":13,"n_rows":55,"n_cols":4,"rows_kept":55}
["CDS","PsortB Localization","Score","Gram"]
["CLOSTRIBL6_v1_3221","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_3223","CytoplasmicMembrane",10,"+"]
["CLOSTRIBL6_v1_2713","Cytoplasmic",9.97,"+"]
["CLOSTRIBL6_v1_0279","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_3009","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_3010","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_3011","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_3012","Unknown",2.5,"+"]
["CLOSTRIBL6_v1_0126","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_0127","Cytoplasmic",9.67,"+"]
["CLOSTRIBL6_v1_0555","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_0556","Cytoplasmic",9.97,"+"]
["CLOSTRIBL6_v1_0558","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_0559","Cytoplasmic",9.97,"+"]
["CLOSTRIBL6_v1_0560","CytoplasmicMembrane",8.16,"+"]
["CLOSTRIBL6_v1_0561","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_0562","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_0871","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_2953","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_0031","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_1904","Cytoplasmic",9.97,"+"]
["CLOSTRIBL6_v1_3062","Cytoplasmic",9.67,"+"]
["CLOSTRIBL6_v1_0135","Cytoplasmic",9.97,"+"]
["CLOSTRIBL6_v1_0136","Unknown",2.5,"+"]
["CLOSTRIBL6_v1_0137","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_3216","Cytoplasmic",9.97,"+"]
["CLOSTRIBL6_v1_3217","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_3218","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_3220","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_2270","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_2820","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_2821","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_0258","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_0260","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_1906","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_2017","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_2260","Cytoplasmic",9.97,"+"]
["CLOSTRIBL6_v1_1872","Unknown",2.5,"+"]
["CLOSTRIBL6_v1_0095","Cytoplasmic",9.97,"+"]
["CLOSTRIBL6_v1_1804","Cytoplasmic",9.97,"+"]
["CLOSTRIBL6_v1_2186","Cytoplasmic",9.97,"+"]
["CLOSTRIBL6_v1_2879","Cytoplasmic",9.97,"+"]
["CLOSTRIBL6_v1_3434","Cytoplasmic",9.67,"+"]
["CLOSTRIBL6_v1_1351","Cytoplasmic",9.97,"+"]
["CLOSTRIBL6_v1_2699","CytoplasmicMembrane",10,"+"]
["CLOSTRIBL6_v1_2700","CytoplasmicMembrane",10,"+"]
["CLOSTRIBL6_v1_2701","CytoplasmicMembrane",9.51,"+"]
["CLOSTRIBL6_v1_2702","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_2703","Cytoplasmic",9.97,"+"]
["CLOSTRIBL6_v1_2704","Unknown",2.5,"+"]
["CLOSTRIBL6_v1_2705","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_2706","Cytoplasmic",7.5,"+"]
["CLOSTRIBL6_v1_2707","Unknown",2.5,"+"]
["CLOSTRIBL6_v1_2708","Cytoplasmic",7.5,"+"]