{"text_format":"3","workbook":"xlsx","n_sheets":15,"sheets":["reactions","instruction","start","gene features","protein features","MaGe-Curated annotations","SwissProt","UniFIRE ","PRIAM EC number","COG","EGGNOG","FigFam","InterProScan","Sheet1","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 10. Functional annotations of strain Megasphaera hexanoica MH"]
["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":48,"n_cols":13,"rows_kept":48}
["CDS","Strand","length","Begin","End","AMIGene Start","AMIGene Lpcod","AMIGene Apcod","Matrix","Prodigal Begin","Prodigal End","Glimmer Begin","Glimmer End"]
["ACT01_13720","R",1284,2870047,2871330,2871330,0.958814,0.958814,1,2870047,2871330,2870047,2871330]
["ACT01_13730","R",1536,2873015,2874550,2874550,0.870387,0.870387,1,2873015,2874550,2873015,2874550]
["ACT01_00410","R",957,82629,83585,83585,0.934454,0.934454,1,82629,83585,82629,83585]
["ACT01_04310","D",993,929265,930281,929265,0.932811,0.932811,1,929289,930281,929289,930281]
["ACT01_03310","D",546,722291,722836,722291,0.906037,0.906037,2,722291,722836,722291,722836]
["ACT01_03315","D",303,722838,723140,722838,0.7908,0.7908,2,722838,723140,722838,723140]
["ACT01_03320","D",1182,723095,724318,723095,0.924363,0.924363,1,723137,724318,723137,724318]
["ACT01_03325","D",894,724311,725213,724311,0.843631,0.843631,1,724320,725213,724320,725213]
["ACT01_00445","R",3525,88660,92190,92190,0.960629,0.960629,1,88660,92184,88660,92184]
["ACT01_00545","R",3516,114053,117568,117568,0.957369,0.957369,1,114053,117568,114053,117568]
["ACT01_02090","R",3534,444651,448184,448184,0.903165,0.903165,1,444651,448184,444651,448184]
["ACT01_02810","D",3513,596765,600277,596765,0.952087,0.952087,1,596765,600277,596765,600277]
["ACT01_03520","D",3543,762936,766517,762936,0.96161,0.96161,1,762984,766517,762984,766517]
["ACT01_06665","D",3513,1431065,1434691,1431065,0.956648,0.956648,1,1431176,1434691,1431176,1434691]
["ACT01_12570","R",3513,2614910,2618422,2618422,0.984267,0.984267,1,2614910,2618422,2614910,2618422]
["ACT01_05435","D",1194,1166355,1167548,1166355,0.909268,0.909268,1,1166355,1167548,1166355,1167548]
["ACT01_13325","R",1035,2773307,2774350,2774350,0.956383,0.956383,1,2773307,2774341,2773307,2774341]
["ACT01_04870","D",1488,1046336,1047823,1046336,0.970058,0.970058,1,1046336,1047823,1046336,1047823]
["ACT01_02465","D",1020,521154,522200,521154,0.95447,0.95447,1,521181,522200,521181,522200]
["ACT01_03450","D",1029,750673,751713,750673,0.898192,0.898192,1,750685,751713,750685,751713]
["ACT01_04805","D",1137,1035329,1036465,1035329,0.928089,0.928089,1,1035329,1036465,1035329,1036465]
["ACT01_04800","D",1536,1033769,1035328,1033769,0.902612,0.902612,1,1033790,1035328,1033793,1035328]
["ACT01_05115","D",1098,1094209,1095306,1094209,0.952511,0.952511,1,1094209,1095306,1094209,1095306]
["ACT01_06790","R",1158,1469972,1471138,1471138,0.983037,0.983037,1,1469972,1471138,1469972,1471138]
["ACT01_11045","R",1089,2325930,2327018,2327018,0.939782,0.939782,1,2325930,2327018,2325930,2327018]
["ACT01_07765","R",1194,1658098,1659357,1659357,0.94161,0.94161,1,1658098,1659291,1658098,1659291]
["ACT01_10830","R",783,2275554,2276366,2276366,0.911704,0.911704,1,2275554,2276336,2275554,2276336]
["ACT01_10835","R",858,2276382,2277344,2277239,0.858082,0.949217,1,2276382,2277239,2276382,2277239]
["ACT01_12410","R",933,2579438,2580403,2580403,0.880525,0.880525,2,2579438,2580370,2579438,2580361]
["ACT01_02995","D",417,645313,645729,645313,0.931936,0.931936,2,645313,645729,645313,645729]
["ACT01_00280","R",1140,54829,56010,56010,0.945574,0.945574,2,54829,56004,54829,55968]
["ACT01_02990","D",1190,644107,645285,644107,0.947605,0.947605,1,644146,645285,644146,645285]
["ACT01_10950","R",1152,2299886,2301061,2301061,0.975913,0.975913,1,2299886,2301037,2299886,2301037]
["ACT01_11040","R",1209,2324220,2325428,2325428,0.93964,0.93964,1,2324220,2325428,2324220,2325428]
["ACT01_09515","R",1005,2015024,2016034,2016034,0.960929,0.960929,2,2015024,2016028,2015024,2016028]
["ACT01_09520","R",786,2016043,2016828,2016828,0.897165,0.897165,1,2016043,2016828,2016043,2016828]
["ACT01_10940","R",1008,2297971,2298984,2298984,0.966143,0.966143,1,2297971,2298978,2297971,2298978]
["ACT01_10945","R",816,2299000,2299815,2299815,0.929192,0.929192,1,2299000,2299815,2299000,2299815]
["ACT01_02540","D",1338,538940,540277,538940,0.903171,0.903171,1,538940,540277,538940,540277]
["ACT01_02765","D",1359,586114,587496,586114,0.944452,0.944452,1,586138,587496,586138,587496]
["ACT01_03685","D",1338,800258,801637,800258,0.885892,0.885892,1,800300,801637,800300,801637]
["ACT01_04510","D",1356,976512,977870,976512,0.847853,0.847853,1,976515,977870,976515,977870]
["ACT01_04515","D",1038,977888,978925,977888,0.907817,0.907817,1,977888,978925,977888,978925]
["ACT01_04520","D",549,978927,979475,978927,0.870911,0.870911,1,978927,979475,978927,979475]
["ACT01_04525","D",624,979472,980101,979472,0.815598,0.815598,1,979478,980101,979478,980101]
["ACT01_04530","D",576,980101,980676,980221,0.772049,0.915884,2,980101,980676,980101,980676]
["ACT01_04535","D",864,980702,981565,980702,0.905003,0.905003,1,980702,981565,980702,981565]

{"sheet":"gene features","index":3,"n_rows":48,"n_cols":8,"rows_kept":48}
["CDS","GC Content","GC1 Content","GC2 Content","GC3 Content","CAI","GCskew","R/Y ratio"]
["ACT01_13720",47.9,58.64,37.15,47.9,0.7,-0.041,1.098]
["ACT01_13730",49.74,52.73,44.14,52.34,0.63,-0.052,0.839]
["ACT01_00410",46.29,55.8,37.62,45.45,0.73,-0.124,1.122]
["ACT01_04310",59.62,67.67,42.3,68.88,0.59,-0.01,0.998]
["ACT01_03310",49.63,64.29,40.66,43.96,0.69,-0.07,1.124]
["ACT01_03315",48.18,56.44,41.58,46.53,0.67,0.014,0.955]
["ACT01_03320",49.83,61.17,39.59,48.73,0.7,-0.036,1.014]
["ACT01_03325",48.99,53.36,45.64,47.99,0.66,-0.05,1.108]
["ACT01_00445",49.25,56.68,39.4,51.66,0.8,0.035,0.999]
["ACT01_00545",49.72,59.3,39.85,50,0.83,0.015,0.986]
["ACT01_02090",47.57,54.67,40.66,47.37,0.65,0.051,1.019]
["ACT01_02810",51.15,56.87,39.71,56.87,0.77,-0.034,1.146]
["ACT01_03520",50.72,57.24,39.88,55.04,0.79,0.008,1.055]
["ACT01_06665",55.31,58.33,40.31,67.29,0.77,0.023,1.127]
["ACT01_12570",55.85,58.67,40.65,68.23,0.76,0.031,1.118]
["ACT01_05435",51.34,57.79,38.44,57.79,0.82,0.047,1.034]
["ACT01_13325",52.17,62.32,41.16,53.04,0.81,0.052,0.971]
["ACT01_04870",51.75,57.26,42.34,55.65,0.68,-0.034,1.15]
["ACT01_02465",53.24,62.65,37.65,59.41,0.72,0.009,1.061]
["ACT01_03450",54.13,61.22,43.44,57.73,0.58,-0.102,1.108]
["ACT01_04805",49.87,55.94,40.37,53.3,0.64,-0.016,1.056]
["ACT01_04800",50.07,57.62,40.62,51.95,0.58,-0.048,1.197]
["ACT01_05115",56.1,62.84,41.8,63.66,0.78,0.088,1.007]
["ACT01_06790",52.59,59.33,40.93,57.51,0.7,0.084,0.976]
["ACT01_11045",52.71,58.68,42.7,56.75,0.59,-0.091,1.123]
["ACT01_07765",51.93,61.31,44.47,50,0.83,0.032,1.01]
["ACT01_10830",49.81,56.71,38.7,54.02,0.82,-0.005,1.122]
["ACT01_10835",48.48,57.34,34.96,53.15,0.86,-0.014,1.129]
["ACT01_12410",38.8,48.23,33.44,34.73,0.65,-0.144,1.19]
["ACT01_02995",44.12,48.92,38.85,44.6,0.77,-0.033,1.128]
["ACT01_00280",47.89,58.42,40.79,44.47,0.66,-0.128,1.184]
["ACT01_02990",48.77,56.84,39.21,50.26,0.75,-0.076,1.188]
["ACT01_10950",50.17,57.55,36.72,56.25,0.81,0,1.125]
["ACT01_11040",49.13,57.82,36.23,53.35,0.83,0.04,1.07]
["ACT01_09515",52.54,61.79,40.6,55.22,0.64,-0.11,1.194]
["ACT01_09520",52.42,62.21,42.37,52.67,0.63,-0.112,1.298]
["ACT01_10940",50.6,60.42,38.99,52.38,0.82,0.004,1.045]
["ACT01_10945",49.14,61.03,36.76,49.63,0.8,0.037,1.142]
["ACT01_02540",55.61,58.52,40.81,67.49,0.61,0.024,1.033]
["ACT01_02765",49.96,55.41,36.87,57.62,0.73,-0.025,1.123]
["ACT01_03685",53.21,60.54,41.7,57.4,0.63,-0.034,1.04]
["ACT01_04510",49.26,57.08,41.15,49.56,0.75,-0.042,1.106]
["ACT01_04515",50.29,54.62,43.64,52.6,0.71,-0.015,0.887]
["ACT01_04520",48.27,53.55,41.53,49.73,0.76,-0.049,1.223]
["ACT01_04525",47.92,50.48,36.54,56.73,0.75,0.01,0.857]
["ACT01_04530",47.57,50.52,34.38,57.81,0.71,0.044,0.761]
["ACT01_04535",50.23,57.29,43.75,49.65,0.74,-0.037,1.062]

{"sheet":"protein features","index":4,"n_rows":48,"n_cols":14,"rows_kept":48}
["CDS","Mw (Da)","Hydrophobicity","Tiny","Small","Aliphatic","Aromatic","Non Polar","Polar","Charged","Basic","Acidic","pI","Oxyphobic Index"]
["ACT01_13720",46288.42,-0.04,29.51,51.52,23.42,9.6,56.91,43.09,27.63,14.29,13.35,5.75,8.96]
["ACT01_13730",53017.79,1.21,36.79,55.58,33.07,9.2,75.54,24.46,9.39,4.89,4.5,8.12,8.25]
["ACT01_00410",34787.34,-0.09,30.5,54.4,22.01,10.69,56.92,43.08,26.73,13.52,13.21,5.63,9.72]
["ACT01_04310",36242.24,-0.01,29.39,49.7,24.24,11.21,64.55,35.45,24.24,12.12,12.12,5.57,10.06]
["ACT01_03310",19455.47,0.01,31.49,57.46,24.86,8.29,58.56,41.44,25.97,13.26,12.71,5.93,9.33]
["ACT01_03315",10940.42,0.02,29,56,23,9,62,38,27,15,12,6.45,10.19]
["ACT01_03320",42909.38,-0.04,31.3,52.16,22.65,9.67,59.03,40.97,24.43,10.69,13.74,4.82,9.75]
["ACT01_03325",32074.38,-0.17,36.36,55.89,17.85,11.45,59.6,40.4,22.9,12.79,10.1,8.04,9.66]
["ACT01_00445",129304.78,-0.26,31.26,53.24,18.82,12.01,56.64,43.36,24.79,12.61,12.18,5.79,9.64]
["ACT01_00545",127759.08,-0.23,31.34,53.71,19.13,11.36,57.56,42.44,25.88,12.81,13.07,5.51,9.37]
["ACT01_02090",130118.98,-0.27,31.18,51.32,19.54,11.89,55.23,44.77,25.15,13.59,11.55,6.34,9.44]
["ACT01_02810",129330.46,-0.29,30.6,50.51,17.86,12.14,56.41,43.59,26.58,13.59,12.99,5.86,9.52]
["ACT01_03520",129676.82,-0.2,31.19,52.71,19.66,12.12,57.46,42.54,25,12.97,12.03,5.93,9.53]
["ACT01_06665",128281.58,-0.26,31.88,53.93,18.72,10.94,56.07,43.93,24.02,11.97,12.05,5.57,9.56]
["ACT01_12570",128200.48,-0.25,32.14,54.02,18.72,11.11,56.24,43.76,24.1,12.05,12.05,5.59,9.57]
["ACT01_05435",42808.72,-0.02,31.23,53.65,23.68,7.81,58.19,41.81,24.69,13.1,11.59,6.24,9.53]
["ACT01_13325",36828.76,0,32.56,56.4,24.13,6.1,57.56,42.44,24.42,12.5,11.92,6.43,9.55]
["ACT01_04870",53411.88,-0.1,33.74,54.95,21.82,7.88,56.16,43.84,23.03,11.52,11.52,5.66,9.78]
["ACT01_02465",37054.13,0.02,28.32,52.8,25.37,10.32,58.41,41.59,26.84,14.16,12.68,5.96,9.69]
["ACT01_03450",36916.86,0.02,32.75,55.26,21.93,10.82,60.23,39.77,24.56,12.57,11.99,5.72,9.72]
["ACT01_04805",41350.71,-0.1,32.8,51.32,20.9,10.32,55.56,44.44,24.87,13.23,11.64,6.15,9.38]
["ACT01_04800",55653.82,-0.07,30.72,51.27,23.87,7.63,57.34,42.66,24.46,12.52,11.94,5.96,9.67]
["ACT01_05115",38483.45,0.17,35.07,57.53,24.66,7.12,61.1,38.9,23.56,10.96,12.6,5.07,9.69]
["ACT01_06790",41455.05,0.04,33.51,51.43,22.34,9.61,58.96,41.04,21.82,10.91,10.91,5.54,9.17]
["ACT01_11045",39417.54,-0.04,33.15,53.87,22.38,10.5,57.46,42.54,22.93,10.77,12.15,5.1,9.55]
["ACT01_07765",41766.31,0.03,36.78,55.92,21.91,6.3,59.95,40.05,21.91,11.84,10.08,7.14,9.66]
["ACT01_10830",27776.94,0.03,31.54,52.69,22.31,6.92,61.15,38.85,22.31,11.15,11.15,6.68,9.43]
["ACT01_10835",31062.97,-0.03,27.72,51.23,23.86,7.72,59.3,40.7,28.07,14.04,14.04,5.74,9.52]
["ACT01_12410",35056.06,-0.2,25.16,47.42,23.23,10.65,54.19,45.81,27.1,13.55,13.55,5.74,9.32]
["ACT01_02995",15032.8,-0.03,34.06,53.62,21.01,10.87,55.07,44.93,26.09,14.49,11.59,6.56,9.46]
["ACT01_00280",41062.46,0,32.98,51.98,20.84,8.71,59.37,40.63,23.22,11.08,12.14,5.32,9.92]
["ACT01_02990",41491.82,-0.21,32.72,45.65,19.53,9.76,56.46,43.54,26.39,12.66,13.72,5.38,9.18]
["ACT01_10950",41829.08,-0.22,31.85,48.3,19.58,10.44,56.92,43.08,27.15,12.79,14.36,5.15,9.39]
["ACT01_11040",43995.44,-0.19,29.85,50.5,22.39,9.45,56.47,43.53,26.62,12.44,14.18,5.11,9.48]
["ACT01_09515",35833.58,-0.02,31.74,52.69,25.45,6.89,58.08,41.92,25.45,11.68,13.77,4.99,8.93]
["ACT01_09520",27301.24,0.06,34.87,57.85,24.14,3.45,56.71,43.3,23.75,11.11,12.64,5.1,9.13]
["ACT01_10940",35573.34,0.03,31.34,55.52,24.18,7.76,61.49,38.51,25.07,11.64,13.43,5.03,9.3]
["ACT01_10945",29373.7,-0.17,27.68,51.66,24.72,4.06,55.35,44.65,26.57,12.18,14.39,5.03,9.33]
["ACT01_02540",49468.11,-0.27,30.11,51.24,20,11.91,54.61,45.39,24.72,12.58,12.13,5.61,9.65]
["ACT01_02765",49970.74,-0.25,27.88,52.43,22.35,11.5,54.65,45.35,25.44,12.83,12.61,5.63,9.14]
["ACT01_03685",49548.36,-0.18,29.44,50.56,21.8,12.58,57.08,42.92,24.27,12.13,12.13,5.42,9.67]
["ACT01_04510",48656.53,-0.06,31.49,55.43,21.51,7.54,59.87,40.13,23.5,12.64,10.86,6.8,9.82]
["ACT01_04515",36725.94,0.66,34.78,55.65,26.96,11.01,70.14,29.86,12.17,7.25,4.93,8.68,9.05]
["ACT01_04520",19167.37,-0.13,35.71,56.04,18.68,6.04,57.14,42.86,23.63,13.19,10.44,9.04,8.82]
["ACT01_04525",22647.23,0.86,28.5,50.24,31.88,12.56,71.01,28.99,13.04,8.21,4.83,9.12,9.06]
["ACT01_04530",20761.17,1.2,29.32,49.74,36.13,13.09,72.77,27.23,8.9,4.71,4.19,6.76,8.31]
["ACT01_04535",30002.82,0.2,37.98,60.28,20.56,7.67,64.11,35.89,22.3,12.89,9.41,7.95,9.88]

{"sheet":"MaGe-Curated annotations","index":5,"n_rows":793,"n_cols":26,"rows_kept":793}
["ACT01_13720","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_11700",null,"Clostridium difficile 630","_","Conserved hypothetical protein","_",1.00234,1.00943,57.48,{"v":1e-171,"d":"1.00E-171"},1,1,"_","_","1 : Unknown","_","u : unknown","_","4 : Unknown function but conserved in other organisms",1,427,427,1,424,424]
[null,"CLOSTRIBL3_v1_11116",null,"Clostridiaceae BL-3","larA","Lactate racemase","LACTATE-RACEMASE-RXN ; RHEA:10960 ;",1,1.00708,57.38,{"v":4e-170,"d":"4.00E-170"},1,1,"4.S.107 : L-lactate ;","5.1.2.1","2 : Cytoplasmic","_","e : enzyme",24710389,"1c : Function from experimental evidences in the studied genus",1,426,427,1,423,424]
[null,"CLOSTRIBL6_v1_3221",null,"Clostridiales BL-6","larA","Lactate racemase","LACTATE-RACEMASE-RXN ; RHEA:10963 ;",0.99297,0.99531,57.31,{"v":1e-159,"d":"1.00E-159"},1,1,"_","5.1.2.1","2 : Cytoplasmic","_","e : enzyme",24710389,"2a : Function from experimental evidences in other organisms",6,427,427,5,423,426]
[]
["ACT01_13730","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","_",0.98434,0.99016,46.72,{"v":2E-155,"d":"2.00E-155"},1,1,"4.S.98 : lactate ;","_","11 : Membrane","_","t : transporter",10508058,"2a : Function from experimental evidences in other organisms",1,503,511,6,499,508]
[null,"CLOSTRIBL6_v1_3223",null,"Clostridiales BL-6","lctP","L-lactate permease","_",0.97099,0.98239,47.01,{"v":2e-144,"d":"2.00E-144"},1,1,"_","_","11 : Membrane","_","t : transporter",10508058,"2a : Function from experimental evidences in other organisms",4,498,511,6,504,517]
[null,"ECED1_5018","_","Escherichia coli ED1a","_","L-lactate permease","_",0.97297,0.9863,38.49,{"v":2E-120,"d":"2.00E-120"},1,1,"_","_","1 : Unknown","7 : Transport and binding proteins ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,500,511,6,507,518]
[]
["ACT01_00410","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_1444","_","Clostridiales BL-4","ldh","L-lactate dehydrogenase","L-LACTATE-DEHYDROGENASE-RXN ; RHEA:23447 ;",0.9717,0.97785,51.13,{"v":5e-116,"d":"5.00E-116"},1,1,"_","1.1.1.27","2 : Cytoplasmic","_","e : enzyme",11889109,"2a : Function from experimental evidences in other organisms",3,309,318,1,309,316]
[null,"CD630_21640","_","Clostridium difficile 630","ldh","L-lactate dehydrogenase (L-LDH)","_",0.98758,1,38.05,{"v":2e-76,"d":"2.00E-76"},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",1,310,318,1,317,322]
[null,"Ent638_2002","_","Enterobacter sp. 638","ldh","L-lactate dehydrogenase 2 (L-LDH 2)","_",0.91496,0.98113,37.5,{"v":1e-68,"d":"1.00E-68"},1,1,"_","1.1.1.27","2 : Cytoplasmic","6.8 : Glycolysis/gluconeogenesis ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,311,318,28,339,341]
[]
["ACT01_04310","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_10010",null,"Clostridiaceae BL-3","_","putative Lactate dehydrogenase","RHEA:23447 ;",0.72947,0.91515,41.39,{"v":8e-71,"d":"8.00E-71"},1,1,"_","1.1.1.27","2 : Cytoplasmic","_","e : enzyme",18356528,"3 : Putative function from multiple computational evidences",31,330,330,120,413,414]
[]
["ACT01_03310","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_3009",null,"Clostridiales BL-6","porC","Pyruvate synthase subunit PorC","PYRUFLAVREDUCT-RXN ;",0.97409,1.03867,42.02,{"v":1e-37,"d":"1.00E-37"},1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme","8620891, 7608066, 9495749","2a : Function from experimental evidences in other organisms",1,178,181,5,191,193]
[null,"CLOSTRIBL3_v1_12777",null,"Clostridiaceae BL-3","porC","Pyruvate synthase subunit PorC","PYRUFLAVREDUCT-RXN ; RHEA:12765 ;",0.87565,0.9337,40.83,{"v":3e-35,"d":"3.00E-35"},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",1,165,181,5,172,193]
[null,"NBG4_v1_970004",null,"Candidatus Sulfobium mesophilum","porC","Pyruvate synthase subunit PorC","PYRUFLAVREDUCT-RXN ; RHEA:12765 ;",0.89005,0.93923,40.59,{"v":8e-35,"d":"8.00E-35"},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",1,165,181,4,172,191]
[null,"MGMSRv2_1071",null,"Magnetospirillum gryphiswaldense MSR-1 v2","porC","Pyruvate synthase subunit porC","_",0.94681,0.98343,39.33,{"v":5e-33,"d":"5.00E-33"},1,1,"_","1.2.7.1","1 : Unknown","_","e : enzyme",8688087,"2a : Function from experimental evidences in other organisms",1,177,181,1,177,188]
[]
["ACT01_03315","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","_",0.52,0.91228,40.38,7e-10,3,3,"_","_","9 : Periplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",43,94,100,5,56,57]
[]
["ACT01_03320","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"NBG4_v1_970002",null,"Candidatus Sulfobium mesophilum","porA","Pyruvate synthase subunit PorA","PYRUFLAVREDUCT-RXN ; RHEA:12768 ;",0.93384,0.93622,41.96,{"v":8e-94,"d":"8.00E-94"},1,1,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","11265457, 8305426, 8620891","2a : Function from experimental evidences in other organisms",1,366,393,1,366,392]
[null,"CLOSTRIBL3_v1_12775",null,"Clostridiaceae BL-3","porA","Pyruvate synthase subunit PorA","RHEA:12765 ;",0.94911,0.95396,42.63,{"v":5e-92,"d":"5.00E-92"},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",1,372,393,1,372,391]
[null,"MGMSRv2_1070",null,"Magnetospirillum gryphiswaldense MSR-1 v2","porA","Pyruvate synthase subunit porA","_",0.89567,0.90956,40.62,{"v":4e-88,"d":"4.00E-88"},1,1,"_","1.2.7.1","1 : Unknown","_","e : enzyme","16980466, 8620891","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,360,393,7,355,387]
[null,"NIDE3874",null,"Candidatus Nitrospira defluvii","vorA","2-ketoisovalerate ferredoxin reductase, alpha subunit","_",0.87864,0.92112,42.54,{"v":3e-87,"d":"3.00E-87"},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)",3,360,393,2,361,412]
[null,"CLOSTRIBL6_v1_3011",null,"Clostridiales BL-6","porA","Pyruvate synthase subunit PorA","_",0.93639,0.94118,40.49,{"v":1e-85,"d":"1.00E-85"},1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme","8620891, 7608066, 9495749","2a : Function from experimental evidences in other organisms",7,372,393,7,371,391]
[null,"SCFA_v1_3810001",null,"Ca. Propionivorax syntrophicum F70","porA","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit","PYRUFLAVREDUCT-RXN ; RHEA:12765 ; RHEA:32135 ;",0.8626,0.87824,41.89,{"v":6e-85,"d":"6.00E-85"},1,1,"_","1.2.7.1","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,339,393,2,337,386]
[null,"HELPY_1079",null,"Helicobacter pylori B38","porA","Pyruvate synthase subunit porA (Pyruvate oxidoreductase alpha chain) (POR) (Pyruvic-ferredoxin oxidoreductase subunit alpha)","_",0.9484,0.98219,36.27,{"v":2E-73,"d":"2.00E-73"},1,1,"1.7.28 : Pyruvate catabolism ;","1.2.7.1","1 : Unknown","6.11 : TCA cycle ;","e : enzyme","7608066, 9495749","1a : Function from experimental evidences in the studied strain",9,390,393,15,399,407]
[]
["ACT01_03325","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_3810002",null,"Ca. Propionivorax syntrophicum F70","porB","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit","_",0.85531,0.89562,44.74,{"v":9e-73,"d":"9.00E-73"},1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",11,275,297,13,275,311]
[null,"MGMSRv2_1069",null,"Magnetospirillum gryphiswaldense MSR-1 v2","porB","Pyruvate synthase subunit porB","_",0.78287,0.86195,44.53,{"v":7e-71,"d":"7.00E-71"},1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme",8688087,"2a : Function from experimental evidences in other organisms",16,271,297,21,275,327]
[null,"CLOSTRIBL6_v1_3012",null,"Clostridiales BL-6","porB","Pyruvate synthase subunit PorB","_",0.97742,1.0202,39.27,{"v":2e-68,"d":"2.00E-68"},1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme","8620891, 7608066, 9495749","2a : Function from experimental evidences in other organisms",5,290,297,2,304,310]
[null,"NBG4_v1_970001",null,"Candidatus Sulfobium mesophilum","porB","Pyruvate synthase subunit PorB","PYRUFLAVREDUCT-RXN ; RHEA:12765 ;",0.93266,0.94539,39.71,{"v":1e-64,"d":"1.00E-64"},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",2,271,297,4,280,293]
[null,"CLOSTRIBL3_v1_12774",null,"Clostridiaceae BL-3","porB","Pyruvate synthase subunit PorB","RHEA:12765 ;",0.99676,1.03704,36.69,{"v":2e-64,"d":"2.00E-64"},2,1,"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",1,295,297,1,308,309]
[null,"NIDE3873",null,"Candidatus Nitrospira defluvii","vorB","2-ketoisovalerate ferredoxin reductase, beta subunit","_",0.94231,0.9899,40.14,{"v":1E-53,"d":"1.00E-53"},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)",11,287,297,17,304,312]
[null,"LHAv2_1715","_","Legionella hackeliae","_","transposase (fragment)","_",0.12121,0.87805,44.44,0.011,1,1,"_","_","2 : Cytoplasmic","_","h : extrachromosomal origin","_","3 : Putative function from multiple computational evidences",241,276,297,7,40,41]
[]
["ACT01_00445","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_1030024",null,"Desulfosporosinus sp. SbF1","pfoA_3a","fragment of pyruvate synthase (part 1/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.58603,0.97589,58.28,0,3,6,"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",8,687,1174,7,688,705]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.39097,0.9766,59.48,0,2,5,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"2a : Function from experimental evidences in other organisms",1,458,1174,1,458,470]
[null,"SBF1_v1_1030023",null,"Desulfosporosinus sp. SbF1","pfoA_3b","fragment of pyruvate synthase (part 2/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.39779,1,48.61,{"v":4e-139,"d":"4.00E-139"},5,7,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",712,1174,1174,1,464,467]
[]
["ACT01_00545","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_10343",null,"Clostridiaceae BL-3","pfo","Pyruvate-flavodoxin oxidoreductase","PYFLAVOXRE-RXN ; RHEA:12765 ;",0.99573,0.99829,66.64,0,1,2,"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",1,1162,1171,1,1161,1168]
[null,"CLOAM0324",null,"Candidatus Cloacamonas acidaminovorans Evry","_","putative pyruvate-ferredoxin oxidoreductase (por-like) or pyruvate-flavodoxin oxidoreductase (ydbK-like), 4Fe-4S domain","_",1.00256,1.00427,52.81,0,1,3,"1.7.1 : Unassigned reversible reactions ; 1.1.2.3 : Propionate degradation ; 1.3.5 : Fermentation ;","1.2.7.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",6,1168,1171,8,1173,1173]
[null,"SBF1_v1_1030024",null,"Desulfosporosinus sp. SbF1","pfoA_3a","fragment of pyruvate synthase (part 1/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.58753,0.97589,62.06,0,3,3,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",1,683,1171,1,688,705]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.39112,0.97447,63.97,0,2,3,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"2a : Function from experimental evidences in other organisms",1,457,1171,1,458,470]
[null,"SBF1_v1_1030023",null,"Desulfosporosinus sp. SbF1","pfoA_3b","fragment of pyruvate synthase (part 2/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.39283,0.98501,56.52,{"v":1E-166,"d":"1.00E-166"},4,5,"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",711,1164,1171,4,459,467]
[null,"NBG4_v1_230036","_","Candidatus Sulfobium mesophilum","nifJ","Pyruvate:ferredoxin oxidoreductase","PYRUFLAVREDUCT-RXN ;",0.22801,0.98162,58.05,{"v":2e-96,"d":"2.00E-96"},1,1,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","1 : Unknown","6 : Energy metabolism ;","e : enzyme",11167002,"2a : Function from experimental evidences in other organisms",3,269,1171,4,270,272]
[]
["ACT01_02090","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_1030024",null,"Desulfosporosinus sp. SbF1","pfoA_3a","fragment of pyruvate synthase (part 1/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.58369,0.97447,54.88,0,3,7,"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",6,686,1177,4,688,705]
[null,"SBF1_v1_1030023",null,"Desulfosporosinus sp. SbF1","pfoA_3b","fragment of pyruvate synthase (part 2/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.39932,1.00642,56.81,{"v":8e-180,"d":"8.00E-180"},5,3,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",711,1177,1177,1,464,467]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.38658,0.96809,57.58,{"v":2e-178,"d":"2.00E-178"},2,6,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"2a : Function from experimental evidences in other organisms",6,458,1177,5,458,470]
[]
["ACT01_02810","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_1030024",null,"Desulfosporosinus sp. SbF1","pfoA_3a","fragment of pyruvate synthase (part 1/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.58974,0.97872,57.68,0,3,4,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",1,685,1170,1,688,705]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.38974,0.97021,55.04,{"v":5E-175,"d":"5.00E-175"},2,7,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"2a : Function from experimental evidences in other organisms",4,459,1170,3,458,470]
[null,"SBF1_v1_1030023",null,"Desulfosporosinus sp. SbF1","pfoA_3b","fragment of pyruvate synthase (part 2/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.39316,0.98501,53.7,{"v":2E-169,"d":"2.00E-169"},4,4,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",710,1163,1170,1,460,467]
[]
["ACT01_03520","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_1030024",null,"Desulfosporosinus sp. SbF1","pfoA_3a","fragment of pyruvate synthase (part 1/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.58051,0.97163,56.2,0,3,5,"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",9,689,1180,4,688,705]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.38644,0.97021,60.96,0,2,4,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"2a : Function from experimental evidences in other organisms",7,461,1180,3,458,470]
[null,"SBF1_v1_1030023",null,"Desulfosporosinus sp. SbF1","pfoA_3b","fragment of pyruvate synthase (part 2/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.39746,1.00428,52.67,{"v":3e-166,"d":"3.00E-166"},5,6,"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",714,1177,1180,1,461,467]
[]
["ACT01_06665","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_10343","_","Clostridiaceae BL-3","pfo","Pyruvate-flavodoxin oxidoreductase","PYFLAVOXRE-RXN ; RHEA:12765 ;",0.99573,0.99743,71.24,0,1,1,"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",4,1168,1170,3,1166,1168]
[null,"CD630_26820","_","Clostridium difficile 630","pfo","Pyruvate-ferredoxin oxidoreductase","_",1.00085,1.00855,62.37,0,1,1,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"1c : Function from experimental evidences in the studied genus",1,1168,1170,1,1179,1179]
[null,"SBF1_v1_1620011","_","Desulfosporosinus sp. SbF1","pfoA_2","pyruvate synthase","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.9983,1.00171,60.07,0,1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,1168,1170,1,1171,1174]
[null,"CLOSTRIBL4_v1_0841","_","Clostridiales BL-4","PFOF","Pyruvate:ferredoxin oxidoreductase","PYRUFLAVREDUCT-RXN ; RHEA:12768 ;",0.99747,1.0094,58.76,0,1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme",18631365,"2a : Function from experimental evidences in other organisms",3,1170,1170,4,1184,1184]
[null,"CLOSTRIBL6_v1_0279","_","Clostridiales BL-6","PFOF","Pyruvate:ferredoxin oxidoreductase","PYRUFLAVREDUCT-RXN ; RHEA:12768 ;",0.99747,1.01026,58.46,0,1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme","8620891, 7608066, 9495749","2a : Function from experimental evidences in other organisms",1,1166,1170,1,1182,1185]
[null,"Ent638_2136","_","Enterobacter sp. 638","ydbK","Putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; 4Fe-4S cluster binding protein","_",1.00767,1.01111,46.83,0,1,1,"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)",5,1169,1170,1,1167,1174]
[null,"BN11v3_340013","_","Tetrasphaera australiensis Ben110","_","putative pyruvate-flavodoxin oxidoreductase","_",0.99665,1.01624,46.09,0,1,1,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",8352652,"3 : Putative function from multiple computational evidences",6,1170,1170,7,1181,1193]
[null,"Spro_2604","_","Serratia proteamaculans 568","_","Putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; 4Fe-4S cluster binding protein (NifJ)","_",0.99915,1.00513,46.51,0,1,1,"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",5,1161,1170,1,1162,1177]
[null,"ECK1374","_","Escherichia coli K12","ydbK","putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; 4Fe-4S cluster binding protein","PYRUFLAVREDUCT-RXN ;",1.00681,1.01026,46.02,0,1,1,"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",5,1169,1170,1,1167,1174]
[null,"SBF1_v1_1030024",null,"Desulfosporosinus sp. SbF1","pfoA_3a","fragment of pyruvate synthase (part 1/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.59145,0.98156,62.72,0,3,2,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",4,690,1170,3,694,705]
[null,"VCA0530","_","Vibrio cholerae N16961","_","putative Pyruvate-flavodoxin oxidoreductase","_",0.94615,1.02595,38.93,0,1,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",9,1099,1170,6,1072,1079]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.39145,0.97447,64.85,0,2,1,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"2a : Function from experimental evidences in other organisms",1,458,1170,1,458,470]
[null,"SBF1_v1_1030023",null,"Desulfosporosinus sp. SbF1","pfoA_3b","fragment of pyruvate synthase (part 2/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.39573,0.99143,58.96,0,4,2,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",711,1170,1170,3,464,467]
[]
["ACT01_12570","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_10343","_","Clostridiaceae BL-3","pfo","Pyruvate-flavodoxin oxidoreductase","PYFLAVOXRE-RXN ; RHEA:12765 ;",0.99573,0.99743,71.24,0,1,1,"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",4,1168,1170,3,1166,1168]
[null,"CLOAM0324","_","Candidatus Cloacamonas acidaminovorans Evry","_","putative pyruvate-ferredoxin oxidoreductase (por-like) or pyruvate-flavodoxin oxidoreductase (ydbK-like), 4Fe-4S domain","_",1.00256,1.00513,52.13,0,1,1,"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",7,1168,1170,8,1172,1173]
[null,"AZOLI_p30297","_","Azospirillum lipoferum 4B","_","putative pyruvate-ferredoxin/flavodoxin oxidoreductase","_",1.00512,1.00684,47.62,0,1,1,"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",8,1170,1170,1,1171,1172]
[null,"BN874v1_1210009","_","Candidatus Contendobacter odensis Run_B_J11","_","putative pyruvate-flavodoxin oxidoreductase (nifJ)","_",0.9933,1.01368,46.04,0,1,1,"_","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",4,1169,1170,5,1183,1194]
[null,"BN873v1_150048","_","Candidatus Competibacter denitrificans Run_A_D11","_","putative pyruvate-flavodoxin oxidoreductase (nifJ)","_",1.00503,1.02479,45.95,0,1,1,"_","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",4,1169,1170,5,1183,1193]
[null,"FRAAL3253","_","Frankia alni ACN14a","_","Pyruvate-flavodoxin oxidoreductase","_",1.00681,1.01111,45.31,0,1,1,"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)",3,1167,1170,1,1163,1175]
[null,"SBF1_v1_1030024",null,"Desulfosporosinus sp. SbF1","pfoA_3a","fragment of pyruvate synthase (part 1/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.59145,0.98156,62.86,0,3,1,"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",4,690,1170,3,694,705]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.39145,0.97447,64.41,0,2,2,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"2a : Function from experimental evidences in other organisms",1,458,1170,1,458,470]
[null,"SBF1_v1_1030023",null,"Desulfosporosinus sp. SbF1","pfoA_3b","fragment of pyruvate synthase (part 2/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.39573,0.99143,59.4,0,4,1,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",711,1170,1170,3,464,467]
[]
["ACT01_05435","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_10746",null,"Clostridiaceae BL-3","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ; RHEA:11352 ;",0.98997,0.99496,63.29,0,1,1,"_","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",1,395,397,1,395,399]
[null,"CD630_11750",null,"Clostridium difficile 630","ackA","Acetate kinase (Acetokinase)","_",0.99749,1,58.69,{"v":2e-166,"d":"2.00E-166"},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",1,395,397,1,397,398]
[null,"SBF1_v1_800074","_","Desulfosporosinus sp. SbF1","ackA","acetate kinase","ACETATEKIN-RXN ; RHEA:11355 ;",0.99496,0.99496,57.22,{"v":6e-163,"d":"6.00E-163"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,394,397,1,395,397]
[null,"BSU29470","_","Bacillus subtilis 168","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ; RHEA:11352 ;",0.98741,0.99241,55.61,{"v":7e-157,"d":"7.00E-157"},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",3,394,397,4,393,395]
[null,"CLOSTRIBL6_v1_2260",null,"Clostridiales BL-6","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ; RHEA:11352 ;",0.99252,1.00252,52.26,{"v":2e-144,"d":"2.00E-144"},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",1,395,397,1,398,401]
[null,"CLOSTRIBL4_v1_2217",null,"Clostridiales BL-4","ackA","Acetate kinase","ACETATEKIN-RXN ; RHEA:11355 ;",0.95923,1.00756,52,{"v":3e-142,"d":"3.00E-142"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","10360571, 10074080","2a : Function from experimental evidences in other organisms",1,396,397,1,399,417]
[null,"EFER_2027","_","Escherichia fergusonii ATCC 35469T","_","putative acetate/propionate kinase pduW","_",0.9703,0.98741,47.7,{"v":2E-132,"d":"2.00E-132"},1,1,"_","2.7.2.1","1 : Unknown","_","e : enzyme",10498708,"3 : Putative function from multiple computational evidences",3,394,397,5,392,404]
[null,"BTCD_v1_0691","_","Brochothrix thermosphacta CD337","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ;",0.97756,0.98741,50.51,{"v":2E-132,"d":"2.00E-132"},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",3,390,397,4,393,401]
[null,"SSV_v1_0105","_","Streptococcus sanguinis 2908","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ;",0.97985,0.97985,48.59,{"v":2e-127,"d":"2.00E-127"},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",6,392,397,7,392,397]
[null,"NMA2050","_","Neisseria meningitidis Z2491","ackA2","acetate kinase 2 (acetokinase 2)","_",0.99749,1.00252,46.73,{"v":2e-117,"d":"2.00E-117"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,395,397,5,396,399]
[null,"NMV_0875","_","Neisseria meningitidis NEM8013","ackA1","acetate kinase 1 (acetokinase 1)","_",0.99749,1,45.59,{"v":3e-117,"d":"3.00E-117"},1,1,"1.3.5 : Fermentation ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,394,397,5,395,398]
[null,"VC1098","_","Vibrio cholerae N16961","ackA","acetate kinase","_",1,1.00252,44.72,{"v":2E-113,"d":"2.00E-113"},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",2,396,397,4,397,398]
[null,"VIBNIv4_A2401","_","Vibrio nigripulchritudo SFn1","ackA","acetate kinase","_",0.99497,0.99748,43.94,{"v":6e-110,"d":"6.00E-110"},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",2,394,397,4,395,398]
[null,"BN12v2_1100005","_","Tetrasphaera japonica T1-X7","ackA","Acetate kinase","_",0.99748,0.99748,44.44,{"v":7e-110,"d":"7.00E-110"},1,1,"_","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",2,397,397,5,397,397]
[null,"VIBNIv4_B1211","_","Vibrio nigripulchritudo SFn1","ackA","Acetate kinase","_",1.00252,1.00252,44.72,{"v":8e-110,"d":"8.00E-110"},1,1,"7.1 : Cytoplasm ; 1.7.29 : Acetate catabolism ; 1.3.7 : Anaerobic respiration ; 1.5.3.5 : Coenzyme A ;","2.7.2.1","2 : Cytoplasmic","6.3 : Anaerobic ; 4 : Biosynthesis of cofactors, prosthetic groups, and carriers ;","e : enzyme","2536666, 7883769","2a : Function from experimental evidences in other organisms",3,395,397,6,397,397]
[null,"VS_II1135","_","Vibrio tasmaniensis LGP32","ackA-2","Acetate kinase","ACETATEKIN-RXN ; RXN-7958 ;",1.00252,1.00252,44.47,{"v":1E-107,"d":"1.00E-107"},1,1,"1.3.5 : Fermentation ; 1.5.3.5 : Coenzyme A ;","2.7.2.1","2 : Cytoplasmic","6.3 : Anaerobic ; 6.7 : Fermentation ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,395,397,6,397,397]
[null,"BN13v1_910016","_","Tetrasphaera jenkinsii Ben74","ackA","Acetate kinase","_",0.99748,1.00508,43.69,{"v":2e-104,"d":"2.00E-104"},1,1,"_","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",3,397,397,4,394,394]
[null,"MARHY2148","_","Marinobacter hydrocarbonoclasticus ATCC 49840","ackA","acetate kinase A and propionate kinase 2","_",0.99002,1,41.81,{"v":2e-103,"d":"2.00E-103"},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",3,396,397,5,393,401]
[null,"BN45v3_10447","_","Mycobacterium canettii STB-J","ackA","Putative acetate kinase AckA (acetokinase)","_",0.97985,1.01039,42.93,{"v":3E-98,"d":"3.00E-98"},1,1,"7 : intermediary metabolism and respiration ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",3,390,397,5,375,385]
[null,"BN42v3_20130","_","Mycobacterium canettii STB-K","ackA","Putative acetate kinase AckA (acetokinase)","_",0.97985,1.01039,42.67,{"v":2e-97,"d":"2.00E-97"},1,1,"7 : intermediary metabolism and respiration ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",3,390,397,5,375,385]
[null,"BN44v3_10450","_","Mycobacterium canettii STB-D","ackA","Putative acetate kinase AckA (acetokinase)","_",0.97985,1.01039,42.93,{"v":3e-97,"d":"3.00E-97"},1,1,"7 : intermediary metabolism and respiration ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",3,390,397,5,375,385]
[null,"BN43v3_10442","_","Mycobacterium canettii STB-L","ackA","Putative acetate kinase AckA (acetokinase)","_",0.97985,1.01039,42.67,{"v":1e-96,"d":"1.00E-96"},1,1,"7 : intermediary metabolism and respiration ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",3,390,397,5,375,385]
[null,"BN10v3_560037","_","Tetrasphaera elongata Lp2","ackA","Acetate kinase","_",0.99748,1.05319,41.67,{"v":5e-96,"d":"5.00E-96"},1,1,"_","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",2,396,397,4,371,376]
[null,"BN11v3_1350008","_","Tetrasphaera australiensis Ben110","ackA","acetate kinase A and propionate kinase 2","_",0.98246,0.98741,42.6,{"v":1e-95,"d":"1.00E-95"},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",3,393,397,8,394,399]
[null,"NIDE3516","_","Candidatus Nitrospira defluvii","ackA","Acetate kinase","_",0.98515,1.00252,41.96,{"v":7E-94,"d":"7.00E-94"},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",3,396,397,11,399,404]
[null,"ABAYE3282","_","Acinetobacter baumannii AYE","ack","acetate kinase (propionate kinase)","_",0.99,0.99748,40.15,{"v":5e-93,"d":"5.00E-93"},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",3,395,397,5,387,400]
[null,"BRADO1872","_","Bradyrhizobium sp. ORS278","tdcD","propionate kinase/acetate kinase C, anaerobic","_",1.01008,1.01519,39.4,{"v":3e-92,"d":"3.00E-92"},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",3,397,397,6,393,395]
[null,"BN77v1_3277","_","Rhizobium mesoamericanum STM3625","ackA","Acetate kinase","_",1.00504,1.02308,40.35,{"v":4E-92,"d":"4.00E-92"},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",3,396,397,4,389,390]
[null,"ACIAD0541","_","Acinetobacter baylyi ADP1","ack","acetate kinase (propionate kinase)","ACETATEKIN-RXN ; PROPKIN-RXN ; RXN-7958 ; RHEA:11355 ; RHEA:23151 ;",0.99002,1,41.06,{"v":5e-92,"d":"5.00E-92"},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",3,395,397,5,388,401]
[null,"BN874v1_640030","_","Candidatus Contendobacter odensis Run_B_J11","ackA","Acetate/propionate kinase","_",1.01008,1.02296,40.65,{"v":4e-91,"d":"4.00E-91"},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",3,395,397,5,391,392]
[null,"MGMSRv2_1019","_","Magnetospirillum gryphiswaldense MSR-1 v2","ackA","Acetate kinase","_",0.96163,1.01008,38.65,{"v":9e-89,"d":"9.00E-89"},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",3,394,397,22,408,417]
[null,"p2METDI0002","_","Methylobacterium extorquens DM4","ackA","acetate kinase","_",0.98992,1.00512,39.69,{"v":3e-88,"d":"3.00E-88"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme",10094701,"2a : Function from experimental evidences in other organisms",2,392,397,5,388,391]
[null,"METDI0790","_","Methylobacterium extorquens DM4","_","putative acetate kinase (ackA)","_",1.00504,1.01269,40.35,{"v":4e-87,"d":"4.00E-87"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,395,397,9,391,394]
[null,"AZOLI_p20461","_","Azospirillum lipoferum 4B","ackA2","Acetate kinase","_",0.98529,1.01259,40.3,{"v":2E-85,"d":"2.00E-85"},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",4,396,397,13,400,408]
[null,"HELPY_0888",null,"Helicobacter pylori B38","_","Fragment of putative acetate kinase AckA (Part 1)","_",0.72544,0.96,46.88,{"v":2E-85,"d":"2.00E-85"},1,1,"1.3.5 : Fermentation ;","2.7.2.1","1 : Unknown","6.7 : Fermentation ;","e : enzyme","12634340, 15755952, 17465479, 18223085","5 : Unknown function",1,284,397,1,286,300]
[null,"BN873v1_460010","_","Candidatus Competibacter denitrificans Run_A_D11","ackA","Acetate/propionate kinase","_",1.01425,1.07557,36.07,{"v":2e-84,"d":"2.00E-84"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.3 : Propionate degradation ; 1.7.29 : Acetate catabolism ;","2.7.2.1, 2.7.2.-","2 : Cytoplasmic","_","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",3,395,397,5,419,421]
[null,"RM41v1_pld1870123","_","Sinorhizobium sp. Rm41","ackA","Acetate kinase","_",1.00504,1.01786,39.35,{"v":2e-83,"d":"2.00E-83"},1,1,"1.3.5 : Fermentation ; 1.5.4 : Fatty acid and phosphatidic acid ; 1.7.29 : Acetate catabolism ; 7.1 : Cytoplasm ;","2.7.2.1","2 : Cytoplasmic","6.2 : Amino acids and amines ; 6.7 : Fermentation ;","e : enzyme",10094701,"1b : Function from experimental evidences in the studied species",3,395,397,4,389,392]
[null,"HP0903",null,"Helicobacter pylori 26695","ackA","Fragment of putative acetate kinase (Part 1)","_",0.72544,0.9863,46.53,{"v":5e-83,"d":"5.00E-83"},1,1,"6.7 : Fermentation ;","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,284,397,1,286,292]
[null,"RCFBPv5_mp0810","_","Ralstonia solanacearum CFBP2957","ackA","acetate kinase","_",0.99244,1.0051,38.32,{"v":2e-81,"d":"2.00E-81"},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",2,389,397,3,384,392]
[null,"RPSI07_mp1366","_","Ralstonia solanacearum PSI07","ackA","Acetate kinase","_",0.99496,1.00765,38.73,{"v":1e-80,"d":"1.00E-80"},1,1,"_","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",10094701,"2a : Function from experimental evidences in other organisms",2,389,397,3,384,392]
[null,"RALTA_A1397","_","Cupriavidus taiwanensis LMG19424","_","Acetate kinase","_",1.01511,1.01768,36.48,{"v":2E-78,"d":"2.00E-78"},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)",2,396,397,4,392,396]
[null,"MT37II_v2_a0110","_","Ca. Spiroplasma holothuricola MT37","ackA","acetate kinase (possibly promiscuous)","RXN-7958 ; ACETATEKIN-RXN ; RHEA:11352 ;",0.98272,1.00252,36.43,{"v":8E-78,"d":"8.00E-78"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,391,397,5,394,405]
[null,"AZOLI_0599","_","Azospirillum lipoferum 4B","ackA1","Acetate kinase","_",1.01511,1.02284,36.23,{"v":9e-77,"d":"9.00E-77"},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",3,396,397,5,392,394]
[null,"Rmet_0562","_","Cupriavidus metallidurans CH34","ackA2","acetate kinase","_",1.00741,1.02771,38.97,{"v":1e-76,"d":"1.00E-76"},1,1,"_","2.7.2.1","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,395,397,7,401,405]
[null,"THI_1474","_","Thiomonas sp. 3As","ackA","Acetate kinase AckA","_",1.0175,1.02519,36.36,{"v":1e-72,"d":"1.00E-72"},1,1,"1 : Metabolism ; 1.7.28 : Pyruvate catabolism ; 7.1 : Cytoplasm ;","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,396,397,6,400,400]
[null,"HEAR1515","_","Herminiimonas arsenicoxydans","ackA","Acetate kinase (Acetokinase)","_",0.98786,1.02519,36.61,{"v":7e-70,"d":"7.00E-70"},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)",2,395,397,20,407,412]
[null,"HPP12_0900",null,"Helicobacter pylori P12","ackA-2","Fragment of acetate kinase (Part 2)","_",0.48111,0.94554,49.74,{"v":8e-62,"d":"8.00E-62"},1,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",94,284,397,5,195,202]
[null,"HPB8_649",null,"Helicobacter pylori B8","_","Fragment of acetate kinase AckA (Part 2)","_",0.44332,0.96175,53.41,{"v":1e-60,"d":"1.00E-60"},1,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",109,284,397,1,176,183]
[null,"HPAG1_0884",null,"Helicobacter pylori HPAG1","_","Fragment of acetate kinase (Part 1)","_",0.39043,0.89595,41.94,{"v":1e-32,"d":"1.00E-32"},1,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,151,397,2,154,173]
[null,"HPP12_0899",null,"Helicobacter pylori P12","ackA-3","Fragment of acetate kinase (Part 3)","_",0.28212,0.94915,45.54,{"v":7e-23,"d":"7.00E-23"},2,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",288,397,397,5,116,118]
[null,"HP0903",null,"Helicobacter pylori 26695","ackA","Fragment of putative acetate kinase (Part 2)","_",0.28212,0.94915,42.86,{"v":5e-21,"d":"5.00E-21"},2,1,"6.7 : Fermentation ;","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",288,397,397,5,116,118]
[null,"HPB8_650",null,"Helicobacter pylori B8","_","Fragment of acetate kinase AckA (Part 3)","_",0.28967,0.97458,41.74,{"v":1e-20,"d":"1.00E-20"},2,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",284,397,397,2,116,118]
[null,"HPG27_856","_","Helicobacter pylori G27","_","Fragment of putative acetate kinase AckA (Part 2)","_",0.28212,0.92562,42.86,{"v":7e-20,"d":"7.00E-20"},1,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",288,397,397,8,119,121]
[null,"HPP12_0901",null,"Helicobacter pylori P12","ackA-1","Fragment of acetate kinase (Part 1)","_",0.24937,1.0102,41.41,2e-15,3,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,95,397,1,97,98]
[null,"HPB8_648",null,"Helicobacter pylori B8","_","Fragment of acetate kinase AckA (Part 1)","_",0.24937,0.95192,41.41,3e-15,3,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,95,397,1,97,104]
[null,"HELPY_0887",null,"Helicobacter pylori B38","_","Fragment of putative acetate kinase AckA (Part 2)","_",0.18892,0.85227,48,6e-15,2,1,"1.3.5 : Fermentation ;","2.7.2.1","1 : Unknown","6.7 : Fermentation ;","e : enzyme","12634340, 15755952, 17465479, 18223085","5 : Unknown function",288,360,397,8,82,88]
[null,"HPAG1_0883",null,"Helicobacter pylori HPAG1","_","Fragment of actetate kinase (Part 3)","_",0.18892,0.85227,48,9e-15,2,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",288,360,397,8,82,88]
[]
["ACT01_13325","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_10745","_","Clostridiaceae BL-3","pta","Phosphate acetyltransferase","PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.96221,1,46.83,{"v":1e-93,"d":"1.00E-93"},1,1,"_","2.3.1.8","2 : Cytoplasmic","_","e : enzyme","8702268, 11466286","2a : Function from experimental evidences in other organisms",1,331,344,1,329,331]
[null,"RALTA_B1570","_","Cupriavidus taiwanensis LMG19424","pta","phosphate acetyltransferase (taurine catabolism pathway)","_",0.92151,0.92151,44.16,{"v":3E-79,"d":"3.00E-79"},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",10,326,344,10,324,344]
[null,"CLOSTRIBL6_v1_1872","_","Clostridiales BL-6","pta","Phosphate acetyltransferase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.9186,0.97833,42.41,{"v":1e-74,"d":"1.00E-74"},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",5,320,344,3,312,323]
[null,"CLOSTRIBL4_v1_2331","_","Clostridiales BL-4","pta","phosphotransacetylase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.90988,0.93994,41.85,{"v":4e-74,"d":"4.00E-74"},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",16,326,344,23,328,333]
[null,"BSU37660","_","Bacillus subtilis 168","pta","phosphotransacetylase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.95349,1.01548,39.63,{"v":5E-74,"d":"5.00E-74"},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",7,332,344,8,323,323]
[null,"BN42v3_20129","_","Mycobacterium canettii STB-K","pta","Putative phosphate acetyltransferase Pta (phosphotransacetylase)","_",0.47826,0.9593,43.33,{"v":1e-72,"d":"1.00E-72"},1,1,"7 : intermediary metabolism and respiration ;","2.3.1.8","1 : Unknown","_","e : enzyme",17443846,"3 : Putative function from multiple computational evidences",3,331,344,366,685,690]
[null,"BN12v2_1100006","_","Tetrasphaera japonica T1-X7","pta","phosphate acetyltransferase (fragment)","_",0.71645,0.96221,40.48,{"v":1e-72,"d":"1.00E-72"},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",1,331,344,138,459,462]
[null,"SBF1_v1_1100027","_","Desulfosporosinus sp. SbF1","pta","phosphate acetyltransferase","PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.92151,0.98142,43.22,{"v":1e-72,"d":"1.00E-72"},1,1,"_","2.3.1.8","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",5,320,344,3,312,323]
[null,"VIBNIv4_B0182","_","Vibrio nigripulchritudo SFn1","pta","Phosphate acetyltransferase","_",0.94477,0.97892,39.38,{"v":1e-72,"d":"1.00E-72"},1,1,"7.1 : Cytoplasm ; 1 : Metabolism ;","2.3.1.8","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","8702268, 11466286","2a : Function from experimental evidences in other organisms",1,325,344,1,323,332]
[null,"BN43v3_10441","_","Mycobacterium canettii STB-L","pta","Putative phosphate acetyltransferase Pta (phosphotransacetylase)","_",0.47826,0.9593,43.33,{"v":1e-71,"d":"1.00E-71"},1,1,"7 : intermediary metabolism and respiration ;","2.3.1.8","1 : Unknown","_","e : enzyme",17443846,"3 : Putative function from multiple computational evidences",3,331,344,366,685,690]
[null,"HELPY_0889","_","Helicobacter pylori B38","pta","Phosphotransacetylase","_",0.639,0.96221,38.97,{"v":1e-71,"d":"1.00E-71"},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",1,331,344,195,516,518]
[null,"CDIV41_v1_140089","_","Carnobacterium divergens V41","pta","Phosphate acetyltransferase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.9564,1.0092,37.99,{"v":1e-71,"d":"1.00E-71"},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",5,332,344,5,324,326]
[null,"BN13v1_910015","_","Tetrasphaera jenkinsii Ben74","pta","Phosphate acetyltransferase","_",0.4811,0.96221,40.79,{"v":3e-71,"d":"3.00E-71"},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",1,331,344,363,684,688]
[null,"BN45v3_10446","_","Mycobacterium canettii STB-J","pta","Putative phosphate acetyltransferase Pta (phosphotransacetylase)","_",0.46479,0.9593,43.03,{"v":7e-71,"d":"7.00E-71"},1,1,"7 : intermediary metabolism and respiration ;","2.3.1.8","1 : Unknown","_","e : enzyme",17443846,"3 : Putative function from multiple computational evidences",3,331,344,386,705,710]
[null,"BN44v3_10449","_","Mycobacterium canettii STB-D","pta","Putative phosphate acetyltransferase Pta (phosphotransacetylase)","_",0.46479,0.9593,43.03,{"v":7e-71,"d":"7.00E-71"},1,1,"7 : intermediary metabolism and respiration ;","2.3.1.8","1 : Unknown","_","e : enzyme",17443846,"3 : Putative function from multiple computational evidences",3,331,344,386,705,710]
[null,"ECK2453","_","Escherichia coli K12","eutI","putative phosphotransacetylase subunit","PHOSACETYLTRANS-RXN ;",0.92151,0.93787,42.27,{"v":3e-70,"d":"3.00E-70"},1,1,"1.1.4 : Amines ;","_","1 : Unknown","6.2 : Amino acids and amines ;","e : enzyme","10464203, 16291677","3 : Putative function from multiple computational evidences",13,326,344,12,318,338]
[null,"BN11v3_1350009","_","Tetrasphaera australiensis Ben110","pta","Phosphate acetyltransferase","_",0.48321,0.96221,40.48,{"v":5e-70,"d":"5.00E-70"},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",1,331,344,362,683,685]
[null,"NMCC_0579","_","Neisseria meningitidis 053442","_","putative phosphate acetyltransferase (phosphotransacetylase)","_",0.58824,0.93023,42.5,{"v":1e-69,"d":"1.00E-69"},1,1,"_","2.3.1.8","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",13,331,344,231,539,544]
[null,"NMV_1777","_","Neisseria meningitidis NEM8013","pta","phosphate acetyltransferase (phosphotransacetylase)","_",0.64,0.93023,42.5,{"v":4e-69,"d":"4.00E-69"},1,1,"1.3.5 : Fermentation ;","2.3.1.8","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",13,331,344,187,495,500]
[null,"RM41v1_pld1620006","_","Sinorhizobium sp. Rm41","pta","Phosphate acetyltransferase","_",0.92151,0.96061,41.96,{"v":1e-68,"d":"1.00E-68"},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",13,326,344,13,324,330]
[null,"MARHY2149","_","Marinobacter hydrocarbonoclasticus ATCC 49840","pta","phosphate acetyltransferase","_",0.50076,0.9593,42.12,{"v":4e-67,"d":"4.00E-67"},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",3,331,344,332,650,659]
[null,"SSV_v1_1079","_","Streptococcus sanguinis 2908","pta","phosphate acetyltransferase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ;",0.97674,1.03385,36.61,{"v":1e-66,"d":"1.00E-66"},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",1,332,344,1,322,325]
[null,"BN424_559","_","Carnobacterium maltaromaticum LMA28 v1","pta","phosphate acetyltransferase","PHOSACETYLTRANS-RXN ; RHEA:19521 ;",0.84302,0.99315,41.03,{"v":2E-66,"d":"2.00E-66"},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",44,332,344,10,290,292]
[null,"BN10v3_560038","_","Tetrasphaera elongata Lp2","pta","Phosphate acetyltransferase","_",0.47025,0.94186,41.36,{"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",9,331,344,375,686,689]
[null,"BTCD_v1_2175","_","Brochothrix thermosphacta CD337","pta","phosphotransacetylase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ;",0.95349,1.00923,36.89,{"v":2e-65,"d":"2.00E-65"},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",6,333,344,7,324,325]
[null,"VIBNIv4_A2402","_","Vibrio nigripulchritudo SFn1","pta","phosphate acetyltransferase","_",0.46583,0.97093,38.92,{"v":7e-62,"d":"7.00E-62"},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",3,335,344,391,713,717]
[null,"BN874v1_910011","_","Candidatus Contendobacter odensis Run_B_J11","pta","Phosphate acetyltransferase","_",0.46944,0.98256,38.46,{"v":3e-61,"d":"3.00E-61"},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",3,339,344,390,716,720]
[null,"BN873v1_160014","_","Candidatus Competibacter denitrificans Run_A_D11","pta","phosphate acetyltransferase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ;",0.46843,0.92733,40.13,{"v":4e-61,"d":"4.00E-61"},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",14,331,344,369,676,681]
[null,"ABAYE3283","_","Acinetobacter baumannii AYE","pta","phosphate acetyltransferase","_",0.46499,0.96512,38.55,{"v":7e-59,"d":"7.00E-59"},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",3,331,344,390,707,714]
[null,"ACIAD0540","_","Acinetobacter baylyi ADP1","pta","phosphate acetyltransferase","PTAALT-RXN ; PHOSACETYLTRANS-RXN ; RHEA:19524 ; RHEA:28049 ;",0.45972,0.96221,37.46,{"v":4e-56,"d":"4.00E-56"},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",3,331,344,390,707,720]
[null,"PSEEN0916","_","Pseudomonas entomophila L48","pta","phosphate acetyltransferase","_",0.4661,0.9593,36.06,{"v":1E-52,"d":"1.00E-52"},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",3,331,344,386,704,708]
[null,"HPP12_0902","_","Helicobacter pylori P12","pta-2","Fragment of phosphotransacetylase (Part 2)","_",0.52907,1.01676,44.51,{"v":2e-44,"d":"2.00E-44"},1,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",150,331,344,4,177,179]
[null,"HPAG1_0885","_","Helicobacter pylori HPAG1","_","Fragment of phosphotransacetylase (Part 3)","_",0.52907,1.01676,44.51,{"v":5e-44,"d":"5.00E-44"},1,1,"_","2.3.1.8","1 : Unknown","_","u : unknown","_","5 : Unknown function",150,331,344,4,177,179]
[null,"HP0904",null,"Helicobacter pylori 26695","pta","Fragment of putative phosphotransacetylase (Part 4)","_",0.20349,0.9589,57.14,{"v":4e-20,"d":"4.00E-20"},1,1,"6.7 : Fermentation ;","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",262,331,344,2,71,73]
[null,"HP0904",null,"Helicobacter pylori 26695","pta","Fragment of putative phosphotransacetylase (Part 3)","_",0.34593,0.96748,36.13,{"v":7e-18,"d":"7.00E-18"},2,1,"6.7 : Fermentation ;","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",150,268,344,4,114,123]
[]
["ACT01_04870","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_12484",null,"Clostridiaceae BL-3","_","putative acetaldehyde dehydrogenase","ACETALD-DEHYDROG-RXN ; RHEA:23288 ;",0.89057,0.95354,66.31,0,1,1,"_","1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,465,495,1,471,530]
[null,"SSV_v1_0420",null,"Streptococcus sanguinis 2908","_","putative acetaldehyde dehydrogenase","_",0.98586,0.99187,53.28,{"v":3e-180,"d":"3.00E-180"},1,1,"_","1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,490,495,5,492,492]
[null,"EFER_1992",null,"Escherichia fergusonii ATCC 35469T","_","putative Aldehyde dehydrogenase","_",0.84053,0.90505,49.11,{"v":1e-157,"d":"1.00E-157"},1,2,"_","1.2.1.10","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,451,495,10,457,533]
[null,"ECIAI39_4208",null,"Escherichia coli IAI39","_","putative Aldehyde dehydrogenase","_",0.84053,0.90505,49.11,{"v":2e-157,"d":"2.00E-157"},1,2,"_","_","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,451,495,10,457,533]
[null,"BTCD_v1_1434",null,"Brochothrix thermosphacta CD337","eutE","Ethanolamine acetaldehyde oxydoreductase","_",0.93333,0.95851,49.35,{"v":3E-152,"d":"3.00E-152"},1,1,"_","1.2.1.10","2 : Cytoplasmic","_","e : enzyme","19246383, 18776017, 10464203, 8113167, 18689481, 18790863, 20234377","2a : Function from experimental evidences in other organisms",5,463,495,4,465,482]
[null,"CD630_19170",null,"Clostridium difficile 630","eutE","Ethanolamine acetaldehyde oxydoreductase","_",0.90909,0.92025,50,{"v":9e-152,"d":"9.00E-152"},1,1,"1.1.4 : Amines ;","1.2.1.10","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","19246383, 18776017, 10464203, 8113167, 18689481, 18790863, 20234377","2a : Function from experimental evidences in other organisms",5,452,495,5,454,489]
[null,"BTCD_v1_1045",null,"Brochothrix thermosphacta CD337","_","putative acetaldehyde dehydrogenase (Acetylating)","_",0.90707,0.99778,47.66,{"v":2e-141,"d":"2.00E-141"},2,1,"_","1.2.1.10","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,448,495,2,450,450]
[null,"BTCD_v1_1042",null,"Brochothrix thermosphacta CD337","_","putative succinate-semialdehyde dehydrogenase (acetylating)","RXN-8891 ;",0.88081,0.97758,48.17,{"v":8e-138,"d":"8.00E-138"},3,1,"_","1.2.1.76","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",13,447,495,10,445,446]
[null,"CLOSTRIBL3_v1_12496",null,"Clostridiaceae BL-3","_","putative Aldehyde dehydrogenase","ACETALD-DEHYDROG-RXN ; RHEA:23288 ;",0.91129,0.91313,42.7,{"v":3e-129,"d":"3.00E-129"},2,2,"_","1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,451,495,1,452,496]
[null,"AZOLI_p20688","_","Azospirillum lipoferum 4B","adhE","Aldehyde-alcohol dehydrogenase","_",0.48253,0.89293,45.25,{"v":6e-122,"d":"6.00E-122"},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",10,445,495,35,475,916]
[null,"AZOLI_p10253","_","Azospirillum lipoferum 4B","adhE2","Aldehyde-alcohol dehydrogenase","_",0.49224,0.89697,44.82,{"v":1e-121,"d":"1.00E-121"},1,1,"1.1.5.2 : Ethanol degradation ; 1.3.5 : Fermentation ; 5.5.6 : Other stresses (mechanical, nutritional, oxidative) ;","1.2.1.10, 1.1.1.1","2 : Cytoplasmic","6.7 : Fermentation ; 15.10 : Adaptations to atypical conditions ;","e : enzyme","12783863, 4301680","2a : Function from experimental evidences in other organisms",8,445,495,5,447,902]
[null,"VIBNIv4_A0888","_","Vibrio nigripulchritudo SFn1","adhE","Aldehyde-alcohol dehydrogenase [Includes: Alcohol dehydrogenase ; Acetaldehyde dehydrogenase [acetylating] ; Pyruvate-formate-lyase deactivase]","_",0.47845,0.87475,44.11,{"v":5e-114,"d":"5.00E-114"},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",20,445,495,15,446,905]
[null,"VS_0958","_","Vibrio tasmaniensis LGP32","adhE","Fused acetaldehyde-CoA dehydrogenase ; iron-dependent alcohol dehydrogenase","ACETALD-DEHYDROG-RXN ; ALCOHOL-DEHYDROG-RXN ; RHEA:10736 ; RHEA:23288 ;",0.48337,0.88081,43.35,{"v":3e-111,"d":"3.00E-111"},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",17,445,495,12,446,902]
[null,"CLOSTRIBL6_v1_2186","_","Clostridiales BL-6","adhE","fused acetaldehyde-CoA dehydrogenase ; iron-dependent alcohol dehydrogenase ; pyruvate-formate lyase deactivase","ALCOHOL-DEHYDROG-RXN ; ACETALD-DEHYDROG-RXN ; ALCOHOL-DEHYDROG-GENERIC-RXN ;",0.5023,0.88081,43.12,{"v":6e-110,"d":"6.00E-110"},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","12783863, 4301680","2a : Function from experimental evidences in other organisms",12,444,495,17,452,868]
[null,"SCFA_v1_940003","_","Ca. Propionivorax syntrophicum F70","adhE","Alcohol dehydrogenase / Acetaldehyde dehydrogenase [acetylating] / Pyruvate-formate-lyase deactivase (fragment)","ALCOHOL-DEHYDROG-RXN ;",0.76162,0.92402,46.42,{"v":3e-99,"d":"3.00E-99"},1,1,"_","1.1.1.1, 1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,366,495,33,408,408]
[]
["ACT01_02465","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_p50105",null,"Azospirillum lipoferum 4B","rspB","Oxidoreductase, Zn-dependent and NAD(P)-binding","_",0.99415,1.00295,44.71,{"v":3e-101,"d":"3.00E-101"},1,1,"_","1.1.1.-","2 : Cytoplasmic","18.1 : Enzymes of unknown specificity ;","e : enzyme","16738553, 7545940, 9097039, 9278503","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,339,339,3,341,342]
[null,"ECK1575","_","Escherichia coli K12","rspB","putative oxidoreductase, Zn-dependent and NAD(P)-binding","_",1.00295,1.00295,45.29,{"v":3e-100,"d":"3.00E-100"},1,1,"5.5.3 : Starvation response ;","_","1 : Unknown","16.12 : Sense ; 15.10 : Adaptations to atypical conditions ;","e : enzyme",7545940,"3 : Putative function from multiple computational evidences",1,338,339,1,337,339]
[null,"BSU12330",null,"Bacillus subtilis 168","yjmD","putative oxidoreductase","_",1.00295,1.00295,43.82,{"v":2e-97,"d":"2.00E-97"},1,1,"2.1.1 : Specific pathways ;","1.1.1.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","9579062, 9882655","3 : Putative function from multiple computational evidences",1,339,339,1,339,339]
[null,"EFER_1526","_","Escherichia fergusonii ATCC 35469T","rspB","putative dehydrogenase, starvation-sensing protein with NAD(P)-binding and GroES domains","_",0.98271,1.0059,42.52,{"v":2e-89,"d":"2.00E-89"},1,1,"_","_","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme",7545940,"3 : Putative function from multiple computational evidences",1,338,339,9,344,347]
[null,"RALTA_A2841",null,"Cupriavidus taiwanensis LMG19424","rspB","starvation-sensing protein,  putative oxidoreductase, Zn-dependent and NAD(P)-binding","_",0.98547,1,43.07,{"v":3e-89,"d":"3.00E-89"},1,1,"5.5.3 : Starvation response ;","1.1.1.-","1 : Unknown","15.10 : Adaptations to atypical conditions ;","e : enzyme",7545940,"2a : Function from experimental evidences in other organisms",1,336,339,1,338,344]
[null,"BBta_2119",null,"Bradyrhizobium sp. BTAi1","_","putative dehydrogenase, starvation-sensing protein with NAD(P)-binding and GroES domains","_",1,1.00295,42.06,{"v":6e-86,"d":"6.00E-86"},1,1,"5.5.3 : Starvation response ;","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,338,339,5,340,340]
[null,"RM41v1_480079","_","Sinorhizobium sp. Rm41","_","putative alcohol dehydrogenase","_",0.83862,0.85841,36.43,{"v":2E-50,"d":"2.00E-50"},1,1,"7.1 : Cytoplasm ;","_","2 : Cytoplasmic","6.7 : Fermentation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,286,339,1,289,347]
[null,"BN11v3_4860005","_","Tetrasphaera australiensis Ben110","tdh","threonine 3-dehydrogenase","_",0.97414,1,35.4,{"v":9e-49,"d":"9.00E-49"},1,1,"_","1.1.1.103","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","16817900, 8519804","2a : Function from experimental evidences in other organisms",1,321,339,1,331,348]
[]
["ACT01_04805","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"EFER_1994",null,"Escherichia fergusonii ATCC 35469T","_","putative Alcohol dehydrogenase, iron-dependent","_",0.97423,1,44.18,{"v":2e-104,"d":"2.00E-104"},1,1,"_","1.1.1.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,378,378,5,380,388]
[null,"ECIAI39_4210",null,"Escherichia coli IAI39","_","putative Alcohol dehydrogenase, iron-dependent","_",0.97423,1,43.92,{"v":2e-103,"d":"2.00E-103"},1,1,"1.1.5.2 : Ethanol degradation ; 1.3.5 : Fermentation ;","1.1.1.1","1 : Unknown","6.7 : Fermentation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,378,378,5,380,388]
[null,"CLOSTRIBL3_v1_20137",null,"Clostridiaceae BL-3","adh","Alcohol dehydrogenase","RXN-12448 ; RHEA:25290 ;",1.00785,1.01852,42.86,{"v":3E-102,"d":"3.00E-102"},1,1,"_","1.1.1.1","2 : Cytoplasmic","_","e : enzyme",2673928,"2a : Function from experimental evidences in other organisms",1,378,378,1,381,382]
[null,"CD630_19070",null,"Clostridium difficile 630","eutG","Ethanolamine iron-dependent Alcohol dehydrogenase","_",1.00529,1.01064,41.32,{"v":3e-94,"d":"3.00E-94"},1,1,"1.1.4 : Amines ;","1.1.1.1","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","19246383, 18776017, 10464203, 8113167, 18689481, 18790863, 20234377","2a : Function from experimental evidences in other organisms",1,375,378,1,373,376]
[null,"BTCD_v1_1443",null,"Brochothrix thermosphacta CD337","eutG","Ethanolamine iron-dependent Alcohol dehydrogenase","_",1.00529,1.00796,39.74,{"v":3e-94,"d":"3.00E-94"},1,1,"1.1.4 : Amines ;","1.1.1.1","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","19246383, 18776017, 10464203, 8113167, 18689481, 18790863, 20234377","2a : Function from experimental evidences in other organisms",1,375,378,1,374,377]
[null,"SSV_v1_0411",null,"Streptococcus sanguinis 2908","pduQ","NADPH-dependent butanol dehydrogenase","_",1.01579,1.02116,39.64,{"v":7e-92,"d":"7.00E-92"},1,1,"_","1.1.1.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,378,378,1,380,380]
[null,"CLOSTRIBL6_v1_2186",null,"Clostridiales BL-6","adhE","fused acetaldehyde-CoA dehydrogenase ; iron-dependent alcohol dehydrogenase ; pyruvate-formate lyase deactivase","ALCOHOL-DEHYDROG-RXN ; ACETALD-DEHYDROG-RXN ; ALCOHOL-DEHYDROG-GENERIC-RXN ;",0.47005,1.07937,40.2,{"v":1e-86,"d":"1.00E-86"},1,3,"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","12783863, 4301680","2a : Function from experimental evidences in other organisms",1,378,378,459,865,868]
[null,"SCFA_v1_2560001","_","Ca. Propionivorax syntrophicum F70","adhE","fused acetaldehyde-CoA dehydrogenase ; iron-dependent alcohol dehydrogenase ; pyruvate-formate lyase deactivase (fragment)","ALCOHOL-DEHYDROG-RXN ; ACETALD-DEHYDROG-RXN ; ALCOHOL-DEHYDROG-GENERIC-RXN ; R542-RXN ; RXN-5424 ; RXN-5444 ; RXN-6021 ; RXN-7657 ; RXN-7693 ; RXN-7694 ; RXN-7700 ; RXN-7706 ; RXN3O-4113 ; RXN-10915 ; RXN-10911 ; RXN-10781 ; RXN-12448 ; RHEA:10736 ; RHEA:10740 ; RHEA:23288 ; RHEA:25290 ;",0.89538,0.97354,39.4,{"v":3e-75,"d":"3.00E-75"},1,1,"_","1.2.1.10, 1.1.1.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",39,378,378,1,367,411]
[null,"SSV_v1_2152",null,"Streptococcus sanguinis 2908","adhE","aldehyde-alcohol dehydrogenase [includes: alcohol dehydrogenase ; acetaldehyde dehydrogenase]","_",0.46041,1.07672,37.59,{"v":4e-75,"d":"4.00E-75"},2,3,"_","1.1.1.1, 1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,378,378,468,873,884]
[null,"ECED1_3448",null,"Escherichia coli ED1a","_","putative propanol dehydrogenase","_",0.96561,0.98118,35.07,{"v":7E-72,"d":"7.00E-72"},1,1,"_","1.1.1.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",8,370,378,9,363,372]
[null,"CD630_03340",null,"Clostridium difficile 630","adhE","Aldehyde-alcohol dehydrogenase","_",0.46364,1.07937,35.78,{"v":8e-71,"d":"8.00E-71"},2,3,"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",4,378,378,470,877,880]
[null,"AZOLI_p10253",null,"Azospirillum lipoferum 4B","adhE2","Aldehyde-alcohol dehydrogenase","_",0.44346,1.0582,38.25,{"v":2E-70,"d":"2.00E-70"},1,3,"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",10,378,378,462,860,902]
[null,"AZOLI_p20688",null,"Azospirillum lipoferum 4B","adhE","Aldehyde-alcohol dehydrogenase","_",0.43668,1.0582,38,{"v":8E-70,"d":"8.00E-70"},1,3,"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",10,378,378,490,888,916]
[null,"CD630_29660",null,"Clostridium difficile 630","adhE","Aldehyde-alcohol dehydrogenase","_",0.47059,1.07937,35.05,{"v":1e-67,"d":"1.00E-67"},3,3,"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",4,378,378,457,864,867]
[null,"VIBNIv4_A0888",null,"Vibrio nigripulchritudo SFn1","adhE","Aldehyde-alcohol dehydrogenase [Includes: Alcohol dehydrogenase ; Acetaldehyde dehydrogenase [acetylating] ; Pyruvate-formate-lyase deactivase]","_",0.44309,1.06085,35.66,{"v":2E-66,"d":"2.00E-66"},1,3,"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",10,378,378,461,861,905]
[null,"EFER_2022",null,"Escherichia fergusonii ATCC 35469T","_","putative Propanediol utilization propanol dehydrogenase pduQ","_",0.9709,0.99189,36.51,{"v":9E-61,"d":"9.00E-61"},3,1,"_","1.1.1.1","1 : Unknown","6 : Energy metabolism ;","e : enzyme",10498708,"3 : Putative function from multiple computational evidences",1,363,378,1,355,370]
[]
["ACT01_04800","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_12496",null,"Clostridiaceae BL-3","_","putative Aldehyde dehydrogenase","ACETALD-DEHYDROG-RXN ; RHEA:23288 ;",0.97652,1.00605,56.91,0,1,1,"_","1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",4,502,511,1,496,496]
[null,"ECIAI39_4208",null,"Escherichia coli IAI39","_","putative Aldehyde dehydrogenase","_",0.85366,0.89041,52.53,{"v":5e-167,"d":"5.00E-167"},1,1,"_","_","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,458,511,6,460,533]
[null,"EFER_1992",null,"Escherichia fergusonii ATCC 35469T","_","putative Aldehyde dehydrogenase","_",0.85366,0.89041,52.53,{"v":6e-167,"d":"6.00E-167"},1,1,"_","1.2.1.10","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,458,511,6,460,533]
[null,"SSV_v1_0420",null,"Streptococcus sanguinis 2908","_","putative acetaldehyde dehydrogenase","_",0.96869,1.0061,49.7,{"v":2e-164,"d":"2.00E-164"},1,2,"_","1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",8,502,511,5,492,492]
[null,"CD630_19170",null,"Clostridium difficile 630","eutE","Ethanolamine acetaldehyde oxydoreductase","_",0.89824,0.93865,47.49,{"v":2e-148,"d":"2.00E-148"},1,2,"1.1.4 : Amines ;","1.2.1.10","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","19246383, 18776017, 10464203, 8113167, 18689481, 18790863, 20234377","2a : Function from experimental evidences in other organisms",4,461,511,1,459,489]
[null,"BTCD_v1_1434",null,"Brochothrix thermosphacta CD337","eutE","Ethanolamine acetaldehyde oxydoreductase","_",0.92955,0.98548,45.47,{"v":3e-144,"d":"3.00E-144"},1,2,"_","1.2.1.10","2 : Cytoplasmic","_","e : enzyme","19246383, 18776017, 10464203, 8113167, 18689481, 18790863, 20234377","2a : Function from experimental evidences in other organisms",7,481,511,3,473,482]
[null,"CLOSTRIBL3_v1_12484",null,"Clostridiaceae BL-3","_","putative acetaldehyde dehydrogenase","ACETALD-DEHYDROG-RXN ; RHEA:23288 ;",0.86604,0.89824,43.79,{"v":9e-129,"d":"9.00E-129"},2,2,"_","1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",4,461,511,1,457,530]
[null,"BTCD_v1_1042",null,"Brochothrix thermosphacta CD337","_","putative succinate-semialdehyde dehydrogenase (acetylating)","RXN-8891 ;",0.85323,0.97758,43.81,{"v":3E-122,"d":"3.00E-122"},2,2,"_","1.2.1.76","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",16,451,511,10,445,446]
[null,"BTCD_v1_1045",null,"Brochothrix thermosphacta CD337","_","putative acetaldehyde dehydrogenase (Acetylating)","_",0.84736,0.96222,42.03,{"v":4e-118,"d":"4.00E-118"},3,2,"_","1.2.1.10","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",20,452,511,18,450,450]
[null,"CD630_03340",null,"Clostridium difficile 630","adhE","Aldehyde-alcohol dehydrogenase","_",0.50909,0.87671,39.29,{"v":1e-95,"d":"1.00E-95"},2,2,"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",13,455,511,23,467,880]
[null,"AZOLI_p10253",null,"Azospirillum lipoferum 4B","adhE2","Aldehyde-alcohol dehydrogenase","_",0.49667,0.87671,38.17,{"v":3e-95,"d":"3.00E-95"},1,2,"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",13,455,511,7,453,902]
[null,"AZOLI_p20688",null,"Azospirillum lipoferum 4B","adhE","Aldehyde-alcohol dehydrogenase","_",0.48908,0.87671,37.95,{"v":8e-95,"d":"8.00E-95"},1,2,"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",13,455,511,35,481,916]
[null,"CLOSTRIBL6_v1_2186",null,"Clostridiales BL-6","adhE","fused acetaldehyde-CoA dehydrogenase ; iron-dependent alcohol dehydrogenase ; pyruvate-formate lyase deactivase","ALCOHOL-DEHYDROG-RXN ; ACETALD-DEHYDROG-RXN ; ALCOHOL-DEHYDROG-GENERIC-RXN ;",0.5023,0.85323,37.84,{"v":2E-91,"d":"2.00E-91"},1,2,"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","12783863, 4301680","2a : Function from experimental evidences in other organisms",15,448,511,17,452,868]
[null,"CD630_29660",null,"Clostridium difficile 630","adhE","Aldehyde-alcohol dehydrogenase","_",0.50288,0.85323,38.53,{"v":1E-87,"d":"1.00E-87"},3,2,"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",25,455,511,22,454,867]
[null,"SSV_v1_2152",null,"Streptococcus sanguinis 2908","adhE","aldehyde-alcohol dehydrogenase [includes: alcohol dehydrogenase ; acetaldehyde dehydrogenase]","_",0.51697,0.89432,35.23,{"v":3e-86,"d":"3.00E-86"},2,2,"_","1.1.1.1, 1.2.1.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,455,511,12,468,884]
[null,"VIBNIv4_A0888",null,"Vibrio nigripulchritudo SFn1","adhE","Aldehyde-alcohol dehydrogenase [Includes: Alcohol dehydrogenase ; Acetaldehyde dehydrogenase [acetylating] ; Pyruvate-formate-lyase deactivase]","_",0.49945,0.88454,35.18,{"v":8e-84,"d":"8.00E-84"},1,2,"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",13,455,511,5,452,905]
[]
["ACT01_05115","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,"BN424_3628","_","Carnobacterium maltaromaticum LMA28 v1","dhaD","Glycerol dehydrogenase (GLDH)","GLYCDEH-RXN ; RHEA:13769 ;",0.97082,1.00274,43.44,{"v":5e-85,"d":"5.00E-85"},1,1,"_","1.1.1.6","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",23377788,"2a : Function from experimental evidences in other organisms",10,363,365,10,370,377]
[null,"Spro_4273","_","Serratia proteamaculans 568","dhaD","Glycerol dehydrogenase (GLDH)","_",0.98913,0.99726,40.11,{"v":3e-83,"d":"3.00E-83"},1,1,"1.7.6 : Glycerol metabolism ;","1.1.1.6","2 : Cytoplasmic","5 : Central intermediary metabolism ; 6.2 : Amino acids and amines ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,364,365,1,361,368]
[null,"SSV_v1_0204","_","Streptococcus sanguinis 2908","gldA","glycerol dehydrogenase","AMINOPROPDEHYDROG-RXN ; GLYCDEH-RXN ; RXN-8632 ;",0.96175,0.96438,38.07,{"v":1E-70,"d":"1.00E-70"},1,1,"1.1.3.7 : Threonine catabolism ; 1.7.6.2 : Glycerol degradation II ;","1.1.1.6","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme",8132480,"2a : Function from experimental evidences in other organisms",10,360,365,9,357,366]
[]
["ACT01_06790","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_1804","_","Clostridiales BL-6","adh","Alcohol dehydrogenase","_",0.98205,0.99481,52.22,{"v":8E-136,"d":"8.00E-136"},1,1,"_","1.1.1.1","2 : Cytoplasmic","_","e : enzyme",2673928,"2a : Function from experimental evidences in other organisms",3,385,385,8,390,390]
[null,"CLOSTRIBL4_v1_2290","_","Clostridiales BL-4","adh","Alcohol dehydrogenase","RXN-12448 ;",0.99481,0.9974,48.56,{"v":6E-124,"d":"6.00E-124"},1,1,"_","1.1.1.1","2 : Cytoplasmic","_","e : enzyme",2673928,"2a : Function from experimental evidences in other organisms",3,385,385,7,384,384]
[]
["ACT01_07765","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_10590","_","Clostridium difficile 630","thlA1","Acetoacetyl-CoA thiolase 1","_",0.99244,1.00767,58.63,{"v":5e-160,"d":"5.00E-160"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","11075929, 2191949","1c : Function from experimental evidences in the studied genus",1,394,397,1,390,391]
[null,"CLOSTRIBL3_v1_12838","_","Clostridiaceae BL-3","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99244,1.0051,57.61,{"v":2E-155,"d":"2.00E-155"},1,1,"_","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","7867955, 11075929, 11466286, 1685080","2a : Function from experimental evidences in other organisms",1,394,397,1,391,392]
[null,"AZOLI_2388","_","Azospirillum lipoferum 4B","phbA3","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.99244,1.00767,56.6,{"v":6e-147,"d":"6.00E-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",1,394,397,1,389,391]
[null,"HEAR0577","_","Herminiimonas arsenicoxydans","phbA","acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.98747,0.99244,53.81,{"v":8e-145,"d":"8.00E-145"},1,1,"1.3 : Energy metabolism (carbon) ; 7.1 : Cytoplasm ;","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","1396692, 2670935","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,397,9,398,399]
[null,"Rmet_1357",null,"Cupriavidus metallidurans CH34","phaA","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.99244,1.00254,53.3,{"v":3e-143,"d":"3.00E-143"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,397,1,391,393]
[null,"METDI4272","_","Methylobacterium extorquens DM4","phaA","beta-ketothiolase","_",0.98992,0.99746,53.94,{"v":1E-141,"d":"1.00E-141"},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",2,394,397,5,392,394]
[null,"NT26v4_3604","_","Rhizobium sp. NT-26","phbA","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98741,0.99746,53.06,{"v":3e-141,"d":"3.00E-141"},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)",3,394,397,5,391,393]
[null,"RALTA_A1351","_","Cupriavidus taiwanensis LMG19424","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.99244,1.00254,52.54,{"v":8e-141,"d":"8.00E-141"},1,1,"1.6 : Macromolecules (cellular constituent) biosynthesis ;","2.3.1.9","1 : Unknown","_","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",1,394,397,1,391,393]
[null,"MARHY3102","_","Marinobacter hydrocarbonoclasticus ATCC 49840","phbA","acetyl-CoA acetyltransferase with thiolase domain, PHB biosynthesis","_",0.99244,1.0051,52.54,{"v":3e-140,"d":"3.00E-140"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",1396692,"2a : Function from experimental evidences in other organisms",1,394,397,1,391,392]
[null,"RM41v1_110012","_","Sinorhizobium sp. Rm41","phbA","acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98741,0.99746,53.32,{"v":2e-138,"d":"2.00E-138"},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",3,394,397,5,391,393]
[null,"BRADO0562","_","Bradyrhizobium sp. ORS278","phbA","acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98489,0.99239,54.22,{"v":7e-137,"d":"7.00E-137"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.9","1 : Unknown","16.2 : Construct biomass (Anabolism) ;","e : enzyme",7582015,"2b : Function from indirect experimental evidences (e.g. phenotypes)",3,393,397,6,391,394]
[null,"Spro_0592","_","Serratia proteamaculans 568","atoB","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.98254,0.99244,51.27,{"v":2E-136,"d":"2.00E-136"},1,1,"1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,397,9,399,401]
[null,"PP_4636","_","Pseudomonas putida KT2440","yqeF","acetyl-CoA acetyltransferase","METHYLACETOACETYLCOATHIOL-RXN ; RXN-12561 ; ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",0.99244,1.0051,51.27,{"v":9e-136,"d":"9.00E-136"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","4150713, 773366, 236278, 9904, 2883931","2a : Function from experimental evidences in other organisms",1,394,397,1,391,392]
[null,"THI_1641","_","Thiomonas sp. 3As","phbA1","acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.99244,1.0051,50.76,{"v":2e-135,"d":"2.00E-135"},1,1,"1.3 : Energy metabolism (carbon) ;","2.3.1.9","2 : Cytoplasmic","15 : Cellular processes ; 6 : Energy metabolism ;","e : enzyme","2670935, 2670936","2a : Function from experimental evidences in other organisms",1,394,397,1,391,392]
[null,"PSEEN4635","_","Pseudomonas entomophila L48","phbA","acetyl-CoA acetyltransferase","_",0.96806,0.99244,51.27,{"v":1E-134,"d":"1.00E-134"},1,1,"5.6.2 : Detoxification (xenobiotic metabolism) ;","2.3.1.9","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,394,397,15,405,407]
[null,"CMR15v5_2547","_","Ralstonia solanacearum CMR15","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.99244,1.00254,50.25,{"v":2e-134,"d":"2.00E-134"},1,1,"1.6 : Macromolecules (cellular constituent) biosynthesis ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",1,394,397,1,391,393]
[null,"CLOSTRIBL4_v1_1867","_","Clostridiales BL-4","thlA","acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.93365,0.99244,50.76,{"v":8e-132,"d":"8.00E-132"},1,1,"_","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","7867955, 11075929","2a : Function from experimental evidences in other organisms",2,394,397,29,418,422]
[null,"CLOSTRIBL6_v1_0127","_","Clostridiales BL-6","phaA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99748,1.00253,50.76,{"v":7e-131,"d":"7.00E-131"},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",2,395,397,3,395,395]
[null,"BN874v1_850028","_","Candidatus Contendobacter odensis Run_B_J11","phaA","Acetyl-CoA acetyltransferase","_",0.99244,1.00254,50,{"v":2e-129,"d":"2.00E-129"},1,1,"1.3 : Energy metabolism (carbon) ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ; 6 : Energy metabolism ; 16.14 : Store ;","e : enzyme","1685080, 1755959, 7867955, 9904","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,397,1,391,393]
[null,"MGMSRv2_1838","_","Magnetospirillum gryphiswaldense MSR-1 v2","phbA","acetyl-CoA acetyltransferase containing thiolase domain (Acetoacetyl-CoA thiolase)","_",0.99244,1.01026,49.49,{"v":2e-128,"d":"2.00E-128"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 1.7 : Central intermediary metabolism ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,397,1,389,390]
[null,"VIBNIv4_B0465","_","Vibrio nigripulchritudo SFn1","phbA","acetyl-CoA acetyltransferase","_",1.00746,1.02015,49.14,{"v":4e-128,"d":"4.00E-128"},1,1,"1.1.2.7 : Acetoacetate degradation ; 7.1 : Cytoplasm ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","2670935, 16964242, 2670936","2a : Function from experimental evidences in other organisms",1,396,397,1,401,402]
[null,"AZOLI_p10676","_","Azospirillum lipoferum 4B","phbA2","Acetyl-CoA acetyltransferase with thiolase domain (Beta-ketothiolase)","_",0.99244,1.00254,51.02,{"v":7e-127,"d":"7.00E-127"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.9","1 : Unknown","3.1 : Biosynthesis ; 3 : Fatty acid and phospholipid metabolism ;","e : enzyme","12534463, 9851987","2a : Function from experimental evidences in other organisms",3,394,397,4,391,393]
[null,"BN873v1_100077","_","Candidatus Competibacter denitrificans Run_A_D11","phaA","Acetyl-CoA acetyltransferase","_",0.99244,1.00254,48.98,{"v":1e-126,"d":"1.00E-126"},1,1,"_","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ; 6 : Energy metabolism ; 16.14 : Store ;","e : enzyme","1685080, 1755959, 7867955, 9904","2a : Function from experimental evidences in other organisms",1,394,397,1,391,393]
[null,"ECIAI1_1489","_","Escherichia coli IAI1","_","putative acetyl-CoA acetyltransferase","_",0.98504,0.99496,48.61,{"v":3e-126,"d":"3.00E-126"},1,1,"1 : Metabolism ; 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 ; 18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,394,397,1,392,401]
[null,"RPSI07_1730",null,"Ralstonia solanacearum PSI07","phaA","acetyl-CoA acetyltransferase, thiolase-like","_",0.99496,1.00254,49.62,{"v":5e-123,"d":"5.00E-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)",2,394,397,3,392,394]
[null,"BTCD_v1_1714","_","Brochothrix thermosphacta CD337","mevB","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.98992,1.01289,48.85,{"v":2E-120,"d":"2.00E-120"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme",7763384,"2a : Function from experimental evidences in other organisms",1,393,397,1,385,388]
[null,"BN424_3179","_","Carnobacterium maltaromaticum LMA28 v1","thlA","Acetoacetyl-CoA thiolase","METHYLACETOACETYLCOATHIOL-RXN ; RXN-12561 ; ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99244,1.01285,46.45,{"v":7e-119,"d":"7.00E-119"},1,1,"_","2.3.1.9","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,397,1,387,389]
[null,"BSU24170","_","Bacillus subtilis 168","mmgA","degradative acetoacetyl-CoA thiolase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99496,1.00509,47.09,{"v":9e-119,"d":"9.00E-119"},1,1,"2.4 : Metabolism of lipids ;","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","16352833, 18246303, 19016856, 28956599","1a : Function from experimental evidences in the studied strain",1,395,397,1,392,393]
[null,"METUNv2_520573","_","Methyloversatilis universalis FAM5","phbA","Acetyl-CoA acetyltransferase","_",0.99244,0.99747,48.22,{"v":3e-118,"d":"3.00E-118"},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",2,394,397,5,393,395]
[null,"VS_II0585","_","Vibrio tasmaniensis LGP32","_","Acetyl-CoA C acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",1,1.01511,44.42,{"v":3e-117,"d":"3.00E-117"},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",1,394,397,1,399,403]
[null,"NBG4_v1_200004","_","Candidatus Sulfobium mesophilum","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.98992,0.99494,43.51,{"v":7e-116,"d":"7.00E-116"},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",2,394,397,9,394,395]
[null,"Rmet_1362",null,"Cupriavidus metallidurans CH34","bktB","acetyl-CoA acetyltransferase","_",0.98489,0.99239,48.08,{"v":3e-115,"d":"3.00E-115"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,390,397,3,388,394]
[null,"NIDE3116","_","Candidatus Nitrospira defluvii","atoB","Acetyl-CoA acetyltransferase","_",0.98741,0.99492,44.39,{"v":3e-115,"d":"3.00E-115"},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",3,394,397,6,393,394]
[null,"HELPY_0683","_","Helicobacter pylori B38","atoB","Acetyl coenzyme A acetyltransferase","_",0.99244,1.00767,45.94,{"v":3e-115,"d":"3.00E-115"},1,1,"1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.1 : General ;","e : enzyme",3025185,"2a : Function from experimental evidences in other organisms",1,394,397,1,389,391]
[null,"VIBNIv4_B1306",null,"Vibrio nigripulchritudo SFn1","phbA","acetyl-CoA acetyltransferase","_",1.00499,1.01511,44.91,{"v":1e-113,"d":"1.00E-113"},2,1,"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",1,394,397,1,399,401]
[null,"Atu3475","_","Agrobacterium tumefaciens C58","fadAx","acetyl-CoA C-acetyltransferase","_",0.95146,0.98741,47.96,{"v":2e-112,"d":"2.00E-112"},1,1,"1 : Metabolism ;","_","2 : Cytoplasmic","_","e : enzyme",11251808,"2b : Function from indirect experimental evidences (e.g. phenotypes)",4,394,397,32,410,412]
[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 ;",0.99496,1.01023,46.08,{"v":4e-112,"d":"4.00E-112"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.16, 2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","11075929, 18246303, 21209787","2a : Function from experimental evidences in other organisms",1,395,397,1,390,391]
[null,"pRALTA_0081","_","Cupriavidus taiwanensis LMG19424","_","acetyl-CoA acetyltransferase","_",0.99,0.99748,46.46,{"v":4e-111,"d":"4.00E-111"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,395,397,9,399,400]
[null,"LEPBIa0355","_","Leptospira biflexa serovar Patoc Patoc 1","thiL1","Putative acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.99496,1.00509,46.08,{"v":7e-109,"d":"7.00E-109"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme",15733928,"2a : Function from experimental evidences in other organisms",1,394,397,1,389,393]
[null,"PSHAa1586","_","Pseudoalteromonas haloplanktis TAC125","atoB","acetyl-CoA acetyltransferase with thiolase domain, Acetoacetyl-CoA thiolase","_",0.95844,0.98741,45.92,{"v":2e-108,"d":"2.00E-108"},1,1,"_","2.3.1.9","cytoplasm (undefined)","_","e : enzyme",7867955,"2a : Function from experimental evidences in other organisms",3,390,397,20,403,409]
[null,"BN381v2_150043","_","Candidatus Microthrix parvicella RN1","phaA","acetyl-CoA acetyltransferase","_",0.99244,1.00254,44.42,{"v":9e-108,"d":"9.00E-108"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","18246303, 10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",1,394,397,1,391,393]
[null,"VIBNIv4_A1234","_","Vibrio nigripulchritudo SFn1","phbA","Acetyl-CoA acetyltransferase","_",0.99496,1.00254,40.25,{"v":2e-106,"d":"2.00E-106"},1,1,"1.7 : Central intermediary metabolism ; 7.1 : Cytoplasm ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",1396692,"2a : Function from experimental evidences in other organisms",3,397,397,5,394,394]
[null,"FRAAL5910","_","Frankia alni ACN14a","atoB","acetyl-CoA acetyltransferase with thiolase domain","_",0.99496,1,43.29,{"v":8e-102,"d":"8.00E-102"},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)",1,395,397,1,392,395]
[null,"Rmet_3669","_","Cupriavidus metallidurans CH34","pcaF","acetyl-CoA acetyltransferase","_",1.005,1.01259,44.03,{"v":9E-102,"d":"9.00E-102"},1,1,"1.1.2.7 : Acetoacetate degradation ;","_","1 : Unknown","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,394,397,1,398,400]
[null,"BN12v2_3170003","_","Tetrasphaera japonica T1-X7","phaA","acetyl-CoA acetyltransferase (fadA) (Acetoacetyl-CoA thiolase) (beta-ketothiolase)","_",0.98995,0.99244,42.89,{"v":1e-101,"d":"1.00E-101"},1,1,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",5,395,397,7,395,398]
[null,"Pars_0309","_","Pyrobaculum arsenaticum DSM 13514","thlA","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.98771,1.01259,45.27,{"v":3e-101,"d":"3.00E-101"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11075929, 11466286, 1685080, 7867955","2a : Function from experimental evidences in other organisms",4,395,397,16,406,407]
[null,"RALTA_B0208","_","Cupriavidus taiwanensis LMG19424","pcaF","Beta-ketoadipyl CoA thiolase","_",1.005,1.01259,42.79,{"v":2E-99,"d":"2.00E-99"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.16","1 : Unknown","6 : Energy metabolism ;","e : enzyme",7961399,"2a : Function from experimental evidences in other organisms",1,394,397,1,398,400]
[null,"BN13v1_460011","_","Tetrasphaera jenkinsii Ben74","_","putative Acetyl-CoA acetyltransferase (beta-ketothiolase) (phaA)","_",0.98744,0.98992,44.27,{"v":7e-99,"d":"7.00E-99"},1,1,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","3 : Putative function from multiple computational evidences",5,395,397,7,395,398]
[null,"AZOLI_p40026","_","Azospirillum lipoferum 4B","pcaF","Beta-ketoadipyl CoA thiolase","_",0.99015,1.01259,43.28,{"v":1e-98,"d":"1.00E-98"},1,1,"1.1 : Carbon compound utilization ;","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",9582432,"2a : Function from experimental evidences in other organisms",1,394,397,8,404,406]
[null,"BN45v3_30404","_","Mycobacterium canettii STB-J","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98237,1.00257,42.31,{"v":7e-97,"d":"7.00E-97"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,394,397,1,387,389]
[null,"BN44v3_11488","_","Mycobacterium canettii STB-D","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98237,1.00257,42.31,{"v":1e-96,"d":"1.00E-96"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,394,397,1,387,389]
[null,"BN43v3_30420","_","Mycobacterium canettii STB-L","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98237,1.00257,42.31,{"v":1e-96,"d":"1.00E-96"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,394,397,1,387,389]
[null,"BN11v3_1860009","_","Tetrasphaera australiensis Ben110","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.98496,0.98992,42.75,{"v":3e-96,"d":"3.00E-96"},1,1,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",5,395,397,8,396,399]
[null,"BN42v3_21228","_","Mycobacterium canettii STB-K","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98237,1.00257,42.05,{"v":6e-96,"d":"6.00E-96"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,394,397,1,387,389]
[null,"XDD1v4_3927","_","Xenorhabdus doucetiae FRM16","paaJ","protein PaaJ; Beta-ketoadipyl-CoA thiolase","_",1,1.01763,42.08,{"v":4E-92,"d":"4.00E-92"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.174","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,394,397,1,401,404]
[null,"AZOLI_p30161","_","Azospirillum lipoferum 4B","phbA4","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.99496,1.01542,39.49,{"v":4e-88,"d":"4.00E-88"},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",2,394,397,3,387,389]
[null,"BN10v3_1170012","_","Tetrasphaera elongata Lp2","_","putative acetyl-CoA acetyltransferase (phaA)","_",0.80605,0.94675,43.75,{"v":3e-78,"d":"3.00E-78"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,322,397,7,325,338]
[null,"BN11v3_1350015",null,"Tetrasphaera australiensis Ben110","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",1.01724,1.0403,38.5,{"v":2e-77,"d":"2.00E-77"},2,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",1,394,397,1,403,406]
[null,"BN11v3_1360003",null,"Tetrasphaera australiensis Ben110","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase)","_",0.99496,1.02067,36.71,{"v":2e-75,"d":"2.00E-75"},3,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",17189250,"3 : Putative function from multiple computational evidences",2,395,397,4,386,387]
[null,"BN10v3_920035",null,"Tetrasphaera elongata Lp2","_","Putative 3-ketoacyl-CoA thiolase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",1.00737,1.03275,35.12,{"v":6e-75,"d":"6.00E-75"},2,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,394,397,5,404,407]
[null,"AZCBGv1_p150132","_","Azospirillum brasilense CBG497","phaA","Beta-ketothiolase (acetyl-CoA acetyltransferase with thiolase domain)(Acetyl-CoA C-acyltransferase)","_",0.98992,1.0155,37.66,{"v":4E-73,"d":"4.00E-73"},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",4,394,397,13,385,387]
[null,"RALSYv5_mp0378","_","Ralstonia syzygii R24","_","putative 3-ketoacyl-CoA thiolase / acetyl-CoA acetyltransferase (fragment)","_",0.42569,0.9235,42.6,{"v":2e-36,"d":"2.00E-36"},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",221,389,397,12,176,183]
[]
["ACT01_10830","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_20308",null,"Clostridiaceae BL-3","crt","Short-chain-enoyl-CoA hydratase","ENOYL-COA-HYDRAT-RXN ; RHEA:16105 ;",1,1.00386,56.54,{"v":8e-96,"d":"8.00E-96"},1,1,"_","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 5057466","1c : Function from experimental evidences in the studied genus",1,260,260,1,259,259]
[null,"CD630_08000","_","Clostridium difficile 630","crt1","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.98462,0.98462,48.05,{"v":2E-85,"d":"2.00E-85"},1,1,"1.6 : Macromolecules (cellular constituent) biosynthesis ;","4.2.1.55","1 : Unknown","6 : Energy metabolism ;","e : enzyme","8001771, 16346566, 11263873","2a : Function from experimental evidences in other organisms",5,260,260,6,260,260]
[null,"CD630_10570",null,"Clostridium difficile 630","crt2","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.96226,0.98077,52.16,{"v":4e-81,"d":"4.00E-81"},2,1,"_","4.2.1.55","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,257,260,9,262,265]
[null,"CLOSTRIBL4_v1_1868",null,"Clostridiales BL-4","crt","Short-chain-enoyl-CoA hydratase","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; RHEA:17852 ;",0.95769,0.96512,51,{"v":7e-79,"d":"7.00E-79"},1,1,"_","4.2.1.55","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286, 5057466","2a : Function from experimental evidences in other organisms",6,254,260,4,251,258]
[null,"CLOSTRIBL4_v1_1161",null,"Clostridiales BL-4","crt","Short-chain-enoyl-CoA hydratase","ENOYL-COA-HYDRAT-RXN ; RHEA:16108 ;",0.9529,1.01154,51.71,{"v":7e-78,"d":"7.00E-78"},2,1,"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",1,259,260,17,275,276]
[null,"CLOSTRIBL6_v1_0558",null,"Clostridiales BL-6","crt","Short-chain-enoyl-CoA hydratase","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; RHEA:52667 ;",1.00382,1.01154,49.05,{"v":6e-76,"d":"6.00E-76"},1,1,"_","4.2.1.150, 4.2.1.55","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286, 5057466","2a : Function from experimental evidences in other organisms",1,259,260,3,261,262]
[null,"BSU18220","_","Bacillus subtilis 168","ldeF","methylglutaconyl-CoA hydratase (leucine degradation)","METHYLGLUTACONYL-COA-HYDRATASE-RXN ; RHEA:21536 ;",0.98846,0.98846,46.3,{"v":5e-73,"d":"5.00E-73"},1,1,"_","4.2.1.18","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",19935659,"2b : Function from indirect experimental evidences (e.g. phenotypes)",4,259,260,3,259,260]
[null,"BN873v1_210051",null,"Candidatus Competibacter denitrificans Run_A_D11","_","putative enoyl-CoA hydratase-isomerase","_",1.00769,1.0155,47.33,{"v":6e-73,"d":"6.00E-73"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","_","e : enzyme","8655474, 10727085, 2204034, 1743516","3 : Putative function from multiple computational evidences",1,258,260,1,256,258]
[null,"BN874v1_720037",null,"Candidatus Contendobacter odensis Run_B_J11","_","putative enoyl-CoA hydratase-isomerase","_",1.00769,1.0155,46.56,{"v":6e-71,"d":"6.00E-71"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.-","1 : Unknown","_","e : enzyme","8655474, 10727085, 2204034, 1743516","3 : Putative function from multiple computational evidences",1,258,260,1,256,258]
[null,"MGMSRv2_2895",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaF","enoyl-CoA hydratase-isomerase","_",1,1.00775,45.77,{"v":2E-70,"d":"2.00E-70"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",1,258,260,1,256,258]
[null,"IBTHAUMv1_18460003","_","Ianthella basta symbiont thaum","crt","3-hydroxybutyryl-CoA dehydratase","_",0.93077,0.96032,46.28,{"v":2e-69,"d":"2.00E-69"},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)",13,254,260,10,251,252]
[null,"NVIE_008340","_","Nitrososphaera viennensis EN76","_","3-hydroxybutyryl-CoA dehydratase","_",0.90635,1.04231,43.17,{"v":2e-68,"d":"2.00E-68"},1,1,"_","4.2.1.55","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",14,254,260,28,298,299]
[null,"LEPBIa0927","_","Leptospira biflexa serovar Patoc Patoc 1","crt","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.95385,0.97638,45.97,{"v":2e-68,"d":"2.00E-68"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.55","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","12379132, 8490573","2a : Function from experimental evidences in other organisms",10,257,260,8,254,254]
[null,"SCFA_v1_1190005","_","Ca. Phosphitivorax anaerolimi F81","crt","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.97308,1,47.04,{"v":3E-68,"d":"3.00E-68"},1,1,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,260,260,6,253,253]
[null,"AZOLI_3178","_","Azospirillum lipoferum 4B","paaF1","Enoyl-CoA hydratase-isomerase","_",1.00769,1.0155,45.42,{"v":8e-68,"d":"8.00E-68"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",1,258,260,1,256,258]
[null,"PSEEN3545","_","Pseudomonas entomophila L48","fadB1x","enoyl-CoA hydratase, FadB1x","_",0.95385,0.992,44.76,{"v":1e-67,"d":"1.00E-67"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","4.2.1.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",11251808,"2a : Function from experimental evidences in other organisms",14,258,260,7,248,250]
[null,"Rru_A3801","_","Rhodospirillum rubrum ATCC 11170","fadB","short chain enoyl-CoA hydratase","_",0.99615,1.00388,43.63,{"v":3e-67,"d":"3.00E-67"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.5.4 : Fatty acid and phosphatidic acid ;","4.2.1.17","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,257,260,1,255,258]
[null,"RM41v1_60029","_","Sinorhizobium sp. Rm41","_","Putative enoyl-CoA hydratase","_",1,1.01167,43.08,{"v":4e-66,"d":"4.00E-66"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","1743516, 2204034, 2806264, 7815937","3 : Putative function from multiple computational evidences",1,258,260,1,255,257]
[null,"ABAYE3764","_","Acinetobacter baumannii AYE","_","putative Enoyl-CoA hydratase","_",1.00769,1.01946,41.22,{"v":5e-66,"d":"5.00E-66"},1,1,"_","4.2.1.17","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,260,260,1,257,257]
[null,"SCFA_v1_100018",null,"Ca. Phosphitivorax anaerolimi F81","_","Enoyl-CoA hydratase","_",1.00769,1.02344,41.22,{"v":5e-66,"d":"5.00E-66"},2,1,"_","4.2.1.17","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,260,260,1,256,256]
[null,"BN44v3_11186","_","Mycobacterium canettii STB-D","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",1,1.01167,42.69,{"v":8e-66,"d":"8.00E-66"},1,1,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",1,257,260,1,254,257]
[null,"BN43v3_30123","_","Mycobacterium canettii STB-L","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",1,1.01167,42.69,{"v":8e-66,"d":"8.00E-66"},1,1,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",1,257,260,1,254,257]
[null,"HEAR0207","_","Herminiimonas arsenicoxydans","ech","Enoyl-CoA hydratase","_",0.99231,1,44.96,{"v":4e-65,"d":"4.00E-65"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",8012501,"2a : Function from experimental evidences in other organisms",1,258,260,1,256,258]
[null,"BN11v3_3200006","_","Tetrasphaera australiensis Ben110","_","putative enoyl-CoA hydratase echA8","_",0.99231,0.99614,44.57,{"v":6E-65,"d":"6.00E-65"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,259,260,3,258,259]
[null,"ACIAD1608","_","Acinetobacter baylyi ADP1","FadB","Enoyl-CoA hydratase (valine degradation) (valine degradation)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; ENOYL-COA-HYDRAT-RXN ; METHYLACYLYLCOA-HYDROXY-RXN ; RXN-902 ; TIGLYLCOA-HYDROXY-RXN ; RHEA:31178 ;",1.00385,1.01556,41.76,{"v":1e-64,"d":"1.00E-64"},1,1,"1.1.3.14 : Valine degradation ; 1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","7122152, 8938168, 21104317","2a : Function from experimental evidences in other organisms",1,258,260,1,255,257]
[null,"BN45v3_30109","_","Mycobacterium canettii STB-J","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",1,1.01167,42.31,{"v":2e-64,"d":"2.00E-64"},1,1,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",1,257,260,1,254,257]
[null,"BN42v3_20918","_","Mycobacterium canettii STB-K","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",1,1.01167,41.92,{"v":2e-64,"d":"2.00E-64"},1,1,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",1,257,260,1,254,257]
[null,"Rmet_2603","_","Cupriavidus metallidurans CH34","paaG1","Enoyl-CoA hydratase/isomerase","_",0.9962,1.00769,42.37,{"v":2e-64,"d":"2.00E-64"},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)",1,259,260,1,262,263]
[null,"BN10v3_570010","_","Tetrasphaera elongata Lp2","_","putative enoyl-CoA hydratase echA8","_",0.98846,0.99612,44.75,{"v":1e-63,"d":"1.00E-63"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,259,260,3,257,258]
[null,"BRADO2663","_","Bradyrhizobium sp. ORS278","_","Putative enoyl-CoA hydratase","_",0.95489,0.97692,43.31,{"v":2e-63,"d":"2.00E-63"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","1743516, 2204034, 2806264, 7815937","3 : Putative function from multiple computational evidences",3,254,260,11,260,266]
[null,"BN13v1_100067","_","Tetrasphaera jenkinsii Ben74","_","putative enoyl-CoA hydratase echA8","_",0.99615,1,42.47,{"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",4,259,260,3,258,259]
[null,"NIDE3102",null,"Candidatus Nitrospira defluvii","paaF","putative Enoyl-CoA hydratase","_",0.9542,0.96154,40.4,{"v":6e-62,"d":"6.00E-62"},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",9,257,260,12,259,262]
[null,"CLOSTRIBL3_v1_13112",null,"Clostridiaceae BL-3","crt","Short-chain-enoyl-CoA hydratase","RXN-11667 ; RHEA:52664 ;",0.99231,1.01176,42.25,{"v":6e-62,"d":"6.00E-62"},2,1,"_","4.2.1.150","2 : Cytoplasmic","_","e : enzyme","8655474, 5057466","1c : Function from experimental evidences in the studied genus",4,260,260,2,255,255]
[null,"BN12v2_350029","_","Tetrasphaera japonica T1-X7","_","putative enoyl-CoA hydratase echA8","_",0.98855,0.99615,43.63,{"v":8e-62,"d":"8.00E-62"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,259,260,5,261,262]
[null,"RALTA_A2759","_","Cupriavidus taiwanensis LMG19424","badK","cyclohex-1-ene-1-carboxyl-CoA hydratase","_",1,1.00775,41.54,{"v":2e-60,"d":"2.00E-60"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9177244,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,258,260,1,256,258]
[null,"VIBNIv4_A2943","_","Vibrio nigripulchritudo SFn1","Echs1","Enoyl-CoA hydratase","_",0.95385,0.97638,43.15,{"v":4e-60,"d":"4.00E-60"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 7.1 : Cytoplasm ;","4.2.1.17","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","2806264, 15489334, 7883013, 8895557, 9480773, 11851409, 12445775","2a : Function from experimental evidences in other organisms",14,259,260,11,253,254]
[null,"THI_0338","_","Thiomonas sp. 3As","fadB","enoyl-CoA hydratase-isomerase","_",0.94253,0.94615,43.5,{"v":5e-59,"d":"5.00E-59"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",14,257,260,17,258,261]
[null,"BDBv6_60063","_","Blood disease bacterium R229","paaF","enoyl-CoA hydratase-isomerase","_",0.99615,1.00388,41.7,{"v":2e-58,"d":"2.00E-58"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9748275,"2a : Function from experimental evidences in other organisms",1,254,260,1,252,258]
[null,"CMR15v5_1457","_","Ralstonia solanacearum CMR15","paaF","enoyl-CoA hydratase-isomerase","_",1.01154,1.01938,41.83,{"v":3e-58,"d":"3.00E-58"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9748275,"2a : Function from experimental evidences in other organisms",1,258,260,1,256,258]
[null,"SCFA_v1_130011",null,"Ca. Phosphitivorax anaerolimi F81","paaF","Enoyl-CoA hydratase/isomerase family (3-hydroxybutyryl-CoA dehydratase (Crotonase))","RXN-11667 ;",0.3921,0.99231,43.02,{"v":4e-57,"d":"4.00E-57"},3,2,"_","4.2.1.17, 5.1.2.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,258,260,401,656,658]
[null,"PP_3284",null,"Pseudomonas putida KT2440","paaF","enoyl-CoA hydratase-isomerase","RXN0-6513 ; RHEA:34866 ;",0.98077,0.99222,39.61,{"v":5e-57,"d":"5.00E-57"},2,1,"_","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","12846838, 15137080, 18437357","2a : Function from experimental evidences in other organisms",11,259,260,11,256,257]
[null,"FRAAL5882","_","Frankia alni ACN14a","echA","enoyl-CoA hydratase-isomerase","_",0.96923,0.97674,40.08,{"v":1E-56,"d":"1.00E-56"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","4.2.1.17","1 : Unknown","16.2 : Construct biomass (Anabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",10,259,260,8,257,258]
[null,"ACIAD1692",null,"Acinetobacter baylyi ADP1","dcaE","Enoyl-CoA hydratase (branched-chain amino acid degradation)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; ENOYL-COA-HYDRAT-RXN ; METHYLACYLYLCOA-HYDROXY-RXN ; RXN-2425 ; RXN-902 ; TIGLYLCOA-HYDROXY-RXN ; RXN0-6513 ; RXN-7838 ; RHEA:16107 ; RHEA:17850 ; RHEA:31178 ; RHEA:31122 ;",0.98851,0.99231,38.76,{"v":7e-55,"d":"7.00E-55"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921, 11571189","1a : Function from experimental evidences in the studied strain",3,260,260,8,261,261]
[null,"ABAYE2304",null,"Acinetobacter baumannii AYE","dcaE","enoyl-CoA hydratase","_",0.95203,0.99231,37.98,{"v":1E-54,"d":"1.00E-54"},2,1,"1.1.1 : carbon compounds ;","4.2.1.17","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",3,260,260,18,271,271]
[null,"PSEEN2791",null,"Pseudomonas entomophila L48","phaA","enoyl-CoA hydratase/isomerase PhaA","_",0.97692,0.98833,38.58,{"v":1E-54,"d":"1.00E-54"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","Cytoplasmic","6 : Energy metabolism ;","e : enzyme","12534466, 15474299, 9600981","2a : Function from experimental evidences in other organisms",12,259,260,12,256,257]
[null,"PSHAa0882","_","Pseudoalteromonas haloplanktis TAC125","paaF","putative enoyl-CoA hydratase-isomerase","_",0.95785,0.96154,37.2,{"v":9e-54,"d":"9.00E-54"},1,1,"2 : Intermediary metabolism ;","4.2.1.17","unknown","_","e : enzyme",9748275,"3 : Putative function from multiple computational evidences",11,260,260,15,261,261]
[null,"SCFA_v1_3390003",null,"Ca. Phosphitivorax butyraticus R76","hbd","3-hydroxybutyryl-CoA dehydrogenase (modular protein)","_",0.3921,0.99231,39.92,{"v":5E-52,"d":"5.00E-52"},2,2,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,258,260,401,656,658]
[null,"MGMSRv2_3173",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaF","enoyl-CoA hydratase-isomerase","_",0.94231,0.94595,39.59,{"v":6E-51,"d":"6.00E-51"},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",17,259,260,19,258,259]
[null,"ABAYE2370",null,"Acinetobacter baumannii AYE","paaF","enoyl-CoA hydratase, phenylacetic acid degradation","_",1.00385,1.01556,37.16,{"v":7e-51,"d":"7.00E-51"},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)",9,260,260,9,257,257]
[null,"MARHY1100","_","Marinobacter hydrocarbonoclasticus ATCC 49840","paaF","enoyl-CoA hydratase-isomerase","_",0.94615,0.94981,38.62,{"v":2E-50,"d":"2.00E-50"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",14,258,260,13,257,259]
[null,"XDD1v4_3923",null,"Xenorhabdus doucetiae FRM16","paaF","protein PaaF; enoyl-CoA hydratase-isomerase","_",0.99615,1.00778,35.52,{"v":2e-49,"d":"2.00E-49"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,259,260,1,256,257]
[null,"RALTA_B1107",null,"Cupriavidus taiwanensis LMG19424","_","putative ENOYL-COA HYDRATASE ISOMERASE; similar to paaF (E.coli)","_",0.97692,0.99219,36.61,{"v":7e-49,"d":"7.00E-49"},1,1,"1 : Metabolism ;","4.2.1.-","2 : Cytoplasmic","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,258,260,2,254,256]
[null,"AZCBGv1_p1100088","_","Azospirillum brasilense CBG497","_","enoyl-CoA hydratase-isomerase","_",0.95849,0.97692,36.22,{"v":1E-46,"d":"1.00E-46"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","e : enzyme","1743516, 2204034, 2806264, 7815937","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,258,260,14,263,265]
[null,"ECS88_4526",null,"Escherichia coli S88","_","putative Enoyl-CoA hydratase/carnithine racemase","_",0.94231,0.94595,35.51,{"v":7e-46,"d":"7.00E-46"},3,1,"_","4.2.1.17","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",14,257,260,14,256,259]
[null,"BN381v2_10064","_","Candidatus Microthrix parvicella RN1","_","putative enoyl-CoA hydratase-isomerase","_",0.81685,0.85769,38.12,{"v":1e-43,"d":"1.00E-43"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","8655474, 10727085, 2204034, 1743516","3 : Putative function from multiple computational evidences",46,251,260,46,262,273]
[null,"VIBNIv4_A2412",null,"Vibrio nigripulchritudo SFn1","menB","Naphthoate synthase","_",0.87153,0.96538,37.05,{"v":3E-43,"d":"3.00E-43"},5,1,"1.5.3.11 : Menaquinone (MK), ubiquinone (Q) ; 7.1 : Cytoplasm ;","4.1.3.36","2 : Cytoplasmic","4.5 : Menaquinone and ubiquinone ;","e : enzyme","1629162, 6454056, 6754698, 9325429","2a : Function from experimental evidences in other organisms",11,257,260,34,281,288]
[null,"CMR15v5_mp0937","_","Ralstonia solanacearum CMR15","_","putative enoyl-CoA hydratase/isomerase (paaF)","_",0.92857,0.95,35.22,{"v":4E-41,"d":"4.00E-41"},1,1,"1 : Metabolism ;","4.2.1.-","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",14,259,260,12,257,266]
[null,"METDI5699","_","Methylobacterium extorquens DM4","croA","3-hydroxybutyryl-CoA dehydratase","_",0.93929,1.01154,36.5,{"v":3e-40,"d":"3.00E-40"},1,1,"_","4.2.1.17","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",4,259,260,17,279,280]
[null,"NBG4_v1_200001",null,"Candidatus Sulfobium mesophilum","echA","3-hydroxybutyryl-CoA dehydratase (fragment)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; RHEA:17849 ;",0.48077,0.88652,46.4,{"v":6e-31,"d":"6.00E-31"},1,1,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",11,135,260,17,139,141]
[null,"NT26v4_0121",null,"Rhizobium sp. NT-26","_","putative bifunctional anaerobic fatty acid oxidation complex protein (fadJ/fadB-like): enoyl-CoA hydratase/epimerase/isomerase (N-terminal); 3-hydroxyacyl-CoA dehydrogenase (C-terminal)","_",0.29986,0.85,35.29,{"v":3E-23,"d":"3.00E-23"},10,3,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.4 : Anaerobic fatty acid oxidation pathway ;","4.2.1.17, 1.1.1.35, 5.3.3.8","2 : Cytoplasmic","_","e : enzyme","12270828, 12535077","3 : Putative function from multiple computational evidences",8,206,260,6,221,737]
[]
["ACT01_10835","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_20313",null,"Clostridiaceae BL-3","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.99298,1.00355,60.42,{"v":5e-113,"d":"5.00E-113"},1,1,"_","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286, 8001771","1c : Function from experimental evidences in the studied genus",3,285,285,2,282,282]
[null,"BSU24160","_","Bacillus subtilis 168","mmgB","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.98606,0.99298,55.48,{"v":1e-109,"d":"1.00E-109"},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",3,285,285,4,284,287]
[null,"CD630_10580",null,"Clostridium difficile 630","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.98947,1.00356,56.38,{"v":9E-103,"d":"9.00E-103"},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",4,285,285,2,281,281]
[null,"AZCBGv1_p190002","_","Azospirillum brasilense CBG497","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.96918,0.99298,52.3,{"v":6E-102,"d":"6.00E-102"},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",3,285,285,5,285,292]
[null,"MGMSRv2_3942","_","Magnetospirillum gryphiswaldense MSR-1 v2","mmgB","3-hydroxybutyryl-CoA dehydrogenase (Beta- hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.96575,0.98947,53.9,{"v":1E-100,"d":"1.00E-100"},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)",3,284,285,5,284,292]
[null,"AZOLI_p50301","_","Azospirillum lipoferum 4B","hbdA1","3-hydroxybutyryl-CoA dehydrogenase","_",0.96918,0.99298,51.59,{"v":2E-100,"d":"2.00E-100"},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",3,285,285,5,285,292]
[null,"CLOSTRIBL4_v1_1869",null,"Clostridiales BL-4","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.99649,1.01792,55.99,{"v":6E-98,"d":"6.00E-98"},1,1,"_","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",4,285,285,2,279,279]
[null,"BRADO6490","_","Bradyrhizobium sp. ORS278","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta- hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.89457,0.98246,52.14,{"v":2e-96,"d":"2.00E-96"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.1.1.157","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme",8655474,"2b : Function from indirect experimental evidences (e.g. phenotypes)",4,283,285,27,304,313]
[null,"NBG4_v1_200002",null,"Candidatus Sulfobium mesophilum","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:22432 ;",0.98596,0.99645,51.6,{"v":3e-96,"d":"3.00E-96"},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",3,283,285,4,281,282]
[null,"Mchl_1824","_","Methylobacterium extorquens CM4","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.95904,0.98596,51.6,{"v":8e-96,"d":"8.00E-96"},1,1,"_","1.1.1.157","1 : Unknown","_","e : enzyme","2687255, 8655474","2a : Function from experimental evidences in other organisms",3,283,285,6,284,293]
[null,"METDI2209","_","Methylobacterium extorquens DM4","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.92739,0.98596,51.6,{"v":1e-95,"d":"1.00E-95"},1,1,"_","1.1.1.157","1 : Unknown","_","e : enzyme","2687255, 8655474","2a : Function from experimental evidences in other organisms",3,283,285,16,294,303]
[null,"BBta_1142","_","Bradyrhizobium sp. BTAi1","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.9589,0.98246,51.43,{"v":1e-95,"d":"1.00E-95"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.1.1.157","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,283,285,6,283,292]
[null,"ADVE02_v2_10866","_","Methylosinus trichosporium OB3b","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.95904,0.98596,51.25,{"v":4e-94,"d":"4.00E-94"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,283,285,6,284,293]
[null,"RM41v1_680007","_","Sinorhizobium sp. Rm41","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta- hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.97586,0.99298,49.82,{"v":1e-93,"d":"1.00E-93"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 7.1 : Cytoplasm ;","1.1.1.157","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",8655474,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,283,285,1,281,290]
[null,"RALTA_A0220","_","Cupriavidus taiwanensis LMG19424","_","3-HYDROXYBUTYRYL-COA DEHYDROGENASE","_",0.99298,0.99648,50.88,{"v":1e-92,"d":"1.00E-92"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","1 : Unknown","3.2 : Degradation ;  6 : Energy metabolism ;","e : enzyme",8655474,"2b : Function from indirect experimental evidences (e.g. phenotypes)",3,285,285,4,284,284]
[null,"Rmet_0212","_","Cupriavidus metallidurans CH34","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.99298,0.99648,49.82,{"v":1E-89,"d":"1.00E-89"},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",3,285,285,4,284,284]
[null,"CLOSTRIBL6_v1_0126","_","Clostridiales BL-6","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.98947,1.01439,51.42,{"v":1e-88,"d":"1.00E-88"},1,1,"_","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8759838, 18461320, 28956599","2a : Function from experimental evidences in other organisms",4,284,285,2,278,278]
[null,"BDBv6_40067","_","Blood disease bacterium R229","_","3-HYDROXYBUTYRYL-COA DEHYDROGENASE","_",0.98596,0.98944,49.47,{"v":7e-88,"d":"7.00E-88"},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)",5,285,285,6,284,284]
[null,"CMR15v5_0701","_","Ralstonia solanacearum CMR15","_","3-HYDROXYBUTYRYL-COA DEHYDROGENASE","_",0.98596,0.98944,49.11,{"v":1E-87,"d":"1.00E-87"},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)",5,285,285,6,284,284]
[null,"BN381v2_100132","_","Candidatus Microthrix parvicella RN1","_","putative dehydrogenase","_",0.94059,1,47.37,{"v":3e-86,"d":"3.00E-86"},1,1,"_","_","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","12846838, 8001771, 1699931","3 : Putative function from multiple computational evidences",1,285,285,21,303,303]
[null,"NIDE3117","_","Candidatus Nitrospira defluvii","paaH","3-hydroxybutyryl-CoA dehydrogenase","_",0.95578,0.98596,46.26,{"v":2e-84,"d":"2.00E-84"},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)",3,283,285,7,285,294]
[null,"PSEEN3198","_","Pseudomonas entomophila L48","paaH","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.97193,1.00727,46.21,{"v":7e-84,"d":"7.00E-84"},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)",7,283,285,1,275,275]
[null,"BN42v3_20192","_","Mycobacterium canettii STB-K","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98951,0.99298,43.46,{"v":4e-74,"d":"4.00E-74"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",3,283,285,6,286,286]
[null,"BN44v3_10518","_","Mycobacterium canettii STB-D","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98951,0.99298,43.11,{"v":2E-73,"d":"2.00E-73"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",3,283,285,6,286,286]
[null,"BN43v3_10507","_","Mycobacterium canettii STB-L","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98951,0.99298,43.11,{"v":2E-73,"d":"2.00E-73"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",3,283,285,6,286,286]
[null,"BN45v3_10517","_","Mycobacterium canettii STB-J","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98951,0.99298,42.76,{"v":7e-73,"d":"7.00E-73"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",3,283,285,6,286,286]
[null,"BN12v2_1150036","_","Tetrasphaera japonica T1-X7","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD))","_",0.47804,0.99298,42.4,{"v":2e-72,"d":"2.00E-72"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,284,285,5,285,592]
[null,"PSHAa0399","_","Pseudoalteromonas haloplanktis TAC125","bhbD","3-hydroxybutyryl-CoA dehydrogenase (Beta- hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.98947,1.00356,44.68,{"v":3e-72,"d":"3.00E-72"},1,1,"_","1.1.1.157","unknown","_","e : enzyme",8001771,"2a : Function from experimental evidences in other organisms",4,283,285,2,281,281]
[null,"Npun_R3442","_","Nostoc punctiforme ATCC 29133; PCC 73102","_","3-hydroxybutyryl-CoA dehydrogenase","_",0.97917,0.98947,41.84,{"v":1E-70,"d":"1.00E-70"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,284,285,7,285,288]
[null,"SCFA_v1_130011",null,"Ca. Phosphitivorax anaerolimi F81","paaF","Enoyl-CoA hydratase/isomerase family (3-hydroxybutyryl-CoA dehydratase (Crotonase))","RXN-11667 ;",0.43009,0.99298,43.46,{"v":3e-69,"d":"3.00E-69"},3,1,"_","4.2.1.17, 5.1.2.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,284,285,5,284,658]
[null,"BN13v1_460001","_","Tetrasphaera jenkinsii Ben74","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD))","_",0.47804,0.99298,41.34,{"v":7e-69,"d":"7.00E-69"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,284,285,5,285,592]
[null,"BN10v3_1170022","_","Tetrasphaera elongata Lp2","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD))","_",0.47547,0.98596,43.77,{"v":9E-68,"d":"9.00E-68"},1,1,"_","1.1.1.157","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,283,285,313,591,591]
[null,"BN11v3_1490005","_","Tetrasphaera australiensis Ben110","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD)","_",0.47804,0.99298,40.99,{"v":1e-67,"d":"1.00E-67"},1,1,"_","1.1.1.157","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",1444364,"3 : Putative function from multiple computational evidences",2,284,285,5,285,592]
[null,"XDD1v4_1792","_","Xenorhabdus doucetiae FRM16","xcnB","3-hydroxyacyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",1.01404,1.01404,39.79,{"v":6e-67,"d":"6.00E-67"},1,1,"_","1.1.1.157","1 : Unknown","15.11 : Biosynthesis of natural products ;","e : enzyme","16349198, 1955881","2a : Function from experimental evidences in other organisms",4,284,285,2,281,285]
[null,"NIDE3103",null,"Candidatus Nitrospira defluvii","_","putative 3-hydroxyacyl-CoA dehydrogenase","_",0.69042,0.98596,43.06,{"v":2E-66,"d":"2.00E-66"},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",4,284,285,5,281,407]
[null,"PP_3282",null,"Pseudomonas putida KT2440","paaH","3-hydroxyadipyl-CoA dehydrogenase","RXN0-2044 ; RHEA:16199 ;",0.5604,0.99298,43.11,{"v":1e-65,"d":"1.00E-65"},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",4,285,285,9,289,505]
[null,"SCFA_v1_100019",null,"Ca. Phosphitivorax anaerolimi F81","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.7467,0.99298,44.52,{"v":3E-65,"d":"3.00E-65"},4,1,"_","1.1.1.157","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,284,285,4,282,379]
[null,"XNC1_1710","_","Xenorhabdus nematophila ATCC19061","xcnB","3-hydroxyacyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",1.00351,1.00351,38.46,{"v":3E-65,"d":"3.00E-65"},1,1,"_","1.1.1.157","1 : Unknown","15.11 : Biosynthesis of natural products ;","e : enzyme","16349198, 1955881","1a : Function from experimental evidences in the studied strain",4,284,285,2,281,285]
[null,"MGMSRv2_3175",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaH","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.5505,0.97544,41.37,{"v":2e-64,"d":"2.00E-64"},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",7,283,285,12,287,505]
[null,"PSEEN2793",null,"Pseudomonas entomophila L48","paaC","3-hydroxyacyl-CoA dehydrogenase phaC","_",0.55512,0.98947,42.91,{"v":5e-64,"d":"5.00E-64"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.-","Cytoplasmic","6 : Energy metabolism ;","e : enzyme","12534466, 15474299, 9600981","2a : Function from experimental evidences in other organisms",4,284,285,12,291,508]
[null,"AZOLI_p40260",null,"Azospirillum lipoferum 4B","paaH","3-hydroxybutyryl-CoA dehydrogenase","_",0.50722,0.98596,41.99,{"v":5e-64,"d":"5.00E-64"},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",5,284,285,10,288,554]
[null,"ABAYE2368",null,"Acinetobacter baumannii AYE","paaH","3-hydroxybutyryl-CoA dehydrogenase, phenylacetic acid degradation","_",0.55273,0.99298,39.93,{"v":2e-63,"d":"2.00E-63"},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",4,285,285,10,290,512]
[null,"SCFA_v1_3390003",null,"Ca. Phosphitivorax butyraticus R76","hbd","3-hydroxybutyryl-CoA dehydrogenase (modular protein)","_",0.42857,0.98947,40.43,{"v":6e-63,"d":"6.00E-63"},3,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,284,285,5,284,658]
[null,"CLOSTRIBL3_v1_13113",null,"Clostridiaceae BL-3","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.98958,1,41.05,{"v":1E-62,"d":"1.00E-62"},2,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 25112316","1c : Function from experimental evidences in the studied genus",3,283,285,4,287,288]
[null,"BN874v1_720038",null,"Candidatus Contendobacter odensis Run_B_J11","_","putative hydroxyacyl/hydroxybutyrl -CoA dehydrogenase","RXN0-2044 ;",0.94631,0.98947,39.36,{"v":7e-62,"d":"7.00E-62"},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",3,284,285,4,283,298]
[null,"BN873v1_210050",null,"Candidatus Competibacter denitrificans Run_A_D11","_","putative hydroxyacyl/hydroxybutyrl -CoA dehydrogenase","_",0.94631,0.98947,40.07,{"v":3e-61,"d":"3.00E-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",3,284,285,4,283,298]
[null,"CLOSTRIBL4_v1_1158",null,"Clostridiales BL-4","hbd","3-hydroxybutyryl-CoA dehydrogenase","RXN-12570 ; RHEA:16200 ;",0.96633,1.00702,38.33,{"v":8e-60,"d":"8.00E-60"},2,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",3,284,285,7,292,297]
[null,"NVIE_010920","_","Nitrososphaera viennensis EN76","_","hydroxyacyl-CoA dehydrogenase","_",0.73177,0.98596,39.15,{"v":6e-59,"d":"6.00E-59"},1,1,"_","1.1.1.35","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,283,285,9,287,384]
[null,"ABAYE2306",null,"Acinetobacter baumannii AYE","dcaH","dehydrogenase","_",0.55621,0.98947,40.43,{"v":2e-58,"d":"2.00E-58"},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",3,283,285,6,285,507]
[null,"XDD1v4_3925",null,"Xenorhabdus doucetiae FRM16","paaH","protein PaaH; 3-hydroxybutyryl-CoA dehydrogenase","_",0.51188,0.98246,39.64,{"v":9e-56,"d":"9.00E-56"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",5,283,285,10,287,547]
[null,"ACIAD1690",null,"Acinetobacter baylyi ADP1","dcaH","dehydrogenase","1.1.1.259-RXN ; METHELENE-THMPT-OXI-RXN ; RXN0-2044 ;",0.55842,0.98947,39.72,{"v":5e-55,"d":"5.00E-55"},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",3,283,285,6,285,505]
[null,"IBTHAUMv1_1140010","_","Ianthella basta symbiont thaum","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.84561,0.94141,40.25,{"v":9e-55,"d":"9.00E-55"},1,1,"1.3 : Energy metabolism (carbon) ;","1.1.1.157","2 : Cytoplasmic","_","e : enzyme",11772643,"2b : Function from indirect experimental evidences (e.g. phenotypes)",2,241,285,3,242,256]
[null,"THI_0464","_","Thiomonas sp. 3As","_","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.56375,0.99298,37.46,{"v":2e-54,"d":"2.00E-54"},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",4,285,285,12,291,502]
[null,"CLOSTRIBL6_v1_0555",null,"Clostridiales BL-6","hbd","3-hydroxybutyryl-CoA dehydrogenase","RXN-12705 ; RHEA:16200 ;",0.95987,1.00702,36.24,{"v":2e-54,"d":"2.00E-54"},2,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 25112316","2a : Function from experimental evidences in other organisms",3,284,285,7,292,299]
[null,"Rmet_0974",null,"Cupriavidus metallidurans CH34","paaH","3-hydroxybutyryl-CoA dehydrogenase","_",0.54832,0.97544,36.69,{"v":3e-53,"d":"3.00E-53"},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)",7,283,285,11,286,507]
[null,"VCR9J2v1_150068","_","Vibrio crassostreae J2-9","fadB","Putative 3-hydroxybutyryl-CoA epimerase","OHBUTYRYL-COA-EPIM-RXN ; RHEA:21760 ;",0.39415,0.99298,37.1,{"v":8e-52,"d":"8.00E-52"},1,1,"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",4,285,285,319,597,718]
[null,"VS_0041","_","Vibrio tasmaniensis LGP32","_","3-hydroxybutyryl-CoA epimerase, Fatty acid oxidation complex subunit alpha","_",0.39281,0.99649,37.68,{"v":2E-51,"d":"2.00E-51"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.6 : Aerobic fatty acid oxidation pathway ;","5.1.2.3","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ; 3.2 : Degradation ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,284,285,315,594,723]
[null,"RALTA_A1087",null,"Cupriavidus taiwanensis LMG19424","paaH1","3-hydroxybutyryl-CoA dehydrogenase, phenylacetic acid degradation","_",0.54599,0.97895,35.48,{"v":2E-51,"d":"2.00E-51"},3,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",7,284,285,15,291,511]
[null,"VIBNIv4_A0032","_","Vibrio nigripulchritudo SFn1","fadB","Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase ; 3-hydroxyacyl-CoA dehydrogenase]","_",0.39004,0.98947,35.46,{"v":7e-51,"d":"7.00E-51"},1,1,"1.1.2.6 : Aerobic fatty acid oxidation pathway ; 7.1 : Cytoplasm ;","5.3.3.8, 4.2.1.17, 5.1.2.3, 1.1.1.35","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","1699931, 1712230, 2204034","2a : Function from experimental evidences in other organisms",4,284,285,316,594,723]
[null,"MARHY2136","_","Marinobacter hydrocarbonoclasticus ATCC 49840","fadB","Fatty acid oxidation complex subunit alpha","_",0.39161,0.98246,37.14,{"v":9e-51,"d":"9.00E-51"},1,1,"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",7,285,285,319,594,715]
[null,"AZOLI_p30575","_","Azospirillum lipoferum 4B","pimF","Enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase","_",0.39745,0.98596,39.15,{"v":2E-50,"d":"2.00E-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",3,283,285,306,581,707]
[null,"BN43v3_20311",null,"Mycobacterium canettii STB-L","fadB","Putative fatty acid oxidation protein FadB","_",0.39861,1.00702,35.54,{"v":6E-49,"d":"6.00E-49"},2,1,"1 : lipid metabolism ;","_","2 : Cytoplasmic","_","e : enzyme","11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",3,284,285,326,608,720]
[null,"BN42v3_20640",null,"Mycobacterium canettii STB-K","fadB","Putative fatty acid oxidation protein FadB","_",0.39861,1.00702,35.54,{"v":6E-49,"d":"6.00E-49"},2,1,"1 : lipid metabolism ;","_","2 : Cytoplasmic","_","e : enzyme","11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",3,284,285,326,608,720]
[null,"BN45v3_20151",null,"Mycobacterium canettii STB-J","fadB","Putative fatty acid oxidation protein FadB","_",0.39861,1.00702,35.54,{"v":1e-48,"d":"1.00E-48"},2,1,"1 : lipid metabolism ;","_","2 : Cytoplasmic","_","e : enzyme","11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",3,284,285,326,608,720]
[null,"BN44v3_10941",null,"Mycobacterium canettii STB-D","fadB","Putative fatty acid oxidation protein FadB","_",0.39586,1.00702,35.54,{"v":2e-48,"d":"2.00E-48"},2,1,"1 : lipid metabolism ;","_","2 : Cytoplasmic","_","e : enzyme","11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",3,284,285,326,608,725]
[null,"Rmet_5110",null,"Cupriavidus metallidurans CH34","fadB1","short chain enoyl-CoA hydratase / 3-hydroxyacyl-CoA dehydrogenase","_",0.4,1.00351,38.46,{"v":7e-48,"d":"7.00E-48"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","5.1.2.3, 1.1.1.35, 4.2.1.17","2 : Cytoplasmic","3.2 : Degradation ; 6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,283,285,312,587,715]
[null,"NT26v4_0121",null,"Rhizobium sp. NT-26","_","putative bifunctional anaerobic fatty acid oxidation complex protein (fadJ/fadB-like): enoyl-CoA hydratase/epimerase/isomerase (N-terminal); 3-hydroxyacyl-CoA dehydrogenase (C-terminal)","_",0.38535,0.99649,36.62,{"v":7e-47,"d":"7.00E-47"},2,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.4 : Anaerobic fatty acid oxidation pathway ;","4.2.1.17, 1.1.1.35, 5.3.3.8","2 : Cytoplasmic","_","e : enzyme","12270828, 12535077","3 : Putative function from multiple computational evidences",3,283,285,327,606,737]
[null,"LMIv2_1447","_","Legionella micdadei","_","3-hydroxybutyryl-CoA epimerase","_",0.41456,0.97895,36.2,{"v":5e-43,"d":"5.00E-43"},1,1,"_","5.1.2.3","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,283,285,310,577,673]
[]
["ACT01_12410","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_0871","_","Clostridiales BL-6","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16199 ;",1.00318,1.01613,37.78,{"v":2e-64,"d":"2.00E-64"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",6,310,310,7,314,314]
[null,"CLOSTRIBL3_v1_11276","_","Clostridiaceae BL-3","_","putative 3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16200 ;",0.98071,0.98387,37.7,{"v":3e-60,"d":"3.00E-60"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",6,305,310,6,309,311]
[null,"BN45v3_40195",null,"Mycobacterium canettii STB-J","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB3 (beta-hydroxybutyryl-CoA dehydrogenase) (BhbD)","_",0.96129,0.98026,37.58,{"v":1E-59,"d":"1.00E-59"},1,1,"1 : lipid metabolism ;","1.1.1.157","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",10,307,310,12,295,304]
[null,"BN43v3_30839",null,"Mycobacterium canettii STB-L","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB3 (beta-hydroxybutyryl-CoA dehydrogenase) (BhbD)","_",0.96452,0.98355,37.79,{"v":2e-59,"d":"2.00E-59"},1,1,"1 : lipid metabolism ;","1.1.1.157","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",10,307,310,12,295,304]
[null,"BN44v3_20286",null,"Mycobacterium canettii STB-D","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB3 (beta-hydroxybutyryl-CoA dehydrogenase) (BhbD)","_",0.96452,0.98355,37.79,{"v":2e-59,"d":"2.00E-59"},1,1,"1 : lipid metabolism ;","1.1.1.157","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",10,307,310,12,295,304]
[null,"BN42v3_21646",null,"Mycobacterium canettii STB-K","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB3 (beta-hydroxybutyryl-CoA dehydrogenase) (BhbD)","_",0.96129,0.98026,37.25,{"v":1E-58,"d":"1.00E-58"},1,1,"1 : lipid metabolism ;","1.1.1.157","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",10,307,310,12,295,304]
[]
["ACT01_02995","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_2229","_","Magnetospirillum gryphiswaldense MSR-1 v2","_","MaoC-like dehydratase, putative","_",0.90278,0.94203,52.31,{"v":3e-40,"d":"3.00E-40"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,136,138,11,139,144]
[null,"SCFA_v1_450041","_","Ca. Phosphitivorax anaerolimi F81","phaJ","crotonase","_",0.88435,0.94203,51.54,{"v":4e-39,"d":"4.00E-39"},1,1,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,135,138,5,134,147]
[null,"AZOLI_0508","_","Azospirillum lipoferum 4B","_","Putative acyl dehydratase","_",0.86577,0.93478,48.06,{"v":2e-37,"d":"2.00E-37"},1,1,"_","_","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",8,136,138,17,144,149]
[null,"LEPBIa1114",null,"Leptospira biflexa serovar Patoc Patoc 1","_","Putative MaoC family dehydratase","_",0.92857,0.94203,41.54,{"v":3e-33,"d":"3.00E-33"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",7,136,138,8,137,140]
[null,"CLOSTRIBL3_v1_20109",null,"Clostridiaceae BL-3","corR","enoyl-CoA hydratase","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; RHEA:17849 ;",0.95652,0.95652,43.94,{"v":4e-31,"d":"4.00E-31"},1,1,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme",18218779,"1c : Function from experimental evidences in the studied genus",5,136,138,4,134,138]
[null,"MARHY1690","_","Marinobacter hydrocarbonoclasticus ATCC 49840","_","conserved hypothetical protein","_",0.81988,0.95652,40.91,{"v":4e-30,"d":"4.00E-30"},1,1,"_","_","1 : Unknown","18 : Unknown function ;","u : unknown","_","4 : Unknown function but conserved in other organisms",5,136,138,11,141,161]
[null,"PSEEN3977","_","Pseudomonas entomophila L48","phaJ1","enoyl-CoA hydratase, R-specific","_",0.83333,0.94203,40.77,{"v":1e-29,"d":"1.00E-29"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","_","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",12115060,"2a : Function from experimental evidences in other organisms",7,136,138,9,137,156]
[null,"Rmet_1672","_","Cupriavidus metallidurans CH34","_","MaoC-like dehydratase","_",0.89041,0.94203,43.08,{"v":3e-29,"d":"3.00E-29"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,136,138,9,137,146]
[null,"METDI4248","_","Methylobacterium extorquens DM4","croR","crotonase","_",0.70588,0.95652,40.15,{"v":5e-26,"d":"5.00E-26"},1,1,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme",11872727,"1b : Function from experimental evidences in the studied species",4,135,138,37,167,187]
[null,"THI_1475","_","Thiomonas sp. 3As","_","phosphate butyltransferase","_",0.27083,0.94203,36.15,{"v":3e-25,"d":"3.00E-25"},1,1,"1 : Metabolism ;","2.3.1.19","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,135,138,9,138,480]
[null,"ADVE02_v2_12431","_","Methylosinus trichosporium OB3b","croR","Crotonase","_",0.82278,0.94203,40,{"v":1e-24,"d":"1.00E-24"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,136,138,10,138,158]
[null,"AZOLI_p20460","_","Azospirillum lipoferum 4B","pta2","phosphate acetyltransferase","_",0.275,0.95652,35.61,{"v":2e-24,"d":"2.00E-24"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.8","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme","10094701, 8226623","2a : Function from experimental evidences in other organisms",5,136,138,19,150,480]
[null,"HEAR1516","_","Herminiimonas arsenicoxydans","_","putative phosphate acetyltransferase","_",0.25056,0.80435,39.64,{"v":2E-19,"d":"2.00E-19"},1,1,"1.1 : Carbon compound utilization ; 1.7.28 : Pyruvate catabolism ;","2.3.1.8","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",26,136,138,9,119,443]
[null,"VIBNIv4_A1239","_","Vibrio nigripulchritudo SFn1","_","putative Acyl dehydratase","_",0.83108,0.8913,37.4,2e-15,1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",15,128,138,16,134,148]
[]
["ACT01_00280","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,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.97889,0.98933,41.51,{"v":6e-94,"d":"6.00E-94"},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",6,374,379,4,372,375]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.97625,0.98143,41.62,{"v":1e-93,"d":"1.00E-93"},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",7,374,379,5,372,377]
[null,"Npun_R3440","_","Nostoc punctiforme ATCC 29133; PCC 73102","_","putative acyl-CoA dehydrogenase","_",0.95685,0.99472,39.79,{"v":2e-80,"d":"2.00E-80"},1,1,"_","1.3.99.2","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,374,379,1,370,394]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.96923,0.99736,37.57,{"v":5E-80,"d":"5.00E-80"},3,3,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,376,379,9,384,390]
[]
["ACT01_02990","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_20310","_","Clostridiaceae BL-3","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24004 ;",1,1,57.52,{"v":5e-157,"d":"5.00E-157"},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,"BSU37170","_","Bacillus subtilis 168","acdA","acyl-CoA dehydrogenase","ACYLCOADEHYDROG-RXN ;",0.99472,0.99472,58.62,{"v":3e-156,"d":"3.00E-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_10540","_","Clostridium difficile 630","bcd2","Butyryl-CoA dehydrogenase","_",0.98681,0.98942,59.09,{"v":1e-154,"d":"1.00E-154"},1,1,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",6,379,379,5,378,378]
[null,"CLOSTRIBL4_v1_1870","_","Clostridiales BL-4","bcd","butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24007 ;",0.99221,1.00792,53.4,{"v":6e-141,"d":"6.00E-141"},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,"SCFA_v1_2690009","_","Ca. Phosphitivorax butyraticus R76","acdA","Acyl-CoA dehydrogenase (Butyryl-CoA dehydrogenase)","_",0.99215,1,50.13,{"v":3e-127,"d":"3.00E-127"},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,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.98681,0.99204,47.06,{"v":3e-127,"d":"3.00E-127"},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",6,379,379,4,377,377]
[null,"PP_2216","_","Pseudomonas putida KT2440","acd","short-chain acyl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24007 ;",0.98153,0.992,48.39,{"v":1E-125,"d":"1.00E-125"},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",6,377,379,4,375,375]
[null,"SCFA_v1_190035","_","Ca. Phosphitivorax anaerolimi F81","bcd","acyl-CoA dehydrogenase, short-chain specific (Butyryl-CoA dehydrogenase)","_",0.99215,1,48.81,{"v":1E-125,"d":"1.00E-125"},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,"PSEEN3546","_","Pseudomonas entomophila L48","fadFx","acyl-CoA dehydrogenase protein FadFx","_",0.98153,0.992,47.85,{"v":4e-124,"d":"4.00E-124"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",11251808,"2a : Function from experimental evidences in other organisms",6,377,379,4,375,375]
[null,"ACIAD1607","_","Acinetobacter baylyi ADP1","acads","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; RXN0-2301 ; RHEA:24007 ; RHEA:12277 ;",0.98681,0.99733,47.33,{"v":5e-124,"d":"5.00E-124"},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",4,377,379,2,375,375]
[null,"BN873v1_590034","_","Candidatus Competibacter denitrificans Run_A_D11","_","putative acyl-CoA dehydrogenase","_",0.97098,0.97098,48.37,{"v":3E-122,"d":"3.00E-122"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.8.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",6,373,379,4,371,379]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.98681,0.99468,46.52,{"v":1e-121,"d":"1.00E-121"},1,1,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",8,377,379,6,375,376]
[null,"MGMSRv2_0193","_","Magnetospirillum gryphiswaldense MSR-1 v2","_","Acyl-CoA dehydrogenase","_",0.97895,0.98153,47.85,{"v":1e-120,"d":"1.00E-120"},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",6,377,379,4,375,380]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.98681,0.99468,45.45,{"v":7e-120,"d":"7.00E-120"},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)",8,377,379,6,375,376]
[null,"CMR15v5_mp0941","_","Ralstonia solanacearum CMR15","_","putative Butyryl-CoA dehydrogenase","_",0.97625,0.98143,48.38,{"v":3e-116,"d":"3.00E-116"},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",5,374,379,5,374,377]
[null,"RALSYv5_mp0315","_","Ralstonia syzygii R24","_","putative Butyryl-CoA dehydrogenase","_",0.97625,0.98143,48.38,{"v":5e-116,"d":"5.00E-116"},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",5,374,379,5,374,377]
[null,"CMR15v5_0672",null,"Ralstonia solanacearum CMR15","_","putative acyl CoA dehydrogenase oxidoreductase protein","_",0.98681,0.99468,44.65,{"v":2e-115,"d":"2.00E-115"},1,1,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",8,377,379,6,375,376]
[null,"RSK60v3_mp750032","_","Ralstonia solanacearum K60","_","putative Butyryl-CoA dehydrogenase","_",0.97625,0.98143,48.65,{"v":2e-115,"d":"2.00E-115"},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",5,374,379,5,374,377]
[null,"BN43v3_60289","_","Mycobacterium canettii STB-L","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.97172,0.99736,46.83,{"v":2E-109,"d":"2.00E-109"},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,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.98153,0.992,43.82,{"v":2E-109,"d":"2.00E-109"},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",6,377,379,4,375,375]
[null,"RALTA_B1110","_","Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.9657,0.99728,46.99,{"v":1E-107,"d":"1.00E-107"},1,1,"1 : Metabolism ;","1.3.99.-","2 : Cytoplasmic","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",12,377,379,2,367,367]
[null,"MARHY1166","_","Marinobacter hydrocarbonoclasticus ATCC 49840","ivdA","Isovaleryl-coenzyme A dehydrogenase","_",0.97165,0.99472,42.71,{"v":2E-107,"d":"2.00E-107"},1,1,"1.1.3 : Amino acids ;","1.3.99.10","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",14612443,"2a : Function from experimental evidences in other organisms",1,377,379,8,384,388]
[null,"LEPBIa0057","_","Leptospira biflexa serovar Patoc Patoc 1","acdA2","Acyl-CoA dehydrogenase","_",0.96392,0.98681,44.65,{"v":8E-107,"d":"8.00E-107"},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,"BN12v2_560002","_","Tetrasphaera japonica T1-X7","_","Acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.97638,0.98153,44.35,{"v":4e-106,"d":"4.00E-106"},1,1,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",6,377,379,9,377,381]
[null,"AZOLI_p40074","_","Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.98425,0.98945,45.33,{"v":4e-105,"d":"4.00E-105"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.-","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,374,379,1,373,381]
[null,"RM41v1_pld1500078","_","Sinorhizobium sp. Rm41","_","acyl-CoA dehydrogenase","_",0.99737,1,44.06,{"v":1e-104,"d":"1.00E-104"},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,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,378,379,1,377,380]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.97179,1,40.63,{"v":2e-104,"d":"2.00E-104"},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,"VIBNIv4_A0948","_","Vibrio nigripulchritudo SFn1","ACAD8","Isobutyryl-CoA dehydrogenase","_",0.98958,1.00264,44.47,{"v":3E-103,"d":"3.00E-103"},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,"BRADO1447","_","Bradyrhizobium sp. ORS278","ivd2","isovaleryl-CoA dehydrogenase","_",0.9641,0.99208,41.49,{"v":2e-102,"d":"2.00E-102"},1,1,"1.1.3.12 : Leucine degradation ;","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,377,379,10,385,390]
[null,"BN13v1_350002","_","Tetrasphaera jenkinsii Ben74","_","Acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.97922,0.99472,42.71,{"v":1E-100,"d":"1.00E-100"},1,1,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",6,378,379,9,383,385]
[null,"lpg1824","_","Legionella pneumophila subsp. pneumophila Philadelphia 1","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.97429,1,41.42,{"v":2E-100,"d":"2.00E-100"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,8,386,389]
[null,"lpp1787","_","Legionella pneumophila Paris","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.97429,1,41.42,{"v":2E-100,"d":"2.00E-100"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,8,386,389]
[null,"LPVv2_2096","_","Legionella pneumophila subsp. pneumophila HL06041035","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.98187,1,41.42,{"v":2E-100,"d":"2.00E-100"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,5,383,386]
[null,"LPOv2_1885","_","Legionella pneumophila subsp. pneumophila Lorraine","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.98187,1,41.42,{"v":2E-100,"d":"2.00E-100"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,5,383,386]
[null,"LPC_1268","_","Legionella pneumophila Corby","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.98187,1,41.42,{"v":2E-100,"d":"2.00E-100"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,5,383,386]
[null,"lpl1788","_","Legionella pneumophila Lens","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.97429,1,41.16,{"v":8e-100,"d":"8.00E-100"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,379,8,386,389]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.97201,1.00792,40.84,{"v":2e-96,"d":"2.00E-96"},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,"RALTA_A0110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL-COA DEHYDROGENASE OXIDOREDUCTASE","_",0.97201,1.00792,40.05,{"v":3e-96,"d":"3.00E-96"},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,"VIBNIv4_B0452","_","Vibrio nigripulchritudo SFn1","_","putative Acyl-CoA dehydrogenase","_",0.96632,0.98417,42.9,{"v":4e-96,"d":"4.00E-96"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",7,379,379,10,381,386]
[null,"THI_3281",null,"Thiomonas sp. 3As","ivd","Isovaleryl-CoA dehydrogenase","_",0.97449,1.00792,40.58,{"v":6e-96,"d":"6.00E-96"},2,1,"1.1.3.12 : Leucine degradation ;","1.3.99.10","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","10677295, 12477932, 12665801, 1310317, 2318964, 7640268, 8468053, 921428","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,377,379,6,387,392]
[null,"CMR15v5_0667",null,"Ralstonia solanacearum CMR15","_","putative acyl-CoA dehydrogenase oxidoreductase","_",0.97201,1.00792,38.48,{"v":2e-94,"d":"2.00E-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,"SCFA_v1_1630002","_","Ca. Propionivorax syntrophicum F70","acdB","Acyl-CoA dehydrogenase, short-chain specific","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47196 ; RHEA:24004 ;",0.96429,0.99736,40.48,{"v":7e-87,"d":"7.00E-87"},1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,379,379,16,391,392]
[null,"Rmet_5024","_","Cupriavidus metallidurans CH34","_","putative acyl-CoA dehydrogenase oxidoreductase protein","_",0.98417,0.98417,37.27,{"v":4e-82,"d":"4.00E-82"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ; 1.4 : Energy production/transport ; 1.5.4 : Fatty acid and phosphatidic acid ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,377,379,8,379,379]
[null,"LEPBIa1112",null,"Leptospira biflexa serovar Patoc Patoc 1","_","Acyl-CoA dehydrogenase","_",0.7271,1.00528,39.9,{"v":3e-81,"d":"3.00E-81"},3,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.8.1","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,374,379,6,383,524]
[null,"RALTA_B1742",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.94221,0.98945,40.27,{"v":8e-80,"d":"8.00E-80"},4,1,"1.4 : Energy production/transport ;","1.3.99.-","2 : Cytoplasmic","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",12,378,379,2,373,398]
[null,"NBG4_v1_200003","_","Candidatus Sulfobium mesophilum","acdA","Acyl-CoA dehydrogenase","RHEA:47196 ; RHEA:24004 ;",0.95373,0.97889,39.62,{"v":4E-78,"d":"4.00E-78"},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",6,374,379,18,382,389]
[null,"BN381v2_80083","_","Candidatus Microthrix parvicella RN1","_","putative acyl-CoA dehydrogenase","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; LONG-CHAIN-ACYL-COA-DEHYDROGENASE-RXN ;",0.98168,0.98945,35.73,{"v":1e-77,"d":"1.00E-77"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.8.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,377,379,6,380,382]
[null,"Rmet_2531",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase (IVDHase)","_",0.98417,0.98417,35.12,{"v":3e-74,"d":"3.00E-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)",5,377,379,8,379,379]
[null,"Rmet_2530",null,"Cupriavidus metallidurans CH34","ivd","isovaleryl-CoA dehydrogenase (IVDHase)","_",0.98417,0.98677,35.39,{"v":3e-72,"d":"3.00E-72"},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)",5,377,379,8,378,378]
[null,"META1_2223","_","Methylobacterium extorquens AM1","mcd","methylsuccinyl-CoA dehydrogenase, putative isobutyryl-CoA dehydrogenase","_",0.69395,1.02902,37.69,{"v":2e-71,"d":"2.00E-71"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","16856937, 17548827","2a : Function from experimental evidences in other organisms",7,379,379,179,561,562]
[null,"METDI3005","_","Methylobacterium extorquens DM4","msd","methylsuccinyl-CoA dehydrogenase","_",0.69395,1.02902,37.44,{"v":3e-70,"d":"3.00E-70"},1,1,"_","1.3.8.4","2 : Cytoplasmic","_","e : enzyme","16856937, 17548827","1c : Function from experimental evidences in the studied genus",7,379,379,179,561,562]
[null,"XDD1v4_1795","_","Xenorhabdus doucetiae FRM16","xcnE","Acyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",0.95822,0.96834,36.51,{"v":7e-69,"d":"7.00E-69"},1,1,"_","1.3.8.1","1 : Unknown","_","e : enzyme","16349198, 1955881","2a : Function from experimental evidences in other organisms",15,379,379,12,373,383]
[null,"XNC1_1707","_","Xenorhabdus nematophila ATCC19061","xcnE","Acyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",0.95822,0.96834,36.51,{"v":8e-69,"d":"8.00E-69"},1,1,"_","1.3.99.2","1 : Unknown","_","e : enzyme","16349198, 1955881","1a : Function from experimental evidences in the studied strain",15,379,379,12,373,383]
[null,"Rmet_6103","_","Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase-like protein (fragment)","_",0.55409,0.98131,36.19,{"v":3e-36,"d":"3.00E-36"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",171,379,379,3,210,214]
[]
["ACT01_10950","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_0135",null,"Clostridiales BL-6","bcd","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47199 ;",1,1.01055,62.66,{"v":2E-160,"d":"2.00E-160"},1,1,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","2a : Function from experimental evidences in other organisms",1,383,383,1,379,379]
[null,"CD630_10540",null,"Clostridium difficile 630","bcd2","Butyryl-CoA dehydrogenase","_",0.99217,1.00529,61.32,{"v":8e-153,"d":"8.00E-153"},1,2,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",5,383,383,3,378,378]
[null,"CLOSTRIBL3_v1_20310",null,"Clostridiaceae BL-3","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24004 ;",1,1.01055,60.05,{"v":6E-152,"d":"6.00E-152"},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",1,383,383,1,379,379]
[null,"CLOSTRIBL6_v1_3216",null,"Clostridiales BL-6","bud","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; RHEA:47199 ;",0.99478,1.00263,55.38,{"v":9e-140,"d":"9.00E-140"},4,2,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","2a : Function from experimental evidences in other organisms",1,381,383,1,377,380]
[null,"CLOSTRIBL4_v1_2140","_","Clostridiales BL-4","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47196 ;",0.60063,0.99739,57.07,{"v":4e-138,"d":"4.00E-138"},1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286, 8399220, 7857927","2a : Function from experimental evidences in other organisms",1,382,383,1,378,636]
[null,"CLOSTRIBL4_v1_1870",null,"Clostridiales BL-4","bcd","butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24007 ;",1.0026,1.00783,54.66,{"v":2E-137,"d":"2.00E-137"},2,2,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","2a : Function from experimental evidences in other organisms",1,381,383,1,382,385]
[null,"CD630_03990",null,"Clostridium difficile 630","acdB","Acyl-CoA dehydrogenase, short-chain specific","_",0.98695,1.00265,53.7,{"v":1e-126,"d":"1.00E-126"},2,1,"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",6,383,383,4,377,377]
[null,"CD630_08030",null,"Clostridium difficile 630","_","Putative acyl-CoA dehydrogenase","_",1.00261,1.01053,50.52,{"v":7e-119,"d":"7.00E-119"},3,2,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,382,383,1,379,380]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.953,0.96817,45.21,{"v":3e-111,"d":"3.00E-111"},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",19,383,383,17,377,377]
[null,"BN45v3_60311","_","Mycobacterium canettii STB-J","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.98201,0.99739,49.48,{"v":3e-110,"d":"3.00E-110"},1,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","10510226, 12775759, 15525680","3 : Putative function from multiple computational evidences",3,383,383,13,389,389]
[null,"BN44v3_70065","_","Mycobacterium canettii STB-D","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.98201,0.99739,49.48,{"v":3e-110,"d":"3.00E-110"},1,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","10510226, 12775759, 15525680","3 : Putative function from multiple computational evidences",3,383,383,13,389,389]
[null,"BN42v3_41331","_","Mycobacterium canettii STB-K","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.98201,0.99739,49.48,{"v":3e-110,"d":"3.00E-110"},1,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","10510226, 12775759, 15525680","3 : Putative function from multiple computational evidences",3,383,383,13,389,389]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.953,0.97074,45.75,{"v":1E-107,"d":"1.00E-107"},1,2,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",9,373,383,7,367,376]
[null,"CLOSTRIBL3_v1_10853",null,"Clostridiaceae BL-3","carC","Caffeyl-CoA reductase-Etf complex subunit CarC","RHEA:46956 ;",0.99217,1.00264,47.37,{"v":2E-107,"d":"2.00E-107"},4,2,"_","1.3.1.108","2 : Cytoplasmic","_","e : enzyme",23479729,"2a : Function from experimental evidences in other organisms",5,383,383,3,378,379]
[null,"SCFA_v1_1080002",null,"Ca. Phosphitivorax butyraticus R76","acdA","Acyl-CoA dehydrogenase","_",0.9765,0.9765,45.72,{"v":2e-106,"d":"2.00E-106"},3,2,"_","1.3.8.-","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",10,382,383,10,379,383]
[null,"SCFA_v1_500014",null,"Ca. Phosphitivorax anaerolimi F81","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.9765,0.9765,44.92,{"v":5e-106,"d":"5.00E-106"},2,2,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",10,382,383,10,379,383]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.953,0.97074,44.38,{"v":4e-103,"d":"4.00E-103"},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)",9,373,383,7,367,376]
[null,"CMR15v5_0672",null,"Ralstonia solanacearum CMR15","_","putative acyl CoA dehydrogenase oxidoreductase protein","_",0.953,0.97074,44.11,{"v":2e-101,"d":"2.00E-101"},1,2,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",9,373,383,7,367,376]
[null,"CLOSTRIBL3_v1_12012",null,"Clostridiaceae BL-3","carC","Caffeyl-CoA reductase-Etf complex subunit CarC","RHEA:46956 ;",0.97389,0.98158,45.31,{"v":8e-100,"d":"8.00E-100"},5,4,"_","1.3.1.108","2 : Cytoplasmic","_","e : enzyme",23479729,"2a : Function from experimental evidences in other organisms",9,381,383,9,375,380]
[null,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.97128,0.992,43.55,{"v":2E-95,"d":"2.00E-95"},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",5,376,383,3,370,375]
[null,"MARHY1166",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","ivdA","Isovaleryl-coenzyme A dehydrogenase","_",0.96907,0.98172,40.16,{"v":4e-88,"d":"4.00E-88"},2,2,"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",1,376,383,8,379,388]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.98205,1,37.6,{"v":2e-86,"d":"2.00E-86"},2,2,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,383,383,9,387,390]
[null,"BRADO1447",null,"Bradyrhizobium sp. ORS278","ivd2","isovaleryl-CoA dehydrogenase","_",0.96154,0.97911,38.93,{"v":6e-85,"d":"6.00E-85"},1,2,"1.1.3.12 : Leucine degradation ;","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,376,383,10,380,390]
[null,"VIBNIv4_B0452",null,"Vibrio nigripulchritudo SFn1","_","putative Acyl-CoA dehydrogenase","_",0.97668,0.98433,39.52,{"v":3e-81,"d":"3.00E-81"},1,2,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",7,383,383,10,381,386]
[null,"THI_3281",null,"Thiomonas sp. 3As","ivd","Isovaleryl-CoA dehydrogenase","_",0.97194,0.99478,38.06,{"v":1e-80,"d":"1.00E-80"},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)",1,376,383,6,382,392]
[null,"RALTA_A0110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL-COA DEHYDROGENASE OXIDOREDUCTASE","_",0.96183,0.98695,37.83,{"v":2e-76,"d":"2.00E-76"},3,2,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",7,376,383,10,383,393]
[null,"LEPBIa1138",null,"Leptospira biflexa serovar Patoc Patoc 1","_","Putative acyl-CoA dehydrogenase, short-chain specific (SCAD) (Butyryl-CoA dehydrogenase)","_",0.91117,0.93734,38.16,{"v":3e-76,"d":"3.00E-76"},4,2,"_","1.3.8.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",14,371,383,25,378,394]
[null,"CMR15v5_0667",null,"Ralstonia solanacearum CMR15","_","putative acyl-CoA dehydrogenase oxidoreductase","_",0.96183,0.98695,37.04,{"v":5e-76,"d":"5.00E-76"},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",7,376,383,10,383,393]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.96183,0.98695,37.57,{"v":2e-75,"d":"2.00E-75"},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",7,376,383,10,383,393]
[null,"MARHY1169",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","fadE","long chain acyl coenzyme A dehydrogenase","_",0.85379,0.85602,40.06,{"v":4e-74,"d":"4.00E-74"},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)",48,372,383,48,370,382]
[null,"BN11v3_2390004",null,"Tetrasphaera australiensis Ben110","_","Putative Acyl-CoA dehydrogenase (Butyryl-CoA dehydrogenase)","_",0.89688,0.9765,37.43,{"v":4E-73,"d":"4.00E-73"},5,2,"_","1.3.99.-","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,373,383,34,401,417]
[null,"SCFA_v1_1630002",null,"Ca. Propionivorax syntrophicum F70","acdB","Acyl-CoA dehydrogenase, short-chain specific","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47196 ; RHEA:24004 ;",0.97449,0.99739,36.13,{"v":1e-68,"d":"1.00E-68"},1,3,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,383,383,16,391,392]
[null,"Rmet_2530",null,"Cupriavidus metallidurans CH34","ivd","isovaleryl-CoA dehydrogenase (IVDHase)","_",0.8329,0.84392,40.13,{"v":1e-67,"d":"1.00E-67"},5,2,"1.1.1 : Carbohydrates/Carbon compounds ;","1.3.99.10","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",57,372,383,59,369,378]
[null,"Rmet_2531",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase (IVDHase)","_",0.93995,0.94987,37.22,{"v":4e-62,"d":"4.00E-62"},6,2,"1.1.1 : Carbohydrates/Carbon compounds ;","1.3.99.10","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",19,372,383,22,370,379]
[null,"BRADO1442",null,"Bradyrhizobium sp. ORS278","_","acyl-CoA dehydrogenase","_",0.8634,0.87467,36.12,{"v":2E-55,"d":"2.00E-55"},5,2,"1.1.3.12 : Leucine degradation ;","1.3.99.10","2 : Cytoplasmic","_","e : enzyme",9535763,"2a : Function from experimental evidences in other organisms",42,365,383,43,365,388]
[null,"MGMSRv2_1553",null,"Magnetospirillum gryphiswaldense MSR-1 v2","_","putative Acyl-CoA dehydrogenase","_",0.63185,0.96345,35.77,{"v":1e-47,"d":"1.00E-47"},6,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.-","1 : Unknown","15.7 : Sporulation and germination ;","e : enzyme","8759838, 19383706","3 : Putative function from multiple computational evidences",45,373,383,83,444,584]
[]
["ACT01_09515","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_3217",null,"Clostridiales BL-6","etfA","Electron transfer flavoprotein subunit alpha","_",0.99701,0.99701,41.14,{"v":3e-81,"d":"3.00E-81"},1,2,"_","_","2 : Cytoplasmic","_","e : enzyme",9694853,"2a : Function from experimental evidences in other organisms",3,330,334,4,331,334]
[null,"SBF1_v1_550002",null,"Desulfosporosinus sp. SbF1","etfA","electron-transferring flavoprotein, alpha subunit EtfA","_",0.98503,1.00305,37.69,{"v":3e-71,"d":"3.00E-71"},1,2,"_","_","2 : Cytoplasmic","_","c : carrier",23468890,"2a : Function from experimental evidences in other organisms",7,331,334,5,326,328]
[null,"AZOLI_0536",null,"Azospirillum lipoferum 4B","fixB","electron transfer flavoprotein alpha chain","_",0.89972,0.96707,37.77,{"v":7e-70,"d":"7.00E-70"},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",6,324,334,23,344,359]
[null,"MGMSRv2_1064",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.90437,0.99102,37.76,{"v":4e-69,"d":"4.00E-69"},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)",5,330,334,29,357,366]
[null,"CLOSTRIBL3_v1_20312",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.97904,0.98198,36.09,{"v":1e-68,"d":"1.00E-68"},2,2,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","c : carrier","17189250, 20059546, 21398533, 8655474, 11466286","2a : Function from experimental evidences in other organisms",7,332,334,9,333,333]
[null,"RM41v1_psym670029",null,"Sinorhizobium sp. Rm41","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.93768,0.99102,36.86,{"v":5e-68,"d":"5.00E-68"},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",6,330,334,14,341,353]
[null,"SBF1_v1_470014",null,"Desulfosporosinus sp. SbF1","fixB","electron-transferring flavoprotein, subunit FixB","_",0.73363,0.97305,36,{"v":2e-67,"d":"2.00E-67"},2,2,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,330,334,113,435,443]
[null,"MGMSRv2_0361",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","Electron transfer flavoprotein, alpha subunit","_",0.89402,0.98503,36.78,{"v":1e-65,"d":"1.00E-65"},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",6,330,334,33,359,368]
[null,"CLOSTRIBL3_v1_11487",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.98802,1.0061,38.18,{"v":2e-65,"d":"2.00E-65"},4,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,329,334,1,323,328]
[null,"CLOSTRIBL3_v1_20125",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.98802,0.99099,35.45,{"v":7e-64,"d":"7.00E-64"},5,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",7,334,334,4,331,333]
[null,"BRADO5385",null,"Bradyrhizobium sp. ORS278","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.88043,0.97006,37.04,{"v":5e-63,"d":"5.00E-63"},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)",6,324,334,30,350,368]
[null,"CD630_10560",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.98214,0.98802,35.15,{"v":2e-60,"d":"2.00E-60"},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",6,334,334,3,330,336]
[null,"CLOSTRIBL6_v1_2820",null,"Clostridiales BL-6","etfA","Electron transfer flavoprotein subunit alpha","_",0.98503,1.00305,35.56,{"v":5e-55,"d":"5.00E-55"},3,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",7,334,334,8,328,328]
[null,"SCFA_v1_1630004",null,"Ca. Propionivorax syntrophicum F70","FixB","Electron transfer flavoprotein, alpha subunit (partial)","_",0.13772,0.83636,43.48,0.0003,1,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,50,334,7,52,55]
[]
["ACT01_09520","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_470015",null,"Desulfosporosinus sp. SbF1","fixA","electron-transferring flavoprotein, subunit FixA","_",0.88448,0.9387,41.63,{"v":8e-59,"d":"8.00E-59"},1,2,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,241,261,1,245,277]
[null,"CLOSTRIBL3_v1_20311",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1,1.00772,39.08,{"v":8e-58,"d":"8.00E-58"},3,2,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286, 9694853","2a : Function from experimental evidences in other organisms",1,261,261,1,259,259]
[null,"SCFA_v1_1630003",null,"Ca. Propionivorax syntrophicum F70","FixA","Electron transfer flavoproteins subunit beta","_",0.9697,0.98084,39.84,{"v":8E-55,"d":"8.00E-55"},1,2,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,253,261,1,255,264]
[null,"CD630_10550",null,"Clostridium difficile 630","etfB","Electron transfer flavoproteins subunit beta","_",0.93585,0.95019,37.9,{"v":5e-54,"d":"5.00E-54"},2,2,"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",1,247,261,6,252,265]
[null,"CLOSTRIBL3_v1_20124",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.96604,0.98084,36.72,{"v":4e-53,"d":"4.00E-53"},4,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,255,261,1,255,265]
[null,"BN11v3_3200005","_","Tetrasphaera australiensis Ben110","etfB","Electron transfer flavoprotein subunit beta","_",1.00758,1.01916,39.1,{"v":4e-53,"d":"4.00E-53"},1,1,"_","_","2 : Cytoplasmic","6.5 : Electron transport ;","e : enzyme","10026281, 9694853","2a : Function from experimental evidences in other organisms",1,261,261,5,264,264]
[null,"MGMSRv2_0362",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","Electron transfer flavoprotein, beta-subunit","_",0.85211,0.9272,40.91,{"v":7e-53,"d":"7.00E-53"},1,2,"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",1,234,261,1,242,284]
[null,"AZOLI_0535",null,"Azospirillum lipoferum 4B","fixA","electron transfer flavoprotein beta subunit","_",0.84806,0.91954,40,{"v":9e-53,"d":"9.00E-53"},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",1,234,261,1,240,283]
[null,"CLOSTRIBL3_v1_11488",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.99623,1.01149,39.02,{"v":1E-52,"d":"1.00E-52"},5,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,261,261,1,264,265]
[null,"BRADO5386",null,"Bradyrhizobium sp. ORS278","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.86121,0.9272,39.67,{"v":2E-52,"d":"2.00E-52"},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)",1,234,261,1,242,281]
[null,"MGMSRv2_1063",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.96403,1.02682,38.43,{"v":2E-52,"d":"2.00E-52"},2,2,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,258,261,1,268,278]
[null,"CLOSTRIBL6_v1_3218",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein subunit beta","_",0.96269,0.98851,37.21,{"v":3e-50,"d":"3.00E-50"},2,2,"_","_","2 : Cytoplasmic","_","e : enzyme",9694853,"2a : Function from experimental evidences in other organisms",1,251,261,1,258,268]
[null,"BN42v3_41032","_","Mycobacterium canettii STB-K","fixA","Putative electron transfer flavoprotein (beta-subunit) FixA (beta-ETF) (electron transfer flavoprotein small subunit) (ETFSS)","_",0.97719,0.98467,37.74,{"v":4e-46,"d":"4.00E-46"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,253,261,3,259,263]
[null,"CLOSTRIBL6_v1_2821",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein, beta subunit","_",1.02256,1.04215,36.4,{"v":5e-46,"d":"5.00E-46"},3,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,261,261,1,266,266]
[null,"RM41v1_psym670028",null,"Sinorhizobium sp. Rm41","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.81507,0.91188,37.39,{"v":6e-46,"d":"6.00E-46"},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)",1,230,261,1,238,292]
[null,"BN45v3_60006","_","Mycobacterium canettii STB-J","fixA","Putative electron transfer flavoprotein (beta-subunit) FixA (beta-ETF) (electron transfer flavoprotein small subunit) (ETFSS)","_",0.97744,0.99617,36.92,{"v":8e-45,"d":"8.00E-45"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,253,261,3,262,266]
[null,"BN44v3_60523","_","Mycobacterium canettii STB-D","fixA","Putative electron transfer flavoprotein (beta-subunit) FixA (beta-ETF) (electron transfer flavoprotein small subunit) (ETFSS)","_",0.97744,0.99617,36.92,{"v":8e-45,"d":"8.00E-45"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,253,261,3,262,266]
[null,"BN43v3_60008","_","Mycobacterium canettii STB-L","fixA","Putative electron transfer flavoprotein (beta-subunit) FixA (beta-ETF) (electron transfer flavoprotein small subunit) (ETFSS)","_",0.97744,0.99617,36.92,{"v":8e-45,"d":"8.00E-45"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,253,261,3,262,266]
[null,"CLOSTRIBL4_v1_1871",null,"Clostridiales BL-4","etfB","Electron transfer flavoprotein subunit beta","_",1.00376,1.02299,35.58,{"v":8e-45,"d":"8.00E-45"},1,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,261,261,1,266,266]
[null,"SBF1_v1_550001",null,"Desulfosporosinus sp. SbF1","etfB","electron-transferring flavoprotein, beta subunit EtfB","_",0.95019,0.96498,35.89,{"v":5e-39,"d":"5.00E-39"},3,1,"_","_","2 : Cytoplasmic","_","c : carrier",23468890,"2a : Function from experimental evidences in other organisms",1,247,261,1,243,257]
[null,"MAGMOv5_4038","_","Magnetotactic ovoidal bacterium MO-1","etfB","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.81992,0.8629,35.05,{"v":4e-30,"d":"4.00E-30"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier",8599534,"2a : Function from experimental evidences in other organisms",1,212,261,1,211,248]
[]
["ACT01_10940","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","_",0.99701,1.003,57.49,{"v":2e-129,"d":"2.00E-129"},1,1,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","c : carrier","17189250, 20059546, 21398533, 8655474, 11466286","2a : Function from experimental evidences in other organisms",1,334,335,1,333,333]
[null,"CLOSTRIBL3_v1_12010",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.99702,1,53.73,{"v":4e-126,"d":"4.00E-126"},2,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,334,335,1,334,336]
[null,"CD630_04010",null,"Clostridium difficile 630","etfA1","Alpha-subunit of electron transfer flavoprotein","_",0.96232,0.99104,57.53,{"v":4E-125,"d":"4.00E-125"},1,1,"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",2,333,335,6,336,345]
[null,"CLOSTRIBL6_v1_0137",null,"Clostridiales BL-6","etfA","electron transfer flavoprotein (alpha subunit)","_",0.95954,0.99104,54.52,{"v":6e-122,"d":"6.00E-122"},1,1,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 20059546, 21398533","2a : Function from experimental evidences in other organisms",1,332,335,8,338,346]
[null,"CD630_08050",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein alpha-subunit","_",0.97647,0.99104,49.1,{"v":6e-113,"d":"6.00E-113"},2,1,"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",1,332,335,10,340,340]
[null,"CLOSTRIBL6_v1_3217",null,"Clostridiales BL-6","etfA","Electron transfer flavoprotein subunit alpha","_",0.98507,0.98802,52.73,{"v":7e-112,"d":"7.00E-112"},2,1,"_","_","2 : Cytoplasmic","_","e : enzyme",9694853,"2a : Function from experimental evidences in other organisms",7,334,335,6,333,334]
[null,"CLOSTRIBL4_v1_1872",null,"Clostridiales BL-4","etfA","Electron transfer flavoprotein subunit alpha","_",0.97283,1.06866,49.16,{"v":5e-106,"d":"5.00E-106"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",2,334,335,8,365,368]
[null,"CD630_10560",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.97024,0.97313,48.77,{"v":7e-103,"d":"7.00E-103"},3,1,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",9,334,335,4,328,336]
[null,"SBF1_v1_470014",null,"Desulfosporosinus sp. SbF1","fixB","electron-transferring flavoprotein, subunit FixB","_",0.73815,0.97612,47.4,{"v":1e-98,"d":"1.00E-98"},1,1,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,332,335,110,435,443]
[null,"pRALTA_0380",null,"Cupriavidus taiwanensis LMG19424","fixB","Electron transfer flavoprotein, alpha subunit","_",0.88267,0.98806,46.53,{"v":6E-98,"d":"6.00E-98"},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",3,329,335,29,358,375]
[null,"BURPHP2_0598",null,"Burkholderia phymatum STM815","fixB","Protein fixB, Electron transfer flavoprotein, alpha subunit","_",0.88503,0.98806,45.92,{"v":2e-96,"d":"2.00E-96"},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",3,329,335,29,358,374]
[null,"CLOSTRIBL3_v1_20125",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.98209,0.98799,46.5,{"v":2E-95,"d":"2.00E-95"},4,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",7,334,335,2,329,333]
[null,"MGMSRv2_1064",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.91803,1.00299,44.05,{"v":3e-92,"d":"3.00E-92"},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)",2,332,335,24,357,366]
[null,"AZOLI_0536",null,"Azospirillum lipoferum 4B","fixB","electron transfer flavoprotein alpha chain","_",0.92201,0.98806,46.53,{"v":2e-89,"d":"2.00E-89"},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",3,329,335,18,347,359]
[null,"MGMSRv2_0361",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","Electron transfer flavoprotein, alpha subunit","_",0.90217,0.99104,43.07,{"v":9e-89,"d":"9.00E-89"},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",5,332,335,30,359,368]
[null,"CLOSTRIBL3_v1_11487",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.9791,1,47.56,{"v":1E-87,"d":"1.00E-87"},5,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",5,331,335,4,323,328]
[null,"BSU28520",null,"Bacillus subtilis 168","etfA","electron transfer flavoprotein (alpha subunit)","_",0.98209,1.01231,44.98,{"v":3e-87,"d":"3.00E-87"},1,1,"1.4 : Membrane bioenergetics (electron transport chain and ATP synthase) ;","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 20059546, 21398533","1a : Function from experimental evidences in the studied strain",7,333,335,3,321,325]
[null,"CLOSTRIBL3_v1_11114",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.83911,1.01194,41.3,{"v":6e-85,"d":"6.00E-85"},6,1,"_","_","2 : Cytoplasmic","_","c : carrier",17189250,"2a : Function from experimental evidences in other organisms",1,335,335,66,399,404]
[null,"BRADO5385",null,"Bradyrhizobium sp. ORS278","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.89674,0.98507,42.73,{"v":1e-82,"d":"1.00E-82"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",6,331,335,28,355,368]
[null,"SBF1_v1_6700004",null,"Desulfosporosinus sp. SbF1","etfA_2","electron-transferring flavoprotein, alpha subunit EtfA (lutD-associated)","_",0.82836,0.99403,42.64,{"v":1e-81,"d":"1.00E-81"},3,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,331,335,66,393,402]
[null,"CD630_11720",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.81281,0.98507,40,{"v":3e-80,"d":"3.00E-80"},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",5,334,335,68,394,406]
[null,"SCFA_v1_130009",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",0.98806,1.02795,45.32,{"v":9e-79,"d":"9.00E-79"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,335,335,3,322,322]
[null,"RM41v1_psym670029",null,"Sinorhizobium sp. Rm41","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.94334,0.99403,39.34,{"v":2e-76,"d":"2.00E-76"},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",5,332,335,11,341,353]
[null,"CLOSTRIBL6_v1_2820",null,"Clostridiales BL-6","etfA","Electron transfer flavoprotein subunit alpha","_",0.98209,1.00305,43.77,{"v":2e-74,"d":"2.00E-74"},3,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",7,334,335,6,326,328]
[null,"LEPBIa1132",null,"Leptospira biflexa serovar Patoc Patoc 1","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.97612,1.02508,43.12,{"v":2e-74,"d":"2.00E-74"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","16.10 : Respire ;","c : carrier","_","2a : Function from experimental evidences in other organisms",9,335,335,4,319,319]
[null,"SCFA_v1_500012",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",0.97313,0.97898,40.18,{"v":1e-72,"d":"1.00E-72"},2,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,332,335,6,329,333]
[null,"SCFA_v1_2400007","_","Ca. Phosphitivorax butyraticus R76","etfA","Electron transfer flavoprotein subunit alpha","_",0.98806,0.99399,40.18,{"v":2e-71,"d":"2.00E-71"},1,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,332,335,1,329,333]
[null,"FRAAL5877",null,"Frankia alni ACN14a","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.9791,1.025,40.85,{"v":8e-63,"d":"8.00E-63"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","16.1 : Circulate ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,334,335,4,318,320]
[null,"BN45v3_60005","_","Mycobacterium canettii STB-J","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97612,1.0283,38.84,{"v":3e-60,"d":"3.00E-60"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",9,335,335,4,318,318]
[null,"BN44v3_60522","_","Mycobacterium canettii STB-D","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97612,1.0283,38.84,{"v":3e-60,"d":"3.00E-60"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",9,335,335,4,318,318]
[null,"BN43v3_60007","_","Mycobacterium canettii STB-L","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97612,1.0283,38.84,{"v":3e-60,"d":"3.00E-60"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",9,335,335,4,318,318]
[null,"BN42v3_41031","_","Mycobacterium canettii STB-K","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97612,1.0283,38.84,{"v":4e-60,"d":"4.00E-60"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",9,335,335,4,318,318]
[null,"BN11v3_3200004","_","Tetrasphaera australiensis Ben110","etfA","Electron transfer flavoprotein subunit alpha","_",0.9791,1.03145,35.98,{"v":5E-56,"d":"5.00E-56"},1,1,"_","_","1 : Unknown","6.5 : Electron transport ;","e : enzyme","10026281, 9694853","2a : Function from experimental evidences in other organisms",9,335,335,4,318,318]
[null,"MARHY1802",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","etfA","electron transfer flavoprotein alpha-subunit","_",0.97313,1.04153,36.5,{"v":9e-56,"d":"9.00E-56"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6 : Energy metabolism ;","c : carrier",3415685,"2a : Function from experimental evidences in other organisms",9,333,335,3,312,313]
[null,"AZOLI_p50300","_","Azospirillum lipoferum 4B","etfA2","Electron transfer flavoprotein alpha-subunit","_",0.95522,1.02564,39.69,{"v":2E-55,"d":"2.00E-55"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier","10984043, 16159782, 8599534","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,327,335,4,308,312]
[null,"BURPHK2_1883","_","Burkholderia phymatum STM815","etfA","electron transfer flavoprotein, alpha subunit","_",0.98507,1.05769,37.27,{"v":4e-54,"d":"4.00E-54"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","4 : Biosynthesis of cofactors, prosthetic groups, and carriers ;","c : carrier",10026281,"2a : Function from experimental evidences in other organisms",9,331,335,3,311,312]
[null,"AZOLI_0089",null,"Azospirillum lipoferum 4B","etfA3","Electron transfer flavoprotein alpha-subunit","_",0.88657,0.96429,37.37,{"v":5E-52,"d":"5.00E-52"},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)",35,330,335,25,308,308]
[null,"CMR15v5_3436","_","Ralstonia solanacearum CMR15","etfA","Electron transfer flavoprotein, alpha-subunit","_",0.89254,0.96141,39.8,{"v":1e-48,"d":"1.00E-48"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",39,330,335,29,310,311]
[null,"PSHAa1617",null,"Pseudoalteromonas haloplanktis TAC125","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.95821,1.04221,35.51,{"v":2e-48,"d":"2.00E-48"},1,1,"2.5.4 : Menaquinone and ubiquinone ;","_","unknown","_","u : unknown",8599534,"2a : Function from experimental evidences in other organisms",11,330,335,5,308,308]
[null,"METDI2208",null,"Methylobacterium extorquens DM4","etfA","electron transfer flavoprotein, NAD/FAD-binding domain and ETFP adenine nucleotide-binding domain-like","_",0.96716,1.02208,37.04,{"v":3e-48,"d":"3.00E-48"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","15188393, 16926146, 8599534","2a : Function from experimental evidences in other organisms",14,334,335,8,315,317]
[null,"Rmet_0738","_","Cupriavidus metallidurans CH34","etfA","Electron transfer flavoprotein subunit alpha (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.89254,0.96141,39.13,{"v":4e-48,"d":"4.00E-48"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",39,330,335,29,310,311]
[null,"MGMSRv2_1555",null,"Magnetospirillum gryphiswaldense MSR-1 v2","etfA","electron transfer flavoprotein (alpha subunit)","_",0.95224,1.03571,37.3,{"v":7e-48,"d":"7.00E-48"},4,1,"1.4 : Energy production/transport ; 1.4.3 : Electron carrier ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme",17189250,"2a : Function from experimental evidences in other organisms",9,326,335,3,304,308]
[null,"Mchl_1823","_","Methylobacterium extorquens CM4","etfA","electron transfer flavoprotein alpha subunit","_",0.96716,1.02208,36.73,{"v":1e-47,"d":"1.00E-47"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","15188393, 16926146, 8599534","2a : Function from experimental evidences in other organisms",14,334,335,8,315,317]
[null,"RALTA_A0796","_","Cupriavidus taiwanensis LMG19424","etfA","ELECTRON TRANSFER FLAVOPROTEIN, ALPHA-SUBUNIT","_",0.97313,1.04823,36.2,{"v":1e-47,"d":"1.00E-47"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",11,330,335,5,310,311]
[null,"Rmet_5518","_","Cupriavidus metallidurans CH34","etfA","electron transfer flavoprotein, alpha subunit","_",0.88955,0.96129,37.92,{"v":4e-47,"d":"4.00E-47"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier","10026281, 1576992, 8376381, 8599534","2a : Function from experimental evidences in other organisms",39,330,335,29,310,310]
[null,"HEAR0620",null,"Herminiimonas arsenicoxydans","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.96119,1.04207,37.89,{"v":7e-47,"d":"7.00E-47"},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",11,326,335,5,304,309]
[null,"NT26v4_3414",null,"Rhizobium sp. NT-26","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.90149,0.97735,35.43,{"v":4e-46,"d":"4.00E-46"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",30,330,335,20,309,309]
[null,"BBta_1141",null,"Bradyrhizobium sp. BTAi1","etfA","Electron transfer flavoprotein alpha-subunit","_",0.91045,0.97134,35.41,{"v":2E-45,"d":"2.00E-45"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",30,333,335,20,312,314]
[null,"THI_1679","_","Thiomonas sp. 3As","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF)(Electron transfer flavoprotein large subunit) (ETFLS)","_",0.95821,1.03548,37.38,{"v":2E-45,"d":"2.00E-45"},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",11,330,335,5,310,310]
[null,"BRADO6491",null,"Bradyrhizobium sp. ORS278","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.90746,0.97749,36.51,{"v":5e-45,"d":"5.00E-45"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",30,332,335,20,311,311]
[null,"PSEEN3657",null,"Pseudomonas entomophila L48","etfA","electron transfer flavoprotein alpha-subunit","_",0.6806,0.82609,42.54,{"v":2E-41,"d":"2.00E-41"},1,1,"1.4.3 : Electron carrier ;","_","Unknown","6 : Energy metabolism ;","c : carrier","_","2a : Function from experimental evidences in other organisms",99,326,335,55,272,276]
[null,"SCFA_v1_3390001",null,"Ca. Phosphitivorax butyraticus R76","etfA","putative electron transfer flavoprotein subunit alpha (fragment)","_",0.65075,0.99543,36.7,{"v":2e-29,"d":"2.00E-29"},3,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",8,224,335,10,217,219]
[]
["ACT01_10945","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","_",1.00369,1.03817,52.57,{"v":3e-89,"d":"3.00E-89"},1,1,"1.3 : Energy metabolism (carbon) ;","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,271,271,1,262,262]
[null,"CD630_08040",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein beta-subunit, core","_",1.01107,1.03788,49.64,{"v":3e-82,"d":"3.00E-82"},1,1,"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",1,271,271,1,264,264]
[null,"CLOSTRIBL6_v1_3218",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein subunit beta","_",0.98893,1,48.88,{"v":8e-81,"d":"8.00E-81"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme",9694853,"2a : Function from experimental evidences in other organisms",1,266,271,1,263,268]
[null,"CLOSTRIBL6_v1_0136",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein subunit beta","_",0.97786,1.02317,50.19,{"v":9e-81,"d":"9.00E-81"},2,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,265,271,1,253,259]
[null,"CLOSTRIBL3_v1_20311",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.91144,0.95367,51.82,{"v":4e-80,"d":"4.00E-80"},2,1,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286, 9694853","2a : Function from experimental evidences in other organisms",1,247,271,1,238,259]
[null,"SBF1_v1_470015",null,"Desulfosporosinus sp. SbF1","fixA","electron-transferring flavoprotein, subunit FixA","_",0.97834,1,45.76,{"v":7e-76,"d":"7.00E-76"},1,1,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,271,271,1,266,277]
[null,"AZOLI_0535",null,"Azospirillum lipoferum 4B","fixA","electron transfer flavoprotein beta subunit","_",0.94346,0.98524,47.19,{"v":4e-75,"d":"4.00E-75"},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",1,261,271,1,264,283]
[null,"CD630_04000",null,"Clostridium difficile 630","etfB1","Beta-subunit of electron transfer flavoprotein","_",0.93358,0.96935,49.01,{"v":2e-74,"d":"2.00E-74"},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",1,252,271,1,245,261]
[null,"BRADO5386",null,"Bradyrhizobium sp. ORS278","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.95018,0.98524,45.32,{"v":5e-72,"d":"5.00E-72"},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)",1,265,271,1,263,281]
[null,"CLOSTRIBL4_v1_1871",null,"Clostridiales BL-4","etfB","Electron transfer flavoprotein subunit beta","_",1.01476,1.03383,45.82,{"v":5e-72,"d":"5.00E-72"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,271,271,1,266,266]
[null,"MGMSRv2_0362",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","Electron transfer flavoprotein, beta-subunit","_",0.85563,0.89668,47.33,{"v":2e-71,"d":"2.00E-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",1,241,271,1,241,284]
[null,"CD630_10550",null,"Clostridium difficile 630","etfB","Electron transfer flavoproteins subunit beta","_",1.00369,1.02642,45.22,{"v":2e-69,"d":"2.00E-69"},3,1,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",1,271,271,6,265,265]
[null,"CLOSTRIBL3_v1_20124",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1.00369,1.02642,40.81,{"v":2e-67,"d":"2.00E-67"},4,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,271,271,1,265,265]
[null,"CLOSTRIBL3_v1_11115",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1.00738,1.04198,42.86,{"v":1e-66,"d":"1.00E-66"},5,1,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,271,271,1,262,262]
[null,"BURPHP2_0599",null,"Burkholderia phymatum STM815","fixA","protein fixA, electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.86879,0.90406,44.08,{"v":1e-66,"d":"1.00E-66"},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",1,243,271,1,242,282]
[null,"pRALTA_0381",null,"Cupriavidus taiwanensis LMG19424","fixA","Electron transfer flavoprotein beta-subunit","_",0.96099,1,42.07,{"v":2E-66,"d":"2.00E-66"},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",1,268,271,1,268,282]
[null,"CD630_11710",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein subunit alpha","_",0.98524,1.00755,42.7,{"v":8e-66,"d":"8.00E-66"},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",1,265,271,4,262,265]
[null,"SBF1_v1_6700003",null,"Desulfosporosinus sp. SbF1","etfB_2","electron-transferring flavoprotein, beta subunit EtfB (lutD-associated)","_",0.87823,0.94071,45.38,{"v":1e-64,"d":"1.00E-64"},2,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,236,271,1,230,253]
[null,"MGMSRv2_1063",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.97482,1,40.59,{"v":2e-64,"d":"2.00E-64"},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)",1,268,271,1,268,278]
[null,"RM41v1_psym670028",null,"Sinorhizobium sp. Rm41","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.83904,0.90406,43.27,{"v":4e-61,"d":"4.00E-61"},1,1,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ; 16.15 : Symbiosis ;","c : carrier","15028689, 16453824","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,243,271,1,243,292]
[null,"CLOSTRIBL3_v1_11488",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1.01107,1.03396,39.42,{"v":2e-57,"d":"2.00E-57"},6,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,271,271,1,264,265]
[null,"CLOSTRIBL6_v1_2821",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein, beta subunit","_",1.01476,1.03383,40,{"v":2e-57,"d":"2.00E-57"},3,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,271,271,1,266,266]
[null,"SCFA_v1_1630003",null,"Ca. Propionivorax syntrophicum F70","FixA","Electron transfer flavoproteins subunit beta","_",0.94096,0.96591,39.22,{"v":3e-55,"d":"3.00E-55"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,252,271,1,247,264]
[null,"FRAAL5878",null,"Frankia alni ACN14a","fixA","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",1.00369,1.04215,36.76,{"v":3e-54,"d":"3.00E-54"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","16.1 : Circulate ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,271,271,1,261,261]
[null,"SCFA_v1_500013",null,"Ca. Phosphitivorax anaerolimi F81","etfB","Electron transfer flavoprotein, beta subunit","_",0.90842,0.91513,35.89,{"v":3E-52,"d":"3.00E-52"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,247,271,2,242,273]
[null,"SCFA_v1_130010",null,"Ca. Phosphitivorax anaerolimi F81","etfB","Electron transfer flavoprotein subunit beta","_",0.9262,0.97287,38.65,{"v":1E-42,"d":"1.00E-42"},2,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,251,271,4,239,258]
[null,"SCFA_v1_3390002",null,"Ca. Phosphitivorax butyraticus R76","etfB","Electron transfer flavoprotein subunit beta","_",0.92251,0.96899,36.8,{"v":3e-42,"d":"3.00E-42"},1,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,251,271,4,239,258]
[null,"SCFA_v1_1080001",null,"Ca. Phosphitivorax butyraticus R76","etfB","Electron transfer flavoprotein subunit beta (fragment)","_",0.67897,1.01657,38.04,{"v":1e-40,"d":"1.00E-40"},2,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,184,271,2,178,181]
[null,"BBta_1140",null,"Bradyrhizobium sp. BTAi1","etfB","Electron transfer flavoprotein beta-subunit","_",0.82288,0.89558,36.77,{"v":1e-31,"d":"1.00E-31"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,221,271,1,212,249]
[null,"BRADO6492",null,"Bradyrhizobium sp. ORS278","etfB","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.82288,0.89558,37.22,{"v":2e-31,"d":"2.00E-31"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8599534,"2a : Function from experimental evidences in other organisms",1,221,271,1,212,249]
[]
["ACT01_02765","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_13110","_","Clostridiaceae BL-3","_","Butyryl-CoA:acetate CoA-transferase","_",1.00664,1.00664,55.82,0,1,1,"_","2.8.3.-","2 : Cytoplasmic","_","e : enzyme","18218779, 8550525","2a : Function from experimental evidences in other organisms",1,452,452,1,452,452]
[]
["ACT01_04510","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_10629",null,"Clostridiaceae BL-3","rnfC","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit C","_",0.98687,1,58.54,0,1,1,"_","7.1.1.-","2 : Cytoplasmic","_","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",1,448,451,1,447,457]
[null,"NBG4_v1_240018",null,"Candidatus Sulfobium mesophilum","rnfC","Electron transport complex protein RnfC","_",0.96674,1.0023,49.77,{"v":1e-147,"d":"1.00E-147"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 21747791","2a : Function from experimental evidences in other organisms",2,434,451,3,434,435]
[null,"SCFA_v1_1220012",null,"Ca. Phosphitivorax butyraticus R76","rnfC","Electron transport complex subunit RnfC","_",0.99335,1.0205,47.54,{"v":1e-143,"d":"1.00E-143"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,444,451,1,436,439]
[null,"SCFA_v1_420042",null,"Ca. Phosphitivorax anaerolimi F81","rnfC","Electron transport complex subunit RnfC","_",0.99113,1.02523,48.99,{"v":3e-143,"d":"3.00E-143"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,443,451,1,435,436]
[null,"CD630_11370",null,"Clostridium difficile 630","rnfC","Electron transport complex protein","_",0.99113,1.00449,44.3,{"v":3e-129,"d":"3.00E-129"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 12773378, 11160111","2a : Function from experimental evidences in other organisms",2,443,451,3,444,445]
[null,"MAGMOv5_3971",null,"Magnetotactic ovoidal bacterium MO-1","rnfC","Electron transport complex protein rnfC. 4Fe-4S","_",0.73226,1.00665,40.53,{"v":1e-121,"d":"1.00E-121"},1,1,"6.1 : Membrane ; 7.3 : Inner membrane ;","_","6 : Inner membrane-associated","6 : Energy metabolism ;","c : carrier",9492268,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,450,451,7,456,620]
[null,"CLOSTRIBL4_v1_2199",null,"Clostridiales BL-4","rnfC","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit C","_",0.98261,1.00222,41.81,{"v":2E-107,"d":"2.00E-107"},1,1,"_","7.1.1.1","2 : Cytoplasmic","_","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",8,450,451,14,454,460]
[null,"MARHY2352",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","rnfC","Electron transport complex, RnfABCDGE type, C subunit. Required for the reduction of SoxR","_",0.73727,0.99557,39.2,{"v":1e-106,"d":"1.00E-106"},1,1,"_","_","11 : Membrane","_","t : transporter","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,450,451,9,451,609]
[null,"PSHAa1103",null,"Pseudoalteromonas haloplanktis TAC125","rsxC","Electron transport complex protein rnfC","_",0.52837,0.99113,38.48,{"v":1e-98,"d":"1.00E-98"},1,1,"1.4.2 : Electron transport ;","_","inner membrane associated","_","t : transporter","_","2a : Function from experimental evidences in other organisms",8,450,451,18,459,846]
[null,"VIBNIv4_A0907",null,"Vibrio nigripulchritudo SFn1","_","putative Electron transport complex protein rnfC","_",0.43854,0.98891,37.22,{"v":2E-90,"d":"2.00E-90"},1,1,"1.4.3 : Electron carrier ; 7.5 : Extracellular ;","_","10 : Secreted","6.5 : Electron transport ;","c : carrier","_","3 : Putative function from multiple computational evidences",8,448,451,18,459,1017]
[null,"MALCv4_3938",null,"Methylomicrobium alcaliphilum 20Z","rnfC","electron transport complex protein RnfC","_",0.96009,0.97085,38.11,{"v":2E-90,"d":"2.00E-90"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8264535,"2b : Function from indirect experimental evidences (e.g. phenotypes)",4,430,451,8,433,446]
[null,"ECK1625",null,"Escherichia coli K12","rsxC","putative 4Fe-4S ferredoxin-type protein fused with unknown protein","_",0.61486,1.00887,37.58,{"v":3e-89,"d":"3.00E-89"},1,1,"6.1 : Membrane ; 7.3 : Inner membrane ;","_","6 : Inner membrane-associated","18.1 : Enzymes of unknown specificity ;","c : carrier","_","3 : Putative function from multiple computational evidences",8,450,451,18,466,740]
[null,"VS_0976",null,"Vibrio tasmaniensis LGP32","_","Putative membrane protein","_",0.54545,0.8913,35.77,{"v":3E-43,"d":"3.00E-43"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","18 : Unknown function ;","m : membrane component","_","3 : Putative function from multiple computational evidences",8,250,451,30,271,276]
[]
["ACT01_04515","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_10630",null,"Clostridiaceae BL-3","rnfD","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit D","_",0.92754,0.96677,57.81,{"v":6e-127,"d":"6.00E-127"},1,1,"_","7.1.1.-","5 : Inner membrane protein","_","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",23,337,345,12,328,331]
[null,"SCFA_v1_420043",null,"Ca. Phosphitivorax anaerolimi F81","rnfD","Electron transport complex subunit D","_",0.95652,0.95652,50.61,{"v":9e-104,"d":"9.00E-104"},1,1,"_","_","5 : Inner membrane protein","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",19,340,345,20,345,345]
[null,"CD630_11380",null,"Clostridium difficile 630","rnfD","Electron transport complex protein","_",0.94783,1.00615,49.54,{"v":2E-95,"d":"2.00E-95"},1,1,"6.1 : Membrane ;","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","e : enzyme","9492268, 9154934, 8264535, 12773378, 11160111","2a : Function from experimental evidences in other organisms",19,339,345,2,323,325]
[null,"SCFA_v1_190017",null,"Ca. Phosphitivorax butyraticus R76","rnfD","putative Ion-translocating oxidoreductase complex subunit D","_",0.87246,1.03082,50.17,{"v":1e-90,"d":"1.00E-90"},1,1,"6.1 : Membrane ;","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","e : enzyme","10637328, 12773378","3 : Putative function from multiple computational evidences",54,340,345,2,292,292]
[null,"NBG4_v1_240019",null,"Candidatus Sulfobium mesophilum","_","Putative electron transport complex protein RnfD","_",0.97971,0.97971,42.6,{"v":3e-89,"d":"3.00E-89"},1,1,"1.4.3 : Electron carrier ;","_","5 : Inner membrane protein","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 21747791","3 : Putative function from multiple computational evidences",18,342,345,6,340,345]
[null,"MALCv4_3937",null,"Methylomicrobium alcaliphilum 20Z","rnfD","electron transport complex protein RnfD","_",0.97971,1.01807,44.08,{"v":3e-85,"d":"3.00E-85"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier",8264535,"2a : Function from experimental evidences in other organisms",22,337,345,6,331,332]
[null,"CLOSTRIBL4_v1_2200",null,"Clostridiales BL-4","rnfD","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit D","RHEA:47995 ;",0.93043,1.02885,43.93,{"v":8e-84,"d":"8.00E-84"},1,1,"_","7.1.1.1","2 : Cytoplasmic","_","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",22,342,345,5,311,312]
[null,"MAGMOv5_3970",null,"Magnetotactic ovoidal bacterium MO-1","rnfD","Electron transport complex protein rnfD","_",1.00279,1.04348,38.89,{"v":1e-82,"d":"1.00E-82"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","18.1 : Enzymes of unknown specificity ;","c : carrier","10637328, 12773378","2b : Function from indirect experimental evidences (e.g. phenotypes)",20,345,345,1,354,359]
[]
["ACT01_04520","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_10631",null,"Clostridiaceae BL-3","rnfG","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit G","_",0.98378,1,52.2,{"v":5e-59,"d":"5.00E-59"},1,1,"_","7.1.1.-","5 : Inner membrane protein","_","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",3,182,182,4,185,185]
[null,"NBG4_v1_240020",null,"Candidatus Sulfobium mesophilum","_","Putative electron transport complex protein RnfG","_",0.87755,0.94505,37.21,{"v":3e-25,"d":"3.00E-25"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 21747791","3 : Putative function from multiple computational evidences",9,173,182,6,176,196]
[]
["ACT01_04525","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_10632",null,"Clostridiaceae BL-3","rnfE","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit E","_",0.95755,0.98068,64.53,{"v":2e-89,"d":"2.00E-89"},1,1,"_","7.1.1.-","5 : Inner membrane protein","_","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",1,203,207,1,203,212]
[null,"CD630_11400",null,"Clostridium difficile 630","rnfE","Electron transport complex protein","_",0.91304,0.95939,53.44,{"v":2e-69,"d":"2.00E-69"},1,1,"_","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","c : carrier","11160111, 12773378, 8264535, 9154934, 9492268","2a : Function from experimental evidences in other organisms",1,189,207,1,189,197]
[null,"SCFA_v1_190015",null,"Ca. Phosphitivorax butyraticus R76","rnfE","Ion-translocating oxidoreductase complex subunit E (Predicted NADH:ubiquinone oxidoreductase, subunit RnfE)","_",0.93578,0.98551,46.08,{"v":6e-62,"d":"6.00E-62"},1,1,"6.1 : Membrane ;","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","c : carrier","10411911, 10637328, 12773378","3 : Putative function from multiple computational evidences",1,196,207,1,204,218]
[null,"SCFA_v1_420045",null,"Ca. Phosphitivorax anaerolimi F81","rnfE","Ion-translocating oxidoreductase complex subunit E (Predicted NADH:ubiquinone oxidoreductase, subunit RnfE)","_",0.95814,0.99517,47.57,{"v":2e-61,"d":"2.00E-61"},1,1,"6.1 : Membrane ;","1.18.1.-","5 : Inner membrane protein","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,198,207,1,206,215]
[null,"CLOSTRIBL4_v1_2202",null,"Clostridiales BL-4","rnfE","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit E","_",0.8087,0.89855,44.62,{"v":8e-54,"d":"8.00E-54"},1,1,"6.1 : Membrane ;","7.1.1.1","2 : Cytoplasmic","6.5 : Electron transport ;","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",2,187,207,6,191,230]
[null,"NBG4_v1_240021",null,"Candidatus Sulfobium mesophilum","rnfE","Electron transport complex protein RnfE","_",0.90278,0.94203,44.62,{"v":6E-51,"d":"6.00E-51"},1,1,"1.4.3 : Electron carrier ;","_","5 : Inner membrane protein","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 21747791","2a : Function from experimental evidences in other organisms",2,189,207,8,202,216]
[null,"MAGMOv5_3968",null,"Magnetotactic ovoidal bacterium MO-1","rnfE","Electron transport complex protein rnfE","_",0.88393,0.95652,42.42,{"v":2e-49,"d":"2.00E-49"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","18.1 : Enzymes of unknown specificity ;","c : carrier","10411911, 10637328, 12773378","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,201,207,8,201,224]
[null,"MALCv4_3935",null,"Methylomicrobium alcaliphilum 20Z","rnfE","electron transport complex protein RnfE","_",0.85915,0.88406,42.08,{"v":1e-47,"d":"1.00E-47"},1,1,"1.4.3 : Electron carrier ;","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","c : carrier",8264535,"2b : Function from indirect experimental evidences (e.g. phenotypes)",7,189,207,21,203,213]
[null,"VIBNIv4_A0904",null,"Vibrio nigripulchritudo SFn1","rnfE","Electron transport complex protein rnfE","_",0.88696,0.98551,39.22,{"v":6e-46,"d":"6.00E-46"},1,1,"1.4.3 : Electron carrier ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","6.5 : Electron transport ;","c : carrier","9097039, 9278503, 16738553, 10411911, 15919996","2a : Function from experimental evidences in other organisms",10,200,207,11,214,230]
[null,"ECK1628",null,"Escherichia coli K12","rsxE","putative inner membrane NADH-quinone reductase","_",0.90476,1.00966,35.89,{"v":2e-42,"d":"2.00E-42"},1,1,"6.1 : Membrane ;","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","c : carrier","10411911, 10637328, 12773378","3 : Putative function from multiple computational evidences",6,200,207,7,214,231]
[null,"ECUMN_1923",null,"Escherichia coli UMN026","rsxE","putative inner membrane NADH-quinone reductase","_",0.90476,1.00966,35.89,{"v":2e-42,"d":"2.00E-42"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","18.1 : Enzymes of unknown specificity ;","c : carrier","10411911, 10637328, 12773378, 15849754, 16850406","3 : Putative function from multiple computational evidences",6,200,207,7,214,231]
[null,"ECS88_1680",null,"Escherichia coli S88","rsxE","putative inner membrane NADH-quinone reductase","_",0.90043,1.00483,36.06,{"v":3e-42,"d":"3.00E-42"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","18.1 : Enzymes of unknown specificity ;","c : carrier","10411911, 10637328, 12773378, 15849754, 16850406","3 : Putative function from multiple computational evidences",6,200,207,7,214,231]
[null,"MARHY2355",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","rsxE","Electron transport complex protein rnfE. Required for the reduction of SoxR","_",0.88235,1.01449,36.19,{"v":3e-42,"d":"3.00E-42"},1,1,"6.1 : Membrane ;","_","11 : Membrane","_","t : transporter","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,201,207,8,217,238]
[null,"EFER_1411",null,"Escherichia fergusonii ATCC 35469T","rsxE","putative inner membrane NADH-quinone reductase","_",0.9087,1.00966,35.41,{"v":6e-42,"d":"6.00E-42"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","18.1 : Enzymes of unknown specificity ;","c : carrier","10411911, 10637328, 12773378, 15849754, 16850406","3 : Putative function from multiple computational evidences",6,200,207,7,214,230]
[null,"PSHAa1100",null,"Pseudoalteromonas haloplanktis TAC125","rsxE","Electron transport complex protein rnfE","_",0.90086,1.00966,35.89,{"v":1e-39,"d":"1.00E-39"},1,1,"1.4.2 : Electron transport ;","_","integral inner membrane","_","t : transporter","_","2a : Function from experimental evidences in other organisms",6,200,207,7,214,232]
[null,"MARHY1377",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","nqrD","Na(+)-translocating NADH-quinone reductase subunit D","_",0.8733,0.93237,37.31,{"v":1e-37,"d":"1.00E-37"},2,1,"1.4 : Energy production/transport ;","_","5 : Inner membrane protein","6 : Energy metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",5,192,207,8,200,221]
[null,"VC2292",null,"Vibrio cholerae N16961","nqrD","Na(+)-translocating NADH-quinone reductase subunit D","_",0.95714,0.97101,36.32,{"v":1e-37,"d":"1.00E-37"},2,1,"4.S.130 : Na+ ; 7.3 : Inner membrane ;","1.6.5.-","5 : Inner membrane protein","7.4 : Cations and iron carrying compounds ;","t : transporter","7805867, 7729558, 9490015, 10549856, 11248187, 11248188","2a : Function from experimental evidences in other organisms",11,206,207,15,210,210]
[null,"VIBNIv4_A0569",null,"Vibrio nigripulchritudo SFn1","nqrD","Na(+)-translocating NADH-quinone reductase subunit D","_",0.95714,0.97101,35.32,{"v":2E-35,"d":"2.00E-35"},2,1,"4.S.130 : Na+ ; 7.3 : Inner membrane ;","1.6.5.-","5 : Inner membrane protein","7.4 : Cations and iron carrying compounds ;","t : transporter","7805867, 7729558, 9490015, 10549856, 11248187, 11248188","1c : Function from experimental evidences in the studied genus",11,206,207,15,210,210]
[]
["ACT01_04530","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_10633",null,"Clostridiaceae BL-3","rnfA","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit A","_",0.98964,1,70.68,{"v":1e-98,"d":"1.00E-98"},1,1,"6.1 : Membrane ;","7.1.1.-","5 : Inner membrane protein","14 : Cell envelope ;","e : enzyme","20616070, 23269825","1c : Function from experimental evidences in the studied genus",1,191,191,1,191,193]
[null,"NBG4_v1_240022",null,"Candidatus Sulfobium mesophilum","rnfA","Electron transport complex protein RnfA","_",0.94924,0.97906,54.01,{"v":2e-71,"d":"2.00E-71"},1,1,"1.4.3 : Electron carrier ;","_","5 : Inner membrane protein","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 21747791","2a : Function from experimental evidences in other organisms",5,191,191,9,195,197]
[null,"VIBNIv4_A0909",null,"Vibrio nigripulchritudo SFn1","rnfA","Electron transport complex protein rnfA","_",0.98964,1,51.31,{"v":1e-69,"d":"1.00E-69"},1,1,"1.4.3 : Electron carrier ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","6.5 : Electron transport ;","c : carrier","9278503, 16738553, 10411911, 15919996","2a : Function from experimental evidences in other organisms",1,191,191,1,191,193]
[null,"ECK1623",null,"Escherichia coli K12","rsxA","putative inner membrane subunit of an electron transport system","_",0.98964,1,50.26,{"v":2e-68,"d":"2.00E-68"},1,1,"6.1 : Membrane ;","_","11 : Membrane","14 : Cell envelope ;","m : membrane component","10411911, 10637328, 12773378","3 : Putative function from multiple computational evidences",1,191,191,1,191,193]
[null,"ECUMN_1918",null,"Escherichia coli UMN026","rsxA","putative inner membrane subunit of an electron transport system","_",0.98964,1,50.26,{"v":2e-68,"d":"2.00E-68"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","14 : Cell envelope ;","m : membrane component","10411911, 10637328, 12773378, 15849754, 16850406","3 : Putative function from multiple computational evidences",1,191,191,1,191,193]
[null,"ECS88_1675",null,"Escherichia coli S88","rsxA","putative inner membrane subunit of an electron transport system","_",0.98964,1,50.26,{"v":3E-68,"d":"3.00E-68"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","14 : Cell envelope ;","m : membrane component","10411911, 10637328, 12773378, 15849754, 16850406","3 : Putative function from multiple computational evidences",1,191,191,1,191,193]
[null,"EFER_1416",null,"Escherichia fergusonii ATCC 35469T","rsxA","putative inner membrane subunit of an electron transport system","_",0.98964,1,49.74,{"v":1e-67,"d":"1.00E-67"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","14 : Cell envelope ;","m : membrane component","10411911, 10637328, 12773378, 15849754, 16850406","3 : Putative function from multiple computational evidences",1,191,191,1,191,193]
[null,"SCFA_v1_1220010",null,"Ca. Phosphitivorax butyraticus R76","rnfA","Electron transport complex protein rnfA","_",0.98429,0.98429,50,{"v":2e-67,"d":"2.00E-67"},1,1,"6.1 : Membrane ;","_","11 : Membrane","14 : Cell envelope ;","m : membrane component","10411911, 10637328, 12773378","3 : Putative function from multiple computational evidences",4,191,191,3,190,191]
[null,"SCFA_v1_420040",null,"Ca. Phosphitivorax anaerolimi F81","rnfA","Electron transport complex protein rnfA","_",0.89952,0.98429,50,{"v":9e-67,"d":"9.00E-67"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","14 : Cell envelope ;","m : membrane component","10411911, 10637328, 12773378","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,191,191,21,208,209]
[null,"PSHAa1105",null,"Pseudoalteromonas haloplanktis TAC125","rsxA","Electron transport complex protein rnfA, inner membrane protein","_",0.98964,1,47.64,{"v":3E-65,"d":"3.00E-65"},1,1,"1.4.2 : Electron transport ;","_","integral inner membrane","_","t : transporter",10411911,"2a : Function from experimental evidences in other organisms",1,191,191,1,191,193]
[null,"MAGMOv5_3973",null,"Magnetotactic ovoidal bacterium MO-1","rnfA","Electron transport complex protein rnfA","_",0.95431,0.98429,48.94,{"v":3e-64,"d":"3.00E-64"},1,1,"6.1 : Membrane ;","_","5 : Inner membrane protein","14 : Cell envelope ;","c : carrier","10411911, 10637328, 12773378","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,191,191,9,196,197]
[null,"MARHY2350",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","rsxA","Electron transport complex protein rnfA","_",0.98964,1,47.12,{"v":3e-63,"d":"3.00E-63"},1,1,"6.1 : Membrane ;","_","11 : Membrane","_","t : transporter","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,191,191,1,191,193]
[null,"CD630_11410",null,"Clostridium difficile 630","rnfA","Electron transport complex protein","_",0.96859,0.96859,49.19,{"v":1E-61,"d":"1.00E-61"},1,1,"6.1 : Membrane ;","_","11 : Membrane","14 : Cell envelope ;","m : membrane component","9492268, 9154934, 8264535, 12773378, 11160111","2a : Function from experimental evidences in other organisms",7,191,191,6,189,191]
[null,"MALCv4_3934",null,"Methylomicrobium alcaliphilum 20Z","rnfA","electron transport complex protein RnfA","_",0.97409,0.98429,48.4,{"v":7e-59,"d":"7.00E-59"},2,1,"1.4.3 : Electron carrier ;","_","11 : Membrane","14 : Cell envelope ;","m : membrane component","8264535, 9154934","2a : Function from experimental evidences in other organisms",3,190,191,5,191,193]
[null,"CLOSTRIBL4_v1_2203",null,"Clostridiales BL-4","rnfA","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit A","_",0.93434,0.96859,44.86,{"v":2e-58,"d":"2.00E-58"},1,1,"6.1 : Membrane ;","7.1.1.1","11 : Membrane","14 : Cell envelope ;","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",7,191,191,9,193,198]
[null,"NMV_1858",null,"Neisseria meningitidis NEM8013","nqrE","Na(+)-translocating NADH-quinone reductase subunit E (Na(+)-translocating NQR subunit E; Na(+)-NQR subunit E; NQR complex subunit E; NQR-1 subunit E)","_",0.98985,1.02094,41.03,{"v":2e-48,"d":"2.00E-48"},1,1,"_","1.6.5.8","11 : Membrane","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,190,191,1,195,197]
[null,"MARHY1378",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","nqrE","Na(+)-translocating NADH-quinone reductase subunit E","_",0.9901,1.04712,39,{"v":2e-47,"d":"2.00E-47"},2,1,"1.4 : Energy production/transport ;","_","5 : Inner membrane protein","6 : Energy metabolism ;","m : membrane component","7805867, 9490015","2a : Function from experimental evidences in other organisms",1,190,191,1,200,202]
[null,"VIBNIv4_A0570",null,"Vibrio nigripulchritudo SFn1","nqrE","Na(+)-translocating NADH-quinone reductase subunit E","_",0.9899,1.02618,39.29,{"v":1E-46,"d":"1.00E-46"},2,1,"4.S.130 : Na+ ; 7.3 : Inner membrane ;","1.6.5.-","5 : Inner membrane protein","7.4 : Cations and iron carrying compounds ;","t : transporter",10587447,"1c : Function from experimental evidences in the studied genus",1,190,191,1,196,198]
[]
["ACT01_04535","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_10634",null,"Clostridiaceae BL-3","rnfB","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit B","_",0.97909,0.97909,56.23,{"v":3e-113,"d":"3.00E-113"},1,1,"_","7.1.1.-","5 : Inner membrane protein","_","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",6,284,287,4,281,287]
[null,"NBG4_v1_240023",null,"Candidatus Sulfobium mesophilum","_","Putative electron transport complex protein RnfB","_",0.66414,0.91638,46.39,{"v":3e-81,"d":"3.00E-81"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 21747791","3 : Putative function from multiple computational evidences",11,273,287,58,315,396]
[null,"CD630_11420",null,"Clostridium difficile 630","rnfB","Electron transport complex protein","_",0.83385,0.94425,39.85,{"v":3e-64,"d":"3.00E-64"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 12773378, 11160111","2a : Function from experimental evidences in other organisms",5,274,287,3,266,325]
[null,"SCFA_v1_420041",null,"Ca. Phosphitivorax anaerolimi F81","RnfB","electron transport complex protein RnfB","_",0.8179,0.92334,37.74,{"v":8e-61,"d":"8.00E-61"},1,1,"_","1.18.1.-","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,272,287,2,261,324]
[null,"SCFA_v1_1220011",null,"Ca. Phosphitivorax butyraticus R76","rnfB","Electron transport complex protein RnfB","_",0.81173,0.91638,37.64,{"v":3E-57,"d":"3.00E-57"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,269,287,2,258,324]
[null,"MALCv4_3932",null,"Methylomicrobium alcaliphilum 20Z","rnfB","electron transport complex protein RnfB","_",0.98258,0.98258,35.46,{"v":3e-55,"d":"3.00E-55"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,280,287,1,275,287]
[null,"CLOSTRIBL4_v1_2204",null,"Clostridiales BL-4","rnfB","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit B","_",0.8885,0.96591,36.47,{"v":2e-54,"d":"2.00E-54"},1,1,"_","7.1.1.1","2 : Cytoplasmic","_","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",11,265,287,8,255,264]
[null,"SCFA_v1_1550009",null,"Ca. Phosphitivorax anaerolimi F81","_","putative ferredoxin","_",0.18467,0.92982,39.62,7e-08,3,8,"_","_","9 : Periplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",217,269,287,7,54,57]

{"sheet":"SwissProt","index":6,"n_rows":766,"n_cols":22,"rows_kept":766}
["ACT01_13720","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?",1.00234,1.00469,57.71,{"v":1E-172,"d":"1.00E-172"},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)","_",1,427,427,1,424,426]
[null,"F9USS9","IPMed?",1.00234,1.00943,56.78,{"v":1e-159,"d":"1.00E-159"},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",1,427,427,1,424,424]
[]
["ACT01_13730","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?",0.89432,0.96414,43.76,{"v":1E-127,"d":"1.00E-127"},1,1,"lctP","L-lactate permease","_","Cell membrane, Membrane, Transmembrane, Transmembrane helix, Transport",10508058,"Streptococcus iniae","_",3,455,511,5,451,474]
[null,"Q46839","IPMed?",0.95893,1.05088,33.52,{"v":1E-83,"d":"1.00E-83"},2,2,"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",3,504,511,19,549,560]
[null,"P71067","IPMed?",0.96803,1.06654,33.03,{"v":9e-77,"d":"9.00E-77"},3,1,"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",3,504,511,19,553,563]
[null,"Q8ZL63","_",0.96915,1.04501,31.84,{"v":1E-73,"d":"1.00E-73"},4,2,"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",3,510,511,19,547,551]
[null,"P33231","IPMed?",0.96733,1.04305,31.71,{"v":1e-72,"d":"1.00E-72"},5,2,"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",3,510,511,19,547,551]
[null,"Q8Z2E3","_",0.96915,1.04501,31.65,{"v":1e-72,"d":"1.00E-72"},6,2,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Transmembrane, Transmembrane helix, Transport","11677608, 12644504","Salmonella typhi","CT18 / ATCC 700931 / Ty2",3,510,511,19,547,551]
[null,"P65254","_",0.96733,1.04305,31.52,{"v":3e-72,"d":"3.00E-72"},7,2,"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",3,510,511,19,547,551]
[null,"P65253","_",0.96733,1.04305,31.52,{"v":3e-72,"d":"3.00E-72"},7,2,"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",3,510,511,19,547,551]
[null,"Q9K5Z9","_",0.98282,1.00783,29.51,{"v":3e-69,"d":"3.00E-69"},8,2,"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",4,505,511,18,520,524]
[null,"P55910","IPMed?",0.98891,1.04697,31.96,{"v":2e-67,"d":"2.00E-67"},9,2,"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",3,505,511,17,536,541]
[null,"Q57251","_",1.03008,1.07241,25,{"v":6E-34,"d":"6.00E-34"},10,2,"_","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",3,511,511,5,532,532]
[null,"P39835","IPMed?",0.90215,1.05251,19.96,2E-3,11,4,"gntT","High-affinity gluconate transporter","_","Cell inner membrane, Cell membrane, Complete proteome, Gluconate utilization, Membrane, Reference proteome, Sugar transport, Transmembrane, Transmembrane helix, Transport","8987614, 9278503, 16397293, 16738553, 2845225, 7984428, 3040894, 9045817, 15919996","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",1,456,511,3,389,438]
[null,"P27611","IPMed?",0.26223,0.29004,20.9,0.045,12,5,"nhaC","Na(+)/H(+) antiporter NhaC","_","Antiport, Cell membrane, Complete proteome, Ion transport, Membrane, Reference proteome, Sodium, Sodium transport, Transmembrane, Transmembrane helix, Transport","1660475, 9190799, 21951522","Bacillus pseudofirmus (strain OF4)","OF4 / OF4 / OF4",332,464,511,35,168,462]
[null,"E7DNB6","IPMed?",0.41427,0.93151,21.22,0.056,13,3,"TMP","Tape measure protein","_","Complete proteome, Host membrane, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Viral release from host cell, Viral tail assembly, Virion","21097633, 22151602","Pneumococcus phage Dp-1","_",18,478,511,542,964,1149]
[null,"P39344","IPMed?",0.9002,1.04784,18.04,0.058,14,3,"idnT","Gnt-II system L-idonate transporter","_","Cell inner membrane, Cell membrane, Complete proteome, Gluconate utilization, Membrane, Reference proteome, Sugar transport, Transmembrane, Transmembrane helix, Transport","7610040, 9278503, 16738553, 9658018, 15919996, 17088549","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",1,456,511,3,389,439]
[null,"A1L4X0","IPMed?",0.3816,0.45244,24.1,0.17,15,1,"CLT2","Protein CLT2, chloroplastic","_","Alternative splicing, Chloroplast, Complete proteome, Membrane, Plastid, Reference proteome, Transit peptide, Transmembrane, Transmembrane helix, Transport","10617198, 27862469, 14593172, 20080670, 24204368","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia",159,322,511,158,334,431]
[]
["ACT01_00410","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q8RED8","_",0.99686,0.99686,40.06,{"v":1E-79,"d":"1.00E-79"},1,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Reference proteome",11889109,"Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)","ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131",3,315,318,2,315,318]
[null,"E8MJ15","_",0.9717,0.97785,37.22,{"v":2e-64,"d":"2.00E-64"},2,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Cytoplasm, NAD, Oxidoreductase",21270894,"Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b)","ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b",1,306,318,2,309,316]
[null,"P59050","_",0.9717,0.97785,37.22,{"v":2e-64,"d":"2.00E-64"},2,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Reference proteome",12381787,"Bifidobacterium longum (strain NCC 2705)","NCC 2705",1,306,318,2,309,316]
[null,"Q815X8","_",0.95597,0.96203,36.18,{"v":9e-63,"d":"9.00E-63"},3,1,"ldh3","L-lactate dehydrogenase 3","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, 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",6,306,318,6,308,316]
[null,"P62049","_",0.9717,0.97785,35.28,{"v":3e-62,"d":"3.00E-62"},4,1,"ldh3","L-lactate dehydrogenase 3","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase",14960714,"Bacillus cereus (strain ATCC 10987 / NRS 248)","ATCC 10987 / NRS 248",1,306,318,1,308,316]
[null,"Q631X2","_",0.95597,0.96203,35.53,{"v":5e-62,"d":"5.00E-62"},5,1,"ldh3","L-lactate dehydrogenase 3","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase",16621833,"Bacillus cereus (strain ZK / E33L)","ZK / E33L",6,306,318,6,308,316]
[null,"Q6HBQ8","_",0.95597,0.96203,35.53,{"v":5e-62,"d":"5.00E-62"},5,1,"ldh3","L-lactate dehydrogenase 3","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase",16621833,"Bacillus thuringiensis subsp. konkukian (strain 97-27)","97-27",6,306,318,6,308,316]
[null,"Q81XJ7","_",0.95597,0.96203,35.53,{"v":7e-62,"d":"7.00E-62"},6,1,"ldh3","L-lactate dehydrogenase 3","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Reference proteome","12721629, 18952800","Bacillus anthracis","Ames / isolate Porton / Ames ancestor",6,306,318,6,308,316]
[null,"Q71ZD6","_",0.96855,0.99035,37.01,{"v":2e-61,"d":"2.00E-61"},7,1,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Cytoplasm, NAD, Oxidoreductase",15115801,"Listeria monocytogenes serotype 4b (strain F2365)","F2365",3,309,318,1,308,311]
[null,"Q8Y6Z6","_",0.9717,0.99357,36.57,{"v":5e-61,"d":"5.00E-61"},8,1,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Reference proteome",11679669,"Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)","ATCC BAA-679 / EGD-e",3,310,318,1,309,311]
[null,"Q92BI0","_",0.96855,0.99035,36.69,{"v":5e-60,"d":"5.00E-60"},9,1,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase",11679669,"Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)","ATCC BAA-680 / CLIP 11262",3,309,318,1,308,311]
[null,"A8F9Q8","_",0.95912,0.96825,35.74,{"v":2e-58,"d":"2.00E-58"},10,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome",17895969,"Bacillus pumilus (strain SAFR-032)","SAFR-032",8,310,318,9,312,315]
[null,"D8KFT1","IPMed?",0.96855,0.98089,32.47,{"v":4e-56,"d":"4.00E-56"},11,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","12867459, 20639323","Lactococcus lactis subsp. cremoris (strain NZ9000)","NZ9000 / NZ9000",1,306,318,1,307,314]
[null,"Q59244","IPMed?",0.96541,0.96845,34.85,{"v":5e-54,"d":"5.00E-54"},12,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",3675869,"Bacillus caldolyticus","_",8,311,318,9,313,317]
[null,"P00343","IPMed?",0.91718,0.94025,34.11,{"v":9e-54,"d":"9.00E-54"},13,1,"ldh","L-lactate dehydrogenase","1.1.1.27","3D-structure, Allosteric enzyme, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","1768113, 6411465, 14601, 7766183, 19787773","Lactobacillus casei","ATCC 393 / DSM 20011 / JCM 1134 / NBRC 15883 / NCIMB 11970 / NCDO 161 / ATCC 393 / DSM 20011 / JCM 1134 / NBRC 15883 / NCIMB 11970 / NCDO 161 / ATCC 393 / DSM 20011 / JCM 1134 / NBRC 15883 / NCIMB 11970 / NCDO 161",10,306,318,14,310,326]
[null,"P00344","IPMed?",0.96855,0.97161,35.06,{"v":2e-53,"d":"2.00E-53"},14,1,"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",8,312,318,9,314,317]
[null,"P10655","IPMed?",0.96541,0.96845,35.18,{"v":3e-53,"d":"3.00E-53"},15,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","3675869, 3297694","Bacillus caldotenax","_",8,311,318,9,313,317]
[null,"P50934","IPMed?",0.94462,0.96541,33.88,{"v":3E-52,"d":"3.00E-52"},16,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",9884224,"Lactobacillus sakei",207,10,312,318,13,315,325]
[null,"P13714","IPMed?",0.95625,0.96226,34.31,{"v":3E-52,"d":"3.00E-52"},17,1,"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",8,311,318,8,311,320]
[null,"P14561","IPMed?",0.95912,0.95912,32.13,{"v":8e-52,"d":"8.00E-52"},18,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Allosteric enzyme, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","2334516, 3435642","Bacillus psychrosaccharolyticus","_",8,310,318,9,312,318]
[null,"P20619","IPMed?",0.9185,0.92138,33.45,{"v":2E-51,"d":"2.00E-51"},19,1,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",2334516,"Bacillus psychrosaccharolyticus","_",8,298,318,9,300,319]
[null,"Q5HJD7","IPMed?",0.96855,0.97161,32.79,{"v":9e-51,"d":"9.00E-51"},20,1,"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",8,314,318,9,315,317]
[null,"A6QDL6","IPMed?",0.96855,0.97161,32.79,{"v":9e-51,"d":"9.00E-51"},20,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Stress response","17951380, 18356528","Staphylococcus aureus (strain Newman)","Newman",8,314,318,9,315,317]
[]
["ACT01_04310","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q7SI97","IPMed?",0.53333,0.55696,26.14,0.014,1,2,"_","L-lactate dehydrogenase","1.1.1.27","3D-structure, NAD, Oxidoreductase, Pyruvate","15637271, 12967707","Plasmodium berghei (strain Anka)","ANKA",102,261,330,66,240,316]
[null,"P19629","IPMed?",0.79819,0.80303,23.4,0.019,3,2,"Ldhc","L-lactate dehydrogenase C chain","1.1.1.27","Complete proteome, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Reference proteome","7937776, 6343385, 22673903","Rattus norvegicus","_",32,274,330,20,268,332]
[null,"P00344","IPMed?",0.56667,0.58991,22.46,0.019,4,2,"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",33,219,330,7,181,317]
[null,"P16115","IPMed?",0.49394,0.51097,26.99,0.019,2,2,"ldh","L-lactate dehydrogenase","1.1.1.27","3D-structure, Allosteric enzyme, Complete proteome, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","8404889, 10360571, 2318202, 9655830","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",34,193,330,2,148,319]
[null,"Q27743","IPMed?",0.5303,0.5538,24.57,0.033,5,2,"_","L-lactate dehydrogenase","1.1.1.27","3D-structure, NAD, Oxidoreductase, Pyruvate","8515777, 8901865, 10187806","Plasmodium falciparum (isolate CDC / Honduras)","_",102,261,330,66,240,316]
[null,"P13714","IPMed?",0.88485,0.9125,19.18,0.033,6,2,"ldh","L-lactate dehydrogenase","1.1.1.27","3D-structure, Allosteric enzyme, Complete proteome, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","8969502, 9384377, 19383706, 3098260, 10809684, 17218307","Bacillus subtilis (strain 168)","168 / 168 / 168",34,295,330,7,286,320]
[null,"E8MJ15","_",0.33939,0.35443,24.11,0.044,7,2,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Cytoplasm, NAD, Oxidoreductase",21270894,"Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b)","ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b",108,219,330,74,181,316]
[null,"P59050","_",0.33939,0.35443,24.11,0.044,7,2,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Reference proteome",12381787,"Bifidobacterium longum (strain NCC 2705)","NCC 2705",108,219,330,74,181,316]
[null,"Q9YEA1","IPMed?",0.54848,0.58766,22.1,0.077,8,2,"mdh","Malate dehydrogenase","1.1.1.299","3D-structure, Complete proteome, NAD, NADP, Oxidoreductase, Reference proteome, Tricarboxylic acid cycle","10382966, 19555779","Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)","ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1",104,274,330,63,234,308]
[null,"P14561","IPMed?",0.46364,0.48113,24.84,0.078,9,2,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Allosteric enzyme, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","2334516, 3435642","Bacillus psychrosaccharolyticus","_",34,186,330,8,148,318]
[null,"Q59244","IPMed?",0.56364,0.58675,22.04,0.078,10,2,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",3675869,"Bacillus caldolyticus","_",34,219,330,8,181,317]
[null,"P00342","IPMed?",0.79819,0.80303,21.89,0.11,11,2,"Ldhc","L-lactate dehydrogenase C chain","1.1.1.27","3D-structure, Complete proteome, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Reference proteome","2439071, 3619944, 15489334, 468774, 7429427, 6343385, 3754749, 21183079, 23055941, 468772","Mus musculus","DBA/2J",32,274,330,20,268,332]
[]
["ACT01_03310","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q57717","_",0.97238,0.98876,52.84,{"v":4e-49,"d":"4.00E-49"},1,1,"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",1,175,181,1,171,178]
[null,"O27772","_",0.98895,0.99444,50.28,{"v":2E-46,"d":"2.00E-46"},2,1,"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",1,178,181,1,174,180]
[null,"Q5JIK2","_",0.96757,0.98895,50.84,{"v":7e-46,"d":"7.00E-46"},3,1,"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",1,175,181,1,178,185]
[null,"P84820","IPMed?",0.92973,0.95028,51.16,{"v":2e-44,"d":"2.00E-44"},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","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",1,168,181,1,171,185]
[null,"P80523","IPMed?",1,1.00552,44.51,{"v":3e-44,"d":"3.00E-44"},5,1,"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",1,181,181,1,181,182]
[null,"Q51799","IPMed?",0.96216,0.98343,50,{"v":5e-44,"d":"5.00E-44"},6,1,"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",1,174,181,1,177,185]
[null,"P80902","IPMed?",0.98895,1.0113,49.16,{"v":6e-43,"d":"6.00E-43"},7,1,"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",1,178,181,1,174,177]
[null,"Q9UYY9","_",0.92973,0.95028,50,{"v":7e-43,"d":"7.00E-43"},8,1,"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",1,168,181,1,171,185]
[null,"O58411","_",0.92973,0.95028,50.58,{"v":1E-42,"d":"1.00E-42"},9,1,"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",1,168,181,1,171,185]
[null,"O05650","IPMed?",0.94792,1.00552,39.56,{"v":8e-36,"d":"8.00E-36"},10,1,"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",3,178,181,9,189,192]
[null,"Q8L3B3","IPMed?",0.83684,0.87845,42.14,{"v":1E-26,"d":"1.00E-26"},11,1,"padE","NADH-dependent phenylglyoxylate dehydrogenase subunit gamma","1.2.1.58","Direct protein sequencing, NAD, Oxidoreductase",9490067,"Azoarcus evansii","KB740 / DSM 6898",1,156,181,1,157,190]
[null,"P80906","IPMed?",0.94086,0.96685,30.86,2e-11,12,3,"korC","2-oxoglutarate synthase subunit KorC","1.2.7.3","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",3,172,181,4,176,186]
[null,"Q2RI40","IPMed?",0.50794,0.88398,29.38,1e-07,13,2,"_","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",26,161,181,39,197,315]
[null,"Q2RMD6","IPMed?",0.15884,1.02762,23.12,1E-4,14,11,"_","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Reference proteome, Transport","18631365, 9214293, 10878009, 29581263","Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320 / ATCC 39073 / JCM 9320",5,177,181,418,602,1171]
[null,"P80907","IPMed?",0.29079,0.76796,25.18,0.0004,15,7,"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",2,140,181,297,430,478]
[]
["ACT01_03315","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q9UYZ0","_",0.84762,0.89,46.07,{"v":9e-22,"d":"9.00E-22"},1,1,"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",10,97,100,15,103,105]
[null,"O58412","_",0.84762,0.89,46.07,{"v":1e-21,"d":"1.00E-21"},2,1,"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",10,97,100,15,103,105]
[null,"Q51800","IPMed?",0.81905,0.86,43.02,{"v":8e-20,"d":"8.00E-20"},3,1,"vorD","Ketoisovalerate oxidoreductase subunit VorD","1.2.7.7","4Fe-4S, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","8550425, 10430560","Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)","ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 / ATCC 43587 / DSM 3638 / JCM 8422 / Vc1",13,97,100,18,103,105]
[null,"Q57716","_",0.62,0.72093,53.23,{"v":2E-19,"d":"2.00E-19"},4,1,"porD","Pyruvate synthase subunit PorD","_","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Reference proteome, Repeat, Transport",8688087,"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440",37,97,100,23,84,86]
[null,"P80903","IPMed?",0.61,0.75309,55.74,{"v":3e-19,"d":"3.00E-19"},5,1,"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",37,97,100,23,80,81]
[null,"P56815","_",0.73,0.90123,45.21,{"v":1e-18,"d":"1.00E-18"},6,1,"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",25,97,100,11,80,81]
[null,"Q9UYZ3","_",0.72381,0.76,40.79,{"v":5e-17,"d":"5.00E-17"},7,1,"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",25,99,100,30,105,105]
[null,"Q51803","IPMed?",0.72381,0.76,39.47,{"v":1e-16,"d":"1.00E-16"},8,1,"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",25,99,100,30,105,105]
[null,"O58415","_",0.72381,0.76,39.47,{"v":3e-16,"d":"3.00E-16"},9,1,"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",25,99,100,30,105,105]
[null,"P80524","IPMed?",0.76,0.8,39.47,{"v":4e-16,"d":"4.00E-16"},10,1,"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",23,97,100,18,93,95]
[null,"Q8L3B2","IPMed?",0.66,0.70968,42.42,8E-14,11,1,"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",24,87,100,22,87,93]
[null,"Q2RI40","IPMed?",0.21587,0.68,36.76,1e-12,12,1,"_","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",32,99,100,245,312,315]
[null,"Q56316","IPMed?",0.64,0.64646,39.06,4e-11,13,1,"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",37,99,100,30,93,99]
[null,"Q57661","IPMed?",0.22358,0.55,45.45,6e-08,14,1,"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",43,97,100,154,208,246]
[null,"P00196","IPMed?",0.47,0.85455,42.55,3e-06,15,3,"_","Ferredoxin","_","4Fe-4S, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",5227671,"Clostridium butyricum","_",45,91,100,5,51,55]
[null,"Q8TM02","IPMed?",0.0971,0.77,33.77,5e-06,16,3,"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",21,94,100,550,626,793]
[]
["ACT01_03320","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O73986","_",0.90886,0.91349,49.86,{"v":5e-111,"d":"5.00E-111"},1,1,"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",10,367,393,10,367,395]
[null,"Q9UYZ4","_",0.91646,0.92112,48.62,{"v":1e-110,"d":"1.00E-110"},2,1,"porA","Pyruvate synthase subunit PorA","1.2.7.1","Complete proteome, Oxidoreductase","12622808, 22057919","Pyrococcus abyssi (strain GE5 / Orsay)","GE5 / Orsay / GE5 / Orsay",10,370,393,10,370,395]
[null,"P56810","_",0.91603,0.93995,47.22,{"v":1e-110,"d":"1.00E-110"},3,1,"porA","Pyruvate synthase subunit PorA","1.2.7.1","Complete proteome, Oxidoreductase, Reference proteome",9371463,"Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)","ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H",7,366,393,6,360,383]
[null,"Q51804","IPMed?",0.90404,0.91094,48.88,{"v":9e-109,"d":"9.00E-109"},4,1,"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",10,366,393,10,366,396]
[null,"Q57715","_",0.93893,0.94859,48.78,{"v":4e-108,"d":"4.00E-108"},5,1,"porA","Pyruvate synthase subunit PorA","1.2.7.1","Complete proteome, Oxidoreductase, Reference proteome",8688087,"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440",1,366,393,4,368,389]
[null,"P80900","IPMed?",0.91349,0.93734,47.08,{"v":1E-107,"d":"1.00E-107"},6,1,"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",7,365,393,6,359,383]
[null,"P80521","IPMed?",0.8806,0.90076,47.18,{"v":9e-105,"d":"9.00E-105"},7,1,"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",9,360,393,15,368,402]
[null,"Q51801","IPMed?",0.91624,0.91858,44.88,{"v":3E-102,"d":"3.00E-102"},8,1,"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",7,366,393,10,368,394]
[null,"O58413","_",0.92386,0.92621,43.68,{"v":3e-100,"d":"3.00E-100"},9,1,"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",4,366,393,7,368,394]
[null,"Q9UYZ1","_",0.92152,0.92621,42.86,{"v":3E-98,"d":"3.00E-98"},10,1,"vorA","Ketoisovalerate oxidoreductase subunit VorA","1.2.7.7","Complete proteome, Oxidoreductase","12622808, 22057919","Pyrococcus abyssi (strain GE5 / Orsay)","GE5 / Orsay / GE5 / Orsay",4,366,393,8,369,395]
[null,"O05651","IPMed?",0.94656,0.94898,44.35,{"v":1E-87,"d":"1.00E-87"},11,1,"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",3,369,393,6,372,392]
[null,"Q8L3B1","IPMed?",0.8729,0.92621,39.56,{"v":4e-77,"d":"4.00E-77"},12,1,"padG","NADH-dependent phenylglyoxylate dehydrogenase subunit alpha","1.2.1.58","Direct protein sequencing, NAD, Oxidoreductase",9490067,"Azoarcus evansii","KB740 / DSM 6898",9,360,393,25,385,417]
[null,"Q2RI41","IPMed?",0.93418,0.93893,36.86,{"v":3e-73,"d":"3.00E-73"},13,1,"_","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",7,372,393,7,375,395]
[null,"P03833","IPMed?",0.32878,0.97964,29.35,{"v":3e-33,"d":"3.00E-33"},14,9,"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","_",1,372,393,1,381,1171]
[null,"P19543","IPMed?",0.33078,0.98728,28.61,{"v":2e-32,"d":"2.00E-32"},15,9,"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",1,375,393,1,384,1173]
[null,"P52647","IPMed?",0.31431,0.93893,29.81,{"v":7e-31,"d":"7.00E-31"},16,9,"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",7,363,393,4,368,1174]
[]
["ACT01_03325","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O27771","_",0.94613,0.97569,48.4,{"v":3e-89,"d":"3.00E-89"},1,1,"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",11,291,297,7,287,288]
[null,"P80901","IPMed?",0.94613,0.97569,47.69,{"v":2e-88,"d":"2.00E-88"},2,1,"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",11,291,297,7,287,288]
[null,"O58414","_",0.92926,0.97306,49.13,{"v":2E-87,"d":"2.00E-87"},3,1,"vorB","Ketoisovalerate oxidoreductase subunit VorB","1.2.7.7","Complete proteome, Oxidoreductase",9679194,"Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)","ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3",11,292,297,17,305,311]
[null,"Q9UYZ2","_",0.92926,0.97306,48.79,{"v":6e-86,"d":"6.00E-86"},4,1,"vorB","Ketoisovalerate oxidoreductase subunit VorB","1.2.7.7","Complete proteome, Oxidoreductase","12622808, 22057919","Pyrococcus abyssi (strain GE5 / Orsay)","GE5 / Orsay / GE5 / Orsay",11,292,297,17,305,311]
[null,"Q51802","IPMed?",0.93248,0.97643,48.62,{"v":5e-85,"d":"5.00E-85"},5,1,"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",11,292,297,16,305,311]
[null,"Q57714","_",0.95302,0.95623,47.89,{"v":9e-85,"d":"9.00E-85"},6,1,"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",11,286,297,9,292,298]
[null,"P80522","IPMed?",0.9596,0.96284,45.61,{"v":2E-73,"d":"2.00E-73"},7,1,"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",16,297,297,13,291,296]
[null,"Q56317","IPMed?",0.89506,0.97643,42.07,{"v":2e-71,"d":"2.00E-71"},8,1,"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",16,290,297,22,311,324]
[null,"Q2RI42","IPMed?",0.94268,0.99663,42.91,{"v":2E-70,"d":"2.00E-70"},9,1,"_","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",11,290,297,13,303,314]
[null,"O58417","_",0.96073,1.07071,40.88,{"v":4e-69,"d":"4.00E-69"},10,1,"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",1,287,297,1,317,331]
[null,"Q51805","IPMed?",0.96073,1.07071,40.88,{"v":7e-68,"d":"7.00E-68"},11,1,"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",1,287,297,1,317,331]
[null,"Q8L3A9","IPMed?",0.63453,0.95286,39.58,{"v":1E-52,"d":"1.00E-52"},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",11,281,297,152,427,446]
[null,"P94692","IPMed?",0.15828,0.65657,32.31,{"v":1e-16,"d":"1.00E-16"},13,10,"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",97,283,297,960,1149,1232]
[null,"Q53046","IPMed?",0.18808,0.75421,29.46,{"v":6e-16,"d":"6.00E-16"},14,10,"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",84,294,297,956,1171,1191]
[null,"Q94IN5","IPMed?",0.10039,0.60943,30.39,8E-14,15,10,"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",99,272,297,1029,1204,1803]
[]
["ACT01_00445","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?",1.0017,1.00427,54.51,0,1,7,"_","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",8,1171,1174,6,1169,1171]
[null,"P19543","IPMed?",1.0017,1.00256,52.98,0,2,7,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Plasmid, Repeat, Transport","2504647, 1708766","Enterobacter agglomerans","333 / 333",8,1171,1174,8,1171,1173]
[null,"P94692","IPMed?",0.95536,1.00256,51.49,0,3,7,"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",1,1171,1174,1,1167,1232]
[null,"P03833","IPMed?",1.00085,1.00342,51.83,0,4,7,"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","_",8,1174,1174,8,1171,1171]
[null,"Q06879","IPMed?",1.00751,1.02896,45.45,0,5,6,"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",1,1173,1174,1,1199,1199]
[null,"Q94IN5","IPMed?",0.65391,1.00426,45.89,0,6,7,"PNO","Pyruvate dehydrogenase [NADP(+)], mitochondrial","1.2.1.51","4Fe-4S, Direct protein sequencing, Electron transport, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, Mitochondrion, NADP, Oxidoreductase, Repeat, Thiamine pyrophosphate, Transit peptide, Transport","11023353, 11319255, 1910287, 8373179, 3110154, 12623066","Euglena gracilis","SAG1224-5/25",8,1170,1174,72,1232,1803]
[null,"P52965","_",0.99583,1.01704,45.56,0,7,7,"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",5,1173,1174,6,1175,1199]
[null,"Q3M8N0","IPMed?",1.00588,1.01959,45.95,0,8,7,"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",3,1174,1174,4,1186,1190]
[null,"P52647","IPMed?",1.00426,1.00426,44.11,0,9,5,"ydbK","Probable pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","9097039, 9278503, 16738553, 9025293","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",6,1173,1174,2,1167,1174]
[null,"Q53046","IPMed?",0.99664,1.01107,45.66,0,10,4,"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",3,1172,1174,4,1179,1191]
[null,"Q968X7","IPMed?",0.64374,1.06048,43.29,0,11,7,"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",7,1162,1174,6,1239,1934]
[]
["ACT01_00545","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P19543","IPMed?",0.99915,1.00085,62.2,0,1,3,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Plasmid, Repeat, Transport","2504647, 1708766","Enterobacter agglomerans","333 / 333",3,1162,1171,4,1167,1173]
[null,"P03833","IPMed?",0.99658,0.99658,61.18,0,2,3,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","3062178, 3060860, 8483412, 6306580","Klebsiella pneumoniae","_",3,1164,1171,4,1166,1171]
[null,"Q2RMD6","IPMed?",1.00427,1.00427,59.86,0,3,3,"_","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Reference proteome, Transport","18631365, 9214293, 10878009, 29581263","Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320 / ATCC 39073 / JCM 9320",5,1168,1171,4,1171,1171]
[null,"P94692","IPMed?",0.94643,0.99573,55.23,0,4,3,"por","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Calcium, Cytoplasm, Direct protein sequencing, Disulfide bond, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Thiamine pyrophosphate, Transport","9294422, 7612653, 10048931, 11752578, 16472741","Desulfocurvibacter africanus","ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi / ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi",3,1158,1171,4,1159,1232]
[null,"Q94IN5","IPMed?",0.65169,1.00342,49.7,0,5,3,"PNO","Pyruvate dehydrogenase [NADP(+)], mitochondrial","1.2.1.51","4Fe-4S, Direct protein sequencing, Electron transport, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, Mitochondrion, NADP, Oxidoreductase, Repeat, Thiamine pyrophosphate, Transit peptide, Transport","11023353, 11319255, 1910287, 8373179, 3110154, 12623066","Euglena gracilis","SAG1224-5/25",4,1168,1171,69,1235,1803]
[null,"Q06879","IPMed?",0.99833,1.0222,47.54,0,7,4,"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","8415612, 11759840","Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)","PCC 7120 / SAG 25.82 / UTEX 2576",4,1162,1171,5,1193,1199]
[null,"Q3M8N0","IPMed?",1.00084,1.01708,48.19,0,6,3,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","25197444, 8352652","Trichormus variabilis (strain ATCC 29413 / PCC 7937)","ATCC 29413 / PCC 7937",4,1162,1171,6,1179,1190]
[null,"Q968X7","IPMed?",0.64168,1.05978,46.49,0,8,5,"PFOR","Pyruvate dehydrogenase [NADP(+)]","1.2.1.51","4Fe-4S, Electron transport, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat, Thiamine pyrophosphate, Transport",11319255,"Cryptosporidium parvum","KSU-1",1,1160,1171,1,1235,1934]
[null,"P52965","_",0.98165,1.00512,46.98,0,9,4,"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",4,1162,1171,6,1169,1199]
[null,"Q53046","IPMed?",0.98992,1.00683,46.14,0,10,3,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8736535, 21886856","Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)","ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1",3,1158,1171,5,1170,1191]
[null,"P52647","IPMed?",0.9983,1.00085,44.97,0,11,6,"ydbK","Probable pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","9097039, 9278503, 16738553, 9025293","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",6,1158,1171,3,1157,1174]
[]
["ACT01_02090","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?",1.0017,1.00683,56.57,0,1,5,"_","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",7,1175,1177,4,1170,1171]
[null,"P19543","IPMed?",0.99915,1.00256,54.68,0,2,6,"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",6,1174,1177,5,1171,1173]
[null,"P03833","IPMed?",0.99915,1.00427,54.25,0,3,6,"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","_",6,1177,1177,5,1171,1171]
[null,"P94692","IPMed?",0.95292,0.99745,52.81,0,4,5,"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",8,1174,1177,7,1167,1232]
[null,"Q94IN5","IPMed?",0.65391,1.0017,47.07,0,5,6,"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",7,1175,1177,70,1234,1803]
[null,"Q968X7","IPMed?",0.64116,1.05353,46.13,0,6,3,"PFOR","Pyruvate dehydrogenase [NADP(+)]","1.2.1.51","4Fe-4S, Electron transport, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat, Thiamine pyrophosphate, Transport",11319255,"Cryptosporidium parvum","KSU-1",9,1175,1177,7,1242,1934]
[null,"P52965","_",0.99917,1.01784,45.83,0,7,5,"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",1,1175,1177,1,1174,1199]
[null,"Q06879","IPMed?",1.01084,1.02974,44.97,0,9,5,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8415612, 11759840","Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)","PCC 7120 / SAG 25.82 / UTEX 2576",8,1174,1177,7,1197,1199]
[null,"Q3M8N0","IPMed?",1,1.01105,46.05,0,8,4,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","25197444, 8352652","Trichormus variabilis (strain ATCC 29413 / PCC 7937)","ATCC 29413 / PCC 7937",8,1177,1177,8,1186,1190]
[null,"P52647","IPMed?",1.0102,1.01278,44.91,0,10,3,"ydbK","Probable pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","9097039, 9278503, 16738553, 9025293","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",8,1174,1177,3,1165,1174]
[null,"Q53046","IPMed?",1,1.01189,44.5,0,11,6,"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",9,1174,1177,9,1178,1191]
[]
["ACT01_02810","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P19543","IPMed?",0.99915,1.00171,58.45,0,1,4,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Plasmid, Repeat, Transport","2504647, 1708766","Enterobacter agglomerans","333 / 333",7,1166,1170,6,1173,1173]
[null,"P03833","IPMed?",0.99231,0.99316,57.92,0,2,4,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","3062178, 3060860, 8483412, 6306580","Klebsiella pneumoniae","_",7,1163,1170,6,1167,1171]
[null,"Q2RMD6","IPMed?",1,1.00085,57.64,0,3,4,"_","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",7,1165,1170,4,1170,1171]
[null,"P94692","IPMed?",0.94724,0.99744,52.1,0,4,6,"por","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Calcium, Cytoplasm, Direct protein sequencing, Disulfide bond, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Thiamine pyrophosphate, Transport","9294422, 7612653, 10048931, 11752578, 16472741","Desulfocurvibacter africanus","ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi / ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi",1,1158,1170,1,1161,1232]
[null,"Q94IN5","IPMed?",0.65225,1.00513,47.7,0,5,5,"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",4,1170,1170,67,1239,1803]
[null,"Q968X7","IPMed?",0.63857,1.05556,45.67,0,6,4,"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",9,1158,1170,7,1235,1934]
[null,"Q06879","IPMed?",1,1.02479,45.12,0,7,7,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8415612, 11759840","Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)","PCC 7120 / SAG 25.82 / UTEX 2576",6,1160,1170,5,1193,1199]
[null,"Q3M8N0","IPMed?",1,1.01709,45.21,0,9,6,"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",1,1160,1170,1,1179,1190]
[null,"P52965","_",0.98415,1.00855,46.19,0,8,6,"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",1,1165,1170,1,1174,1199]
[null,"Q53046","IPMed?",0.99916,1.01709,43.95,0,10,7,"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",1,1170,1170,1,1184,1191]
[null,"P52647","IPMed?",0.99659,1,42.48,0,11,7,"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",8,1158,1170,3,1159,1174]
[]
["ACT01_03520","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?",0.99576,1.00342,54.89,0,1,6,"_","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Reference proteome, Transport","18631365, 9214293, 10878009, 29581263","Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320 / ATCC 39073 / JCM 9320",10,1177,1180,4,1169,1171]
[null,"P19543","IPMed?",0.99831,1.00426,54.33,0,2,5,"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",9,1178,1180,5,1172,1173]
[null,"P03833","IPMed?",0.99576,1.00342,54.38,0,3,5,"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","_",9,1179,1180,5,1170,1171]
[null,"P94692","IPMed?",0.96104,1.00339,52.36,0,4,4,"por","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Calcium, Cytoplasm, Direct protein sequencing, Disulfide bond, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Thiamine pyrophosphate, Transport","9294422, 7612653, 10048931, 11752578, 16472741","Desulfocurvibacter africanus","ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi / ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi",7,1178,1180,3,1168,1232]
[null,"Q94IN5","IPMed?",0.65336,0.99831,47.71,0,5,4,"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",7,1176,1180,67,1232,1803]
[null,"Q06879","IPMed?",1.00417,1.02034,45.6,0,6,3,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8415612, 11759840","Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)","PCC 7120 / SAG 25.82 / UTEX 2576",11,1178,1180,7,1198,1199]
[null,"P52965","_",0.98666,1.00254,45.9,0,7,3,"nifJ","Putative pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8590279, 8905231","Synechocystis sp. (strain PCC 6803 / Kazusa)","ATCC 27184 / PCC 6803 / N-1 / PCC 6803 / Kazusa",11,1177,1180,8,1173,1199]
[null,"Q968X7","IPMed?",0.64168,1.05169,45.37,0,8,6,"PFOR","Pyruvate dehydrogenase [NADP(+)]","1.2.1.51","4Fe-4S, Electron transport, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat, Thiamine pyrophosphate, Transport",11319255,"Cryptosporidium parvum","KSU-1",12,1180,1180,7,1244,1934]
[null,"Q3M8N0","IPMed?",1.00168,1.01017,45.89,0,9,5,"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",11,1178,1180,8,1184,1190]
[null,"P52647","IPMed?",1.00763,1.01278,44.41,0,10,4,"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",9,1179,1180,1,1167,1174]
[null,"Q53046","IPMed?",1.00336,1.01271,44.69,0,11,5,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8736535, 21886856","Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)","ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1",9,1177,1180,6,1178,1191]
[]
["ACT01_06665","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P19543","IPMed?",0.99915,1.00171,66.21,0,1,1,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Plasmid, Repeat, Transport","2504647, 1708766","Enterobacter agglomerans","333 / 333",1,1166,1170,1,1170,1173]
[null,"P03833","IPMed?",0.99829,0.99915,63.73,0,2,2,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","3062178, 3060860, 8483412, 6306580","Klebsiella pneumoniae","_",1,1166,1170,1,1167,1171]
[null,"Q2RMD6","IPMed?",1.00342,1.00427,60.17,0,3,2,"_","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Reference proteome, Transport","18631365, 9214293, 10878009, 29581263","Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320 / ATCC 39073 / JCM 9320",7,1168,1170,5,1170,1171]
[null,"P94692","IPMed?",0.9513,1.00171,57.51,0,4,1,"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",1,1166,1170,1,1163,1232]
[null,"Q94IN5","IPMed?",0.64892,1,48.55,0,5,2,"PNO","Pyruvate dehydrogenase [NADP(+)], mitochondrial","1.2.1.51","4Fe-4S, Direct protein sequencing, Electron transport, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, Mitochondrion, NADP, Oxidoreductase, Repeat, Thiamine pyrophosphate, Transit peptide, Transport","11023353, 11319255, 1910287, 8373179, 3110154, 12623066","Euglena gracilis","SAG1224-5/25",7,1168,1170,71,1234,1803]
[null,"Q968X7","IPMed?",0.64529,1.06667,46.71,0,6,2,"PFOR","Pyruvate dehydrogenase [NADP(+)]","1.2.1.51","4Fe-4S, Electron transport, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat, Thiamine pyrophosphate, Transport",11319255,"Cryptosporidium parvum","KSU-1",1,1168,1170,1,1242,1934]
[null,"Q3M8N0","IPMed?",0.9958,1.01282,48.27,0,7,2,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","25197444, 8352652","Trichormus variabilis (strain ATCC 29413 / PCC 7937)","ATCC 29413 / PCC 7937",7,1170,1170,8,1186,1190]
[null,"Q06879","IPMed?",1.00834,1.03333,47.73,0,8,2,"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",1,1169,1170,1,1199,1199]
[null,"P52965","_",0.97998,1.00427,47.91,0,9,2,"nifJ","Putative pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8590279, 8905231","Synechocystis sp. (strain PCC 6803 / Kazusa)","ATCC 27184 / PCC 6803 / N-1 / PCC 6803 / Kazusa",7,1169,1170,8,1175,1199]
[null,"Q53046","IPMed?",0.99748,1.01538,45.96,0,10,2,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8736535, 21886856","Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)","ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1",3,1166,1170,4,1177,1191]
[null,"P52647","IPMed?",1.00681,1.01026,46.02,0,11,1,"ydbK","Probable pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","9097039, 9278503, 16738553, 9025293","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",5,1169,1170,1,1167,1174]
[]
["ACT01_12570","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P19543","IPMed?",1,1.00256,65.98,0,1,2,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Plasmid, Repeat, Transport","2504647, 1708766","Enterobacter agglomerans","333 / 333",1,1167,1170,1,1171,1173]
[null,"P03833","IPMed?",0.99915,1,63.76,0,2,1,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","3062178, 3060860, 8483412, 6306580","Klebsiella pneumoniae","_",1,1167,1170,1,1168,1171]
[null,"Q2RMD6","IPMed?",1.00683,1.00769,60.31,0,3,1,"_","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Reference proteome, Transport","18631365, 9214293, 10878009, 29581263","Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320 / ATCC 39073 / JCM 9320",3,1168,1170,1,1170,1171]
[null,"P94692","IPMed?",0.95211,1.00256,56.86,0,4,2,"por","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Calcium, Cytoplasm, Direct protein sequencing, Disulfide bond, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Thiamine pyrophosphate, Transport","9294422, 7612653, 10048931, 11752578, 16472741","Desulfocurvibacter africanus","ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi / ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi",1,1167,1170,1,1167,1232]
[null,"Q94IN5","IPMed?",0.65169,1.00427,48.68,0,5,1,"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",2,1168,1170,66,1234,1803]
[null,"Q3M8N0","IPMed?",0.9958,1.01282,48.52,0,6,1,"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",7,1170,1170,8,1186,1190]
[null,"Q968X7","IPMed?",0.64168,1.06068,46.82,0,7,1,"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",8,1168,1170,7,1242,1934]
[null,"Q06879","IPMed?",1.00834,1.03333,47.81,0,8,1,"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",1,1169,1170,1,1199,1199]
[null,"P52965","_",0.97998,1.00427,48.17,0,9,1,"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",7,1169,1170,8,1175,1199]
[null,"Q53046","IPMed?",0.99748,1.01538,46.3,0,10,1,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8736535, 21886856","Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)","ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1",4,1167,1170,5,1178,1191]
[null,"P52647","IPMed?",1.00681,1.01026,46.11,0,11,2,"ydbK","Probable pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","9097039, 9278503, 16738553, 9025293","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",5,1169,1170,1,1167,1174]
[]
["ACT01_05435","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q895N2","_",0.9925,1,63.48,0,1,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase",12552129,"Clostridium tetani (strain Massachusetts / E88)","Massachusetts / E88",1,396,397,1,397,400]
[null,"C1FSN0","_",1,1,63.98,{"v":1E-180,"d":"1.00E-180"},2,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase","_","Clostridium botulinum (strain Kyoto / Type A2)","_",1,397,397,1,397,397]
[null,"B1KWP9","_",1,1,63.98,{"v":3e-180,"d":"3.00E-180"},3,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase",18060065,"Clostridium botulinum (strain Loch Maree / Type A3)","Loch Maree / Type A3",1,397,397,1,397,397]
[null,"C3L0F7","_",1,1,63.73,{"v":4e-180,"d":"4.00E-180"},4,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase","_","Clostridium botulinum (strain 657 / Type Ba4)","_",1,397,397,1,397,397]
[null,"A7FW24","_",1,1,63.73,{"v":2E-179,"d":"2.00E-179"},5,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase",18060065,"Clostridium botulinum (strain ATCC 19397 / Type A)","ATCC 19397 / Type A",1,397,397,1,397,397]
[null,"A5I4N7","_",1,1,63.73,{"v":2E-179,"d":"2.00E-179"},5,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","17519437, 18060065","Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)","Hall / ATCC 3502 / NCTC 13319 / Type A / Hall / ATCC 3502 / NCTC 13319 / Type A",1,397,397,1,397,397]
[null,"A7GG48","_",1,1,63.22,{"v":1e-178,"d":"1.00E-178"},6,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase","_","Clostridium botulinum (strain Langeland / NCTC 10281 / Type F)","_",1,397,397,1,397,397]
[null,"B1II90","_",1,1,63.48,{"v":2e-178,"d":"2.00E-178"},7,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Transferase",18060065,"Clostridium botulinum (strain Okra / Type B1)","Okra / Type B1",1,397,397,1,397,397]
[null,"Q8XJN2","_",1,1.00252,62.06,{"v":2e-177,"d":"2.00E-177"},8,1,"ackA2","Acetate kinase 2","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase",11792842,"Clostridium perfringens (strain 13 / Type A)","13 / Type A",1,397,397,1,398,398]
[null,"A0Q0Z5","_",0.99002,1,62.72,{"v":9E-176,"d":"9.00E-176"},9,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase",17115055,"Clostridium novyi (strain NT)","NT",1,397,397,1,397,401]
[null,"A6TRU6","_",0.99748,1,60.1,{"v":6E-175,"d":"6.00E-175"},10,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase",27811105,"Alkaliphilus metalliredigens (strain QYMF)","QYMF",1,395,397,1,396,396]
[null,"Q9WYB1","IPMed?",0.99256,1.00756,57.5,{"v":1E-165,"d":"1.00E-165"},11,1,"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",1,397,397,1,400,403]
[null,"P38502","IPMed?",0.97059,0.99748,58.08,{"v":4E-165,"d":"4.00E-165"},12,1,"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",1,395,397,1,396,408]
[null,"P71104","IPMed?",0.99751,1.00756,54,{"v":3e-155,"d":"3.00E-155"},13,1,"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",4,397,397,4,399,401]
[null,"P37877","IPMed?",0.98741,0.99241,55.61,{"v":1e-154,"d":"1.00E-154"},14,1,"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",3,394,397,4,393,395]
[null,"P74879","IPMed?",0.9703,0.98741,47.19,{"v":2e-129,"d":"2.00E-129"},15,1,"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",3,394,397,5,392,404]
[null,"Q9X4M1","IPMed?",0.98992,0.99746,47.84,{"v":3e-121,"d":"3.00E-121"},16,1,"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",3,394,397,4,393,394]
[null,"P77845","IPMed?",0.98741,0.98741,46.17,{"v":5e-113,"d":"5.00E-113"},17,1,"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",2,389,397,3,391,397]
[null,"P0A6A3","IPMed?",1.0025,1.01008,44.39,{"v":5e-104,"d":"5.00E-104"},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",2,396,397,5,400,400]
[null,"P63411","IPMed?",1.0025,1.01008,43.39,{"v":1e-102,"d":"1.00E-102"},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",2,396,397,5,400,400]
[null,"Q49113","IPMed?",0.99748,1.00763,40.66,{"v":4e-98,"d":"4.00E-98"},20,1,"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)","_",2,395,397,1,392,393]
[]
["ACT01_13325","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P71103","IPMed?",0.94767,0.97898,46.32,{"v":3e-91,"d":"3.00E-91"},1,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","8702268, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,326,344,1,324,333]
[null,"O83132","_",0.9593,0.98214,48.48,{"v":4E-90,"d":"4.00E-90"},2,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",9665876,"Treponema pallidum (strain Nichols)","Nichols",1,326,344,1,328,336]
[null,"Q59330","_",0.96221,1.00915,47.43,{"v":1E-89,"d":"1.00E-89"},3,1,"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)","_",1,331,344,1,327,328]
[null,"P38503","IPMed?",0.96802,1,45.35,{"v":9e-87,"d":"9.00E-87"},4,1,"pta","Phosphate acetyltransferase","2.3.1.8","3D-structure, Acyltransferase, Cell membrane, Direct protein sequencing, Membrane, Transferase","8226623, 9401029, 15062079","Methanosarcina thermophila","ATCC 43570 / DSM 1825 / OCM 12 / TM-1",3,335,344,4,332,333]
[null,"O52593","_",0.97093,1.00602,43.41,{"v":2e-83,"d":"2.00E-83"},5,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","_","Hungateiclostridium thermocellum (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)","_",1,331,344,1,327,332]
[null,"Q5HRF7","_",0.96802,1.01216,42.34,{"v":1e-74,"d":"1.00E-74"},6,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",15774886,"Staphylococcus epidermidis (strain ATCC 35984 / RP62A)","ATCC 35984 / RP62A",7,332,344,8,328,329]
[null,"Q6GJ80","_",0.96221,1.00915,40.79,{"v":2e-74,"d":"2.00E-74"},7,1,"pta","Phosphate acetyltransferase","2.3.1.8","3D-structure, Acyltransferase, Cytoplasm, Transferase",15213324,"Staphylococcus aureus (strain MRSA252)","MRSA252",7,332,344,8,327,328]
[null,"Q8CQ62","_",0.96802,1.01216,42.04,{"v":6e-74,"d":"6.00E-74"},8,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",12950922,"Staphylococcus epidermidis (strain ATCC 12228)","ATCC 12228",7,332,344,8,328,329]
[null,"P65862","_",0.96221,1.00915,40.48,{"v":8e-74,"d":"8.00E-74"},9,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",11418146,"Staphylococcus aureus (strain Mu50 / ATCC 700699)","Mu50 / ATCC 700699",7,332,344,8,327,328]
[null,"P99092","_",0.96221,1.00915,40.48,{"v":8e-74,"d":"8.00E-74"},9,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase","11418146, 15590099","Staphylococcus aureus (strain N315)","N315 / N315",7,332,344,8,327,328]
[null,"Q5HI88","_",0.96221,1.00915,40.48,{"v":8e-74,"d":"8.00E-74"},9,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",15774886,"Staphylococcus aureus (strain COL)","COL",7,332,344,8,327,328]
[null,"Q8NXW4","_",0.96221,1.00915,40.48,{"v":1E-73,"d":"1.00E-73"},10,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",12044378,"Staphylococcus aureus (strain MW2)","MW2",7,332,344,8,327,328]
[null,"Q6GBP8","_",0.96221,1.00915,40.48,{"v":1E-73,"d":"1.00E-73"},10,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Cytoplasm, Transferase",15213324,"Staphylococcus aureus (strain MSSA476)","MSSA476",7,332,344,8,327,328]
[null,"P41790","IPMed?",0.92151,0.93787,42.9,{"v":2e-68,"d":"2.00E-68"},11,1,"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",13,326,344,12,318,338]
[null,"P77844","IPMed?",0.9564,1,39.82,{"v":1e-67,"d":"1.00E-67"},12,1,"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",3,331,344,6,325,329]
[null,"P39197","IPMed?",0.90407,0.97799,39.87,{"v":2e-63,"d":"2.00E-63"},13,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Cytoplasm, Transferase",7480167,"Paracoccus denitrificans","_",16,326,344,16,312,318]
[null,"Q8ZND6","IPMed?",0.46359,0.96221,39.58,{"v":3e-61,"d":"3.00E-61"},14,1,"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",3,331,344,391,709,714]
[null,"P0A9M8","IPMed?",0.45518,0.94477,40,{"v":6e-60,"d":"6.00E-60"},15,1,"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",3,326,344,392,705,714]
[null,"Q9I5A5","IPMed?",0.47869,0.97965,39.76,{"v":3E-57,"d":"3.00E-57"},16,1,"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",3,338,344,380,702,704]
[null,"Q49112","IPMed?",0.93314,0.99689,35.51,{"v":2E-46,"d":"2.00E-46"},17,1,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",8844861,"Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)","_",5,320,344,5,310,322]
[null,"O30808","IPMed?",0.42576,0.94186,30.86,{"v":3e-42,"d":"3.00E-42"},18,2,"tme","NADP-dependent malic enzyme","1.1.1.40","Complete proteome, Metal-binding, Multifunctional enzyme, NADP, Oxidoreductase, Reference proteome","9535928, 11481430, 11474104, 10407149","Rhizobium meliloti (strain 1021)","RCR2011 / SU47 / 1021 / 1021",10,331,344,446,759,761]
[]
["ACT01_04870","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P0A9Q7","IPMed?",0.49495,0.89091,45.8,{"v":2E-120,"d":"2.00E-120"},1,1,"adhE","Alcohol dehydrogenase / Acetaldehyde dehydrogenase [acetylating] / Pyruvate-formate-lyase deactivase","1.1.1.1, 1.2.1.10","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Iron, Multifunctional enzyme, NAD, Oxidoreductase, Reference proteome","2695398, 2015910, 8905232, 9278503, 16738553, 7773397, 7521508, 9298644, 12783863, 18723842","Escherichia coli (strain K12)","K12 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / JW1106",11,445,495,6,445,891]
[null,"P0A9Q8","_",0.49495,0.89091,45.8,{"v":2E-120,"d":"2.00E-120"},1,1,"adhE","Alcohol dehydrogenase / Acetaldehyde dehydrogenase [acetylating] / Pyruvate-formate-lyase deactivase","1.1.1.1, 1.2.1.10","Acetylation, Complete proteome, Iron, Multifunctional enzyme, NAD, Oxidoreductase, Reference proteome","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",11,445,495,6,445,891]
[null,"P33744","IPMed?",0.51276,0.89293,44.57,{"v":1e-112,"d":"1.00E-112"},2,1,"adhE","Alcohol dehydrogenase / Aldehyde dehydrogenase","1.1.1.1, 1.2.1.3","Complete proteome, Multifunctional enzyme, NAD, Oxidoreductase, Plasmid, Reference proteome","8226639, 8300540, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",10,445,495,5,443,862]
[null,"Q24803","IPMed?",0.51609,0.90707,43.88,{"v":4e-106,"d":"4.00E-106"},3,1,"ADH2","Alcohol dehydrogenase / Acetaldehyde dehydrogenase","1.1.1.1, 1.2.1.10","Direct protein sequencing, Iron, Multifunctional enzyme, NAD, Oxidoreductase","7935603, 7980441","Entamoeba histolytica","ATCC 30459 / HM-1:IMSS / ATCC 30459 / HM-1:IMSS",10,445,495,8,456,870]
[null,"P38947","IPMed?",0.88889,0.9713,37.95,{"v":2e-98,"d":"2.00E-98"},4,1,"sucD","Succinate-semialdehyde dehydrogenase (acetylating)","1.2.1.76","Complete proteome, Direct protein sequencing, NADP, Oxidoreductase, Reference proteome","8550525, 18218779","Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)","ATCC 8527 / DSM 555 / NCIMB 10680",15,452,495,8,444,453]
[null,"Q0K845","IPMed?",0.89697,0.90061,35.36,{"v":3E-68,"d":"3.00E-68"},5,1,"sauS","Sulfoacetaldehyde dehydrogenase (acylating)","1.2.1.81","Complete proteome, Cytoplasm, Direct protein sequencing, NADP, Oxidoreductase, Reference proteome","16964242, 20693281","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337",18,453,495,42,478,493]
[null,"P77445","_",0.74545,0.79015,30.08,{"v":3e-41,"d":"3.00E-41"},6,1,"eutE","Ethanolamine utilization protein EutE","_","Complete proteome, Oxidoreductase, Reference proteome","9205837, 9278503, 16738553","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",48,409,495,68,428,467]
[null,"P41793","IPMed?",0.68889,0.73019,30.5,{"v":3e-40,"d":"3.00E-40"},7,1,"eutE","Ethanolamine utilization protein EutE","_","Complete proteome, Oxidoreductase, Reference proteome","7868611, 10464203, 11677609","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","ATCC 14028s / SGSG 2262 / LT2 / LT2 / SGSC1412 / ATCC 700720",48,381,495,68,400,467]
[null,"Q6L285","IPMed?",0.83838,0.84178,22.65,5e-12,8,2,"_","D-glyceraldehyde dehydrogenase (NADP(+))","1.2.1.89","Complete proteome, NADP, Oxidoreductase, Reference proteome","15184674, 16458304","Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)","ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828",24,412,495,47,447,493]
[null,"P94358","IPMed?",0.60808,0.62062,22.59,8e-12,9,2,"aldY","Putative aldehyde dehydrogenase AldY","1.2.1.3","3D-structure, Complete proteome, NAD, Oxidoreductase, Reference proteome, Stress response","8969509, 9384377, 10482513, 26658822","Bacillus subtilis (strain 168)","168 / BGSC1A1 / 168 / 168 / 3NA",21,313,495,53,345,485]
[null,"P71016","IPMed?",0.50101,0.50612,25.81,1e-11,10,2,"gbsA","Betaine aldehyde dehydrogenase","1.2.1.8","Complete proteome, Direct protein sequencing, NAD, Oxidoreductase, Reference proteome","8752328, 9384377, 9297465, 22408163, 26658822","Bacillus subtilis (strain 168)","168 / JH642 / 168 / 168 / JH642 / 168 / 3NA",38,274,495,68,306,490]
[null,"Q58806","IPMed?",0.53535,0.57235,23.77,2e-11,11,2,"_","Lactaldehyde dehydrogenase","1.2.1.22","3D-structure, Complete proteome, NAD, Oxidoreductase, Reference proteome","8688087, 16585745","Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440",12,271,495,33,294,463]
[]
["ACT01_02465","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P38105","IPMed?",1.00295,1.00295,45.29,{"v":5e-98,"d":"5.00E-98"},1,1,"rspB","Starvation-sensing protein RspB","1.1.1.-","Complete proteome, Metal-binding, Oxidoreductase, Reference proteome, Zinc","7545940, 9097039, 9278503, 16738553, 22972332","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 / W3110 / ATCC 27325 / DSM 5911",1,338,339,1,337,339]
[null,"O35045","IPMed?",1.00295,1.00295,43.82,{"v":4E-95,"d":"4.00E-95"},2,1,"yjmD","Uncharacterized zinc-type alcohol dehydrogenase-like protein YjmD","1.-.-.-","Complete proteome, Metal-binding, Oxidoreductase, Reference proteome, Zinc","9579062, 9384377, 9882655","Bacillus subtilis (strain 168)","168 / 168 / 168 / MB24",1,339,339,1,339,339]
[null,"Q57517","_",0.99415,1.00295,37.94,{"v":2E-70,"d":"2.00E-70"},3,1,"_","Uncharacterized zinc-type alcohol dehydrogenase-like protein HI_0053","1.-.-.-","Complete proteome, Metal-binding, Oxidoreductase, Reference proteome, Zinc",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",1,338,339,5,342,342]
[null,"Q06004","IPMed?",0.96884,1.00885,32.46,{"v":1E-59,"d":"1.00E-59"},4,1,"gutB","Sorbitol dehydrogenase","1.1.1.-","Complete proteome, Direct protein sequencing, Metal-binding, NAD, Oxidoreductase, Reference proteome, Zinc","1460002, 9384377, 8195086","Bacillus subtilis (strain 168)","168 / 168 / 168",1,336,339,9,349,353]
[null,"Q8KQL2","IPMed?",0.93182,0.96755,34.45,{"v":3e-54,"d":"3.00E-54"},5,1,"_","D-arabitol-phosphate dehydrogenase","1.1.1.301","Manganese, Metal-binding, NAD, NADP, Oxidoreductase, Zinc",12467497,"Enterococcus avium","ATCC 35665 / DSM 20063",1,321,339,5,332,352]
[null,"P39400","IPMed?",1,1.00295,31.18,{"v":3e-53,"d":"3.00E-53"},6,1,"lgoD","L-galactonate-5-dehydrogenase","1.1.1.414","Complete proteome, Metal-binding, NAD, Oxidoreductase, Reference proteome, Zinc","7610040, 9278503, 16738553, 17088549, 24861318","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",1,338,339,4,340,340]
[null,"B4F134","_",0.94721,0.9528,33.75,{"v":3e-50,"d":"3.00E-50"},7,1,"tdh","L-threonine 3-dehydrogenase","1.1.1.103","Complete proteome, Cytoplasm, Metal-binding, NAD, Oxidoreductase, Zinc",18375554,"Proteus mirabilis (strain HI4320)","HI4320",8,321,339,10,325,341]
[null,"P77280","_",0.97695,1,31.27,{"v":8e-50,"d":"8.00E-50"},8,1,"ydjJ","Uncharacterized zinc-type alcohol dehydrogenase-like protein YdjJ","1.-.-.-","3D-structure, Complete proteome, Metal-binding, Oxidoreductase, Reference proteome, Zinc","9097039, 9278503, 16738553","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",5,336,339,7,343,347]
[null,"Q5JI69","IPMed?",0.94571,0.9764,35.95,{"v":2e-49,"d":"2.00E-49"},9,1,"tdh","L-threonine 3-dehydrogenase","1.1.1.103","3D-structure, Complete proteome, Cytoplasm, Metal-binding, NAD, Oxidoreductase, Reference proteome, Zinc","15710748, 19307254, 19616102","Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)","ATCC BAA-918 / JCM 12380 / KOD1 / ATCC BAA-918 / JCM 12380 / KOD1",1,321,339,5,332,350]
[null,"Q07W50","_",0.84164,0.84661,36.93,{"v":4e-49,"d":"4.00E-49"},10,1,"tdh","L-threonine 3-dehydrogenase","1.1.1.103","Complete proteome, Cytoplasm, Metal-binding, NAD, Oxidoreductase, Reference proteome, Zinc","_","Shewanella frigidimarina (strain NCIMB 400)","_",1,282,339,1,285,341]
[null,"Q1PSI9","IPMed?",0.86066,0.9292,31.11,{"v":1e-48,"d":"1.00E-48"},11,1,"_","L-idonate 5-dehydrogenase","1.1.1.366","Complete proteome, Metal-binding, NAD, Oxidoreductase, Reference proteome, Zinc","16567629, 17721507, 18094749","Vitis vinifera","cv. Cabernet Sauvignon / cv. Pinot noir / PN40024 / cv. Pinot noir",19,323,339,38,350,366]
[null,"P27867","IPMed?",0.92157,0.9705,35.26,{"v":2e-48,"d":"2.00E-48"},12,1,"Sord","Sorbitol dehydrogenase","1.1.1.-","Acetylation, Cell projection, Cilium, Complete proteome, Flagellum, Membrane, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Phosphoprotein, Reference proteome, Zinc","2050152, 8223590, 15489334, 6862079, 22673903, 11306057","Rattus norvegicus","Sprague-Dawley",3,321,339,11,335,357]
[null,"O58389","IPMed?",0.95115,0.9764,35.65,{"v":3e-48,"d":"3.00E-48"},13,1,"tdh","L-threonine 3-dehydrogenase","1.1.1.103","3D-structure, Complete proteome, Cytoplasm, Metal-binding, NAD, NADP, Oxidoreductase, Zinc","9679194, 15902509, 16233775, 18390572, 17188300","Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)","ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3 / ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3",1,321,339,5,332,348]
[null,"Q8U259","IPMed?",0.94828,0.97345,35.15,{"v":9e-48,"d":"9.00E-48"},14,1,"tdh","L-threonine 3-dehydrogenase","1.1.1.103","Complete proteome, Cytoplasm, Metal-binding, NAD, Oxidoreductase, Reference proteome, Zinc","10430560, 16817900","Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)","ATCC 43587 / DSM 3638 / JCM 8422 / Vc1",1,321,339,5,332,348]
[]
["ACT01_03450","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P35497","IPMed?",0.94678,0.9883,33.73,{"v":3e-53,"d":"3.00E-53"},1,1,"SOR1","Sorbitol dehydrogenase 1","1.1.1.-","Complete proteome, Metal-binding, NAD, Oxidoreductase, Reference proteome, Zinc","8125328, 8641269, 24374639, 17322287","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 204508 / S288c",15,340,342,19,353,357]
[null,"Q07993","IPMed?",0.97191,1.0117,34.39,{"v":7e-53,"d":"7.00E-53"},2,1,"XYL2","D-xylulose reductase","1.1.1.9","Carbohydrate metabolism, Complete proteome, Metal-binding, NAD, Oxidoreductase, Reference proteome, Xylose metabolism, Zinc","9169871, 24374639, 10486580","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c",6,341,342,12,353,356]
[null,"Q07786","_",0.94678,0.9883,33.43,{"v":2E-52,"d":"2.00E-52"},3,1,"SOR2","Sorbitol dehydrogenase 2","1.1.1.-","Complete proteome, Metal-binding, NAD, Oxidoreductase, Reference proteome, Zinc","9169867, 24374639","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c",15,340,342,19,353,357]
[null,"Q06004","IPMed?",0.89518,0.92398,32.59,{"v":7e-51,"d":"7.00E-51"},4,2,"gutB","Sorbitol dehydrogenase","1.1.1.-","Complete proteome, Direct protein sequencing, Metal-binding, NAD, Oxidoreductase, Reference proteome, Zinc","1460002, 9384377, 8195086","Bacillus subtilis (strain 168)","168 / 168 / 168",15,326,342,22,335,353]
[null,"Q5ARL6","_",0.92479,0.97076,33.13,{"v":8e-51,"d":"8.00E-51"},5,1,"xdhA","Probable D-xylulose reductase A","1.1.1.9","Carbohydrate metabolism, Complete proteome, Metal-binding, NAD, Oxidoreductase, Reference proteome, Xylose metabolism, Zinc","16372000, 19146970","Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)","FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139 / FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139",17,340,342,25,353,359]
[null,"Q0CWQ2","_",0.94051,0.97076,33.73,{"v":1e-49,"d":"1.00E-49"},6,1,"xdhA","Probable D-xylulose reductase A","1.1.1.9","Carbohydrate metabolism, Complete proteome, Metal-binding, NAD, Oxidoreductase, Reference proteome, Xylose metabolism, Zinc","_","Aspergillus terreus (strain NIH 2624 / FGSC A1156)","_",17,340,342,20,348,353]
[null,"A1CFY8","_",0.92737,0.97076,33.43,{"v":1e-49,"d":"1.00E-49"},7,1,"xdhA","Probable D-xylulose reductase A","1.1.1.9","Carbohydrate metabolism, Complete proteome, Metal-binding, NAD, Oxidoreductase, Reference proteome, Xylose metabolism, Zinc",18404212,"Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)","ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1",17,340,342,25,353,358]
[null,"Q86ZV0","IPMed?",0.92737,0.97076,33.73,{"v":6E-49,"d":"6.00E-49"},8,1,"xdhA","D-xylulose reductase A","1.1.1.9","Carbohydrate metabolism, Complete proteome, Metal-binding, NAD, Oxidoreductase, Reference proteome, Xylose metabolism, Zinc","16233653, 16372010","Aspergillus oryzae (strain ATCC 42149 / RIB 40)","ATCC 42149 / RIB 40",17,340,342,25,353,358]
[null,"C5FTT1","_",0.97191,1.0117,33.82,{"v":8e-49,"d":"8.00E-49"},9,1,"xdhA","Probable D-xylulose reductase A","1.1.1.9","Carbohydrate metabolism, Complete proteome, Metal-binding, NAD, Oxidoreductase, Reference proteome, Xylose metabolism, Zinc",22951933,"Arthroderma otae (strain ATCC MYA-4605 / CBS 113480)","ATCC MYA-4605 / CBS 113480",5,340,342,11,351,356]
[null,"Q4WAU7","_",0.92737,0.97076,33.43,{"v":9e-49,"d":"9.00E-49"},10,1,"xdhA","Probable D-xylulose reductase A","1.1.1.9","Carbohydrate metabolism, Complete proteome, Metal-binding, NAD, Oxidoreductase, Reference proteome, Xylose metabolism, Zinc",16372009,"Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)","ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100",17,340,342,25,353,358]
[null,"B0YC65","_",0.92737,0.97076,33.43,{"v":9e-49,"d":"9.00E-49"},10,1,"xdhA","Probable D-xylulose reductase A","1.1.1.9","Carbohydrate metabolism, Complete proteome, Metal-binding, NAD, Oxidoreductase, Xylose metabolism, Zinc",18404212,"Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163)","CEA10 / CBS 144.89 / FGSC A1163",17,340,342,25,353,358]
[null,"O34788","IPMed?",0.90462,0.9152,36.74,{"v":1e-47,"d":"1.00E-47"},11,1,"bdhA","(R,R)-butanediol dehydrogenase","1.1.1.4","Complete proteome, Metal-binding, NAD, Oxidoreductase, Reference proteome, Zinc","9455482, 9384377, 18820069","Bacillus subtilis (strain 168)","168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501 / 168 / 168",15,315,342,14,318,346]
[null,"Q1PSI9","IPMed?",0.81967,0.87719,34,{"v":4e-47,"d":"4.00E-47"},12,2,"_","L-idonate 5-dehydrogenase","1.1.1.366","Complete proteome, Metal-binding, NAD, Oxidoreductase, Reference proteome, Zinc","16567629, 17721507, 18094749","Vitis vinifera","cv. Cabernet Sauvignon / cv. Pinot noir / PN40024 / cv. Pinot noir",28,320,342,45,343,366]
[null,"Q8KQL2","IPMed?",0.86648,0.89181,33.44,{"v":3e-44,"d":"3.00E-44"},13,2,"_","D-arabitol-phosphate dehydrogenase","1.1.1.301","Manganese, Metal-binding, NAD, NADP, Oxidoreductase, Zinc",12467497,"Enterococcus avium","ATCC 35665 / DSM 20063",26,326,342,30,333,352]
[null,"O35045","IPMed?",0.95322,0.96165,29.14,{"v":3E-43,"d":"3.00E-43"},14,2,"yjmD","Uncharacterized zinc-type alcohol dehydrogenase-like protein YjmD","1.-.-.-","Complete proteome, Metal-binding, Oxidoreductase, Reference proteome, Zinc","9579062, 9384377, 9882655","Bacillus subtilis (strain 168)","168 / 168 / 168 / MB24",17,342,342,16,338,339]
[null,"Q02912","IPMed?",0.91379,0.92982,31.13,{"v":4e-42,"d":"4.00E-42"},15,1,"SDH","Sorbitol dehydrogenase","1.1.1.-","Complete proteome, Metal-binding, NAD, Oxidoreductase, Reference proteome, Stress response, Zinc","8504807, 8933178","Bombyx mori","Tokai X Asahi",15,326,342,17,332,348]
[null,"P36624","IPMed?",0.94167,0.99123,30.68,{"v":4e-40,"d":"4.00E-40"},16,1,"tms1","Sorbitol dehydrogenase","1.1.1.-","Complete proteome, Metal-binding, NAD, Oxidoreductase, Reference proteome, Zinc","11859360, 8223615","Schizosaccharomyces pombe (strain 972 / ATCC 24843)","972 / ATCC 24843 / 972 / ATCC 24843",15,340,342,18,355,360]
[]
["ACT01_04805","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P13604","IPMed?",1.00773,1.03439,36.32,{"v":3e-77,"d":"3.00E-77"},1,1,"adh1","NADPH-dependent butanol dehydrogenase","1.1.1.-","NADP, Oxidoreductase",2673928,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",1,378,378,1,381,388]
[null,"Q24803","IPMed?",0.46437,1.06878,39.6,{"v":2e-76,"d":"2.00E-76"},2,3,"ADH2","Alcohol dehydrogenase / Acetaldehyde dehydrogenase","1.1.1.1, 1.2.1.10","Direct protein sequencing, Iron, Multifunctional enzyme, NAD, Oxidoreductase","7935603, 7980441","Entamoeba histolytica","ATCC 30459 / HM-1:IMSS / ATCC 30459 / HM-1:IMSS",4,378,378,465,866,870]
[null,"P0A9Q7","IPMed?",0.4523,1.06614,37.97,{"v":6E-65,"d":"6.00E-65"},3,3,"adhE","Alcohol dehydrogenase / Acetaldehyde dehydrogenase [acetylating] / Pyruvate-formate-lyase deactivase","1.1.1.1, 1.2.1.10","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Iron, Multifunctional enzyme, NAD, Oxidoreductase, Reference proteome","2695398, 2015910, 8905232, 9278503, 16738553, 7773397, 7521508, 9298644, 12783863, 18723842","Escherichia coli (strain K12)","K12 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / JW1106",10,378,378,460,862,891]
[null,"P0A9Q8","_",0.4523,1.06614,37.97,{"v":6E-65,"d":"6.00E-65"},3,3,"adhE","Alcohol dehydrogenase / Acetaldehyde dehydrogenase [acetylating] / Pyruvate-formate-lyase deactivase","1.1.1.1, 1.2.1.10","Acetylation, Complete proteome, Iron, Multifunctional enzyme, NAD, Oxidoreductase, Reference proteome","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",10,378,378,460,862,891]
[null,"P0DJA2","IPMed?",0.98956,1.00265,36.15,{"v":9E-61,"d":"9.00E-61"},4,2,"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",14,378,378,16,383,383]
[null,"F8DVL8","IPMed?",0.98956,1.00265,36.15,{"v":9E-61,"d":"9.00E-61"},4,2,"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",14,378,378,16,383,383]
[null,"A6ZTT5","_",1.01832,1.0291,34.7,{"v":2e-60,"d":"2.00E-60"},5,2,"ADH4","Alcohol dehydrogenase 4","1.1.1.1","Complete proteome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Zinc",17652520,"Saccharomyces cerevisiae (strain YJM789)","YJM789",4,378,378,7,380,382]
[null,"P10127","IPMed?",1.01832,1.0291,34.45,{"v":2e-59,"d":"2.00E-59"},6,2,"ADH4","Alcohol dehydrogenase 4","1.1.1.1","Complete proteome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Zinc","2823079, 8972578, 9169869, 24374639, 3282541, 10978274, 10884426, 14562095, 14562106, 17139254, 16503288, 17933919, 17938904","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 96604 / S288c / FY1679 / ATCC 204508 / S288c / ATCC 204508 / S288c",4,378,378,7,380,382]
[null,"P33744","IPMed?",0.47332,1.07937,33.09,{"v":2e-56,"d":"2.00E-56"},7,3,"adhE","Alcohol dehydrogenase / Aldehyde dehydrogenase","1.1.1.1, 1.2.1.3","Complete proteome, Multifunctional enzyme, NAD, Oxidoreductase, Plasmid, Reference proteome","8226639, 8300540, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",4,374,378,452,854,862]
[null,"P37686","IPMed?",0.93995,0.95238,35.28,{"v":2E-55,"d":"2.00E-55"},8,2,"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",30,377,378,36,382,383]
[null,"P0A9S1","IPMed?",1.01047,1.02116,33.94,{"v":8e-54,"d":"8.00E-54"},9,2,"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",11,378,378,12,382,382]
[null,"P0A9S2","_",1.01047,1.02116,33.94,{"v":8e-54,"d":"8.00E-54"},9,2,"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",11,378,378,12,382,382]
[null,"A4IP64","IPMed?",0.93418,0.97619,32.79,{"v":2e-53,"d":"2.00E-53"},10,2,"adh1","Long-chain-alcohol dehydrogenase 1","1.1.1.192","Complete proteome, NAD, Oxidoreductase","17372208, 19383697, 24826896","Geobacillus thermodenitrificans (strain NG80-2)","NG80-2 / NG80-2",20,378,378,26,385,395]
[null,"Q09669","IPMed?",0.90521,1.01058,33.25,{"v":8e-52,"d":"8.00E-52"},11,2,"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",12,377,378,57,421,422]
[]
["ACT01_04800","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P0A9Q7","IPMed?",0.56902,0.99217,34.91,{"v":3e-94,"d":"3.00E-94"},1,2,"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",13,506,511,5,508,891]
[null,"P0A9Q8","_",0.56902,0.99217,34.91,{"v":3e-94,"d":"3.00E-94"},1,2,"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",13,506,511,5,508,891]
[null,"P33744","IPMed?",0.5058,0.85323,36.7,{"v":4e-80,"d":"4.00E-80"},2,2,"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",25,455,511,17,449,862]
[null,"P38947","IPMed?",0.84344,0.95143,34.57,{"v":6E-79,"d":"6.00E-79"},3,2,"sucD","Succinate-semialdehyde dehydrogenase (acetylating)","1.2.1.76","Complete proteome, Direct protein sequencing, NADP, Oxidoreductase, Reference proteome","8550525, 18218779","Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)","ATCC 8527 / DSM 555 / NCIMB 10680",20,450,511,10,438,453]
[null,"Q24803","IPMed?",0.4954,0.84344,35.5,{"v":1e-76,"d":"1.00E-76"},4,2,"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",34,455,511,32,462,870]
[null,"Q0K845","IPMed?",0.85127,0.88235,28.74,{"v":3e-47,"d":"3.00E-47"},5,2,"sauS","Sulfoacetaldehyde dehydrogenase (acylating)","1.2.1.81","Complete proteome, Cytoplasm, Direct protein sequencing, NADP, Oxidoreductase, Reference proteome","16964242, 20693281","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337",20,448,511,38,469,493]
[null,"P77445","_",0.81018,0.88651,28.74,{"v":2e-39,"d":"2.00E-39"},6,2,"eutE","Ethanolamine utilization protein EutE","_","Complete proteome, Oxidoreductase, Reference proteome","9205837, 9278503, 16738553","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",27,431,511,46,434,467]
[null,"P41793","IPMed?",0.81018,0.88651,28.02,{"v":3e-38,"d":"3.00E-38"},7,2,"eutE","Ethanolamine utilization protein EutE","_","Complete proteome, Oxidoreductase, Reference proteome","7868611, 10464203, 11677609","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","ATCC 14028s / SGSG 2262 / LT2 / LT2 / SGSC1412 / ATCC 700720",27,431,511,46,434,467]
[null,"Q2BN77","IPMed?",0.84932,0.95175,21.66,2E-8,8,2,"safD","Sulfoacetaldehyde dehydrogenase","1.2.1.73","Complete proteome, Direct protein sequencing, NAD, Oxidoreductase, Reference proteome",18506422,"Neptuniibacter caesariensis","MED92",13,419,511,26,427,456]
[null,"A4XWE7","_",0.47554,0.49897,27.16,2e-07,9,1,"astD","N-succinylglutamate 5-semialdehyde dehydrogenase","1.2.1.71","Arginine metabolism, Complete proteome, NAD, Oxidoreductase, Reference proteome","_","Pseudomonas mendocina (strain ymp)","_",21,251,511,44,275,487]
[null,"Q0SPX8","_",0.36595,0.4506,27.27,3e-07,10,2,"proA","Gamma-glutamyl phosphate reductase","1.2.1.41","Amino-acid biosynthesis, Complete proteome, Cytoplasm, NADP, Oxidoreductase, Proline biosynthesis",16825665,"Clostridium perfringens (strain SM101 / Type A)","SM101 / Type A",110,290,511,113,296,415]
[null,"O06837","IPMed?",0.51859,0.52789,22.64,8e-06,11,3,"styD","Phenylacetaldehyde dehydrogenase","1.2.1.39","NAD, Oxidoreductase",9172343,"Pseudomonas fluorescens","ST",26,274,511,74,327,502]
[null,"Q6L285","IPMed?",0.41096,0.42596,21.9,8e-06,12,3,"_","D-glyceraldehyde dehydrogenase (NADP(+))","1.2.1.89","Complete proteome, NADP, Oxidoreductase, Reference proteome","15184674, 16458304","Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)","ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828",92,291,511,115,317,493]
[null,"O50174","IPMed?",0.44227,0.46407,25.22,4e-05,13,2,"astD","N-succinylglutamate 5-semialdehyde dehydrogenase","1.2.1.71","3D-structure, Arginine metabolism, Complete proteome, NAD, Oxidoreductase, Reference proteome","9393691, 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 / ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1",41,251,511,64,275,487]
[]
["ACT01_05115","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P0A9S5","IPMed?",0.9782,0.98356,44.29,{"v":1e-94,"d":"1.00E-94"},1,1,"gldA","Glycerol dehydrogenase","1.1.1.6","3D-structure, Complete proteome, Direct protein sequencing, Glycerol metabolism, Metal-binding, NAD, Oxidoreductase, Reference proteome, Zinc","8265357, 9278503, 16738553, 17895580, 40950, 8132480, 18179582, 18632294","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12 / MG1655 / ATCC 47076",4,362,365,4,359,367]
[null,"P0A9S6","_",0.9782,0.98356,44.29,{"v":1e-94,"d":"1.00E-94"},1,1,"gldA","Glycerol dehydrogenase","1.1.1.6","Complete proteome, Glycerol metabolism, Metal-binding, NAD, Oxidoreductase, Zinc",12471157,"Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","CFT073 / ATCC 700928 / UPEC",4,362,365,4,359,367]
[null,"P50173","IPMed?",0.98082,0.98082,42.46,{"v":4e-88,"d":"4.00E-88"},2,1,"gldA","Glycerol dehydrogenase","1.1.1.6","Glycerol metabolism, Metal-binding, NAD, Oxidoreductase, Plasmid, Zinc",8824602,"Pseudomonas putida","ML2",5,362,365,5,359,365]
[null,"P45511","IPMed?",0.99178,0.99178,39.78,{"v":1e-81,"d":"1.00E-81"},3,1,"dhaD","Glycerol dehydrogenase","1.1.1.6","Direct protein sequencing, Glycerol metabolism, Manganese, Metal-binding, NAD, Oxidoreductase",7635824,"Citrobacter freundii","ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK",1,362,365,1,359,365]
[null,"Q9WYQ4","IPMed?",0.97808,0.98077,41.18,{"v":3e-77,"d":"3.00E-77"},4,1,"gldA","Glycerol dehydrogenase","1.1.1.6","3D-structure, Complete proteome, Glycerol metabolism, Metal-binding, NAD, Oxidoreductase, Reference proteome, Zinc","10360571, 12193646","Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 / ATCC 43589 / MSB8 / DSM 3109 / JCM 10099",9,362,365,9,357,364]
[null,"P32816","IPMed?",0.97027,0.98356,39,{"v":1e-64,"d":"1.00E-64"},5,1,"gldA","Glycerol dehydrogenase","1.1.1.6","3D-structure, Direct protein sequencing, Glycerol metabolism, Metal-binding, NAD, Oxidoreductase, Zinc","1339360, 8399385, 2493267, 11566129","Geobacillus stearothermophilus","DSM 2334 / Var. Non-diastaticus",10,364,365,12,363,370]
[null,"O13702","IPMed?",0.78889,0.9726,32.68,{"v":5E-53,"d":"5.00E-53"},6,1,"gld1","Glycerol dehydrogenase 1","1.1.1.6","3D-structure, Complete proteome, Glycerol metabolism, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Zinc","11859360, 16823372, 20396879","Schizosaccharomyces pombe (strain 972 / ATCC 24843)","972 / ATCC 24843",10,359,365,71,418,450]
[null,"P74246","_",0.92727,0.97808,27.73,{"v":1e-32,"d":"1.00E-32"},7,1,"_","Uncharacterized oxidoreductase slr1167","1.1.-.-","Complete proteome, Metal-binding, Oxidoreductase, Reference proteome, Zinc",8905231,"Synechocystis sp. (strain PCC 6803 / Kazusa)","PCC 6803 / Kazusa",18,357,365,27,364,385]
[null,"P45579","IPMed?",0.82192,0.82873,30.33,{"v":1E-25,"d":"1.00E-25"},8,1,"hcxA","Hydroxycarboxylate dehydrogenase A","1.1.1.-","Complete proteome, Metal-binding, NADP, Oxidoreductase, Reference proteome, Zinc","8905232, 9278503, 16738553, 1848300, 7567469, 27941785","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12",64,354,365,67,353,362]
[null,"B8GGP5","_",0.86575,0.88022,26.27,{"v":1e-19,"d":"1.00E-19"},9,1,"egsA","Glycerol-1-phosphate dehydrogenase [NAD(P)+]","1.1.1.261","Complete proteome, Cytoplasm, Lipid biosynthesis, Lipid metabolism, Metal-binding, NAD, NADP, Oxidoreductase, Phospholipid biosynthesis, Phospholipid metabolism, Reference proteome, Zinc","_","Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c)","_",27,339,365,44,338,359]
[null,"A9A2U8","_",0.86575,0.89266,27.53,{"v":6e-19,"d":"6.00E-19"},10,1,"egsA","Glycerol-1-phosphate dehydrogenase [NAD(P)+]","1.1.1.261","Complete proteome, Cytoplasm, Lipid biosynthesis, Lipid metabolism, Metal-binding, NAD, NADP, Oxidoreductase, Phospholipid biosynthesis, Phospholipid metabolism, Reference proteome, Zinc","_","Nitrosopumilus maritimus (strain SCM1)","_",10,319,365,18,313,354]
[null,"Q9YER2","IPMed?",0.91233,0.94602,25.83,{"v":2e-18,"d":"2.00E-18"},11,1,"egsA","Glycerol-1-phosphate dehydrogenase [NAD(P)+]","1.1.1.261","Complete proteome, Cytoplasm, Direct protein sequencing, Lipid biosynthesis, Lipid metabolism, Metal-binding, NAD, NADP, Oxidoreductase, Phospholipid biosynthesis, Phospholipid metabolism, Reference proteome, Zinc","10382966, 11846799, 15876564","Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)","ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1 / ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1 / ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1",12,339,365,15,330,352]
[null,"P72010","IPMed?",0.84384,0.88761,24.35,2e-15,12,1,"egsA","Glycerol-1-phosphate dehydrogenase [NAD(P)+]","1.1.1.261","Complete proteome, Cytoplasm, Direct protein sequencing, Lipid biosynthesis, Lipid metabolism, Metal-binding, NAD, NADP, Oxidoreductase, Phospholipid biosynthesis, Phospholipid metabolism, Reference proteome, Zinc","9419225, 9797414, 9371463, 9348086, 12601138, 12913312","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 / ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H",14,317,365,15,304,347]
[null,"O28599","IPMed?",0.9726,1.0114,24.23,3e-13,13,1,"egsA","Glycerol-1-phosphate dehydrogenase [NAD(P)+]","1.1.1.261","Complete proteome, Cytoplasm, Lipid biosynthesis, Lipid metabolism, Metal-binding, NAD, NADP, Oxidoreductase, Phospholipid biosynthesis, Phospholipid metabolism, Reference proteome, Zinc","9389475, 19558961","Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)","ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126 / ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126",14,364,365,15,351,351]
[]
["ACT01_06790","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q59477","_",1.00775,1.01299,32.05,{"v":1e-49,"d":"1.00E-49"},1,2,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","3D-structure, Iron, NAD, Oxidoreductase","_","Klebsiella pneumoniae","_",3,384,385,10,387,387]
[null,"A6ZTT5","_",1.0026,1.01047,31.35,{"v":3E-49,"d":"3.00E-49"},2,3,"ADH4","Alcohol dehydrogenase 4","1.1.1.1","Complete proteome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Zinc",17652520,"Saccharomyces cerevisiae (strain YJM789)","YJM789",2,385,385,8,381,382]
[null,"P45513","IPMed?",0.94832,0.95325,33.24,{"v":5e-49,"d":"5.00E-49"},3,2,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","Iron, NAD, Oxidoreductase",7721705,"Citrobacter freundii","ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK",24,384,385,33,387,387]
[null,"P10127","IPMed?",1.0026,1.01047,31.09,{"v":3e-48,"d":"3.00E-48"},4,3,"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",2,385,385,8,381,382]
[null,"A4ISB9","IPMed?",0.96641,0.97143,34.22,{"v":7e-46,"d":"7.00E-46"},5,3,"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",4,362,385,9,365,387]
[null,"P31005","IPMed?",0.94286,0.95276,30.85,{"v":2E-45,"d":"2.00E-45"},6,3,"mdh","NAD-dependent methanol dehydrogenase","1.1.1.244","Cytoplasm, Direct protein sequencing, Magnesium, Methanol utilization, NAD, Oxidoreductase, Zinc","1644761, 1995642, 2673121, 1995643, 12089158, 12351635","Bacillus methanolicus","C1 / C1 / C1 / C1 / C1 / C1",3,356,385,6,355,381]
[null,"Q09669","IPMed?",0.66114,0.72468,36.56,{"v":5e-45,"d":"5.00E-45"},7,3,"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",2,279,385,50,321,422]
[null,"P71017","IPMed?",0.97264,1.01558,32.48,{"v":5e-45,"d":"5.00E-45"},8,2,"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",3,384,385,18,395,402]
[null,"P37686","IPMed?",0.93247,0.93734,31.75,{"v":8e-44,"d":"8.00E-44"},9,3,"yiaY","Probable alcohol dehydrogenase","1.1.1.1","Complete proteome, Iron, NAD, Oxidoreductase, Reference proteome","8041620, 9278503, 16397293, 16738553, 7768815","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",29,383,385,35,382,383]
[null,"O05239","_",1.00775,1.01299,32.05,{"v":1E-41,"d":"1.00E-41"},10,3,"yugJ","Probable NADH-dependent butanol dehydrogenase 1","1.1.1.-","Complete proteome, NAD, Oxidoreductase, Reference proteome","9274030, 9384377","Bacillus subtilis (strain 168)","168 / 168",4,379,385,9,382,387]
[null,"P0A9S1","IPMed?",0.94545,0.95288,30.49,{"v":1e-39,"d":"1.00E-39"},11,3,"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",25,384,385,31,382,382]
[null,"P0DJA2","IPMed?",0.94805,0.953,30.41,{"v":1e-39,"d":"1.00E-39"},12,3,"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",24,384,385,30,383,383]
[null,"F8DVL8","IPMed?",0.94805,0.953,30.41,{"v":1e-39,"d":"1.00E-39"},12,3,"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",24,384,385,30,383,383]
[null,"A4IP64","IPMed?",0.96709,0.99221,31.41,{"v":6e-39,"d":"6.00E-39"},13,3,"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",10,384,385,15,385,395]
[]
["ACT01_11045","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?",0.99483,1.06354,31.17,{"v":2e-40,"d":"2.00E-40"},1,4,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","Iron, NAD, Oxidoreductase",7721705,"Citrobacter freundii","ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK",1,360,362,5,385,387]
[null,"P0A9S2","_",0.78534,0.82873,32,{"v":3e-38,"d":"3.00E-38"},2,4,"fucO","Lactaldehyde reductase","1.1.1.77","Carbohydrate metabolism, Complete proteome, Fucose metabolism, Iron, Metal-binding, NAD, Oxidoreductase, Reference proteome","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",11,303,362,12,307,382]
[null,"P0A9S1","IPMed?",0.78534,0.82873,32,{"v":3e-38,"d":"3.00E-38"},2,4,"fucO","Lactaldehyde reductase","1.1.1.77","3D-structure, Carbohydrate metabolism, Complete proteome, Fucose metabolism, Iron, Metal-binding, NAD, Oxidoreductase, Reference proteome","2553671, 2664711, 2661535, 9278503, 16738553, 8385012, 15995211","Escherichia coli (strain K12)","K12 / K12 / K12 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12 / ECL1",11,303,362,12,307,382]
[null,"P0DJA2","IPMed?",0.77023,0.81492,32.2,{"v":4e-38,"d":"4.00E-38"},3,4,"adhB","Alcohol dehydrogenase 2","1.1.1.1","3D-structure, Complete proteome, Direct protein sequencing, Iron, NAD, Oxidoreductase, Reference proteome","3584063, 15592456, 2935393","Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)","ATCC 31821 / ZM4 / CP4 / ATCC 31821 / ZM4 / CP4 / ATCC 31821 / ZM4 / CP4",13,303,362,15,308,383]
[null,"F8DVL8","IPMed?",0.77023,0.81492,32.2,{"v":4e-38,"d":"4.00E-38"},3,4,"adhB","Alcohol dehydrogenase 2","1.1.1.1","Complete proteome, Iron, NAD, Oxidoreductase","2308827, 21725006","Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1)","ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1 / ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1",13,303,362,15,308,383]
[null,"Q59477","_",0.99225,1.06077,29.69,{"v":1e-37,"d":"1.00E-37"},4,4,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","3D-structure, Iron, NAD, Oxidoreductase","_","Klebsiella pneumoniae","_",1,360,362,5,385,387]
[null,"Q9F282","IPMed?",0.94486,1.04144,27.85,{"v":1e-36,"d":"1.00E-36"},5,2,"adhA","Long-chain primary alcohol dehydrogenase AdhA","1.1.1.2","Direct protein sequencing, NADP, Oxidoreductase, Zinc",10981690,"Thermoanaerobacter ethanolicus","ATCC 31550 / DSM 2246 / JW 200",11,360,362,21,397,399]
[null,"Q09669","IPMed?",0.66588,0.77624,30.96,{"v":2e-36,"d":"2.00E-36"},6,4,"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",4,280,362,49,328,422]
[null,"P13604","IPMed?",0.84536,0.90608,30.49,{"v":2e-36,"d":"2.00E-36"},7,4,"adh1","NADPH-dependent butanol dehydrogenase","1.1.1.-","NADP, Oxidoreductase",2673928,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",1,320,362,1,323,388]
[null,"A4IP64","IPMed?",0.76962,0.83978,32.57,{"v":2e-36,"d":"2.00E-36"},8,4,"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",7,303,362,9,309,395]
[null,"P31005","IPMed?",0.83727,0.88122,30.72,{"v":5E-36,"d":"5.00E-36"},9,4,"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",1,311,362,1,316,381]
[null,"Q04945","IPMed?",0.82821,0.89227,31.58,{"v":3e-35,"d":"3.00E-35"},10,4,"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",2,315,362,4,326,390]
[null,"P41795","IPMed?",0.71899,0.78453,32.75,{"v":4e-34,"d":"4.00E-34"},11,4,"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",4,284,362,24,307,395]
[]
["ACT01_07765","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q18AR0","_",0.99244,1.00767,58.63,{"v":9E-158,"d":"9.00E-158"},1,1,"thlA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",16804543,"Peptoclostridium difficile (strain 630)",630,1,394,397,1,390,391]
[null,"P44873","_",0.99496,1.00509,56.71,{"v":3e-154,"d":"3.00E-154"},2,1,"atoB","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",1,394,397,1,391,393]
[null,"P45359","IPMed?",0.99748,1.0102,54.55,{"v":3e-145,"d":"3.00E-145"},3,1,"thlA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","7867955, 11075929, 11466286, 1685080","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,396,397,1,392,392]
[null,"Q0AVM3","IPMed?",1,1.00253,55.16,{"v":2e-142,"d":"2.00E-142"},4,1,"_","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",2,394,397,3,394,396]
[null,"P76461","_",0.99496,1.00254,53.67,{"v":1e-140,"d":"1.00E-140"},5,1,"atoB","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","9097040, 9278503, 16738553","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",1,394,397,1,391,394]
[null,"P14611","IPMed?",0.99244,1.00254,53.05,{"v":8e-139,"d":"8.00E-139"},6,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, PHB biosynthesis, Reference proteome, Transferase","2670935, 16964242, 2670936, 4198758, 1476773, 25152395","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337",1,394,397,1,391,393]
[null,"P45369","IPMed?",0.98992,0.99746,52.42,{"v":4e-137,"d":"4.00E-137"},7,1,"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",2,394,397,3,392,394]
[null,"P50174","IPMed?",0.98741,0.99746,53.32,{"v":2E-136,"d":"2.00E-136"},8,1,"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",3,394,397,5,391,393]
[null,"Q9ZHI1","IPMed?",0.98489,0.99745,51.92,{"v":4e-135,"d":"4.00E-135"},9,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, PHA biosynthesis, Reference proteome, Transferase","14500782, 10427049","Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)","ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757 / ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757",4,394,397,3,390,392]
[null,"Q8CQN7","_",0.98992,0.99746,48.35,{"v":7e-135,"d":"7.00E-135"},10,1,"_","Probable acetyl-CoA acyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Transferase",12950922,"Staphylococcus epidermidis (strain ATCC 12228)","ATCC 12228",1,393,397,1,389,394]
[null,"Q5HS07","_",0.98992,0.99746,48.35,{"v":7e-135,"d":"7.00E-135"},10,1,"_","Probable acetyl-CoA acyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",15774886,"Staphylococcus epidermidis (strain ATCC 35984 / RP62A)","ATCC 35984 / RP62A",1,393,397,1,389,394]
[null,"P45363","IPMed?",0.98489,0.99239,52.43,{"v":4e-134,"d":"4.00E-134"},11,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase","7763384, 1476773","Thiocystis violacea","2311 / DSM 208",4,394,397,5,392,394]
[null,"P07097","IPMed?",0.98237,0.9949,51.28,{"v":6e-132,"d":"6.00E-132"},12,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase","2878929, 2670935, 1673680, 1476773, 10764581, 10545327, 12501183","Zoogloea ramigera","ATCC 19623 / I-16-M / NCIB 10340 / NCTC 10482",5,394,397,6,390,392]
[null,"P54810","IPMed?",0.99244,1.00767,50,{"v":8e-127,"d":"8.00E-127"},13,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase",8566717,"Paracoccus denitrificans","_",1,394,397,1,389,391]
[null,"Q8CAY6","IPMed?",0.98992,0.98992,49.87,{"v":6e-123,"d":"6.00E-123"},14,1,"Acat2","Acetyl-CoA acetyltransferase, cytosolic","2.3.1.9","Acetylation, Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","16141072, 15489334, 2055458, 21183079","Mus musculus","C57BL/6J / C57BL/6J / C57BL/6J",4,394,397,8,395,397]
[]
["ACT01_10830","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P52046","IPMed?",0.98084,0.98462,56.64,{"v":4e-96,"d":"4.00E-96"},1,1,"crt","Short-chain-enoyl-CoA hydratase","4.2.1.150","3D-structure, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","8655474, 11466286, 5057466","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,256,260,1,256,261]
[null,"Q0AVM1","IPMed?",0.98846,0.98846,55.25,{"v":2E-92,"d":"2.00E-92"},2,1,"_","Crotonyl-CoA hydratase","4.2.1.150","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",1,257,260,1,257,260]
[null,"A4YI89","IPMed?",1,1.00386,43.46,{"v":1e-71,"d":"1.00E-71"},3,1,"_","3-hydroxypropionyl-coenzyme A dehydratase","4.2.1.116","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","18083856, 19429610","Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)","ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2",1,260,260,1,259,259]
[null,"O34893","IPMed?",0.98846,0.98846,46.3,{"v":8e-71,"d":"8.00E-71"},4,1,"yngF","Putative enoyl-CoA hydratase/isomerase YngF","_","Complete proteome, Lyase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",4,259,260,3,259,260]
[null,"Q52995","IPMed?",1,1.01167,43.08,{"v":4e-64,"d":"4.00E-64"},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",1,258,260,1,255,257]
[null,"Q1ZXF1","_",0.88809,0.94615,46.75,{"v":7e-64,"d":"7.00E-64"},6,1,"echs1","Probable enoyl-CoA hydratase, mitochondrial","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide",15875012,"Dictyostelium discoideum","AX4",14,253,260,34,270,277]
[null,"P9WNN8","_",1,1.01167,42.69,{"v":1e-63,"d":"1.00E-63"},7,1,"echA8","Probable enoyl-CoA hydratase echA8","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",1,257,260,1,254,257]
[null,"P9WNN9","_",1,1.01167,42.69,{"v":1e-63,"d":"1.00E-63"},7,1,"echA8","Probable enoyl-CoA hydratase echA8","4.2.1.17","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","9634230, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",1,257,260,1,254,257]
[null,"P64017","_",1,1.01167,42.69,{"v":1e-63,"d":"1.00E-63"},7,1,"echA8","Probable enoyl-CoA hydratase echA8","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase","12788972, 28385856","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97",1,257,260,1,254,257]
[null,"Q8BH95","_",0.86552,0.96538,43.03,{"v":3e-61,"d":"3.00E-61"},8,1,"Echs1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Phosphoprotein, Reference proteome, Transit peptide","16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / C57BL/6J",14,258,260,47,288,290]
[null,"P14604","IPMed?",0.86552,0.96538,42.63,{"v":3e-60,"d":"3.00E-60"},9,1,"Echs1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide","2806264, 15489334, 7883013, 8895557, 9480773, 11851409, 12445775","Rattus norvegicus","_",14,258,260,47,288,290]
[null,"O07137","_",0.98846,1,42.41,{"v":3e-60,"d":"3.00E-60"},10,1,"echA8","Probable enoyl-CoA hydratase echA8","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome",11234002,"Mycobacterium leprae (strain TN)","TN",1,257,260,1,254,257]
[null,"P30084","IPMed?",0.87241,0.97308,41.11,{"v":7e-58,"d":"7.00E-58"},11,1,"ECHS1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Disease mutation, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Neurodegeneration, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","8012501, 9073515, 15164054, 15489334, 1286669, 11271497, 19608861, 21269460, 25125611, 24275569, 25393721, 25944712, 26000322, 26251176, 27221955, 26741492","Homo sapiens","_",14,260,260,47,290,290]
[null,"Q9JLZ3","IPMed?",0.80255,0.96923,41.27,{"v":1E-56,"d":"1.00E-56"},12,1,"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",13,260,260,63,314,314]
[null,"F1LU71","IPMed?",0.8,0.96923,40.87,{"v":3e-56,"d":"3.00E-56"},13,1,"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",13,260,260,64,315,315]
[null,"Q13825","IPMed?",0.74336,0.96923,40.87,{"v":5E-56,"d":"5.00E-56"},14,1,"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","_",13,260,260,88,339,339]
[]
["ACT01_10835","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?",0.99649,1.00709,61.62,{"v":1e-113,"d":"1.00E-113"},1,1,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",3,285,285,2,282,282]
[null,"P77851","_",0.98596,1,59.79,{"v":1e-111,"d":"1.00E-111"},2,1,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",3,283,285,2,280,281]
[null,"P45856","IPMed?",0.98606,0.99298,55.48,{"v":2E-107,"d":"2.00E-107"},3,1,"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",3,285,285,4,284,287]
[null,"Q0AVM2","IPMed?",0.98246,1.00358,56.07,{"v":4e-106,"d":"4.00E-106"},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",4,283,285,2,279,279]
[null,"Q45223","_",0.96587,0.99298,53,{"v":1E-97,"d":"1.00E-97"},6,1,"hbdA","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome",12597275,"Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110",1,283,285,4,284,293]
[null,"Q9RVG1","_",0.98246,1.00719,54.29,{"v":1E-97,"d":"1.00E-97"},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",4,283,285,2,278,278]
[null,"P45364","IPMed?",0.98947,1.00356,54.96,{"v":6e-97,"d":"6.00E-97"},7,1,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase",8001771,"Clostridioides difficile","E",4,285,285,2,281,281]
[null,"P9WNP7","IPMed?",0.98951,0.99298,43.11,{"v":3e-71,"d":"3.00E-71"},8,1,"fadB2","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","9634230, 11489128, 12081975, 20378648, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",3,283,285,6,286,286]
[null,"P9WNP6","_",0.98951,0.99298,43.11,{"v":3e-71,"d":"3.00E-71"},8,1,"fadB2","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",3,283,285,6,286,286]
[null,"Q16836","IPMed?",0.91401,1.00702,44.95,{"v":9e-67,"d":"9.00E-67"},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","_",3,283,285,28,313,314]
[null,"P00348","IPMed?",0.92038,1.01404,43.25,{"v":3e-66,"d":"3.00E-66"},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","_",1,283,285,26,313,314]
[null,"P76083","IPMed?",0.58947,0.98246,43.57,{"v":7e-64,"d":"7.00E-64"},11,1,"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",5,283,285,8,285,475]
[null,"Q61425","IPMed?",0.92038,1.01404,43.25,{"v":1e-63,"d":"1.00E-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",1,283,285,26,313,314]
[null,"Q9WVK7","IPMed?",0.92038,1.01404,43.25,{"v":2e-63,"d":"2.00E-63"},13,1,"Hadh","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","Acetylation, Complete proteome, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide",10064895,"Rattus norvegicus","Sprague-Dawley",1,283,285,26,313,314]
[]
["ACT01_12410","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","_",0.92581,1.02135,38.68,{"v":5E-51,"d":"5.00E-51"},1,2,"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)","_",6,287,310,2,280,281]
[null,"P52041","IPMed?",0.92903,1.02128,35.76,{"v":4e-47,"d":"4.00E-47"},2,2,"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",6,289,310,2,282,282]
[null,"Q9RVG1","_",0.9129,1.01799,38.87,{"v":6e-47,"d":"6.00E-47"},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",10,287,310,5,278,278]
[null,"Q0AVM2","IPMed?",0.91935,1.02151,35.09,{"v":9E-47,"d":"9.00E-47"},4,2,"_","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",8,287,310,3,279,279]
[null,"P41938","_",0.93871,0.94175,36.77,{"v":1e-45,"d":"1.00E-45"},5,2,"_","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",7,287,310,24,308,309]
[null,"P45856","IPMed?",0.92903,1.00348,35.07,{"v":2e-44,"d":"2.00E-44"},6,2,"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",6,289,310,4,284,287]
[null,"P34439","_",0.93871,0.97651,34.71,{"v":9e-44,"d":"9.00E-44"},7,2,"_","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",6,287,310,12,296,298]
[null,"P45364","IPMed?",0.91935,1.01423,32.98,{"v":5e-41,"d":"5.00E-41"},8,2,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase",8001771,"Clostridioides difficile","E",10,289,310,5,281,281]
[null,"P00348","IPMed?",0.97134,0.98387,34.1,{"v":7e-41,"d":"7.00E-41"},10,2,"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","_",2,287,310,24,313,314]
[null,"Q16836","IPMed?",0.95541,0.96774,35.33,{"v":7e-41,"d":"7.00E-41"},9,2,"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","_",6,287,310,28,313,314]
[null,"Q9WVK7","IPMed?",0.95541,0.96774,34.67,{"v":2e-40,"d":"2.00E-40"},11,2,"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",6,287,310,28,313,314]
[null,"P76083","IPMed?",0.60421,0.92581,32.4,{"v":7e-40,"d":"7.00E-40"},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",6,287,310,6,285,475]
[null,"Q61425","IPMed?",0.95541,0.96774,34.33,{"v":2e-39,"d":"2.00E-39"},13,2,"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",6,287,310,28,313,314]
[null,"Q9ZPI5","IPMed?",0.42069,0.98387,28.85,{"v":2e-33,"d":"2.00E-33"},14,2,"MFP2","Enoyl-CoA hydratase/3-2-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase / 3-hydroxyacyl-CoA dehydrogenase","4.2.1.17, 5.1.2.3, 5.3.3.8, 1.1.1.35","3D-structure, Complete proteome, Fatty acid metabolism, Glyoxysome, Isomerase, Lipid metabolism, Lyase, Multifunctional enzyme, NAD, Oxidoreductase, Peroxisome, Reference proteome","10521521, 11130713, 27862469, 14593172, 10816107, 16507084, 17272265, 17951448, 24254312, 20463021","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia / cv. Landsberg erecta",6,305,310,313,606,725]
[]
["ACT01_02995","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q2RQ36","IPMed?",0.90278,0.94203,47.69,{"v":6e-33,"d":"6.00E-33"},1,1,"phaJ","(R)-specific enoyl-CoA hydratase","4.2.1.119","Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","10709984, 21886856","Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)","S1 / ATCC 25903 / S1H / ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1",7,136,138,11,139,144]
[null,"C5AZ74","IPMed?",0.84076,0.95652,40.15,{"v":3E-24,"d":"3.00E-24"},2,1,"croR","3-hydroxybutyryl-CoA dehydratase","4.2.1.55","Complete proteome, Lyase, Reference proteome","11872727, 19440302","Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)","ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1 / ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1",4,135,138,7,137,157]
[null,"O32472","IPMed?",0.94928,0.97761,32.82,{"v":3e-19,"d":"3.00E-19"},3,1,"phaJ","(R)-specific enoyl-CoA hydratase","4.2.1.119","3D-structure, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase","9244271, 9457873, 12409309","Aeromonas caviae","FA440 / FA440",5,135,138,1,131,134]
[null,"P86397","IPMed?",0.56548,0.68841,37.89,{"v":3e-16,"d":"3.00E-16"},4,1,"HTD2","Hydroxyacyl-thioester dehydratase type 2, mitochondrial","4.2.1.-","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide","17898086, 16641997","Homo sapiens","_",10,104,138,36,130,168]
[null,"P77455","IPMed?",0.16006,0.78986,29.36,1e-05,5,2,"paaZ","2-oxepin-2(3H)-ylideneacetyl-CoA hydrolase / 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase","3.3.2.12, 1.2.1.91","Complete proteome, Hydrolase, Lyase, Multifunctional enzyme, NADP, Oxidoreductase, Reference proteome","9748275, 9097039, 9278503, 16738553, 10766858, 20660314, 21296885","Escherichia coli (strain K12)","W / ATCC 11105 / DSM 1900 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",7,107,138,531,637,681]
[null,"P49251","IPMed?",0.32239,0.78261,28.7,3e-05,6,1,"maoC","Protein MaoC","_","_",1556068,"Klebsiella aerogenes","W70",7,106,138,198,303,335]
[null,"P34229","IPMed?",0.05129,0.77536,30.84,9e-05,7,2,"FAS1","3-hydroxyacyl-[acyl-carrier-protein] dehydratase / Enoyl-[acyl-carrier-protein] reductase [NADH] / [Acyl-carrier-protein] acetyltransferase / [Acyl-carrier-protein] malonyltransferase / S-acyl fatty acid synthase thioesterase","4.2.1.59, 1.3.1.9, 2.3.1.38, 2.3.1.39, 3.1.2.14","Complete proteome, Fatty acid biosynthesis, Fatty acid metabolism, Hydrolase, Lipid biosynthesis, Lipid metabolism, Lyase, Multifunctional enzyme, NAD, NADP, Oxidoreductase, Reference proteome, Transferase","2034224, 15229592","Yarrowia lipolytica (strain CLIB 122 / E 150)","ATCC 32338 / CX-161-1B / CLIB 122 / E 150",30,135,138,1584,1689,2086]
[null,"Q9VXJ0","IPMed?",0.18896,0.81884,26.55,2E-3,8,10,"Mfe2","(3R)-hydroxyacyl-CoA dehydrogenase / Enoyl-CoA hydratase 2","4.2.1.119","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Multifunctional enzyme, NAD, Oxidoreductase, Peroxisome, Reference proteome","10731132, 12537572, 12537569, 21320074","Drosophila melanogaster","Berkeley / Berkeley / Berkeley",26,137,138,486,592,598]
[null,"Q02207","IPMed?",0.12333,0.80435,27.03,0.004,9,11,"FOX2","2-enoyl-CoA hydratase / (3R)-3-hydroxyacyl-CoA dehydrogenase","4.2.1.119","Complete proteome, Fatty acid metabolism, Isomerase, Lipid metabolism, Lyase, Multifunctional enzyme, NAD, Oxidoreductase, Peroxisome, Reference proteome, Repeat","1551874, 1441752, 8196765, 24374639","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 204508 / S288c",26,136,138,793,893,900]
[null,"P34731","IPMed?",0.03927,0.57971,32.5,0.007,10,2,"FAS1","3-hydroxyacyl-[acyl-carrier-protein] dehydratase / Enoyl-[acyl-carrier-protein] reductase [NADH] / [Acyl-carrier-protein] acetyltransferase / [Acyl-carrier-protein] malonyltransferase / S-acyl fatty acid synthase thioesterase","4.2.1.59, 1.3.1.9, 2.3.1.38, 2.3.1.39, 3.1.2.14","Fatty acid biosynthesis, Fatty acid metabolism, Hydrolase, Lipid biosynthesis, Lipid metabolism, Lyase, Multifunctional enzyme, NAD, NADP, Oxidoreductase, Transferase",8088535,"Candida albicans",4918,30,108,138,1539,1618,2037]
[]
["ACT01_00280","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P45867","IPMed?",0.99208,0.99208,48.14,{"v":1e-116,"d":"1.00E-116"},1,3,"acdA","Acyl-CoA dehydrogenase","1.3.99.-","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid degradation, Lipid metabolism, Oxidoreductase, Reference proteome","9353933, 9384377, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",1,374,379,1,374,379]
[null,"Q06319","IPMed?",1,1.01055,47.78,{"v":1e-112,"d":"1.00E-112"},2,3,"_","Acyl-CoA dehydrogenase, short-chain specific","1.3.8.1","3D-structure, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Oxidoreductase","8399220, 7857927","Megasphaera elsdenii","_",1,378,379,1,382,383]
[null,"G3KIM8","IPMed?",0.96193,1,45.91,{"v":2E-109,"d":"2.00E-109"},3,2,"acrC","Acryloyl-CoA reductase (NADH)","1.3.1.95","Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",1,378,379,14,392,394]
[null,"P52042","IPMed?",0.99736,0.99736,44.44,{"v":3e-108,"d":"3.00E-108"},4,3,"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",1,376,379,1,376,379]
[null,"P45857","IPMed?",0.98681,0.98681,45.72,{"v":1E-107,"d":"1.00E-107"},5,3,"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",7,378,379,5,376,379]
[null,"P63428","_",0.97172,0.99736,45.5,{"v":5e-102,"d":"5.00E-102"},6,3,"fadE25","Probable acyl-CoA dehydrogenase fadE25","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase","12788972, 28385856","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97",3,378,379,13,388,389]
[null,"P9WQG0","_",0.97172,0.99736,45.5,{"v":5e-102,"d":"5.00E-102"},6,3,"fadE25","Probable acyl-CoA dehydrogenase fadE25","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",3,378,379,13,388,389]
[null,"P9WQG1","_",0.97172,0.99736,45.5,{"v":5e-102,"d":"5.00E-102"},6,3,"fadE25","Probable acyl-CoA dehydrogenase fadE25","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9634230, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",3,378,379,13,388,389]
[null,"P15651","IPMed?",0.91019,0.98945,44.53,{"v":1e-101,"d":"1.00E-101"},7,3,"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","_",7,378,379,36,407,412]
[null,"P11310","IPMed?",0.89786,0.99736,44.44,{"v":2E-100,"d":"2.00E-100"},8,1,"ACADM","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","3D-structure, Acetylation, Alternative splicing, Complete proteome, Direct protein sequencing, Disease mutation, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","3035565, 1731887, 14702039, 16710414, 15489334, 2393404, 19608861, 21269460, 24121500, 24275569, 25416781, 25944712, 8823176, 15159392, 15975918, 1363805, 2394825, 2251268, 1684086, 1902818, 1671131, 8198141, 7603790, 7929823, 9158144, 9882619, 10767181, 11349232, 11409868, 11486912, 16959974","Homo sapiens","_",3,376,379,39,414,421]
[null,"P46703","_",0.97172,0.99736,43.92,{"v":2E-100,"d":"2.00E-100"},9,3,"fadE25","Probable acyl-CoA dehydrogenase fadE25","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","7489918, 11234002","Mycobacterium leprae (strain TN)","TN",3,378,379,13,388,389]
[null,"P41367","IPMed?",0.89786,0.99736,46.03,{"v":3e-100,"d":"3.00E-100"},10,1,"ACADM","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","3D-structure, Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide",8356049,"Sus scrofa","_",3,376,379,39,414,421]
[null,"Q07417","IPMed?",0.91019,0.98945,44.27,{"v":3e-100,"d":"3.00E-100"},11,3,"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",7,378,379,36,407,412]
[null,"P45952","IPMed?",0.89786,0.99736,45.77,{"v":9e-100,"d":"9.00E-100"},12,1,"Acadm","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","7829081, 1438358, 21183079, 23806337, 23576753","Mus musculus","BALB/cJ",3,376,379,39,414,421]
[]
["ACT01_10950","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q06319","IPMed?",1.00261,1.00261,72.66,0,1,1,"_","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","_",1,383,383,1,383,383]
[null,"P52042","IPMed?",1,1.01055,58.49,{"v":6e-149,"d":"6.00E-149"},2,2,"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",1,383,383,1,379,379]
[null,"P45867","IPMed?",0.99478,1.00528,55.38,{"v":7e-138,"d":"7.00E-138"},3,2,"acdA","Acyl-CoA dehydrogenase","1.3.99.-","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid degradation, Lipid metabolism, Oxidoreductase, Reference proteome","9353933, 9384377, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",1,381,383,1,377,379]
[null,"P45857","IPMed?",0.96345,0.97361,54.2,{"v":2e-127,"d":"2.00E-127"},4,2,"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",14,382,383,12,376,379]
[null,"H6LGM6","IPMed?",0.98956,1,47.23,{"v":2e-110,"d":"2.00E-110"},5,2,"carC","Caffeyl-CoA reductase-Etf complex subunit CarC","1.3.1.108","3D-structure, Complete proteome, Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",6,383,383,4,378,379]
[null,"Q3ZBF6","IPMed?",0.92233,0.99217,47.37,{"v":1e-109,"d":"1.00E-109"},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",6712627,"Bos taurus","_",4,383,383,33,408,412]
[null,"P15651","IPMed?",0.92233,0.99217,46.32,{"v":5e-109,"d":"5.00E-109"},7,2,"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","_",4,383,383,33,408,412]
[null,"Q07417","IPMed?",0.92233,0.99217,46.32,{"v":5e-109,"d":"5.00E-109"},7,2,"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",4,383,383,33,408,412]
[null,"O34421","IPMed?",1.00261,1.01053,46.88,{"v":8e-109,"d":"8.00E-109"},8,2,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,383,383,1,380,380]
[null,"G3KIM8","IPMed?",0.97716,1.00522,47.27,{"v":9e-109,"d":"9.00E-109"},9,3,"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",1,383,383,14,393,394]
[null,"Q5RAS0","_",0.92233,0.99217,46.58,{"v":3e-108,"d":"3.00E-108"},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","_","Pongo abelii","_",4,383,383,33,408,412]
[null,"P16219","IPMed?",0.92233,0.99217,46.32,{"v":2E-107,"d":"2.00E-107"},11,2,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Disease mutation, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","2565344, 9383286, 15489334, 1286669, 21269460, 21237683, 24275569, 25944712, 1692038, 9499414, 11134486","Homo sapiens","_",4,383,383,33,408,412]
[]
["ACT01_11040","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P45867","IPMed?",0.98756,1.04749,44.33,{"v":3e-99,"d":"3.00E-99"},1,4,"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",1,395,402,1,374,379]
[null,"P11310","IPMed?",0.94774,0.99254,42.11,{"v":2e-93,"d":"2.00E-93"},2,2,"ACADM","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","3D-structure, Acetylation, Alternative splicing, Complete proteome, Direct protein sequencing, Disease mutation, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","3035565, 1731887, 14702039, 16710414, 15489334, 2393404, 19608861, 21269460, 24121500, 24275569, 25416781, 25944712, 8823176, 15159392, 15975918, 1363805, 2394825, 2251268, 1684086, 1902818, 1671131, 8198141, 7603790, 7929823, 9158144, 9882619, 10767181, 11349232, 11409868, 11486912, 16959974","Homo sapiens","_",7,402,402,43,419,421]
[null,"A5A6I0","_",0.94774,0.99254,42.11,{"v":2e-93,"d":"2.00E-93"},2,2,"ACADM","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide",17574350,"Pan troglodytes","_",7,402,402,43,419,421]
[null,"P45952","IPMed?",0.95249,0.99751,41.4,{"v":2e-93,"d":"2.00E-93"},3,2,"Acadm","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","7829081, 1438358, 21183079, 23806337, 23576753","Mus musculus","BALB/cJ",5,402,402,41,419,421]
[null,"Q06319","IPMed?",1.00995,1.06005,43.6,{"v":2e-93,"d":"2.00E-93"},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","_",1,400,402,1,383,383]
[null,"P08503","IPMed?",0.95249,0.99751,40.9,{"v":5e-93,"d":"5.00E-93"},5,2,"Acadm","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","Acetylation, Complete proteome, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","3611054, 2029527","Rattus norvegicus","_",5,402,402,41,419,421]
[null,"Q9VSA3","_",0.94511,0.98507,42.68,{"v":1E-91,"d":"1.00E-91"},6,2,"_","Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Reference proteome, Transit peptide","10731132, 12537572, 12537569","Drosophila melanogaster","Berkeley / Berkeley / Berkeley",3,395,402,35,408,419]
[null,"Q3SZB4","_",0.93112,0.97512,42.86,{"v":2E-91,"d":"2.00E-91"},7,2,"ACADM","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","_","Bos taurus","_",7,395,402,43,412,421]
[null,"P45857","IPMed?",0.97512,1.0343,40.82,{"v":1e-90,"d":"1.00E-90"},8,4,"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",5,395,402,3,372,379]
[null,"P41367","IPMed?",0.93587,0.9801,42.13,{"v":5e-90,"d":"5.00E-90"},9,3,"ACADM","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","3D-structure, Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide",8356049,"Sus scrofa","_",5,395,402,41,412,421]
[null,"Q8HXY8","_",0.94774,0.99254,41.6,{"v":7e-90,"d":"7.00E-90"},10,2,"ACADM","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","_","Macaca fascicularis","_",7,402,402,43,419,421]
[null,"P52042","IPMed?",0.99502,1.05541,40,{"v":4e-89,"d":"4.00E-89"},11,4,"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",1,398,402,1,377,379]
[null,"Q22347","IPMed?",0.95444,0.99005,39.7,{"v":5e-84,"d":"5.00E-84"},12,3,"acdh-10","Probable medium-chain specific acyl-CoA dehydrogenase 10, mitochondrial","1.3.8.7","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Reference proteome, Transit peptide","9851916, 18522834","Caenorhabditis elegans","Bristol N2",1,395,402,27,402,417]
[null,"O34421","IPMed?",1,1.05789,40.05,{"v":5e-84,"d":"5.00E-84"},13,4,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,400,402,1,380,380]
[]
["ACT01_09515","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","_",0.99701,1.00909,37.84,{"v":1e-74,"d":"1.00E-74"},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)","_",1,332,334,1,330,330]
[null,"H6LGM8","IPMed?",0.82323,0.97605,35.58,{"v":2e-67,"d":"2.00E-67"},2,2,"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",7,331,334,71,394,396]
[null,"P09819","IPMed?",0.93768,0.99102,36.86,{"v":4e-66,"d":"4.00E-66"},3,2,"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",6,330,334,14,341,353]
[null,"Q53209","_",0.8916,0.98503,37.39,{"v":2e-65,"d":"2.00E-65"},4,2,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Plasmid, Transport","8796346, 9163424, 19376903","Sinorhizobium fredii (strain NBRC 101917 / NGR234)","NBRC 101917 / NGR234 / NBRC 101917 / NGR234",6,330,334,31,357,369]
[null,"O85692","IPMed?",0.97041,0.98204,37.5,{"v":3E-65,"d":"3.00E-65"},5,2,"etfA","Electron transfer flavoprotein subunit alpha","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",7,330,334,9,333,338]
[null,"P10449","IPMed?",0.87805,0.97006,38.58,{"v":4e-63,"d":"4.00E-63"},6,2,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Reference proteome, Transport","8599534, 11157954, 12597275, 2503674","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","USDA 3I1b110 / USDA 110spc4 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110 / USDA 110spc4",6,324,334,31,351,369]
[null,"P53578","IPMed?",1,1,35.63,{"v":3e-62,"d":"3.00E-62"},7,2,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Transport",7875566,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",7,331,334,9,330,334]
[null,"P26483","IPMed?",0.87805,0.97006,37.35,{"v":4e-62,"d":"4.00E-62"},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)","_",6,324,334,31,351,369]
[null,"P53574","_",0.91389,0.98503,36.17,{"v":7e-62,"d":"7.00E-62"},9,2,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",6,329,334,24,350,360]
[null,"P52039","IPMed?",0.97024,0.97605,34.66,{"v":8e-61,"d":"8.00E-61"},10,2,"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",7,329,334,9,332,336]
[null,"G3KIM6","IPMed?",0.96185,1.05689,33.71,{"v":7e-59,"d":"7.00E-59"},11,2,"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",6,330,334,13,363,367]
[null,"Q0AZ33","IPMed?",0.97006,1.02208,34.57,{"v":2e-58,"d":"2.00E-58"},12,2,"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",8,330,334,5,317,317]
[null,"P53571","IPMed?",0.92814,0.96573,31.61,{"v":8e-38,"d":"8.00E-38"},13,1,"etfA","Electron transfer flavoprotein subunit alpha","_","3D-structure, Direct protein sequencing, Electron transport, FAD, Flavoprotein, Transport","7798207, 12567183","Methylophilus methylotrophus","_",21,328,334,18,319,321]
[]
["ACT01_09520","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?",1,1.03448,39.26,{"v":2e-60,"d":"2.00E-60"},1,2,"etfB","Electron transfer flavoprotein subunit beta","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,261,261,1,270,270]
[null,"H6LGM7","IPMed?",1,1.00383,40.46,{"v":4e-58,"d":"4.00E-58"},2,2,"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",1,261,261,1,262,262]
[null,"P97089","_",1.00383,1.00769,40.84,{"v":3E-57,"d":"3.00E-57"},3,2,"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)","_",1,261,261,1,260,260]
[null,"P52040","IPMed?",0.94636,0.95367,40.08,{"v":8E-55,"d":"8.00E-55"},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",1,247,261,1,246,259]
[null,"P26482","IPMed?",0.91103,0.98084,39.06,{"v":3E-52,"d":"3.00E-52"},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)","_",1,247,261,1,256,281]
[null,"P53577","IPMed?",0.84028,0.9272,39.26,{"v":2E-50,"d":"2.00E-50"},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",1,234,261,1,242,288]
[null,"P53576","_",0.84698,0.91188,40.34,{"v":1e-49,"d":"1.00E-49"},7,2,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",1,231,261,1,238,281]
[null,"Q53210","_",0.93333,1.01916,37.22,{"v":1e-47,"d":"1.00E-47"},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",1,255,261,1,262,285]
[null,"P09818","IPMed?",0.81507,0.91188,37.39,{"v":5e-44,"d":"5.00E-44"},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",1,230,261,1,238,292]
[null,"O33095","_",0.97744,0.99617,37.69,{"v":8e-43,"d":"8.00E-43"},10,1,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport",11234002,"Mycobacterium leprae (strain TN)","TN",2,253,261,3,262,266]
[null,"P64098","IPMed?",0.97744,0.99617,36.92,{"v":1E-42,"d":"1.00E-42"},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",2,253,261,3,262,266]
[null,"Q05559","IPMed?",0.86738,0.9272,37.6,{"v":3e-42,"d":"3.00E-42"},12,2,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport",8369342,"Rhizobium leguminosarum bv. phaseoli","_",1,234,261,1,240,279]
[null,"G3KIM7","IPMed?",1.00375,1.02682,33.58,{"v":2e-36,"d":"2.00E-36"},13,2,"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",1,261,261,1,267,267]
[null,"P53575","IPMed?",0.96552,1.01205,30.95,{"v":3E-28,"d":"3.00E-28"},14,2,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8599534, 12597275","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","USDA 3I1b110 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110",1,238,261,1,249,249]
[]
["ACT01_10940","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O85692","IPMed?",0.99408,1.00299,90.48,0,1,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,335,335,1,336,338]
[null,"P71153","_",0.98507,1,59.39,{"v":1e-131,"d":"1.00E-131"},2,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",5,334,335,3,330,330]
[null,"H6LGM8","IPMed?",0.83838,0.99104,56.02,{"v":6e-122,"d":"6.00E-122"},3,1,"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",2,333,335,64,394,396]
[null,"P53578","IPMed?",0.99701,1,54.79,{"v":8e-117,"d":"8.00E-117"},4,1,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Transport",7875566,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",1,333,335,1,330,334]
[null,"P52039","IPMed?",0.99107,0.99403,52.25,{"v":9e-114,"d":"9.00E-114"},5,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,331,335,1,332,336]
[null,"G3KIM6","IPMed?",0.9782,1.07164,49.03,{"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",2,334,335,7,365,367]
[null,"P94551","_",0.98209,1.01231,44.98,{"v":5e-85,"d":"5.00E-85"},7,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8969504, 9384377","Bacillus subtilis (strain 168)","168 / 168",7,333,335,3,321,325]
[null,"P26483","IPMed?",0.89431,0.98507,43.03,{"v":2e-83,"d":"2.00E-83"},8,1,"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)","_",6,331,335,29,356,369]
[null,"Q53209","_",0.89973,0.99104,42.17,{"v":2e-81,"d":"2.00E-81"},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",5,332,335,28,357,369]
[null,"P53574","_",0.92222,0.99104,42.17,{"v":6E-79,"d":"6.00E-79"},10,1,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",5,331,335,21,350,360]
[null,"P10449","IPMed?",0.89431,0.98507,39.7,{"v":1e-76,"d":"1.00E-76"},11,1,"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",6,331,335,29,356,369]
[null,"Q0AZ33","IPMed?",0.97015,1.02524,42.46,{"v":7e-76,"d":"7.00E-76"},12,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Cytoplasm, Electron transport, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Reference proteome, Transport","21966920, 19648244, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",8,332,335,3,317,317]
[null,"P09819","IPMed?",0.94334,0.99403,39.34,{"v":2e-74,"d":"2.00E-74"},13,1,"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",5,332,335,11,341,353]
[null,"P13803","IPMed?",0.98806,0.99399,35.35,{"v":1e-47,"d":"1.00E-47"},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","_",3,332,335,16,332,333]
[]
["ACT01_10945","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?",1.00369,1.00741,82.35,{"v":4e-152,"d":"4.00E-152"},1,1,"etfB","Electron transfer flavoprotein subunit beta","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,271,271,1,270,270]
[null,"P52040","IPMed?",0.93358,0.97683,54.55,{"v":4e-86,"d":"4.00E-86"},2,1,"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",1,251,271,1,244,259]
[null,"P97089","_",1.00369,1.04615,51.47,{"v":2e-84,"d":"2.00E-84"},3,1,"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)","_",1,271,271,1,260,260]
[null,"H6LGM7","IPMed?",1.00369,1.03817,49.63,{"v":1e-74,"d":"1.00E-74"},4,1,"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",1,271,271,1,262,262]
[null,"P26482","IPMed?",0.95018,0.98524,45.69,{"v":2e-69,"d":"2.00E-69"},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)","_",1,265,271,1,263,281]
[null,"P53577","IPMed?",0.91667,0.97417,42.8,{"v":2e-65,"d":"2.00E-65"},6,1,"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",1,261,271,1,262,288]
[null,"Q53210","_",0.94386,0.99262,42.75,{"v":2e-64,"d":"2.00E-64"},7,1,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Transport","8796346, 9163424, 19376903","Sinorhizobium fredii (strain NBRC 101917 / NGR234)","NBRC 101917 / NGR234 / NBRC 101917 / NGR234",1,267,271,1,265,285]
[null,"G3KIM7","IPMed?",1.02214,1.03745,43.68,{"v":8e-64,"d":"8.00E-64"},8,1,"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",1,271,271,1,267,267]
[null,"P53576","_",0.96441,1,41.33,{"v":6e-60,"d":"6.00E-60"},9,1,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",1,268,271,1,268,281]
[null,"P09818","IPMed?",0.83904,0.90406,43.27,{"v":3e-59,"d":"3.00E-59"},10,1,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104, 6317191","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",1,243,271,1,243,292]
[null,"Q05559","IPMed?",0.87814,0.90406,43.67,{"v":2e-58,"d":"2.00E-58"},11,1,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport",8369342,"Rhizobium leguminosarum bv. phaseoli","_",1,243,271,1,241,279]
[null,"P64098","IPMed?",1.01476,1.03383,31.64,{"v":1e-38,"d":"1.00E-38"},12,2,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Transport","12788972, 28385856, 16006064","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97 / BCG / Pasteur",3,271,271,4,266,266]
[null,"Q9LSW8","IPMed?",0.98524,1.06375,32.58,{"v":1e-33,"d":"1.00E-33"},13,1,"ETFB","Electron transfer flavoprotein subunit beta, mitochondrial","_","Alternative splicing, Complete proteome, Electron transport, FAD, Flavoprotein, Mitochondrion, Reference proteome, Transit peptide, Transport","10718197, 27862469, 14593172, 14671022, 16923016","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia / cv. Landsberg erecta",1,265,271,1,244,251]
[]
["ACT01_02540","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"B0MC58","_",0.99103,0.99326,47.06,{"v":3e-140,"d":"3.00E-140"},1,2,"_","Butyryl-CoA:acetate CoA-transferase","2.8.3.-","Complete proteome, Fatty acid metabolism, Lipid metabolism, Transferase",16385128,"Anaerostipes caccae (strain DSM 14662 / NCIMB 13811 / L1-92)","DSM 14662 / NCIMB 13811 / L1-92",5,444,445,5,446,446]
[null,"G2SYC0","_",0.99103,0.99326,47.74,{"v":4e-138,"d":"4.00E-138"},2,3,"_","Butyryl-CoA:acetate CoA-transferase","2.8.3.-","Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","16385128, 26543119","Roseburia hominis (strain DSM 16839 / NCIMB 14029 / A2-183)","DSM 16839 / NCIMB 14029 / A2-183 / DSM 16839 / NCIMB 14029 / A2-183",5,444,445,5,446,446]
[null,"Q0AVM5","IPMed?",0.99105,0.99551,45.6,{"v":2E-125,"d":"2.00E-125"},3,3,"_","Probable butyrate:acetyl-CoA coenzyme A-transferase","2.8.3.-","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",5,444,445,7,445,447]
[null,"P38942","IPMed?",0.9573,0.99301,38.26,{"v":1e-88,"d":"1.00E-88"},4,5,"cat2","4-hydroxybutyrate coenzyme A transferase","2.8.3.-","Complete proteome, Reference proteome, Transferase","18218779, 8550525","Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)","ATCC 8527 / DSM 555 / NCIMB 10680",5,430,445,5,422,429]
[null,"Q6BKW1","_",0.95029,1.11685,23.74,{"v":8e-18,"d":"8.00E-18"},5,3,"ACH1","Acetyl-CoA hydrolase","3.1.2.1","Complete proteome, Cytoplasm, Hydrolase, Reference proteome",15229592,"Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968)","ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968",7,444,445,14,490,523]
[null,"P38946","IPMed?",0.73234,0.88539,25.38,{"v":2e-17,"d":"2.00E-17"},6,6,"cat1","Succinyl-CoA:coenzyme A transferase","2.8.3.-","Complete proteome, Reference proteome, Transferase","8550525, 18218779","Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)","ATCC 8527 / DSM 555 / NCIMB 10680",88,435,445,137,508,538]
[null,"B3EY95","IPMed?",0.94455,1.07191,24.32,{"v":1e-16,"d":"1.00E-16"},7,2,"_","Succinyl-CoA:acetate CoA-transferase","2.8.3.18","3D-structure, Transferase","18502856, 23030530","Acetobacter aceti","1023 / 1023 / 1023",8,429,445,11,466,505]
[null,"P83773","IPMed?",0.64885,0.76404,25.29,{"v":2E-16,"d":"2.00E-16"},8,6,"ACH1","Acetyl-CoA hydrolase","3.1.2.1","Complete proteome, Cytoplasm, Direct protein sequencing, Hydrolase, Reference proteome","15123810, 17419877, 24025428, 15378761","Candida albicans (strain SC5314 / ATCC MYA-2876)","SC5314 / ATCC MYA-2876 / SC5314 / ATCC MYA-2876 / SC5314 / ATCC MYA-2876 / SC5314 / ATCC MYA-2876",144,444,445,165,491,524]
[null,"P15937","IPMed?",0.69524,0.82022,25.48,{"v":5e-16,"d":"5.00E-16"},9,4,"acu-8","Acetyl-CoA hydrolase","3.1.2.1","Complete proteome, Cytoplasm, Hydrolase, Reference proteome","2140429, 12712197, 1357077","Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)","ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987",109,432,445,133,483,525]
[null,"P32316","IPMed?",0.62167,0.73483,25.08,1E-14,10,5,"ACH1","Acetyl-CoA hydrolase","3.1.2.1","Acetylation, Complete proteome, Cytoplasm, Direct protein sequencing, Glycoprotein, Hydrolase, Phosphoprotein, Reference proteome","1970569, 1441754, 7813418, 24374639, 11502169, 14562106, 17761666, 22814378","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 201238 / W303-1B / ATCC 76625 / YPH499",144,426,445,167,475,526]
[null,"P52043","IPMed?",0.96545,1.06742,24.63,7e-14,11,5,"scpC","Propionyl-CoA:succinate CoA transferase","2.8.3.-","Complete proteome, Reference proteome, Transferase","9278503, 16738553, 10769117","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",13,434,445,9,463,492]
[]
["ACT01_02765","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"G2SYC0","_",0.98673,1,48.88,{"v":4e-140,"d":"4.00E-140"},1,2,"_","Butyryl-CoA:acetate CoA-transferase","2.8.3.-","Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","16385128, 26543119","Roseburia hominis (strain DSM 16839 / NCIMB 14029 / A2-183)","DSM 16839 / NCIMB 14029 / A2-183 / DSM 16839 / NCIMB 14029 / A2-183",9,449,452,5,446,446]
[null,"B0MC58","_",0.98894,1.00224,49.89,{"v":3e-137,"d":"3.00E-137"},2,3,"_","Butyryl-CoA:acetate CoA-transferase","2.8.3.-","Complete proteome, Fatty acid metabolism, Lipid metabolism, Transferase",16385128,"Anaerostipes caccae (strain DSM 14662 / NCIMB 13811 / L1-92)","DSM 14662 / NCIMB 13811 / L1-92",9,449,452,5,446,446]
[null,"Q0AVM5","IPMed?",0.99336,1.00447,48.78,{"v":2E-131,"d":"2.00E-131"},3,2,"_","Probable butyrate:acetyl-CoA coenzyme A-transferase","2.8.3.-","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",6,449,452,4,445,447]
[null,"P38942","IPMed?",0.96239,1.01399,40.92,{"v":2e-88,"d":"2.00E-88"},4,6,"cat2","4-hydroxybutyrate coenzyme A transferase","2.8.3.-","Complete proteome, Reference proteome, Transferase","18218779, 8550525","Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)","ATCC 8527 / DSM 555 / NCIMB 10680",9,440,452,5,427,429]
[null,"P38946","IPMed?",0.9145,1.0885,23.78,{"v":8e-21,"d":"8.00E-21"},5,2,"cat1","Succinyl-CoA:coenzyme A transferase","2.8.3.-","Complete proteome, Reference proteome, Transferase","8550525, 18218779","Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)","ATCC 8527 / DSM 555 / NCIMB 10680",12,440,452,52,508,538]
[null,"P52043","IPMed?",0.93089,1.01327,25.33,{"v":2e-17,"d":"2.00E-17"},6,3,"scpC","Propionyl-CoA:succinate CoA transferase","2.8.3.-","Complete proteome, Reference proteome, Transferase","9278503, 16738553, 10769117","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",11,439,452,55,463,492]
[null,"P83773","IPMed?",0.95992,1.11283,22.07,{"v":2e-17,"d":"2.00E-17"},7,4,"ACH1","Acetyl-CoA hydrolase","3.1.2.1","Complete proteome, Cytoplasm, Direct protein sequencing, Hydrolase, Reference proteome","15123810, 17419877, 24025428, 15378761","Candida albicans (strain SC5314 / ATCC MYA-2876)","SC5314 / ATCC MYA-2876 / SC5314 / ATCC MYA-2876 / SC5314 / ATCC MYA-2876 / SC5314 / ATCC MYA-2876",11,450,452,14,492,524]
[null,"P15937","IPMed?",0.92571,1.07522,23.66,{"v":7e-16,"d":"7.00E-16"},8,6,"acu-8","Acetyl-CoA hydrolase","3.1.2.1","Complete proteome, Cytoplasm, Hydrolase, Reference proteome","2140429, 12712197, 1357077","Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)","ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987",13,436,452,21,482,525]
[null,"Q754Q2","_",0.9522,1.10177,23.09,{"v":9e-16,"d":"9.00E-16"},9,2,"ACH1","Acetyl-CoA hydrolase","3.1.2.1","Complete proteome, Cytoplasm, Hydrolase, Reference proteome","15001715, 23749448","Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)","ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056 / ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056",11,450,452,16,494,523]
[null,"P32316","IPMed?",0.91065,1.05973,24.84,2E-14,10,6,"ACH1","Acetyl-CoA hydrolase","3.1.2.1","Acetylation, Complete proteome, Cytoplasm, Direct protein sequencing, Glycoprotein, Hydrolase, Phosphoprotein, Reference proteome","1970569, 1441754, 7813418, 24374639, 11502169, 14562106, 17761666, 22814378","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 201238 / W303-1B / ATCC 76625 / YPH499",11,431,452,16,475,526]
[null,"B3EY95","IPMed?",0.95446,1.06637,21.58,2e-09,11,8,"_","Succinyl-CoA:acetate CoA-transferase","2.8.3.18","3D-structure, Transferase","18502856, 23030530","Acetobacter aceti","1023 / 1023 / 1023",12,434,452,11,466,505]
[]
["ACT01_03685","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"B0MC58","_",1,1.00225,43.72,{"v":2e-130,"d":"2.00E-130"},1,4,"_","Butyryl-CoA:acetate CoA-transferase","2.8.3.-","Complete proteome, Fatty acid metabolism, Lipid metabolism, Transferase",16385128,"Anaerostipes caccae (strain DSM 14662 / NCIMB 13811 / L1-92)","DSM 14662 / NCIMB 13811 / L1-92",1,444,445,1,446,446]
[null,"G2SYC0","_",1,1.00225,44.62,{"v":4e-130,"d":"4.00E-130"},2,4,"_","Butyryl-CoA:acetate CoA-transferase","2.8.3.-","Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","16385128, 26543119","Roseburia hominis (strain DSM 16839 / NCIMB 14029 / A2-183)","DSM 16839 / NCIMB 14029 / A2-183 / DSM 16839 / NCIMB 14029 / A2-183",1,444,445,1,446,446]
[null,"Q0AVM5","IPMed?",0.98434,0.98876,41.82,{"v":2e-115,"d":"2.00E-115"},3,4,"_","Probable butyrate:acetyl-CoA coenzyme A-transferase","2.8.3.-","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",6,444,445,8,445,447]
[null,"P38942","IPMed?",0.96629,1.00233,39.07,{"v":6e-85,"d":"6.00E-85"},4,7,"cat2","4-hydroxybutyrate coenzyme A transferase","2.8.3.-","Complete proteome, Reference proteome, Transferase","18218779, 8550525","Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)","ATCC 8527 / DSM 555 / NCIMB 10680",1,430,445,1,422,429]
[null,"P38946","IPMed?",0.72119,0.87191,25.52,{"v":5e-19,"d":"5.00E-19"},5,5,"cat1","Succinyl-CoA:coenzyme A transferase","2.8.3.-","Complete proteome, Reference proteome, Transferase","8550525, 18218779","Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)","ATCC 8527 / DSM 555 / NCIMB 10680",88,434,445,137,507,538]
[null,"P52043","IPMed?",0.96748,1.06966,25.63,{"v":2e-17,"d":"2.00E-17"},6,2,"scpC","Propionyl-CoA:succinate CoA transferase","2.8.3.-","Complete proteome, Reference proteome, Transferase","9278503, 16738553, 10769117","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",11,434,445,7,463,492]
[null,"P15937","IPMed?",0.93333,1.10112,22.86,{"v":2E-16,"d":"2.00E-16"},7,3,"acu-8","Acetyl-CoA hydrolase","3.1.2.1","Complete proteome, Cytoplasm, Hydrolase, Reference proteome","2140429, 12712197, 1357077","Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)","ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987",8,432,445,20,483,525]
[null,"P83773","IPMed?",0.9313,1.09663,23.16,{"v":5e-16,"d":"5.00E-16"},8,7,"ACH1","Acetyl-CoA hydrolase","3.1.2.1","Complete proteome, Cytoplasm, Direct protein sequencing, Hydrolase, Reference proteome","15123810, 17419877, 24025428, 15378761","Candida albicans (strain SC5314 / ATCC MYA-2876)","SC5314 / ATCC MYA-2876 / SC5314 / ATCC MYA-2876 / SC5314 / ATCC MYA-2876 / SC5314 / ATCC MYA-2876",7,429,445,14,476,524]
[null,"P32316","IPMed?",0.95817,1.13258,23.21,1E-14,9,4,"ACH1","Acetyl-CoA hydrolase","3.1.2.1","Acetylation, Complete proteome, Cytoplasm, Direct protein sequencing, Glycoprotein, Hydrolase, Phosphoprotein, Reference proteome","1970569, 1441754, 7813418, 24374639, 11502169, 14562106, 17761666, 22814378","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 201238 / W303-1B / ATCC 76625 / YPH499",7,443,445,16,487,526]
[null,"B3EY95","IPMed?",0.94257,1.06966,23.95,6e-14,10,4,"_","Succinyl-CoA:acetate CoA-transferase","2.8.3.18","3D-structure, Transferase","18502856, 23030530","Acetobacter aceti","1023 / 1023 / 1023",9,429,445,12,466,505]
[null,"P23673","IPMed?",0.4427,0.8914,24.37,0.067,11,1,"ctfB","Butyrate--acetoacetate CoA-transferase subunit B","2.8.3.9","Complete proteome, Direct protein sequencing, Plasmid, Reference proteome, Transferase","2254264, 8226639, 8423010, 11466286, 2383002","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 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",209,405,445,20,183,221]
[null,"P13635","IPMed?",0.07838,0.18652,32.53,0.24,12,1,"Cp","Ceruloplasmin","1.16.3.1","3D-structure, Complete proteome, Copper, Copper transport, Disulfide bond, Glycoprotein, Ion transport, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Secreted, Signal, Transport","2332446, 3818625, 14707133","Rattus norvegicus","Sprague-Dawley",286,367,445,233,311,1059]
[]
["ACT01_04510","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"D8GR66","IPMed?",0.99125,1.00443,57.17,{"v":7e-179,"d":"7.00E-179"},1,1,"rnfC","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit C","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Repeat, Translocase, Transport","20616070, 23269825","Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC)","ATCC 55383 / DSM 13528 / PETC / ATCC 55383 / DSM 13528 / PETC",1,450,451,1,449,457]
[null,"H6LC32","IPMed?",0.97783,0.99549,46.26,{"v":2e-134,"d":"2.00E-134"},2,1,"rnfC","Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit C","7.2.1.2","4Fe-4S, Cell membrane, Complete proteome, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Reference proteome, Repeat, Translocase, Transport","17873051, 19222539, 20921383, 24045950","Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",4,438,451,7,440,443]
[null,"Q52716","IPMed?",0.88054,1.0133,40.04,{"v":9E-103,"d":"9.00E-103"},3,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Nitrogen fixation, Repeat, Translocase, Transport","8264535, 9492268","Rhodobacter capsulatus","B10S / ATCC 33303 / B10",7,450,451,19,470,519]
[null,"D5ARZ1","IPMed?",0.88054,1.0133,40.04,{"v":9E-103,"d":"9.00E-103"},3,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Nitrogen fixation, Reference proteome, Repeat, Translocase, Transport","20418398, 9154934","Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)","ATCC BAA-309 / NBRC 16581 / SB1003 / ATCC BAA-309 / NBRC 16581 / SB1003",7,450,451,19,470,519]
[null,"Q9KT88","_",0.57881,0.99335,38.39,{"v":1e-95,"d":"1.00E-95"},4,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport",10952301,"Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","ATCC 39315 / El Tor Inaba N16961",8,450,451,18,458,774]
[null,"A0A0H3AJC2","IPMed?",0.57956,0.99335,38.39,{"v":1e-95,"d":"1.00E-95"},4,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",25831459,"Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395",8,450,451,18,458,773]
[null,"Q1C7K3","_",0.73065,1.00443,37.97,{"v":3e-93,"d":"3.00E-93"},5,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",16740952,"Yersinia pestis bv. Antiqua (strain Antiqua)","Antiqua",8,450,451,18,466,620]
[null,"A1JM81","_",0.6528,1.00887,38.24,{"v":7e-93,"d":"7.00E-93"},6,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",17173484,"Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)","NCTC 13174 / 8081",8,450,451,18,466,697]
[null,"A8GE00","_",0.633,0.9867,38.65,{"v":8e-93,"d":"8.00E-93"},7,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport","_","Serratia proteamaculans (strain 568)","_",8,444,451,18,458,703]
[null,"Q1CIY9","_",0.68741,1.00443,37.97,{"v":9e-93,"d":"9.00E-93"},8,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",16740952,"Yersinia pestis bv. Antiqua (strain Nepal516)","Nepal516",8,450,451,18,466,659]
[null,"A9R8U6","_",0.68741,1.00443,37.97,{"v":9e-93,"d":"9.00E-93"},8,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",20061468,"Yersinia pestis bv. Antiqua (strain Angola)","Angola",8,450,451,18,466,659]
[null,"B2K4K0","_",0.68741,1.00443,37.97,{"v":9e-93,"d":"9.00E-93"},8,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport","_","Yersinia pseudotuberculosis serotype IB (strain PB1/+)","_",8,450,451,18,466,659]
[null,"A7FHZ3","_",0.649,1.00443,37.97,{"v":2E-92,"d":"2.00E-92"},9,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",17784789,"Yersinia pseudotuberculosis serotype O:1b (strain IP 31758)","IP 31758",8,450,451,18,466,698]
[null,"B1JKN4","_",0.649,1.00443,37.97,{"v":8e-92,"d":"8.00E-92"},10,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport","_","Yersinia pseudotuberculosis serotype O:3 (strain YPIII)","_",8,450,451,18,466,698]
[null,"P77611","IPMed?",0.61486,1.00887,37.58,{"v":4e-87,"d":"4.00E-87"},11,1,"rsxC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport","9097039, 9278503, 16738553, 12773378","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",8,450,451,18,466,740]
[null,"Q8TSY4","IPMed?",0.95787,0.96644,30.56,{"v":9e-62,"d":"9.00E-62"},12,1,"rnfC","Ion-translocating oxidoreductase complex subunit C","7.2.1.-","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport","11932238, 23066798","Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)","ATCC 35395 / DSM 2834 / JCM 12185 / C2A / ATCC 35395 / DSM 2834 / JCM 12185 / C2A",24,432,451,17,434,447]
[null,"Q46507","IPMed?",0.6449,0.70067,26.27,9e-07,13,2,"hndC","NADP-reducing hydrogenase subunit HndC","1.12.1.3","4Fe-4S, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat","7751270, 9703971","Desulfovibrio fructosivorans","_",124,380,451,48,357,490]
[null,"P31979","IPMed?",0.5898,0.59775,25.19,5e-06,14,2,"nuoF","NADH-quinone oxidoreductase subunit F","7.1.1.-","4Fe-4S, Complete proteome, Direct protein sequencing, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Ubiquinone","7690854, 8157582, 9205837, 9278503, 16738553, 8366049, 7607227","Escherichia coli (strain K12)","K12 / AN387 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / W3110 / ATCC 27325 / DSM 5911",99,318,451,17,280,445]
[null,"Q56222","IPMed?",0.72062,0.74201,23.38,8e-06,16,2,"nqo1","NADH-quinone oxidoreductase subunit 1","7.1.1.-","3D-structure, 4Fe-4S, Cell membrane, Complete proteome, Direct protein sequencing, Flavoprotein, FMN, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Quinone, Reference proteome, Translocase","9020134, 16584177, 16469879","Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","HB8 / ATCC 27634 / DSM 579 / HB8 / ATCC 27634 / DSM 579",124,390,451,52,372,438]
[null,"P33901","IPMed?",0.5898,0.59775,25.19,8e-06,15,2,"nuoF","NADH-quinone oxidoreductase subunit F","7.1.1.-","4Fe-4S, Complete proteome, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Quinone, Reference proteome, Translocase, Ubiquinone","8234329, 11677609","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720",99,318,451,17,280,445]
[]
["ACT01_04515","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"D8GR67","IPMed?",0.92754,0.96677,59.69,{"v":3E-131,"d":"3.00E-131"},1,1,"rnfD","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit D","7.1.1.-","Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, NAD, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","20616070, 23269825","Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC)","ATCC 55383 / DSM 13528 / PETC / ATCC 55383 / DSM 13528 / PETC",23,337,345,12,328,331]
[null,"H6LC31","IPMed?",0.95072,1.03145,43.9,{"v":3e-87,"d":"3.00E-87"},2,1,"rnfD","Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit D","7.2.1.2","Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, NAD, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","17873051, 19222539, 20921383, 24045950","Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",17,342,345,1,313,318]
[null,"A1WTR8","_",0.96919,1.0029,35.26,{"v":7e-65,"d":"7.00E-65"},3,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","_","Halorhodospira halophila (strain DSM 244 / SL1)","_",26,340,345,6,345,357]
[null,"Q9EVN4","_",0.9435,0.96812,36.83,{"v":4e-63,"d":"4.00E-63"},4,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","_","Pseudomonas stutzeri","_",35,337,345,5,331,354]
[null,"A6VQ43","_",0.99155,1.02029,36.65,{"v":1E-61,"d":"1.00E-61"},5,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",21118570,"Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / 130Z)","ATCC 55618 / DSM 22257 / 130Z",24,337,345,4,348,355]
[null,"Q0VP38","_",0.97971,0.9883,34.02,{"v":4e-60,"d":"4.00E-60"},6,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",16878126,"Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2)","ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2",20,337,345,1,333,342]
[null,"B6IB68","_",1.00284,1.02319,33.14,{"v":2e-59,"d":"2.00E-59"},7,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",18931093,"Escherichia coli (strain SE11)","SE11",24,340,345,5,351,352]
[null,"B7M0I7","_",1.00284,1.02319,33.14,{"v":2e-59,"d":"2.00E-59"},7,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",19165319,"Escherichia coli O8 (strain IAI1)","IAI1",24,340,345,5,351,352]
[null,"B7L5I3","_",1.00284,1.02319,33.14,{"v":2e-59,"d":"2.00E-59"},7,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",19165319,"Escherichia coli (strain 55989 / EAEC)","55989 / EAEC",24,340,345,5,351,352]
[null,"B1LEQ6","_",1.00284,1.02319,33.14,{"v":3e-59,"d":"3.00E-59"},8,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",18708504,"Escherichia coli (strain SMS-3-5 / SECEC)","SMS-3-5 / SECEC",24,340,345,5,351,352]
[null,"B7NU03","_",1.00284,1.02319,32.86,{"v":5e-59,"d":"5.00E-59"},9,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",19165319,"Escherichia coli O7:K1 (strain IAI39 / ExPEC)","IAI39 / ExPEC",24,340,345,5,351,352]
[null,"B5Z464","_",1.00284,1.02319,32.86,{"v":5e-59,"d":"5.00E-59"},9,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",22135463,"Escherichia coli O157:H7 (strain EC4115 / EHEC)","EC4115 / EHEC",24,340,345,5,351,352]
[null,"P58325","_",1.00284,1.02319,32.86,{"v":5e-59,"d":"5.00E-59"},9,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",24,340,345,5,351,352]
[null,"B7URX1","_",1.00284,1.02319,32.86,{"v":5e-59,"d":"5.00E-59"},9,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",18952797,"Escherichia coli O127:H6 (strain E2348/69 / EPEC)","E2348/69 / EPEC",24,340,345,5,351,352]
[null,"B2U2C9","_",0.9858,1.0058,34.01,{"v":7e-59,"d":"7.00E-59"},10,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","_","Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)","_",24,340,345,5,351,352]
[null,"P76182","IPMed?",1.00284,1.02319,32.86,{"v":7e-59,"d":"7.00E-59"},11,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","9278503, 16738553, 12773378","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",24,340,345,5,351,352]
[null,"Q320Y7","_",0.9858,1.0058,34.01,{"v":7e-59,"d":"7.00E-59"},10,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",16275786,"Shigella boydii serotype 4 (strain Sb227)","Sb227",24,340,345,5,351,352]
[null,"A5F2R1","IPMed?",1.01149,1.02029,32.67,{"v":2E-50,"d":"2.00E-50"},12,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","19115014, 18831535, 25831459","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",24,337,345,5,347,348]
[null,"Q8TSY3","IPMed?",0.92754,1.11111,30.94,{"v":6e-50,"d":"6.00E-50"},13,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.2.1.-","Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","11932238, 23066798","Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)","ATCC 35395 / DSM 2834 / JCM 12185 / C2A / ATCC 35395 / DSM 2834 / JCM 12185 / C2A",21,339,345,3,285,288]
[null,"Q52715","IPMed?",0.85475,0.88696,36.93,{"v":1e-49,"d":"1.00E-49"},14,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Electron transport, Flavoprotein, FMN, Membrane, Nitrogen fixation, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","8264535, 9492268","Rhodobacter capsulatus","B10S / ATCC 33303 / B10",26,303,345,6,306,358]
[null,"Q9KPS2","IPMed?",0.89398,1.07536,29.65,{"v":1e-36,"d":"1.00E-36"},15,1,"nqrB","Na(+)-translocating NADH-quinone reductase subunit B","7.2.1.1","3D-structure, Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","10077658, 10952301","Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","ATCC 39315 / El Tor Inaba N16961 / ATCC 39315 / El Tor Inaba N16961",22,331,345,39,400,415]
[null,"A5F5X0","IPMed?",0.89398,1.07536,29.65,{"v":1e-36,"d":"1.00E-36"},15,1,"nqrB","Na(+)-translocating NADH-quinone reductase subunit B","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","19115014, 11888296, 20558724, 22366169","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",22,331,345,39,400,415]
[null,"Q9RFW0","IPMed?",0.60048,0.71884,35.08,{"v":1e-34,"d":"1.00E-34"},16,1,"nqrB","Na(+)-translocating NADH-quinone reductase subunit B","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",10587447,"Vibrio campbellii (strain ATCC BAA-1116 / BB120)","_",97,331,345,160,399,413]
[null,"Q56587","IPMed?",0.89614,1.07536,29.38,{"v":2e-33,"d":"2.00E-33"},17,1,"nqrB","Na(+)-translocating NADH-quinone reductase subunit B","7.2.1.1","Cell inner membrane, Cell membrane, Direct protein sequencing, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7805867, 9490015, 10838078, 10549856, 11163785, 11248187, 11248188","Vibrio alginolyticus","NCIMB 11038 / LMG 3418",22,331,345,39,400,414]
[null,"O05011","IPMed?",0.71533,0.85217,31.63,{"v":3e-31,"d":"3.00E-31"},18,1,"nqrB","Na(+)-translocating NADH-quinone reductase subunit B","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7542800, 8601449","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd / ATCC 51907 / DSM 11121 / KW20 / Rd",52,331,345,120,397,411]
[]
["ACT01_04520","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"D8GR68","IPMed?",0.98378,1,52.2,{"v":2e-57,"d":"2.00E-57"},1,1,"rnfG","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit G","7.1.1.-","Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, NAD, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","20616070, 23269825","Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC)","ATCC 55383 / DSM 13528 / PETC / ATCC 55383 / DSM 13528 / PETC",3,182,182,4,185,185]
[null,"H6LC30","IPMed?",0.90821,1.03297,31.38,{"v":4e-21,"d":"4.00E-21"},2,1,"rnfG","Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit G","7.2.1.2","Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, NAD, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","19222539, 20921383, 24045950","Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",9,174,182,14,200,207]
[null,"A3QEN8","_",0.51887,0.6044,39.09,1E-13,3,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","_","Shewanella loihica (strain ATCC BAA-1088 / PV-4)","_",69,173,182,81,190,212]
[null,"B8E552","_",0.92453,1.07692,31.12,1e-12,4,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","_","Shewanella baltica (strain OS223)","_",6,173,182,7,190,212]
[null,"Q8TSY2","IPMed?",0.98936,1.02198,30.11,4e-12,5,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.2.1.-","Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","11932238, 23066798, 24836163","Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)","ATCC 35395 / DSM 2834 / JCM 12185 / C2A / ATCC 35395 / DSM 2834 / JCM 12185 / C2A",1,174,182,1,181,188]
[null,"C3LTR1","_",0.55024,0.63187,38.26,5e-12,7,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",19115014,"Vibrio cholerae serotype O1 (strain M66-2)","M66-2",69,178,182,80,194,209]
[null,"A4XS49","_",0.52133,0.6044,40,5e-12,6,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","_","Pseudomonas mendocina (strain ymp)","_",69,173,182,84,193,211]
[null,"A5F2S8","IPMed?",0.55024,0.63187,38.26,5e-12,7,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","19115014, 18831535, 25831459","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",69,178,182,80,194,209]
[null,"Q9KT90","_",0.55024,0.63187,38.26,5e-12,7,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",10952301,"Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","ATCC 39315 / El Tor Inaba N16961",69,178,182,80,194,209]
[null,"Q5E6C0","_",0.52381,0.6044,41.82,6e-12,8,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",15703294,"Aliivibrio fischeri (strain ATCC 700601 / ES114)","ATCC 700601 / ES114",69,173,182,81,190,210]
[null,"Q8ZPM4","_",0.5534,0.62637,39.47,8e-12,9,1,"rsxG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",11677609,"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720",64,172,182,74,187,206]
[null,"Q8Z6Q7","_",0.5534,0.62637,38.6,1e-11,10,1,"rsxG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","11677608, 12644504","Salmonella typhi","CT18 / ATCC 700931 / Ty2",64,172,182,74,187,206]
[null,"P77285","IPMed?",0.5534,0.62637,37.72,2e-11,11,1,"rsxG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","9097039, 9278503, 16738553, 12773378","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",64,172,182,74,187,206]
[null,"P97054","IPMed?",0.57604,0.68681,29.6,5e-07,12,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Electron transport, Flavoprotein, FMN, Membrane, Nitrogen fixation, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","8264535, 9492268","Rhodobacter capsulatus","B10S / ATCC 33303 / B10",49,169,182,76,195,217]
[null,"Q56582","IPMed?",0.53516,0.75275,27.74,1E-4,13,1,"nqrC","Na(+)-translocating NADH-quinone reductase subunit C","7.2.1.1","Cell inner membrane, Cell membrane, Direct protein sequencing, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7805867, 7729558, 7805866, 9490015, 10838078, 10549856, 11163785, 11248187, 11248188","Vibrio alginolyticus","NCIMB 11038 / LMG 3418",48,162,182,91,227,256]
[null,"A5F5Y7","IPMed?",0.607,0.85714,25,0.004,14,1,"nqrC","Na(+)-translocating NADH-quinone reductase subunit C","7.2.1.1","3D-structure, Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","10077658, 19115014, 11248234, 11888296, 20558724, 22366169","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",29,162,182,75,228,257]
[null,"Q9RFV9","IPMed?",0.55172,0.79121,27.08,0.013,15,1,"nqrC","Na(+)-translocating NADH-quinone reductase subunit C","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Direct protein sequencing, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",10587447,"Vibrio campbellii (strain ATCC BAA-1116 / BB120)","_",35,161,182,89,231,261]
[null,"P43957","IPMed?",0.56557,0.75824,26.81,0.017,16,1,"nqrC","Na(+)-translocating NADH-quinone reductase subunit C","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7542800, 8601449","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd / ATCC 51907 / DSM 11121 / KW20 / Rd",38,161,182,79,215,244]
[]
["ACT01_04525","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"D8GR69","IPMed?",0.94836,0.97585,64.85,{"v":5e-89,"d":"5.00E-89"},1,1,"rnfE","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit E","7.1.1.-","Cell membrane, Complete proteome, Electron transport, Membrane, NAD, Translocase, Transmembrane, Transmembrane helix, Transport","20616070, 23269825","Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC)","ATCC 55383 / DSM 13528 / PETC / ATCC 55383 / DSM 13528 / PETC",2,203,207,3,204,213]
[null,"H6LC29","IPMed?",0.89855,0.94898,50,{"v":6e-61,"d":"6.00E-61"},2,1,"rnfE","Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit E","7.2.1.2","Cell membrane, Complete proteome, Electron transport, Membrane, NAD, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","19222539, 20921383, 24045950","Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",1,186,207,1,186,196]
[null,"Q8TSY1","IPMed?",0.99061,1.01932,44.55,{"v":6e-48,"d":"6.00E-48"},3,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.2.1.-","Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","11932238, 23066798","Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)","ATCC 35395 / DSM 2834 / JCM 12185 / C2A / ATCC 35395 / DSM 2834 / JCM 12185 / C2A",1,207,207,9,212,213]
[null,"Q8KA17","_",0.89686,0.96618,40.5,{"v":8e-47,"d":"8.00E-47"},4,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",12089438,"Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)","Sg",1,187,207,1,200,223]
[null,"B8F7B0","_",0.87336,0.96618,40.5,{"v":6e-44,"d":"6.00E-44"},5,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",19074396,"Haemophilus parasuis serovar 5 (strain SH0165)","SH0165",2,187,207,21,220,229]
[null,"Q15RL0","_",0.91379,1.02415,40.09,{"v":7e-44,"d":"7.00E-44"},6,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport","_","Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)","_",1,198,207,1,212,232]
[null,"Q4QJQ3","_",0.85106,0.96618,40,{"v":1e-43,"d":"1.00E-43"},7,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",15968074,"Haemophilus influenzae (strain 86-028NP)","86-028NP",2,187,207,26,225,235]
[null,"A3QEN9","_",0.88362,0.99034,39.02,{"v":1e-43,"d":"1.00E-43"},8,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport","_","Shewanella loihica (strain ATCC BAA-1088 / PV-4)","_",9,200,207,10,214,232]
[null,"A5UFC5","_",0.8547,0.96618,40,{"v":1e-43,"d":"1.00E-43"},7,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",17550610,"Haemophilus influenzae (strain PittGG)","PittGG",2,187,207,25,224,234]
[null,"Q57020","_",0.85106,0.96618,40,{"v":1e-43,"d":"1.00E-43"},7,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",2,187,207,26,225,235]
[null,"Q89AW5","_",0.82988,0.96618,38,{"v":2e-43,"d":"2.00E-43"},9,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",12522265,"Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)","Bp",2,188,207,3,202,241]
[null,"B5FCN0","_",0.86344,0.94686,41.33,{"v":9e-43,"d":"9.00E-43"},10,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport","_","Aliivibrio fischeri (strain MJ11)","_",5,187,207,6,201,227]
[null,"A5F2S7","IPMed?",0.87826,0.97585,40.1,{"v":1E-42,"d":"1.00E-42"},11,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport","19115014, 25831459","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",10,196,207,11,210,230]
[null,"P97055","IPMed?",0.8107,0.95169,42.13,{"v":2E-41,"d":"2.00E-41"},12,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Electron transport, Membrane, Nitrogen fixation, Translocase, Transmembrane, Transmembrane helix, Transport","8264535, 9492268","Rhodobacter capsulatus","B10S / ATCC 33303 / B10",5,187,207,7,202,243]
[null,"P77179","IPMed?",0.90476,1.00966,35.89,{"v":2e-40,"d":"2.00E-40"},13,1,"rsxE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","9097039, 9278503, 16738553, 10411911, 12773378, 15919996","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / JM109 / ATCC 53323 / K12 / MG1655 / ATCC 47076",6,200,207,7,214,231]
[null,"P43958","IPMed?",0.89904,0.90338,36.9,{"v":2E-35,"d":"2.00E-35"},14,1,"nqrD","Na(+)-translocating NADH-quinone reductase subunit D","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7542800, 8601449","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd / ATCC 51907 / DSM 11121 / KW20 / Rd",11,192,207,15,201,208]
[null,"A5F5Y6","IPMed?",0.95714,0.97101,36.32,{"v":3e-35,"d":"3.00E-35"},15,1,"nqrD","Na(+)-translocating NADH-quinone reductase subunit D","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","19115014, 11888296, 20558724","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",11,206,207,15,210,210]
[null,"Q9X4Q6","IPMed?",0.95714,0.97101,36.32,{"v":3e-35,"d":"3.00E-35"},15,1,"nqrD","Na(+)-translocating NADH-quinone reductase subunit D","7.2.1.1","3D-structure, Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","10077658, 10952301","Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","ATCC 39315 / El Tor Inaba N16961 / ATCC 39315 / El Tor Inaba N16961",11,206,207,15,210,210]
[null,"Q9RFV8","IPMed?",1,1.01449,35.71,{"v":3e-35,"d":"3.00E-35"},16,1,"nqrD","Na(+)-translocating NADH-quinone reductase subunit D","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",10587447,"Vibrio campbellii (strain ATCC BAA-1116 / BB120)","_",2,206,207,6,210,210]
[null,"Q57095","IPMed?",1,1.01449,35.24,{"v":1e-34,"d":"1.00E-34"},17,1,"nqrD","Na(+)-translocating NADH-quinone reductase subunit D","7.2.1.1","Cell inner membrane, Cell membrane, Direct protein sequencing, Ion transport, Membrane, NAD, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7805867, 7729558, 9490015, 10549856, 11248187, 11248188","Vibrio alginolyticus","NCIMB 11038 / LMG 3418",2,206,207,6,210,210]
[]
["ACT01_04530","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"D8GR70","IPMed?",0.98964,1,70.16,{"v":1e-95,"d":"1.00E-95"},1,1,"rnfA","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit A","7.1.1.-","Cell membrane, Complete proteome, Electron transport, Membrane, NAD, Translocase, Transmembrane, Transmembrane helix, Transport","20616070, 23269825","Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC)","ATCC 55383 / DSM 13528 / PETC / ATCC 55383 / DSM 13528 / PETC",1,191,191,1,191,193]
[null,"Q7MM81","_",0.99479,1,52.88,{"v":6e-70,"d":"6.00E-70"},2,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",14656965,"Vibrio vulnificus (strain YJ016)","YJ016",1,191,191,1,191,192]
[null,"Q8D890","_",0.99479,1,52.88,{"v":6e-70,"d":"6.00E-70"},2,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport","_","Vibrio vulnificus (strain CMCP6)","_",1,191,191,1,191,192]
[null,"B6EGH7","_",0.98964,1,52.88,{"v":2e-69,"d":"2.00E-69"},3,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",19099551,"Aliivibrio salmonicida (strain LFI1238)","LFI1238",1,191,191,1,191,193]
[null,"Q7N4G1","_",0.98964,1,51.31,{"v":3e-69,"d":"3.00E-69"},4,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",14528314,"Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)","DSM 15139 / CIP 105565 / TT01",1,191,191,1,191,193]
[null,"Q5E6B6","_",0.98964,1,53.4,{"v":5e-69,"d":"5.00E-69"},5,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",15703294,"Aliivibrio fischeri (strain ATCC 700601 / ES114)","ATCC 700601 / ES114",1,191,191,1,191,193]
[null,"Q9KT86","_",0.98964,1,52.88,{"v":7e-69,"d":"7.00E-69"},6,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",10952301,"Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","ATCC 39315 / El Tor Inaba N16961",1,191,191,1,191,193]
[null,"A0A0H3AKU6","IPMed?",0.89671,1,52.88,{"v":1e-68,"d":"1.00E-68"},7,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",25831459,"Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395",1,191,191,21,211,213]
[null,"B7VLT9","_",0.99479,1,51.83,{"v":1e-68,"d":"1.00E-68"},8,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","_","Vibrio tasmaniensis (strain LGP32)","_",1,191,191,1,191,192]
[null,"Q87MX4","_",0.99479,1,52.36,{"v":2e-68,"d":"2.00E-68"},9,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",12620739,"Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)","RIMD 2210633",1,191,191,1,191,192]
[null,"A7MVC5","_",0.99479,1,52.36,{"v":3E-68,"d":"3.00E-68"},10,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport","_","Vibrio campbellii (strain ATCC BAA-1116 / BB120)","_",1,191,191,1,191,192]
[null,"P0A766","IPMed?",0.98964,1,50.26,{"v":3e-66,"d":"3.00E-66"},11,1,"rsxA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","9278503, 16738553, 10411911, 12773378, 15919996","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / JM109 / ATCC 53323 / K12 / MG1655 / ATCC 47076",1,191,191,1,191,193]
[null,"H6LC28","IPMed?",0.95833,0.96335,51.09,{"v":4e-63,"d":"4.00E-63"},12,1,"rnfA","Na(+)-translocating ferredoxin:NAD(+) oxidoreductase complex subunit A","7.2.1.2","Cell membrane, Complete proteome, Electron transport, Membrane, NAD, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","19222539, 20921383, 24045950","Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 / ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",7,190,191,6,189,192]
[null,"Q8TSY0","IPMed?",0.94472,0.98429,45.21,{"v":3e-55,"d":"3.00E-55"},13,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.2.1.-","Cell membrane, Complete proteome, Electron transport, Membrane, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","11932238, 23066798","Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)","ATCC 35395 / DSM 2834 / JCM 12185 / C2A / ATCC 35395 / DSM 2834 / JCM 12185 / C2A",5,191,191,9,196,199]
[null,"P0CZ13","IPMed?",0.98964,1,43.98,{"v":2e-53,"d":"2.00E-53"},14,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Electron transport, Membrane, Nitrogen fixation, Translocase, Transmembrane, Transmembrane helix, Transport","8264535, 9492268","Rhodobacter capsulatus","B10S / ATCC 33303 / B10",1,191,191,1,191,193]
[null,"D5ARY9","IPMed?",0.98964,1,43.98,{"v":2e-53,"d":"2.00E-53"},14,1,"rnfA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Complete proteome, Electron transport, Membrane, Nitrogen fixation, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","8199774, 20418398, 9154934","Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)","ATCC BAA-309 / NBRC 16581 / SB1003 / ATCC BAA-309 / NBRC 16581 / SB1003 / ATCC BAA-309 / NBRC 16581 / SB1003",1,191,191,1,191,193]
[null,"P71342","IPMed?",0.9899,1.02618,42.35,{"v":2e-47,"d":"2.00E-47"},15,1,"nqrE","Na(+)-translocating NADH-quinone reductase subunit E","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7542800, 8601449","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd / ATCC 51907 / DSM 11121 / KW20 / Rd",1,190,191,1,196,198]
[null,"Q9X4Q7","IPMed?",0.9899,1.02618,39.8,{"v":7e-46,"d":"7.00E-46"},16,1,"nqrE","Na(+)-translocating NADH-quinone reductase subunit E","7.2.1.1","3D-structure, Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","10077658, 10952301","Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","ATCC 39315 / El Tor Inaba N16961 / ATCC 39315 / El Tor Inaba N16961",1,190,191,1,196,198]
[null,"A5F5Y5","IPMed?",0.9899,1.02618,39.8,{"v":7e-46,"d":"7.00E-46"},16,1,"nqrE","Na(+)-translocating NADH-quinone reductase subunit E","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","19115014, 11888296, 20558724","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",1,190,191,1,196,198]
[null,"Q5E6X2","IPMed?",0.9899,1.02618,38.78,{"v":8e-45,"d":"8.00E-45"},17,1,"nqrE","Na(+)-translocating NADH-quinone reductase subunit E","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","15703294, 18366731","Aliivibrio fischeri (strain ATCC 700601 / ES114)","ATCC 700601 / ES114",1,190,191,1,196,198]
[null,"Q9RFV7","IPMed?",0.9899,1.02618,39.8,{"v":1e-44,"d":"1.00E-44"},18,1,"nqrE","Na(+)-translocating NADH-quinone reductase subunit E","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",10587447,"Vibrio campbellii (strain ATCC BAA-1116 / BB120)","_",1,190,191,1,196,198]
[]
["ACT01_04535","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"D8GR71","IPMed?",0.96864,0.97887,57.91,{"v":3e-118,"d":"3.00E-118"},1,1,"rnfB","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit B","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Repeat, Translocase, Transport","20616070, 23269825","Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC)","ATCC 55383 / DSM 13528 / PETC / ATCC 55383 / DSM 13528 / PETC",6,283,287,3,277,284]
[null,"Q8TSX9","IPMed?",0.91289,0.99242,39.31,{"v":1e-63,"d":"1.00E-63"},2,1,"rnfB","Ion-translocating oxidoreductase complex subunit B","7.2.1.-","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transmembrane, Transmembrane helix, Transport","11932238, 23066798, 24836163","Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)","ATCC 35395 / DSM 2834 / JCM 12185 / C2A / ATCC 35395 / DSM 2834 / JCM 12185 / C2A",8,269,287,6,261,264]
[null,"H6LC27","IPMed?",0.7988,0.92683,38.35,{"v":2E-55,"d":"2.00E-55"},3,1,"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",5,269,287,2,261,333]
[null,"B5FIE6","_",0.66551,0.99479,34.55,{"v":2e-28,"d":"2.00E-28"},4,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",21602358,"Salmonella dublin (strain CT_02021853)","CT_02021853",6,196,287,3,168,192]
[null,"B4THD5","_",0.66551,0.99479,34.55,{"v":2e-28,"d":"2.00E-28"},4,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",21602358,"Salmonella heidelberg (strain SL476)","SL476",6,196,287,3,168,192]
[null,"A9N024","_",0.66551,0.99479,34.55,{"v":2e-28,"d":"2.00E-28"},4,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport","_","Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7)","_",6,196,287,3,168,192]
[null,"Q8ZPM1","_",0.66551,0.99479,34.55,{"v":2e-28,"d":"2.00E-28"},4,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport",11677609,"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720",6,196,287,3,168,192]
[null,"B5F6I9","_",0.66551,0.99479,34.55,{"v":4e-28,"d":"4.00E-28"},5,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",21602358,"Salmonella agona (strain SL483)","SL483",6,196,287,3,168,192]
[null,"Q8Z6R0","_",0.66551,0.99479,34.55,{"v":4e-28,"d":"4.00E-28"},5,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport","11677608, 12644504","Salmonella typhi","CT18 / ATCC 700931 / Ty2",6,196,287,3,168,192]
[null,"B4TV18","_",0.66551,0.99479,34.55,{"v":4e-28,"d":"4.00E-28"},5,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",21602358,"Salmonella schwarzengrund (strain CVM19633)","CVM19633",6,196,287,3,168,192]
[null,"B5BKB1","_",0.66551,0.99479,34.55,{"v":4e-28,"d":"4.00E-28"},5,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",19159446,"Salmonella paratyphi A (strain AKU_12601)","AKU_12601",6,196,287,3,168,192]
[null,"C0Q507","_",0.66551,0.99479,34.55,{"v":4e-28,"d":"4.00E-28"},5,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",19229335,"Salmonella paratyphi C (strain RKS4594)","RKS4594",6,196,287,3,168,192]
[null,"A7MMM3","_",0.65157,0.97396,33.69,{"v":4e-28,"d":"4.00E-28"},6,1,"rnfB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",20221447,"Cronobacter sakazakii (strain ATCC BAA-894)","ATCC BAA-894",8,194,287,5,166,192]
[null,"A9MRW7","_",0.66551,0.99479,33.51,{"v":6e-28,"d":"6.00E-28"},7,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport","_","Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980)","_",6,196,287,3,168,192]
[null,"B4T595","_",0.66551,0.99479,34.03,{"v":1E-27,"d":"1.00E-27"},8,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",21602358,"Salmonella newport (strain SL254)","SL254",6,196,287,3,168,192]
[null,"A8GE01","_",0.67247,1.01579,33.16,{"v":4e-27,"d":"4.00E-27"},9,1,"rnfB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport","_","Serratia proteamaculans (strain 568)","_",5,196,287,1,166,190]
[null,"C4ZY91","_",0.65505,0.97917,30.85,{"v":6e-27,"d":"6.00E-27"},10,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",19376874,"Escherichia coli (strain K12 / MC4100 / BW2952)","K12 / MC4100 / BW2952",9,196,287,6,168,192]
[null,"P77223","IPMed?",0.65505,0.97917,30.85,{"v":6e-27,"d":"6.00E-27"},10,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport","9097039, 9278503, 16738553, 12773378","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",9,196,287,6,168,192]
[null,"B1IQC6","_",0.65505,0.97917,30.85,{"v":6e-27,"d":"6.00E-27"},10,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport","_","Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)","_",9,196,287,6,168,192]
[null,"A8A0H1","_",0.65505,0.97917,30.85,{"v":6e-27,"d":"6.00E-27"},10,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",18676672,"Escherichia coli O9:H4 (strain HS)","HS",9,196,287,6,168,192]
[null,"B1XF93","_",0.65505,0.97917,30.85,{"v":6e-27,"d":"6.00E-27"},10,1,"rsxB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transport",18245285,"Escherichia coli (strain K12 / DH10B)","K12 / DH10B",9,196,287,6,168,192]
[null,"A5F2R3","IPMed?",0.66202,0.97436,30.53,{"v":1e-24,"d":"1.00E-24"},11,1,"rnfB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Repeat, Translocase, Transmembrane, Transmembrane helix, Transport","19115014, 25831459","Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","ATCC 39541 / Classical Ogawa 395 / O395 / ATCC 39541 / Classical Ogawa 395 / O395",6,195,287,3,164,195]
[null,"P0CZ14","IPMed?",0.63763,0.97861,29.51,{"v":2E-19,"d":"2.00E-19"},12,1,"rnfB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Direct protein sequencing, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Nitrogen fixation, Repeat, Translocase, Transport","8264535, 9492268","Rhodobacter capsulatus","B10S / ATCC 33303 / B10",8,190,287,2,157,187]
[null,"D5ARZ0","IPMed?",0.63763,0.97861,29.51,{"v":2E-19,"d":"2.00E-19"},12,1,"rnfB","Ion-translocating oxidoreductase complex subunit B","7.-.-.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Nitrogen fixation, Reference proteome, Repeat, Translocase, Transport","8199774, 20418398, 9154934","Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)","ATCC BAA-309 / NBRC 16581 / SB1003 / ATCC BAA-309 / NBRC 16581 / SB1003 / ATCC BAA-309 / NBRC 16581 / SB1003",8,190,287,2,157,187]
[null,"Q00388","IPMed?",0.36181,0.50174,29.17,2e-09,13,2,"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",128,269,287,44,176,398]
[null,"Q50784","IPMed?",0.3665,0.52613,27.81,4e-09,14,2,"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",123,269,287,125,261,412]
[null,"Q49180","IPMed?",0.51214,0.73519,27.96,1e-07,15,2,"mvhB","Polyferredoxin protein MvhB","_","4Fe-4S, Iron, Iron-sulfur, Metal-binding, Repeat",2115877,"Methanothermus fervidus","_",77,269,287,151,339,412]
[null,"Q01700","IPMed?",0.16725,0.82759,37.5,2e-07,16,4,"_","Probable ferredoxin","_","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",1379583,"Methanosarcina thermophila","ATCC 43570 / DSM 1825 / OCM 12 / TM-1",145,192,287,10,57,58]

{"sheet":"UniFIRE ","index":7,"n_rows":368,"n_cols":8,"rows_kept":368}
["ACT01_00410","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000000418","keyword","Oxidoreductase","_","_","RU003369","RuleBase"]
[null,"UR000000418","similarity","Belongs to the LDH/MDH superfamily","_","_","RU003369","RuleBase"]
[]
["ACT01_00445","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000001527","catalytic activity","Pyruvate + CoA + oxidized flavodoxin = acetyl-CoA + CO(2) + reduced flavodoxin","_","_","PIRNR000159","PIR"]
[null,"UR000001527","function","Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Electron transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Oxidoreductase","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","product - EC number","1.2.7.-","_","_","PIRNR000159","PIR"]
[null,"UR000001527","product name","Pyruvate-flavodoxin oxidoreductase","_","_","PIRNR000159","PIR"]
[null,"UR000001527","similarity","Belongs to the nifJ family","_","_","PIRNR000159","PIR"]
[]
["ACT01_00545","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"]
[]
["ACT01_02090","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","Transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Oxidoreductase","_","_","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"]
[]
["ACT01_02810","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","Transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Oxidoreductase","_","_","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"]
[]
["ACT01_03520","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","Transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Oxidoreductase","_","_","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"]
[]
["ACT01_06665","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000001527","catalytic activity","Pyruvate + CoA + oxidized flavodoxin = acetyl-CoA + CO(2) + reduced flavodoxin","_","_","PIRNR000159","PIR"]
[null,"UR000001527","function","Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Electron transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Oxidoreductase","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","product - EC number","1.2.7.-","_","_","PIRNR000159","PIR"]
[null,"UR000001527","product name","Pyruvate-flavodoxin oxidoreductase","_","_","PIRNR000159","PIR"]
[null,"UR000001527","similarity","Belongs to the nifJ family","_","_","PIRNR000159","PIR"]
[]
["ACT01_12570","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","Transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Electron transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Oxidoreductase","_","_","PIRNR000159","PIR"]
[null,"UR000001527","product - EC number","1.2.7.-","_","_","PIRNR000159","PIR"]
[null,"UR000001527","product name","Pyruvate-flavodoxin oxidoreductase","_","_","PIRNR000159","PIR"]
[null,"UR000001527","similarity","Belongs to the nifJ family","_","_","PIRNR000159","PIR"]
[]
["ACT01_05435","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000037499","catalytic activity","ATP + acetate = ADP + acetyl phosphate","_","_","MF_00020","HAMAP"]
[null,"UR000037499","cofactor","Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Mg(2+). Can also accept Mn(2+)","_","_","MF_00020","HAMAP"]
[null,"UR000037499","function","Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction","_","_","MF_00020","HAMAP"]
[null,"UR000037499","gene name","ackA","_","_","MF_00020","HAMAP"]
[null,"UR000037499","GO","GO:0008776","_","_","MF_00020","HAMAP"]
[null,"UR000037499","GO","GO:0005737","_","_","MF_00020","HAMAP"]
[null,"UR000037499","GO","GO:0000287","_","_","MF_00020","HAMAP"]
[null,"UR000037499","GO","GO:0016310","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Nucleotide-binding","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Magnesium","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Cytoplasm","_","_","MF_00020","HAMAP"]
[null,"UR000000717","keyword","Kinase","_","_","RU003835","RuleBase"]
[null,"UR000037499","keyword","Transferase","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Kinase","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","ATP-binding","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Metal-binding","_","_","MF_00020","HAMAP"]
[null,"UR000000717","keyword","Transferase","_","_","RU003835","RuleBase"]
[null,"UR000037499","metal binding","Magnesium",7,7,"MF_00020","HAMAP"]
[null,"UR000037499","metal binding","Magnesium",383,383,"MF_00020","HAMAP"]
[null,"UR000037499","nucleotide binding","ATP",207,211,"MF_00020","HAMAP"]
[null,"UR000037499","nucleotide binding","ATP",282,284,"MF_00020","HAMAP"]
[null,"UR000037499","nucleotide binding","ATP",330,334,"MF_00020","HAMAP"]
[null,"UR000037499","pathway","Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2","_","_","MF_00020","HAMAP"]
[null,"UR000037499","product  name (synonym)","Acetokinase","_","_","MF_00020","HAMAP"]
[null,"UR000037499","product - EC number","2.7.2.1","_","_","MF_00020","HAMAP"]
[null,"UR000037499","product name","Acetate kinase","_","_","MF_00020","HAMAP"]
[null,"UR000000717","similarity","Belongs to the acetokinase family","_","_","RU003835","RuleBase"]
[null,"UR000037499","similarity","Belongs to the acetokinase family","_","_","MF_00020","HAMAP"]
[null,"UR000037499","site","Transition state stabilizer",179,179,"MF_00020","HAMAP"]
[null,"UR000037499","site","Transition state stabilizer",240,240,"MF_00020","HAMAP"]
[null,"UR000037499","site actif","Proton donor/acceptor",147,147,"MF_00020","HAMAP"]
[null,"UR000037499","site binding","ATP",14,14,"MF_00020","HAMAP"]
[null,"UR000037499","site binding","Substrate",90,90,"MF_00020","HAMAP"]
[null,"UR000037499","subcellular location","Cytoplasm","_","_","MF_00020","HAMAP"]
[null,"UR000037499","subunit","Homodimer","_","_","MF_00020","HAMAP"]
[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"]
[]
["ACT01_13325","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"SAAS00923789","keyword","Acyltransferase"]
[null,"SAAS00923780","keyword","Transferase"]
[]
["ACT01_03450","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000136843","cofactor","Name=Zn(2+); Xref=ChEBI:CHEBI:29105","_","_","RU361277","RuleBase"]
[null,"UR000136843","keyword","Metal-binding","_","_","RU361277","RuleBase"]
[null,"UR000136843","keyword","Zinc","_","_","RU361277","RuleBase"]
[null,"UR000136843","similarity","Belongs to the zinc-containing alcohol dehydrogenase family","_","_","RU361277","RuleBase"]
[]
["ACT01_07765","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"]
[]
["ACT01_10835","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"SAAS00649305","keyword","Oxidoreductase"]
[]
["ACT01_00280","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"]
[]
["ACT01_02990","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"]
[]
["ACT01_10950","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"]
[]
["ACT01_11040","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"]
[]
["ACT01_04510","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000090104","cofactor","Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 2 [4Fe-4S] clusters per subunit","_","_","MF_00461","HAMAP"]
[null,"UR000090104","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane","_","_","MF_00461","HAMAP"]
[null,"UR000090104","gene name","rnfC","_","_","MF_00461","HAMAP"]
[null,"UR000090104","GO","GO:0055114","_","_","MF_00461","HAMAP"]
[null,"UR000090104","GO","GO:0022900","_","_","MF_00461","HAMAP"]
[null,"UR000090104","GO","GO:0005886","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Cell membrane","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Metal-binding","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Oxidoreductase","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Transport","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Repeat","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","4Fe-4S","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Iron-sulfur","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Electron transport","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Iron","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Membrane","_","_","MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 1 (4Fe-4S)",367,367,"MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 1 (4Fe-4S)",370,370,"MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 1 (4Fe-4S)",373,373,"MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 2 (4Fe-4S)",377,377,"MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 2 (4Fe-4S)",406,406,"MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 2 (4Fe-4S)",409,409,"MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 2 (4Fe-4S)",412,412,"MF_00461","HAMAP"]
[null,"UR000090104","metal binding","Iron-sulfur 1 (4Fe-4S)",416,416,"MF_00461","HAMAP"]
[null,"UR000090104","product  name (synonym)","Rnf electron transport complex subunit C","_","_","MF_00461","HAMAP"]
[null,"UR000090104","product - EC number","1.18.1.-","_","_","MF_00461","HAMAP"]
[null,"UR000090104","product name","Ion-translocating oxidoreductase complex subunit C","_","_","MF_00461","HAMAP"]
[null,"UR000090104","similarity","Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC subfamily","_","_","MF_00461","HAMAP"]
[null,"UR000090104","subunit","The complex is composed of six subunits: RnfA, RnfB, RnfC, RnfD, RnfE and RnfG","_","_","MF_00461","HAMAP"]
[null,"SAAS00608488, SAAS01039547","cofactor","Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883"]
[null,"SAAS01036652, SAAS01039352, SAAS01039535","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane"]
[null,"SAAS00028344, SAAS00943857, SAAS01039527","keyword","4Fe-4S"]
[null,"SAAS01036632, SAAS01039362, SAAS01039544","keyword","Electron transport"]
[null,"SAAS00429791, SAAS00943838, SAAS01039522","keyword","Iron"]
[null,"SAAS00028405, SAAS00943845, SAAS01039532","keyword","Iron-sulfur"]
[null,"SAAS01036650, SAAS01039354, SAAS01039538","keyword","Membrane"]
[null,"SAAS00028366, SAAS00943864, SAAS01039539","keyword","Metal-binding"]
[null,"SAAS01033193, SAAS01034144, SAAS01039525","keyword","Oxidoreductase"]
[null,"SAAS01033200, SAAS01034695, SAAS01039528","keyword","Repeat"]
[null,"SAAS01036643, SAAS01039349, SAAS01039533","keyword","Transport"]
[null,"SAAS01036653, SAAS01039348, SAAS01039530","similarity","Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC subfamily"]
[]
["ACT01_04515","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000062690","cofactor","Name=FMN; Xref=ChEBI:CHEBI:58210","_","_","MF_00462","HAMAP"]
[null,"UR000062690","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane","_","_","MF_00462","HAMAP"]
[null,"UR000062690","gene name","rnfD","_","_","MF_00462","HAMAP"]
[null,"UR000062690","GO","GO:0005886","_","_","MF_00462","HAMAP"]
[null,"UR000062690","GO","GO:0055114","_","_","MF_00462","HAMAP"]
[null,"UR000062690","GO","GO:0022900","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Flavoprotein","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Membrane","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Phosphoprotein","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","FMN","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Electron transport","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Transmembrane","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Oxidoreductase","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Cell membrane","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Transmembrane helix","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Transport","_","_","MF_00462","HAMAP"]
[null,"UR000062690","modified residue","FMN phosphoryl threonine",175,175,"MF_00462","HAMAP"]
[null,"UR000062690","product  name (synonym)","Rnf electron transport complex subunit D","_","_","MF_00462","HAMAP"]
[null,"UR000062690","product - EC number","1.18.1.-","_","_","MF_00462","HAMAP"]
[null,"UR000062690","product name","Ion-translocating oxidoreductase complex subunit D","_","_","MF_00462","HAMAP"]
[null,"UR000062690","similarity","Belongs to the NqrB/RnfD family","_","_","MF_00462","HAMAP"]
[null,"UR000062690","subunit","The complex is composed of six subunits: RnfA, RnfB, RnfC, RnfD, RnfE and RnfG","_","_","MF_00462","HAMAP"]
[null,"SAAS01034734, SAAS01035299","cofactor","Name=FMN; Xref=ChEBI:CHEBI:58210"]
[null,"SAAS01034728","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane"]
[null,"SAAS01034737","keyword","Cell membrane"]
[null,"SAAS01034732","keyword","Electron transport"]
[null,"SAAS01034738, SAAS01035302","keyword","Flavoprotein"]
[null,"SAAS01034739, SAAS01035309","keyword","FMN"]
[null,"SAAS00951777, SAAS01034741","keyword","Membrane"]
[null,"SAAS01034735, SAAS01035300","keyword","Oxidoreductase"]
[null,"SAAS00951796, SAAS01034736","keyword","Transmembrane"]
[null,"SAAS00951768, SAAS01034724","keyword","Transmembrane helix"]
[null,"SAAS00951776, SAAS01034740","keyword","Transport"]
[null,"SAAS00951779, SAAS01034714","similarity","Belongs to the NqrB/RnfD family"]
[]
["ACT01_04520","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000064652","cofactor","Name=FMN; Xref=ChEBI:CHEBI:58210","_","_","MF_00479","HAMAP"]
[null,"UR000064652","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane","_","_","MF_00479","HAMAP"]
[null,"UR000064652","gene name","rnfG","_","_","MF_00479","HAMAP"]
[null,"UR000064652","GO","GO:0055114","_","_","MF_00479","HAMAP"]
[null,"UR000064652","GO","GO:0005886","_","_","MF_00479","HAMAP"]
[null,"UR000064652","GO","GO:0022900","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Flavoprotein","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Transport","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Membrane","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Transmembrane helix","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Phosphoprotein","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Cell membrane","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Oxidoreductase","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Electron transport","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Transmembrane","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","FMN","_","_","MF_00479","HAMAP"]
[null,"UR000064652","modified residue","FMN phosphoryl threonine",159,159,"MF_00479","HAMAP"]
[null,"UR000064652","product  name (synonym)","Rnf electron transport complex subunit G","_","_","MF_00479","HAMAP"]
[null,"UR000064652","product - EC number","1.18.1.-","_","_","MF_00479","HAMAP"]
[null,"UR000064652","product name","Ion-translocating oxidoreductase complex subunit G","_","_","MF_00479","HAMAP"]
[null,"UR000064652","similarity","Belongs to the RnfG family","_","_","MF_00479","HAMAP"]
[null,"UR000064652","subunit","The complex is composed of six subunits: RnfA, RnfB, RnfC, RnfD, RnfE and RnfG","_","_","MF_00479","HAMAP"]
[]
["ACT01_04525","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000063677","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane","_","_","MF_00478","HAMAP"]
[null,"UR000063677","gene name","rnfE","_","_","MF_00478","HAMAP"]
[null,"UR000063677","GO","GO:0055114","_","_","MF_00478","HAMAP"]
[null,"UR000063677","GO","GO:0022900","_","_","MF_00478","HAMAP"]
[null,"UR000063677","GO","GO:0005886","_","_","MF_00478","HAMAP"]
[null,"UR000063677","keyword","Transport","_","_","MF_00478","HAMAP"]
[null,"UR000063677","keyword","Transmembrane","_","_","MF_00478","HAMAP"]
[null,"UR000063677","keyword","Electron transport","_","_","MF_00478","HAMAP"]
[null,"UR000063677","keyword","Cell membrane","_","_","MF_00478","HAMAP"]
[null,"UR000063677","keyword","Oxidoreductase","_","_","MF_00478","HAMAP"]
[null,"UR000063677","keyword","Membrane","_","_","MF_00478","HAMAP"]
[null,"UR000063677","keyword","Transmembrane helix","_","_","MF_00478","HAMAP"]
[null,"UR000063677","product  name (synonym)","Rnf electron transport complex subunit E","_","_","MF_00478","HAMAP"]
[null,"UR000063677","product - EC number","1.18.1.-","_","_","MF_00478","HAMAP"]
[null,"UR000063677","product name","Ion-translocating oxidoreductase complex subunit E","_","_","MF_00478","HAMAP"]
[null,"UR000063677","similarity","Belongs to the NqrDE/RnfAE family","_","_","MF_00478","HAMAP"]
[null,"UR000063677","subunit","The complex is composed of six subunits: RnfA, RnfB, RnfC, RnfD, RnfE and RnfG","_","_","MF_00478","HAMAP"]
[null,"SAAS01034762","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane"]
[null,"SAAS01034760","keyword","Cell membrane"]
[null,"SAAS01034757","keyword","Electron transport"]
[null,"SAAS00095226","keyword","Membrane"]
[null,"SAAS01035351","keyword","Oxidoreductase"]
[null,"SAAS00095471","keyword","Transmembrane"]
[null,"SAAS00465084","keyword","Transmembrane helix"]
[null,"SAAS00095348","keyword","Transport"]
[null,"SAAS00573673","similarity","Belongs to the NqrDE/RnfAE family"]
[]
["ACT01_04530","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000062678","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane","_","_","MF_00459","HAMAP"]
[null,"UR000062678","gene name","rnfA","_","_","MF_00459","HAMAP"]
[null,"UR000062678","GO","GO:0022900","_","_","MF_00459","HAMAP"]
[null,"UR000062678","GO","GO:0055114","_","_","MF_00459","HAMAP"]
[null,"UR000062678","GO","GO:0005886","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Cell membrane","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Transport","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Membrane","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Transmembrane","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Oxidoreductase","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Transmembrane helix","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Electron transport","_","_","MF_00459","HAMAP"]
[null,"UR000062678","product  name (synonym)","Rnf electron transport complex subunit A","_","_","MF_00459","HAMAP"]
[null,"UR000062678","product - EC number","1.18.1.-","_","_","MF_00459","HAMAP"]
[null,"UR000062678","product name","Ion-translocating oxidoreductase complex subunit A","_","_","MF_00459","HAMAP"]
[null,"UR000062678","similarity","Belongs to the NqrDE/RnfAE family","_","_","MF_00459","HAMAP"]
[null,"UR000062678","subunit","The complex is composed of six subunits: RnfA, RnfB, RnfC, RnfD, RnfE and RnfG","_","_","MF_00459","HAMAP"]
[null,"SAAS01034726","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane"]
[null,"SAAS01034715","keyword","Electron transport"]
[null,"SAAS00095226","keyword","Membrane"]
[null,"SAAS01035351","keyword","Oxidoreductase"]
[null,"SAAS00095471","keyword","Transmembrane"]
[null,"SAAS00465084","keyword","Transmembrane helix"]
[null,"SAAS00095348","keyword","Transport"]
[null,"SAAS01034710","product - EC number","1.18.1.-"]
[null,"SAAS00573673","similarity","Belongs to the NqrDE/RnfAE family"]
[]
["ACT01_04535","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000090116","cofactor","Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883","_","_","MF_00463","HAMAP"]
[null,"UR000090116","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane","_","_","MF_00463","HAMAP"]
[null,"UR000090116","gene name","rnfB","_","_","MF_00463","HAMAP"]
[null,"UR000090116","GO","GO:0051539","_","_","MF_00463","HAMAP"]
[null,"UR000090116","GO","GO:0055114","_","_","MF_00463","HAMAP"]
[null,"UR000090116","GO","GO:0005886","_","_","MF_00463","HAMAP"]
[null,"UR000090116","GO","GO:0022900","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Iron-sulfur","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Cell membrane","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Repeat","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Membrane","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","4Fe-4S","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Electron transport","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Metal-binding","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Oxidoreductase","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Transport","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Iron","_","_","MF_00463","HAMAP"]
[null,"UR000090116","metal binding","Iron-sulfur 2 (4Fe-4S)",141,141,"MF_00463","HAMAP"]
[null,"UR000090116","metal binding","Iron-sulfur 2 (4Fe-4S)",145,145,"MF_00463","HAMAP"]
[null,"UR000090116","metal binding","Iron-sulfur 2 (4Fe-4S)",151,151,"MF_00463","HAMAP"]
[null,"UR000090116","metal binding","Iron-sulfur 2 (4Fe-4S)",185,185,"MF_00463","HAMAP"]
[null,"UR000090116","product  name (synonym)","Rnf electron transport complex subunit B","_","_","MF_00463","HAMAP"]
[null,"UR000090116","product - EC number","1.18.1.-","_","_","MF_00463","HAMAP"]
[null,"UR000090116","product name","Ion-translocating oxidoreductase complex subunit B","_","_","MF_00463","HAMAP"]
[null,"UR000090116","similarity","Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily","_","_","MF_00463","HAMAP"]
[null,"UR000090116","subunit","The complex is composed of six subunits: RnfA, RnfB, RnfC, RnfD, RnfE and RnfG","_","_","MF_00463","HAMAP"]
[null,"SAAS00617120, SAAS01039554","cofactor","Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883"]
[null,"SAAS01039548","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane"]
[null,"SAAS00617118, SAAS01039526","keyword","4Fe-4S"]
[null,"SAAS01039523","keyword","Electron transport"]
[null,"SAAS00617117, SAAS01039549","keyword","Iron"]
[null,"SAAS00617121, SAAS01039553","keyword","Iron-sulfur"]
[null,"SAAS01039536","keyword","Membrane"]
[null,"SAAS00617119, SAAS01039542","keyword","Metal-binding"]
[null,"SAAS01039529","keyword","Oxidoreductase"]
[null,"SAAS01039551","keyword","Repeat"]
[null,"SAAS01039534","keyword","Transport"]
[null,"SAAS01039531","similarity","Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily"]

{"sheet":"PRIAM EC number","index":8,"n_rows":240,"n_cols":15,"rows_kept":240}
["ACT01_00410","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":9e-75,"d":"9.00E-75"},37,1,307,307,"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":6e-31,"d":"6.00E-31"},26,49,310,262,"Malate dehydrogenase","Malic dehydrogenase","(S)-malate + NAD(+) = oxaloacetate + NADH","_","-!- Also oxidizes some other 2-hydroxydicarboxylic acids"]
[null,"1.1.1.82","no",1,322,2E-12,18,118,293,176,"Malate dehydrogenase (NADP(+))","NADP-linked malate dehydrogenase","(S)-malate + NADP(+) = oxaloacetate + NADPH","_","-!- Activated by light"]
[]
["ACT01_03310","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":4e-45,"d":"4.00E-45"},51,1,175,175,"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-36,"d":"2.00E-36"},43,1,175,175,"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,"1.2.7.3","no",1,180,{"v":2e-17,"d":"2.00E-17"},30,4,174,171,"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"]
[]
["ACT01_03320","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"},53,7,369,363,"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":3e-80,"d":"3.00E-80"},40,7,326,320,"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":2e-25,"d":"2.00E-25"},24,28,363,336,"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-22,"d":"1.00E-22"},26,6,320,315,"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"]
[null,"1.16.1.5","no",1,1803,{"v":2e-20,"d":"2.00E-20"},26,28,321,294,"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"]
[]
["ACT01_03325","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":5e-45,"d":"5.00E-45"},44,20,216,197,"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",1,1928,4e-15,27,99,295,197,"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",1,1803,7e-15,29,99,272,174,"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",2,265,1E-13,27,17,217,201,"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"]
[]
["ACT01_00445","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",1,1928,0,42,8,1170,1163,"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",1,1803,0,45,8,1170,1163,"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":2e-47,"d":"2.00E-47"},30,7,384,378,"Pyruvate synthase","2-oxobutyrate synthase. 2-oxobutyrate-ferredoxin oxidoreductase. Alpha-ketobutyrate synthase. Alpha-ketobutyrate-ferredoxin oxidoreductase. Pyruvate oxidoreductase. Pyruvate synthetase. Pyruvic-ferredoxin oxidoreductase","Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Thiamine diphosphate","-!- The enzyme also decarboxylates 2-oxobutanoate with lower efficiency, but shows no activity with 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to fo"]
[null,"1.2.7.7","no",4,328,{"v":7e-26,"d":"7.00E-26"},23,7,334,328,"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,"1.2.7.1","no",1,184,{"v":1e-16,"d":"1.00E-16"},26,417,608,192,"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"]
[]
["ACT01_00545","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",1,1928,0,45,7,1168,1162,"Pyruvate dehydrogenase (NADP(+))","Pyruvate:NADP(+) oxidoreductase","Pyruvate + CoA + NADP(+) = acetyl-CoA + CO(2) + NADPH","_","-!- The Euglena enzyme can also use FAD or methylviologen as acceptor, more slowly. -!- Inhibited by oxygen"]
[null,"1.16.1.5","no",1,1803,0,49,4,1168,1165,"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":2e-49,"d":"2.00E-49"},31,5,391,387,"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":3e-27,"d":"3.00E-27"},24,5,328,324,"3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)","2-ketoisovalerate ferredoxin reductase. 2-oxoisovalerate ferredoxin reductase. 3-methyl-2-oxobutanoate synthase (ferredoxin). Branched-chain ketoacid ferredoxin reductase. Branched-chain oxo acid ferredoxin reductase. Keto-valine-ferredoxin oxidoreductase. Ketoisovalerate ferredoxin reductase. Ketoisovalerate oxidoreductase. VOR","3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO(2) + 2 reduced ferredoxin + H(+)","Iron-sulfur; Tungstopterin","-!- The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. -!- Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo- pentanoate, and 2-oxobutanoate. -!"]
[null,"1.2.7.3","no",3,344,4e-12,26,3,307,305,"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"]
[]
["ACT01_02090","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",1,1928,0,45,9,1175,1167,"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",1,1803,0,47,7,1175,1169,"Aquacobalamin reductase (NADPH)","Aquacobalamin (reduced nicotinamide adenine dinucleotide phosphate) reductase. NADPH-linked aquacobalamin reductase. NADPH:aquacob(III)alamin oxidoreductase","2 cob(II)alamin + NADP(+) + 2 H(2)O = 2 aquacob(III)alamin + NADPH","Flavoprotein","-!- Acts on aquacob(III)alamin and hydroxycobalamin, but not on cyanocobalamin. -!- Formerly EC 1.6.99.11"]
[null,"1.2.7.1","no",3,395,{"v":5E-51,"d":"5.00E-51"},29,5,386,382,"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-30,"d":"1.00E-30"},22,7,335,329,"3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)","2-ketoisovalerate ferredoxin reductase. 2-oxoisovalerate ferredoxin reductase. 3-methyl-2-oxobutanoate synthase (ferredoxin). Branched-chain ketoacid ferredoxin reductase. Branched-chain oxo acid ferredoxin reductase. Keto-valine-ferredoxin oxidoreductase. Ketoisovalerate ferredoxin reductase. Ketoisovalerate oxidoreductase. VOR","3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO(2) + 2 reduced ferredoxin + H(+)","Iron-sulfur; Tungstopterin","-!- The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. -!- Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo- pentanoate, and 2-oxobutanoate. -!"]
[null,"1.2.7.1","no",1,184,{"v":6e-17,"d":"6.00E-17"},24,417,612,196,"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,"1.2.7.3","no",3,344,1E-13,25,6,309,304,"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"]
[]
["ACT01_02810","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",1,1928,0,45,9,1165,1157,"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",1,1803,0,47,4,1170,1167,"Aquacobalamin reductase (NADPH)","Aquacobalamin (reduced nicotinamide adenine dinucleotide phosphate) reductase. NADPH-linked aquacobalamin reductase. NADPH:aquacob(III)alamin oxidoreductase","2 cob(II)alamin + NADP(+) + 2 H(2)O = 2 aquacob(III)alamin + NADPH","Flavoprotein","-!- Acts on aquacob(III)alamin and hydroxycobalamin, but not on cyanocobalamin. -!- Formerly EC 1.6.99.11"]
[null,"1.2.7.1","no",3,395,{"v":4E-41,"d":"4.00E-41"},29,5,389,385,"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-28,"d":"1.00E-28"},23,7,335,329,"3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)","2-ketoisovalerate ferredoxin reductase. 2-oxoisovalerate ferredoxin reductase. 3-methyl-2-oxobutanoate synthase (ferredoxin). Branched-chain ketoacid ferredoxin reductase. Branched-chain oxo acid ferredoxin reductase. Keto-valine-ferredoxin oxidoreductase. Ketoisovalerate ferredoxin reductase. Ketoisovalerate oxidoreductase. VOR","3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO(2) + 2 reduced ferredoxin + H(+)","Iron-sulfur; Tungstopterin","-!- The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. -!- Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo- pentanoate, and 2-oxobutanoate. -!"]
[null,"1.2.7.3","no",3,344,2e-13,26,9,311,303,"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"]
[null,"1.2.7.1","no",1,184,4e-13,23,448,612,165,"Pyruvate synthase","2-oxobutyrate synthase. 2-oxobutyrate-ferredoxin oxidoreductase. Alpha-ketobutyrate synthase. Alpha-ketobutyrate-ferredoxin oxidoreductase. Pyruvate oxidoreductase. Pyruvate synthetase. Pyruvic-ferredoxin oxidoreductase","Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Thiamine diphosphate","-!- The enzyme also decarboxylates 2-oxobutanoate with lower efficiency, but shows no activity with 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to fo"]
[]
["ACT01_03520","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",1,1928,0,44,12,1176,1165,"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",1,1803,0,47,7,1176,1170,"Aquacobalamin reductase (NADPH)","Aquacobalamin (reduced nicotinamide adenine dinucleotide phosphate) reductase. NADPH-linked aquacobalamin reductase. NADPH:aquacob(III)alamin oxidoreductase","2 cob(II)alamin + NADP(+) + 2 H(2)O = 2 aquacob(III)alamin + NADPH","Flavoprotein","-!- Acts on aquacob(III)alamin and hydroxycobalamin, but not on cyanocobalamin. -!- Formerly EC 1.6.99.11"]
[null,"1.2.7.1","no",3,395,{"v":5e-54,"d":"5.00E-54"},31,8,384,377,"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-31,"d":"4.00E-31"},23,10,333,324,"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. -!"]
[null,"1.2.7.1","no",1,184,{"v":3e-18,"d":"3.00E-18"},28,419,614,196,"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",1,187,2e-11,28,419,609,191,"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,"1.2.7.3","no",3,344,6E-11,24,9,312,304,"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"]
[]
["ACT01_06665","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",1,1928,0,45,8,1168,1161,"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",1,1803,0,48,7,1168,1162,"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"},30,10,383,374,"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":5e-26,"d":"5.00E-26"},23,10,329,320,"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,"1.2.7.1","no",1,184,1e-11,23,420,611,192,"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"]
[]
["ACT01_12570","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",1,1928,0,46,8,1166,1159,"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",1,1803,0,48,2,1166,1165,"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"},30,10,383,374,"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":7e-26,"d":"7.00E-26"},23,10,329,320,"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,"1.2.7.1","no",1,184,1e-11,23,420,611,192,"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"]
[]
["ACT01_05435","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.7.2.1","high",1,410,0,62,3,395,393,"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-117,"d":"1.00E-117"},43,2,394,393,"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":5e-19,"d":"5.00E-19"},25,1,331,331,"Butyrate kinase","_","ATP + butanoate = ADP + butanoyl phosphate","_","-!- The enzyme from Clostridium sp. also acts, more slowly on pentanoate and propanoate, and on some branched-chain fatty acids (cf. EC 2.7.1.14)"]
[]
["ACT01_13325","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":2E-95,"d":"2.00E-95"},50,3,331,329,"Phosphate acetyltransferase","Phosphoacylase. Phosphotransacetylase","Acetyl-CoA + phosphate = CoA + acetyl phosphate","_","-!- Also acts with other short-chain acyl-CoAs"]
[]
["ACT01_04870","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.2.1.10","medium",2,875,{"v":1e-132,"d":"1.00E-132"},46,10,445,436,"Acetaldehyde dehydrogenase (acetylating)","Acylating acetaldehyde dehydrogenase. Aldehyde dehydrogenase (acylating)","Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH","_","-!- Also acts, more slowly, on glycolaldehyde, propanal and butanal. -!- In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39. -!- The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perfor"]
[null,"1.2.1.16","no",1,421,{"v":8e-32,"d":"8.00E-32"},22,11,335,325,"Succinate-semialdehyde dehydrogenase (NAD(P)(+))","_","Succinate semialdehyde + NAD(P)(+) + H(2)O = succinate + NAD(P)H","_","_"]
[null,"1.2.1.22","no",1,475,{"v":3e-16,"d":"3.00E-16"},20,12,403,392,"Lactaldehyde dehydrogenase","_","(S)-lactaldehyde + NAD(+) + H(2)O = (S)-lactate + NADH","_","_"]
[null,"1.2.1.3","no",1,462,6e-14,24,7,274,268,"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"]
[]
["ACT01_02465","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.1.103","high",1,342,{"v":5e-60,"d":"5.00E-60"},35,1,322,322,"L-threonine 3-dehydrogenase","TDH","L-threonine + NAD(+) = L-2-amino-3-oxobutanoate + NADH","_","-!- Acts in concert with EC 2.3.1.29 in the degradation of threonine to glycine. -!- This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex. -!- In aqueous solution, the product L-2-ami"]
[null,"1.1.1.14","no",1,356,{"v":4e-58,"d":"4.00E-58"},34,3,336,334,"L-iditol 2-dehydrogenase","Glucitol dehydrogenase. Polyol dehydrogenase. Sorbitol dehydrogenase","L-iditol + NAD(+) = L-sorbose + NADH","_","-!- This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals. -!- It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol. -!- Enzymes from dif"]
[null,"1.1.1.9","no",1,353,{"v":1E-46,"d":"1.00E-46"},31,1,321,321,"D-xylulose reductase","Xylitol dehydrogenase","Xylitol + NAD(+) = D-xylulose + NADH","_","-!- Also acts as an L-erythrulose reductase"]
[null,"1.1.1.251","no",1,346,{"v":1E-35,"d":"1.00E-35"},32,1,286,286,"Galactitol-1-phosphate 5-dehydrogenase","_","Galactitol 1-phosphate + NAD(+) = D-tagatose 6-phosphate + NADH","Zn(2+)","-!- The enzyme from the bacterium Escherichia coli is involved in a galactitol degradation pathway"]
[null,"1.1.1.264","no",1,343,{"v":2E-35,"d":"2.00E-35"},28,2,323,322,"L-idonate 5-dehydrogenase (NAD(P)(+))","L-idonate 5-dehydrogenase","L-idonate + NAD(P)(+) = 5-dehydrogluconate + NAD(P)H","Zn(2+)","-!- The enzyme from the bacterium Escherichia coli is specific for 5-dehydro-D-gluconate. -!- Cf. EC 1.1.1.366"]
[null,"1.1.1.1","no",1,321,{"v":7e-35,"d":"7.00E-35"},25,26,302,277,"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,"1.1.1.284","no",1,375,{"v":4e-31,"d":"4.00E-31"},25,8,338,331,"S-(hydroxymethyl)glutathione dehydrogenase","ADH3. Chi-ADH. Class III alcohol dehydrogenase. FDH. Formaldehyde dehydrogenase. Formaldehyde dehydrogenase (glutathione). Formic dehydrogenase. GD-FALDH. Glutathione-dependent formaldehyde dehydrogenase. GS-FDH. NAD- and glutathione-dependent formaldehyde dehydrogenase. NAD-dependent formaldehyde dehydrogenase. NAD-linked formaldehyde dehydrogenase","S-(hydroxymethyl)glutathione + NAD(P)(+) = S-formylglutathione + NAD(P)H","_","-!- The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC 4.4.1.22. -!- Forms part of the pathway that detoxifies formaldehyde, since t"]
[null,"1.6.5.5","no",1,331,{"v":1e-30,"d":"1.00E-30"},26,1,320,320,"NADPH:quinone reductase","Quinone oxidoreductase. Zeta-crystallin","NADPH + 2 quinone = NADP(+) + 2 semiquinone","Zn(2+)","-!- Specific for NADPH. -!- Catalyzes the one-electron reduction of certain quinones, with the orthoquinones 1,2-naphthoquinone and 9,10-phenanthrenequinone being the best substrates. -!- Dicoumarol (cf. EC 1.6.5.2) and nitrofurantoin are competitive inhi"]
[null,"1.1.1.4","no",1,382,{"v":3E-28,"d":"3.00E-28"},28,1,337,337,"(R,R)-butanediol dehydrogenase","(R)-2,3-butanediol dehydrogenase. (R)-diacetyl reductase. 1-amino-2-propanol dehydrogenase. 1-amino-2-propanol oxidoreductase. 2,3-butanediol dehydrogenase. Aminopropanol oxidoreductase. Butylene glycol dehydrogenase. Butyleneglycol dehydrogenase. D-(-)-butanediol dehydrogenase. D-1-amino-2-propanol dehydrogenase. D-1-amino-2-propanol:NAD(2) oxidoreductase. D-aminopropanol dehydrogenase. D-butanediol dehydrogenase. Diacetyl (acetoin) reductase","(R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + NADH","_","-!- Also converts diacetyl into acetoin with NADH as reductant"]
[null,"1.1.1.255","no",1,352,{"v":2e-25,"d":"2.00E-25"},28,21,278,258,"Mannitol dehydrogenase","MTD. NAD-dependent mannitol dehydrogenase","D-mannitol + NAD(+) = D-mannose + NADH","_","-!- The enzyme from Apium graveolens (celery) oxidizes alditols with a minimum requirement of 2R chirality at the carbon adjacent to the primary carbon undergoing the oxidation. -!- The enzyme is specific for NAD(+) and does not use NADP(+)"]
[null,"1.1.1.2","no",1,375,{"v":1e-24,"d":"1.00E-24"},26,27,242,216,"Alcohol dehydrogenase (NADP(+))","Aldehyde reductase (NADPH)","An alcohol + NADP(+) = an aldehyde + NADPH","Zn(2+)","-!- Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. -!- May be identical with EC 1.1.1.19, EC 1.1.1.33 and EC 1.1.1.55. -!- Re-specific with respect to NADPH"]
[null,"1.1.1.195","no",1,357,{"v":1e-19,"d":"1.00E-19"},31,27,206,180,"Cinnamyl-alcohol dehydrogenase","CAD","Cinnamyl alcohol + NADP(+) = cinnamaldehyde + NADPH","_","-!- Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and cinnamyl alcohol (cf. EC 1.1.1.194)"]
[null,"1.2.1.46","no",1,399,{"v":3e-19,"d":"3.00E-19"},30,2,214,213,"Formaldehyde dehydrogenase","_","Formaldehyde + NAD(+) + H(2)O = formate + NADH","_","_"]
[null,"1.1.1.90","no",1,366,{"v":1e-18,"d":"1.00E-18"},25,3,325,323,"Aryl-alcohol dehydrogenase","Benzyl alcohol dehydrogenase. p-hydroxybenzyl alcohol dehydrogenase","An aromatic alcohol + NAD(+) = an aromatic aldehyde + NADH","_","-!- A group of enzymes with broad specificity toward primary alcohols with an aromatic or cyclohex-1-ene ring, but with low or no activity toward short-chain aliphatic alcohols"]
[null,"1.2.1.66","no",1,360,{"v":2e-18,"d":"2.00E-18"},24,1,338,338,"Transferred entry: 1.1.1.306","_","_","_","_"]
[null,"1.1.1.73","no",1,379,{"v":2E-16,"d":"2.00E-16"},24,7,321,315,"Octanol dehydrogenase","_","1-octanol + NAD(+) = 1-octanal + NADH","_","-!- Acts, less rapidly, on other long-chain alcohols"]
[]
["ACT01_03450","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.1.14","high",1,356,{"v":2e-61,"d":"2.00E-61"},34,15,340,326,"L-iditol 2-dehydrogenase","Glucitol dehydrogenase. Polyol dehydrogenase. Sorbitol dehydrogenase","L-iditol + NAD(+) = L-sorbose + NADH","_","-!- This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals. -!- It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol. -!- Enzymes from dif"]
[null,"1.1.1.103","no",1,342,{"v":2e-49,"d":"2.00E-49"},31,1,326,326,"L-threonine 3-dehydrogenase","TDH","L-threonine + NAD(+) = L-2-amino-3-oxobutanoate + NADH","_","-!- Acts in concert with EC 2.3.1.29 in the degradation of threonine to glycine. -!- This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex. -!- In aqueous solution, the product L-2-ami"]
[null,"1.1.1.9","no",1,353,{"v":1e-48,"d":"1.00E-48"},32,1,326,326,"D-xylulose reductase","Xylitol dehydrogenase","Xylitol + NAD(+) = D-xylulose + NADH","_","-!- Also acts as an L-erythrulose reductase"]
[null,"1.1.1.1","no",1,321,{"v":9e-35,"d":"9.00E-35"},29,29,298,270,"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,"1.1.1.284","no",1,375,{"v":3e-31,"d":"3.00E-31"},26,8,326,319,"S-(hydroxymethyl)glutathione dehydrogenase","ADH3. Chi-ADH. Class III alcohol dehydrogenase. FDH. Formaldehyde dehydrogenase. Formaldehyde dehydrogenase (glutathione). Formic dehydrogenase. GD-FALDH. Glutathione-dependent formaldehyde dehydrogenase. GS-FDH. NAD- and glutathione-dependent formaldehyde dehydrogenase. NAD-dependent formaldehyde dehydrogenase. NAD-linked formaldehyde dehydrogenase","S-(hydroxymethyl)glutathione + NAD(P)(+) = S-formylglutathione + NAD(P)H","_","-!- The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC 4.4.1.22. -!- Forms part of the pathway that detoxifies formaldehyde, since t"]
[null,"1.1.1.251","no",1,346,{"v":5e-31,"d":"5.00E-31"},30,21,288,268,"Galactitol-1-phosphate 5-dehydrogenase","_","Galactitol 1-phosphate + NAD(+) = D-tagatose 6-phosphate + NADH","Zn(2+)","-!- The enzyme from the bacterium Escherichia coli is involved in a galactitol degradation pathway"]
[null,"1.1.1.4","no",1,382,{"v":9e-30,"d":"9.00E-30"},28,1,306,306,"(R,R)-butanediol dehydrogenase","(R)-2,3-butanediol dehydrogenase. (R)-diacetyl reductase. 1-amino-2-propanol dehydrogenase. 1-amino-2-propanol oxidoreductase. 2,3-butanediol dehydrogenase. Aminopropanol oxidoreductase. Butylene glycol dehydrogenase. Butyleneglycol dehydrogenase. D-(-)-butanediol dehydrogenase. D-1-amino-2-propanol dehydrogenase. D-1-amino-2-propanol:NAD(2) oxidoreductase. D-aminopropanol dehydrogenase. D-butanediol dehydrogenase. Diacetyl (acetoin) reductase","(R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + NADH","_","-!- Also converts diacetyl into acetoin with NADH as reductant"]
[null,"1.1.1.2","no",1,375,{"v":2e-25,"d":"2.00E-25"},28,26,266,241,"Alcohol dehydrogenase (NADP(+))","Aldehyde reductase (NADPH)","An alcohol + NADP(+) = an aldehyde + NADPH","Zn(2+)","-!- Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. -!- May be identical with EC 1.1.1.19, EC 1.1.1.33 and EC 1.1.1.55. -!- Re-specific with respect to NADPH"]
[null,"1.1.1.264","no",1,343,{"v":2e-25,"d":"2.00E-25"},27,31,333,303,"L-idonate 5-dehydrogenase (NAD(P)(+))","L-idonate 5-dehydrogenase","L-idonate + NAD(P)(+) = 5-dehydrogluconate + NAD(P)H","Zn(2+)","-!- The enzyme from the bacterium Escherichia coli is specific for 5-dehydro-D-gluconate. -!- Cf. EC 1.1.1.366"]
[null,"1.1.1.73","no",1,379,{"v":2e-22,"d":"2.00E-22"},26,7,330,324,"Octanol dehydrogenase","_","1-octanol + NAD(+) = 1-octanal + NADH","_","-!- Acts, less rapidly, on other long-chain alcohols"]
[null,"1.2.1.66","no",1,360,{"v":2E-16,"d":"2.00E-16"},28,56,276,221,"Transferred entry: 1.1.1.306","_","_","_","_"]
[null,"1.1.1.255","no",1,352,3e-15,26,26,230,205,"Mannitol dehydrogenase","MTD. NAD-dependent mannitol dehydrogenase","D-mannitol + NAD(+) = D-mannose + NADH","_","-!- The enzyme from Apium graveolens (celery) oxidizes alditols with a minimum requirement of 2R chirality at the carbon adjacent to the primary carbon undergoing the oxidation. -!- The enzyme is specific for NAD(+) and does not use NADP(+)"]
[null,"1.1.1.90","no",1,366,4E-14,25,26,330,305,"Aryl-alcohol dehydrogenase","Benzyl alcohol dehydrogenase. p-hydroxybenzyl alcohol dehydrogenase","An aromatic alcohol + NAD(+) = an aromatic aldehyde + NADH","_","-!- A group of enzymes with broad specificity toward primary alcohols with an aromatic or cyclohex-1-ene ring, but with low or no activity toward short-chain aliphatic alcohols"]
[null,"1.2.1.46","no",1,399,4e-13,25,15,208,194,"Formaldehyde dehydrogenase","_","Formaldehyde + NAD(+) + H(2)O = formate + NADH","_","_"]
[null,"1.6.5.5","no",1,331,7e-13,22,19,326,308,"NADPH:quinone reductase","Quinone oxidoreductase. Zeta-crystallin","NADPH + 2 quinone = NADP(+) + 2 semiquinone","Zn(2+)","-!- Specific for NADPH. -!- Catalyzes the one-electron reduction of certain quinones, with the orthoquinones 1,2-naphthoquinone and 9,10-phenanthrenequinone being the best substrates. -!- Dicoumarol (cf. EC 1.6.5.2) and nitrofurantoin are competitive inhi"]
[null,"1.1.1.195","no",1,357,1e-11,29,28,187,160,"Cinnamyl-alcohol dehydrogenase","CAD","Cinnamyl alcohol + NADP(+) = cinnamaldehyde + NADPH","_","-!- Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and cinnamyl alcohol (cf. EC 1.1.1.194)"]
[]
["ACT01_04805","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.1.1","high",9,419,{"v":9e-89,"d":"9.00E-89"},36,4,378,375,"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":1E-87,"d":"1.00E-87"},39,1,378,378,"Acetaldehyde dehydrogenase (acetylating)","Acylating acetaldehyde dehydrogenase. Aldehyde dehydrogenase (acylating)","Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH","_","-!- Also acts, more slowly, on glycolaldehyde, propanal and butanal. -!- In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39. -!- The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perfor"]
[null,"1.1.1.77","no",1,383,{"v":2e-49,"d":"2.00E-49"},33,11,378,368,"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,"1.1.1.244","no",1,381,{"v":1E-46,"d":"1.00E-46"},30,1,377,377,"Methanol dehydrogenase","_","Methanol + NAD(+) = formaldehyde + NADH","_","_"]
[null,"1.1.1.202","no",1,387,{"v":7e-44,"d":"7.00E-44"},31,26,378,353,"1,3-propanediol dehydrogenase","1,3-propanediol oxidoreductase. 3-hydroxypropionaldehyde reductase","Propane-1,3-diol + NAD(+) = 3-hydroxypropanal + NADH","_","_"]
[null,"1.1.99.24","no",1,479,{"v":2e-33,"d":"2.00E-33"},25,20,377,358,"Hydroxyacid-oxoacid transhydrogenase","_","(1) (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2- hydroxyglutarate. (2) 4-hydroxybutanoate + 2-oxoglutarate = succinic semialdehyde + (R)-2- hydroxyglutarate","_","_"]
[null,"1.3.1.32","no",1,356,{"v":6e-31,"d":"6.00E-31"},27,86,378,293,"Maleylacetate reductase","Maleolylacetate reductase","3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H","_","_"]
[null,"1.1.1.61","no",1,371,{"v":9e-26,"d":"9.00E-26"},26,1,378,378,"4-hydroxybutyrate dehydrogenase","_","4-hydroxybutanoate + NAD(+) = succinate semialdehyde + NADH","_","_"]
[]
["ACT01_04800","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.2.1.10","medium",2,875,{"v":1E-99,"d":"1.00E-99"},36,20,455,436,"Acetaldehyde dehydrogenase (acetylating)","Acylating acetaldehyde dehydrogenase. Aldehyde dehydrogenase (acylating)","Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH","_","-!- Also acts, more slowly, on glycolaldehyde, propanal and butanal. -!- In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39. -!- The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perfor"]
[null,"1.2.1.16","no",1,421,{"v":7e-21,"d":"7.00E-21"},22,13,270,258,"Succinate-semialdehyde dehydrogenase (NAD(P)(+))","_","Succinate semialdehyde + NAD(P)(+) + H(2)O = succinate + NAD(P)H","_","_"]
[]
["ACT01_05115","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.1.6","high",1,365,{"v":2E-87,"d":"2.00E-87"},39,1,362,362,"Glycerol dehydrogenase","NAD-linked glycerol dehydrogenase","Glycerol + NAD(+) = glycerone + NADH","_","-!- Also acts on 1,2-propanediol"]
[null,"1.1.1.261","no",1,350,{"v":4e-24,"d":"4.00E-24"},24,14,339,326,"sn-glycerol-1-phosphate dehydrogenase","Glycerol-1-phosphate dehydrogenase (NAD(P)(+)). Gro1PDH","sn-glycerol 1-phosphate + NAD(P)(+) = glycerone phosphate + NAD(P)H","Zn(2+) or Ni(2+)","-!- Responsible for the formation of archaea-specific sn-glycerol-1- phosphate, the first step in the biosynthesis of polar lipids in archaea. -!- It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryot"]
[null,"4.2.3.4","no",1,371,3E-11,23,14,323,310,"3-dehydroquinate synthase","3-dehydroquinate synthetase. 5-dehydroquinate synthase. 5-dehydroquinic acid synthetase. Dehydroquinate synthase","3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate","Cobalt cation; NAD(+)","-!- The hydrogen atoms on C-7 of the substrate are retained on C-2 of the products. -!- Formerly EC 4.6.1.3"]
[]
["ACT01_06790","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":5e-58,"d":"5.00E-58"},31,3,385,383,"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":4e-46,"d":"4.00E-46"},32,3,384,382,"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-42,"d":"5.00E-42"},30,3,356,354,"Methanol dehydrogenase","_","Methanol + NAD(+) = formaldehyde + NADH","_","_"]
[null,"1.2.1.10","no",2,875,{"v":8e-39,"d":"8.00E-39"},29,3,362,360,"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":2e-37,"d":"2.00E-37"},30,25,384,360,"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,"1.1.99.24","no",1,479,{"v":1e-28,"d":"1.00E-28"},28,47,311,265,"Hydroxyacid-oxoacid transhydrogenase","_","(1) (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2- hydroxyglutarate. (2) 4-hydroxybutanoate + 2-oxoglutarate = succinic semialdehyde + (R)-2- hydroxyglutarate","_","_"]
[null,"1.3.1.32","no",1,356,{"v":3e-18,"d":"3.00E-18"},26,4,356,353,"Maleylacetate reductase","Maleolylacetate reductase","3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H","_","_"]
[null,"1.1.1.61","no",1,371,{"v":9e-16,"d":"9.00E-16"},24,87,384,298,"4-hydroxybutyrate dehydrogenase","_","4-hydroxybutanoate + NAD(+) = succinate semialdehyde + NADH","_","_"]
[]
["ACT01_11045","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":4E-55,"d":"4.00E-55"},30,4,328,325,"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":2e-40,"d":"2.00E-40"},32,1,285,285,"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-39,"d":"7.00E-39"},29,1,360,360,"1,3-propanediol dehydrogenase","1,3-propanediol oxidoreductase. 3-hydroxypropionaldehyde reductase","Propane-1,3-diol + NAD(+) = 3-hydroxypropanal + NADH","_","_"]
[null,"1.1.1.77","no",1,383,{"v":6E-37,"d":"6.00E-37"},32,11,303,293,"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,"1.1.1.244","no",1,381,{"v":4e-34,"d":"4.00E-34"},30,1,311,311,"Methanol dehydrogenase","_","Methanol + NAD(+) = formaldehyde + NADH","_","_"]
[null,"1.1.99.24","no",1,479,{"v":1e-30,"d":"1.00E-30"},26,4,262,259,"Hydroxyacid-oxoacid transhydrogenase","_","(1) (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2- hydroxyglutarate. (2) 4-hydroxybutanoate + 2-oxoglutarate = succinic semialdehyde + (R)-2- hydroxyglutarate","_","_"]
[null,"1.3.1.32","no",1,356,{"v":7e-26,"d":"7.00E-26"},26,7,317,311,"Maleylacetate reductase","Maleolylacetate reductase","3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H","_","_"]
[null,"1.1.1.61","no",1,371,{"v":2e-23,"d":"2.00E-23"},30,80,332,253,"4-hydroxybutyrate dehydrogenase","_","4-hydroxybutanoate + NAD(+) = succinate semialdehyde + NADH","_","_"]
[null,"1.1.1.261","no",1,350,5e-12,30,5,135,131,"sn-glycerol-1-phosphate dehydrogenase","Glycerol-1-phosphate dehydrogenase (NAD(P)(+)). Gro1PDH","sn-glycerol 1-phosphate + NAD(P)(+) = glycerone phosphate + NAD(P)H","Zn(2+) or Ni(2+)","-!- Responsible for the formation of archaea-specific sn-glycerol-1- phosphate, the first step in the biosynthesis of polar lipids in archaea. -!- It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryot"]
[]
["ACT01_07765","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-147,"d":"1.00E-147"},59,5,394,390,"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-106,"d":"1.00E-106"},44,1,393,393,"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-101,"d":"1.00E-101"},45,1,394,394,"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"]
[]
["ACT01_10830","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":1e-80,"d":"1.00E-80"},56,1,256,256,"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":6e-64,"d":"6.00E-64"},41,11,259,249,"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"},40,13,260,248,"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":7e-48,"d":"7.00E-48"},38,10,201,192,"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,"4.1.3.36","no",1,263,{"v":3E-43,"d":"3.00E-43"},35,2,257,256,"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,"5.1.2.3","no",1,707,{"v":2e-42,"d":"2.00E-42"},41,11,199,189,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"1.1.1.211","no",1,763,{"v":3e-25,"d":"3.00E-25"},33,5,183,179,"Long-chain-3-hydroxyacyl-CoA dehydrogenase","Beta-hydroxyacyl-CoA dehydrogenase","A long-chain (S)-3-hydroxyacyl-CoA + NAD(+) = a long-chain 3-oxoacyl-CoA + NADH","_","-!- This enzyme was purified from the mitochondrial inner membrane. -!- The enzyme has a preference for long-chain substrates, and activity with C(16) substrates was 6- to 15-fold higher than with C(4) substrates (cf. EC 1.1.1.35)"]
[null,"4.1.1.41","no",1,261,{"v":3E-24,"d":"3.00E-24"},27,1,259,259,"Transferred entry: 7.2.4.3","_","_","_","_"]
[null,"3.1.2.4","no",1,408,{"v":3E-23,"d":"3.00E-23"},30,4,188,185,"3-hydroxyisobutyryl-CoA hydrolase","_","3-hydroxy-2-methylpropanoyl-CoA + H(2)O = CoA + 3-hydroxy-2- methylpropanoate","_","-!- Also hydrolyzes 3-hydroxypropanoyl-CoA"]
[null,"4.2.1.100","no",1,258,{"v":9e-19,"d":"9.00E-19"},28,17,258,242,"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",43,544,2e-11,20,3,257,255,"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"]
[]
["ACT01_10835","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-107,"d":"1.00E-107"},58,4,283,280,"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":1e-77,"d":"1.00E-77"},40,3,285,283,"3-hydroxyacyl-CoA dehydrogenase","Beta-hydroxyacyl dehydrogenase. Beta-keto-reductase","(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH","_","-!- Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3- hydroxyacylhydrolipoate. -!- Some enzymes act, more slowly, with NADP(+). -!- Broad specificity to acyl chain-length (cf. EC 1.1.1.211)"]
[null,"5.1.2.3","no",1,707,{"v":3e-67,"d":"3.00E-67"},39,3,283,281,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"1.1.1.211","no",1,763,{"v":6e-50,"d":"6.00E-50"},39,3,285,283,"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)"]
[]
["ACT01_12410","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-56,"d":"1.00E-56"},36,8,287,280,"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-56,"d":"5.00E-56"},36,6,289,284,"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":7E-45,"d":"7.00E-45"},30,6,294,289,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"1.1.1.211","no",1,763,{"v":1E-25,"d":"1.00E-25"},28,6,306,301,"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)"]
[]
["ACT01_00280","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-113,"d":"1.00E-113"},48,1,378,378,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":5e-99,"d":"5.00E-99"},46,3,374,372,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":6e-76,"d":"6.00E-76"},34,5,373,369,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":1e-57,"d":"1.00E-57"},34,5,379,375,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":4e-48,"d":"4.00E-48"},30,7,373,367,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":1E-35,"d":"1.00E-35"},28,1,378,378,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":5e-17,"d":"5.00E-17"},23,101,375,275,"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)"]
[]
["ACT01_02990","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-146,"d":"1.00E-146"},59,1,379,379,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":5e-95,"d":"5.00E-95"},40,5,379,375,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":3e-94,"d":"3.00E-94"},44,3,378,376,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":1e-65,"d":"1.00E-65"},36,5,378,374,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":1E-62,"d":"1.00E-62"},35,4,373,370,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":3e-36,"d":"3.00E-36"},30,1,378,378,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":2e-22,"d":"2.00E-22"},19,1,378,378,"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)"]
[]
["ACT01_10950","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-159,"d":"1.00E-159"},59,1,383,383,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":4e-86,"d":"4.00E-86"},37,5,376,372,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":4e-85,"d":"4.00E-85"},41,3,378,376,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":1e-57,"d":"1.00E-57"},36,14,372,359,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":3e-55,"d":"3.00E-55"},32,4,376,373,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":6e-33,"d":"6.00E-33"},28,1,382,382,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":2e-25,"d":"2.00E-25"},22,14,383,370,"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)"]
[]
["ACT01_11040","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":9e-99,"d":"9.00E-99"},40,1,400,400,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":1e-92,"d":"1.00E-92"},43,5,395,391,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":3e-69,"d":"3.00E-69"},31,4,400,397,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":4e-49,"d":"4.00E-49"},32,35,398,364,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":1e-33,"d":"1.00E-33"},28,5,399,395,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":2e-33,"d":"2.00E-33"},28,1,398,398,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":2e-17,"d":"2.00E-17"},21,74,389,316,"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)"]
[]
["ACT01_02540","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"3.1.2.1","high",1,525,{"v":5e-22,"d":"5.00E-22"},25,88,429,342,"Acetyl-CoA hydrolase","Acetyl-CoA acylase. Acetyl-CoA deacylase","Acetyl-CoA + H(2)O = CoA + acetate","_","_"]
[]
["ACT01_02765","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"3.1.2.1","high",1,525,{"v":5e-24,"d":"5.00E-24"},25,10,434,425,"Acetyl-CoA hydrolase","Acetyl-CoA acylase. Acetyl-CoA deacylase","Acetyl-CoA + H(2)O = CoA + acetate","_","_"]
[]
["ACT01_03685","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"3.1.2.1","high",1,525,{"v":4e-26,"d":"4.00E-26"},25,6,429,424,"Acetyl-CoA hydrolase","Acetyl-CoA acylase. Acetyl-CoA deacylase","Acetyl-CoA + H(2)O = CoA + acetate","_","_"]

{"sheet":"COG","index":9,"n_rows":62,"n_cols":7,"rows_kept":62}
["CDS","COG id","Score","Begin","End","Classes","Function"]
["ACT01_13720","COG3875",257,8,264,"S","Uncharacterized conserved protein"]
["ACT01_13730","COG1620",510,2,511,"C","L-lactate permease"]
["ACT01_00410","COG0039",317,2,318,"C","Malate/lactate dehydrogenases"]
["ACT01_04310","COG0039",266,31,296,"C","Malate/lactate dehydrogenases"]
["ACT01_03310","COG1014",179,1,179,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
["ACT01_03315","COG1144",86,14,99,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, delta subunit"]
["ACT01_03320","COG0674",381,1,381,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
["ACT01_03325","COG1013",292,6,297,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
["ACT01_00445","COG0674",406,1,406,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
[null,"COG1014",381,409,789,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
[null,"COG1013",375,800,1174,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
["ACT01_00545","COG0674",410,1,410,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
[null,"COG1014",385,411,795,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
[null,"COG1013",372,796,1167,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
["ACT01_02090","COG0674",405,1,405,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
[null,"COG1013",383,795,1177,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
[null,"COG1014",381,414,794,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
["ACT01_02810","COG0674",414,1,414,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
[null,"COG1014",377,415,791,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
[null,"COG1013",377,794,1170,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
["ACT01_03520","COG0674",409,3,411,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
[null,"COG1013",383,798,1180,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
[null,"COG1014",378,417,794,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
["ACT01_06665","COG0674",411,1,411,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
[null,"COG1013",378,793,1170,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
[null,"COG1014",377,416,792,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
["ACT01_12570","COG0674",411,1,411,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
[null,"COG1013",378,793,1170,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
[null,"COG1014",377,416,792,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
["ACT01_05435","COG0282",397,1,397,"C","Acetate kinase"]
["ACT01_13325","COG0280",338,1,338,"C","Phosphotransacetylase"]
["ACT01_04870","COG1012",444,2,445,"C","NAD-dependent aldehyde dehydrogenases"]
["ACT01_02465","COG1063",339,1,339,"ER","Threonine dehydrogenase and related Zn-dependent dehydrogenases"]
["ACT01_03450","COG1063",342,1,342,"ER","Threonine dehydrogenase and related Zn-dependent dehydrogenases"]
["ACT01_04805","COG1454",378,1,378,"C","Alcohol dehydrogenase, class IV"]
["ACT01_04800","COG1012",448,7,454,"C","NAD-dependent aldehyde dehydrogenases"]
["ACT01_05115","COG0371",361,4,364,"C","Glycerol dehydrogenase and related enzymes"]
["ACT01_06790","COG1454",385,1,385,"C","Alcohol dehydrogenase, class IV"]
["ACT01_11045","COG1454",361,1,361,"C","Alcohol dehydrogenase, class IV"]
["ACT01_07765","COG0183",397,1,397,"I","Acetyl-CoA acetyltransferase"]
["ACT01_10830","COG1024",260,1,260,"I","Enoyl-CoA hydratase/carnithine racemase"]
["ACT01_10835","COG1250",285,1,285,"I","3-hydroxyacyl-CoA dehydrogenase"]
["ACT01_12410","COG1250",304,4,307,"I","3-hydroxyacyl-CoA dehydrogenase"]
["ACT01_02995","COG2030",133,5,137,"I","Acyl dehydratase"]
["ACT01_00280","COG1960",379,1,379,"I","Acyl-CoA dehydrogenases"]
["ACT01_02990","COG1960",379,1,379,"I","Acyl-CoA dehydrogenases"]
["ACT01_10950","COG1960",383,1,383,"I","Acyl-CoA dehydrogenases"]
["ACT01_11040","COG1960",402,1,402,"I","Acyl-CoA dehydrogenases"]
["ACT01_09515","COG2025",334,1,334,"C","Electron transfer flavoprotein, alpha subunit"]
["ACT01_09520","COG2086",261,1,261,"C","Electron transfer flavoprotein, beta subunit"]
["ACT01_10940","COG2025",333,3,335,"C","Electron transfer flavoprotein, alpha subunit"]
["ACT01_10945","COG2086",271,1,271,"C","Electron transfer flavoprotein, beta subunit"]
["ACT01_02540","COG0427",434,5,438,"C","Acetyl-CoA hydrolase"]
["ACT01_02765","COG0427",435,9,443,"C","Acetyl-CoA hydrolase"]
["ACT01_03685","COG0427",442,2,443,"C","Acetyl-CoA hydrolase"]
["ACT01_04510","COG4656",444,7,450,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfC"]
["ACT01_04515","COG4658",321,22,342,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfD"]
["ACT01_04520","COG4659",147,27,173,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfG"]
["ACT01_04525","COG4660",194,1,194,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfE"]
["ACT01_04530","COG4657",191,1,191,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfA"]
["ACT01_04535","COG2878",264,6,269,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfB"]

{"sheet":"EGGNOG","index":10,"n_rows":48,"n_cols":7,"rows_kept":48}
["CDS","OG ID","Score","Eval","Class ID","OG function","KEGG map"]
["ACT01_13720","05QUH","740.3",{"v":1.8e-211,"d":"1.80E-211"},"S","Domain of unknown function (DUF2088)","-"]
["ACT01_13730","05DAA","778.5",{"v":7.3e-223,"d":"7.30E-223"},"C","L-lactate","-"]
["ACT01_00410","05C80","451.8",{"v":9.7e-125,"d":"9.70E-125"},"C","Catalyzes the reversible oxidation of malate to oxaloacetate (By similarity)","00010, 00020, 00270, 00620, 00630, 00640, 00680, 00710, 00720, 01100, 01110, 01120"]
["ACT01_04310","07WFN","469.9",{"v":3.6e-130,"d":"3.60E-130"},"S","Malate lactate","-"]
["ACT01_03310","05EJ5","204.1",{"v":2E-50,"d":"2.00E-50"},"C","oxidoreductase gamma subunit","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 01100, 01120"]
["ACT01_03315","05WGB","136",{"v":3.7e-30,"d":"3.70E-30"},"C","oxidoreductase, delta subunit","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 01100, 01120"]
["ACT01_03320","05D95","517.7",{"v":1.8E-144,"d":"1.80E-144"},"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"]
["ACT01_03325","05DDK","426.8",{"v":3.1e-117,"d":"3.10E-117"},"C","oxidoreductase, beta subunit","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 01100, 01120"]
["ACT01_00445","05D95","1948.7",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"]
["ACT01_00545","05D95","2155.9",0,"C","Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (By similarity)","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 00910, 01100, 01120"]
["ACT01_02090","05D95","1791.5",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"]
["ACT01_02810","05D95","2248.8",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"]
["ACT01_03520","05D95","1667.1",0,"C","Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (By similarity)","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 00910, 01100, 01120"]
["ACT01_06665","05D95","1712.2",0,"C","Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (By similarity)","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 00910, 01100, 01120"]
["ACT01_12570","05D95","1708.3",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"]
["ACT01_05435","05C6H","729.6",{"v":3e-208,"d":"3.00E-208"},"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"]
["ACT01_13325","08IJ2","605.9",{"v":4.4e-171,"d":"4.40E-171"},"C","phosphate acetyltransferase","00430, 00620, 00640, 00680, 00720, 01100, 01120"]
["ACT01_04870","07QIG","676",{"v":4.9E-192,"d":"4.90E-192"},"C","Dehydrogenase","00010, 00071, 00350, 00362, 00620, 00621, 00622, 00625, 00626, 00650, 01100, 01110, 01120"]
["ACT01_02465","05CPQ","388.7",{"v":1.1E-105,"d":"1.10E-105"},"E","Dehydrogenase","00051, 00260, 01100"]
["ACT01_03450","05CPQ","412.1",{"v":9.2e-113,"d":"9.20E-113"},"E","Dehydrogenase","00051, 00260, 01100"]
["ACT01_04805","05C0A","442.2",{"v":9.1e-122,"d":"9.10E-122"},"C","alcohol dehydrogenase","00010, 00071, 00350, 00362, 00620, 00621, 00622, 00625, 00626, 00650, 01100, 01110, 01120"]
["ACT01_04800","07QIG","629.4",{"v":5.5e-178,"d":"5.50E-178"},"C","Dehydrogenase","00010, 00071, 00350, 00362, 00620, 00621, 00622, 00625, 00626, 00650, 01100, 01110, 01120"]
["ACT01_05115","05DCT","459.9",{"v":4.1e-127,"d":"4.10E-127"},"C","glycerol dehydrogenase","00561, 01100"]
["ACT01_06790","05C0A","536.2",{"v":4.7e-150,"d":"4.70E-150"},"C","alcohol dehydrogenase","00010, 00071, 00350, 00362, 00620, 00621, 00622, 00625, 00626, 00650, 01100, 01110, 01120"]
["ACT01_11045","05C0A","506.1",{"v":4.9e-141,"d":"4.90E-141"},"C","alcohol dehydrogenase","00010, 00071, 00350, 00362, 00620, 00621, 00622, 00625, 00626, 00650, 01100, 01110, 01120"]
["ACT01_07765","05CHU","591.3",{"v":1.3e-166,"d":"1.30E-166"},"I","acetyl-coa acetyltransferase","00071, 00072, 00280, 00281, 00310, 00362, 00380, 00592, 00620, 00630, 00640, 00642, 00650, 00720, 00900, 01100, 01110, 01120, 02020"]
["ACT01_10830","05E39","345.9",{"v":6.1e-93,"d":"6.10E-93"},"I","Enoyl-CoA hydratase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00627, 00630, 00640, 00650, 00720, 00903, 00930, 01100, 01110, 01120"]
["ACT01_10835","05DYT","436.8",{"v":2.9E-120,"d":"2.90E-120"},"I","3-hydroxyacyl-CoA dehydrogenase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00640, 00650, 00720, 00903, 00930, 01040, 01100, 01110, 01120"]
["ACT01_12410","05DYT","358.2",{"v":1.4e-96,"d":"1.40E-96"},"I","3-hydroxyacyl-CoA dehydrogenase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00640, 00650, 00720, 00903, 00930, 01040, 01100, 01110, 01120"]
["ACT01_02995","08Z7G","165.2",{"v":7.9E-39,"d":"7.90E-39"},"I","MaoC domain protein dehydratase","-"]
["ACT01_00280","05C1G","698.4",{"v":7.1E-199,"d":"7.10E-199"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["ACT01_02990","05C1G","555.1",{"v":9.7e-156,"d":"9.70E-156"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["ACT01_10950","05C1G","554.7",{"v":1.3E-155,"d":"1.30E-155"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["ACT01_11040","05C1G","598.6",{"v":8.1e-169,"d":"8.10E-169"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["ACT01_09515","05C10","439.1",{"v":6.8E-121,"d":"6.80E-121"},"C","Electron transfer flavoprotein","00910"]
["ACT01_09520","05BZJ","327.8",{"v":1.7e-87,"d":"1.70E-87"},"C","Electron transfer flavoprotein","00910"]
["ACT01_10940","05C10","622.1",{"v":5.7e-176,"d":"5.70E-176"},"C","Electron transfer flavoprotein","00910"]
["ACT01_10945","05BZJ","459.5",{"v":4e-127,"d":"4.00E-127"},"C","Electron transfer flavoprotein","00910"]
["ACT01_02540","COG0427","678.7",{"v":6.8e-193,"d":"6.80E-193"},"C","Acetyl-CoA hydrolase","00620"]
["ACT01_02765","05CYC","692.6",{"v":4.6e-197,"d":"4.60E-197"},"C","Transferase","00620"]
["ACT01_03685","COG0427","533.1",{"v":4.6e-149,"d":"4.60E-149"},"C","Acetyl-CoA hydrolase","00620"]
["ACT01_04510","07QTR","838.6",{"v":5.2e-241,"d":"5.20E-241"},"C","Required for nitrogen fixation. May be part of a membrane complex functioning as an intermediate in the electron transport to nitrogenase (By similarity)","-"]
["ACT01_04515","05D6A","581.6",{"v":8.8e-164,"d":"8.80E-164"},"C","Electron transport complex","-"]
["ACT01_04520","080WF","306.6",{"v":2.9e-81,"d":"2.90E-81"},"C","Electron transport complex, RnfABCDGE type, G subunit","-"]
["ACT01_04525","05DZB","389.4",{"v":3.9e-106,"d":"3.90E-106"},"C","Electron transport complex","-"]
["ACT01_04530","05DGN","322.8",{"v":4.1e-86,"d":"4.10E-86"},"C","Electron transport complex","-"]
["ACT01_04535","07SVV","461.1",{"v":1.4E-127,"d":"1.40E-127"},"C","electron transport complex, RnfABCDGE type, B subunit","-"]

{"sheet":"FigFam","index":11,"n_rows":35,"n_cols":4,"rows_kept":35}
["CDS","FIGFAM id","FIGFAM Description","EC number"]
["ACT01_00410","FIG000812","L-lactate dehydrogenase","1.1.1.27"]
["ACT01_03310","FIG003176","Pyruvate:ferredoxin oxidoreductase, gamma subunit","1.2.7.1"]
["ACT01_03315","FIG135572","Pyruvate:ferredoxin oxidoreductase, gamma subunit","1.2.7.1"]
["ACT01_03320","FIG002975","Pyruvate:ferredoxin oxidoreductase, alpha subunit","1.2.7.1"]
["ACT01_03325","FIG003175","Pyruvate:ferredoxin oxidoreductase, beta subunit","1.2.7.1"]
["ACT01_00445","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["ACT01_00545","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["ACT01_02090","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["ACT01_02810","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["ACT01_03520","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["ACT01_06665","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["ACT01_12570","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["ACT01_05435","FIG134300","Acetate kinase","2.7.2.1"]
["ACT01_13325","FIG000522","Phosphate acetyltransferase","2.3.1.8"]
["ACT01_04870","FIG004876","Acetaldehyde dehydrogenase, ethanolamine utilization cluster","_"]
["ACT01_02465","FIG147895","Starvation sensing protein RspB","_"]
["ACT01_04800","FIG004876","Acetaldehyde dehydrogenase, ethanolamine utilization cluster","_"]
["ACT01_05115","FIG132994","Glycerol dehydrogenase","1.1.1.6"]
["ACT01_07765","FIG002604","Acetyl-CoA acetyltransferase","2.3.1.9"]
["ACT01_10830","FIG002255","3-hydroxybutyryl-CoA dehydratase","4.2.1.55"]
["ACT01_10835","FIG133011","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157"]
["ACT01_00280","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["ACT01_02990","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["ACT01_10950","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["ACT01_11040","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["ACT01_09515","FIG000366","Electron transfer flavoprotein, alpha subunit","_"]
["ACT01_10940","FIG000366","Electron transfer flavoprotein, alpha subunit","_"]
["ACT01_10945","FIG136866","Electron transfer flavoprotein, beta subunit","_"]
["ACT01_04510","FIG018536","Electron transport complex protein RnfC","_"]
["ACT01_04515","FIG022976","Electron transport complex protein RnfD","_"]
["ACT01_04520","FIG002689","Electron transport complex protein RnfG","_"]
["ACT01_04525","FIG134060","Electron transport complex protein RnfE","_"]
["ACT01_04530","FIG001505","Electron transport complex protein RnfA","_"]
["ACT01_04535","FIG133292","Electron transport complex protein RnfB","_"]

{"sheet":"InterProScan","index":12,"n_rows":632,"n_cols":13,"rows_kept":632}
["ACT01_13720","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR018657","PFAM","PF09861","Lar_N",8,213,0.480094,{"v":2.1e-71,"d":"2.10E-71"},"LarA-like_N","Domain","LarA-like, N-terminal","Molecular Function: lactate racemase activity (GO:0050043)"]
[null,"_","_","PTHR33171","_",1,425,0.992974,{"v":7.6e-115,"d":"7.60E-115"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.11440","_",34,269,0.550351,{"v":8.6e-154,"d":"8.60E-154"},"_","_","_","-"]
[null,"_","_","G3DSA:3.90.226.30","_",6,421,0.971897,{"v":8.6e-154,"d":"8.60E-154"},"_","_","_","-"]
[]
["ACT01_13730","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",2,506,0.986301,{"v":4.5e-123,"d":"4.50E-123"},"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",3,504,0.980431,{"v":7.2e-115,"d":"7.20E-115"},"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",3,505,0.982387,{"v":1.9E-109,"d":"1.90E-109"},"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)"]
[]
["ACT01_00410","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036291","SSF","SSF51735","SSF51735",3,148,0.455975,2.71E-34,"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR022383","PFAM","PF02866","Ldh_1_C",149,315,0.522013,{"v":2.9e-24,"d":"2.90E-24"},"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,"IPR015955","CATHGENE3D","G3DSA:3.90.110.10","G3DSA:3.90.110.10",148,312,0.515723,{"v":2.3e-50,"d":"2.30E-50"},"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",147,311,0.515723,1.27E-44,"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,"IPR001557","PIRSF","PIRSF000102","Lac_mal_DH",2,317,0.990566,{"v":2.2e-80,"d":"2.20E-80"},"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",32,56,0.0754717,{"v":5.8e-25,"d":"5.80E-25"},"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",144,162,0.0566038,{"v":5.8e-25,"d":"5.80E-25"},"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",7,31,0.0754717,{"v":5.8e-25,"d":"5.80E-25"},"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",120,140,0.0628931,{"v":5.8e-25,"d":"5.80E-25"},"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",174,187,0.0408805,{"v":5.8e-25,"d":"5.80E-25"},"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",8,146,0.433962,{"v":1.6e-17,"d":"1.60E-17"},"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","_",2,147,0.455975,{"v":3.4e-38,"d":"3.40E-38"},"_","_","_","-"]
[null,"_","_","PTHR43128","_",8,314,0.962264,{"v":1.2E-81,"d":"1.20E-81"},"_","_","_","-"]
[null,"_","_","PTHR43128:SF7","_",8,314,0.962264,{"v":1.2E-81,"d":"1.20E-81"},"_","_","_","-"]
[]
["ACT01_04310","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",31,184,0.463636,1.89e-09,"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"_","_","G3DSA:3.40.50.720","_",27,186,0.481818,{"v":2.6e-21,"d":"2.60E-21"},"_","_","_","-"]
[]
["ACT01_03310","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",10,174,0.906077,{"v":2.9E-37,"d":"2.90E-37"},"Pyrv/ketoisovalerate_OxRed_cat","Domain","Pyruvate/ketoisovalerate oxidoreductase, catalytic domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011894","TIGRFAMs","TIGR02175","PorC_KorC",1,178,0.977901,{"v":8e-62,"d":"8.00E-62"},"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",1,180,0.98895,{"v":3.3E-61,"d":"3.30E-61"},"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",1,178,0.977901,1.57E-44,"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","_",1,179,0.983425,{"v":5.5e-59,"d":"5.50E-59"},"_","_","_","-"]
[]
["ACT01_03315","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR017896","PFAM","PF13237","Fer4_10",41,87,0.46,6.2e-08,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",39,68,0.29,10.709,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",69,97,0.28,8.768,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011898","PANTHER","PTHR43724","PTHR43724",32,98,0.66,{"v":2.9E-21,"d":"2.90E-21"},"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",33,98,0.65,{"v":2.4e-24,"d":"2.40E-24"},"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","_",22,58,0.36,1.2E-5,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",59,99,0.4,3.9e-09,"_","_","_","-"]
[null,"_","_","SSF54862","_",24,98,0.74,{"v":1.11e-18,"d":"1.11E-18"},"_","_","_","-"]
[]
["ACT01_03320","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",262,364,0.259542,{"v":7.3E-29,"d":"7.30E-29"},"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",3,250,0.628499,{"v":6.68e-65,"d":"6.68E-65"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR009014","CATHGENE3D","G3DSA:3.40.50.920","G3DSA:3.40.50.920",252,391,0.35369,{"v":3.6e-41,"d":"3.60E-41"},"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",253,374,0.307888,{"v":1.08e-29,"d":"1.08E-29"},"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",16,231,0.547074,{"v":9.4e-68,"d":"9.40E-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","_",9,169,0.407125,{"v":1.19894E-61,"d":"1.20E-61"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",1,251,0.636132,{"v":9.7e-95,"d":"9.70E-95"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",4,388,0.977099,{"v":1.5e-101,"d":"1.50E-101"},"_","_","_","-"]
[null,"_","_","PTHR32154:SF31","_",4,388,0.977099,{"v":1.5e-101,"d":"1.50E-101"},"_","_","_","-"]
[]
["ACT01_03325","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",5,295,0.976431,{"v":1.33e-71,"d":"1.33E-71"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR011766","PFAM","PF02775","TPP_enzyme_C",58,208,0.50505,{"v":1.2E-21,"d":"1.20E-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","_",4,83,0.265993,4.7e-06,"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",84,296,0.713805,{"v":1.6e-66,"d":"1.60E-66"},"_","_","_","-"]
[null,"_","_","PTHR42897","_",9,293,0.956229,{"v":2.7e-100,"d":"2.70E-100"},"_","_","_","-"]
[null,"_","_","cd03376","_",16,246,0.774411,{"v":1.71549e-117,"d":"1.72E-117"},"_","_","_","-"]
[]
["ACT01_00445","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",269,362,0.0792164,4.2e-14,"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",3,258,0.217206,{"v":5.3e-72,"d":"5.30E-72"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",792,1172,0.32368,{"v":5.42e-111,"d":"5.42E-111"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",425,609,0.156729,{"v":5.6e-30,"d":"5.60E-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",628,681,0.0451448,{"v":5.7e-17,"d":"5.70E-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,"IPR019456","SMART","SM00890","EKR",622,682,0.0511073,3.7e-15,"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",748,759,9.36968E-3,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",739,771,0.0272572,9.348,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",683,712,0.0247019,8.861,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011895","PIRSF","PIRSF000159","NifJ",1,1174,0.999148,0,"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",6,1171,0.992334,0,"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",957,1069,0.0954003,4.9e-11,"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",259,413,0.131175,{"v":4.5E-60,"d":"4.50E-60"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR009014","SSF","SSF52922","SSF52922",259,410,0.12862,{"v":3.34e-45,"d":"3.34E-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",18,247,0.19506,{"v":4.4E-72,"d":"4.40E-72"},"Pyrv_Fd/Flavodoxin_OxRdtase_N","Domain","Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","CATHGENE3D","G3DSA:3.40.920.10","G3DSA:3.40.920.10",415,626,0.179727,{"v":3E-79,"d":"3.00E-79"},"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",417,664,0.210392,{"v":4.05e-75,"d":"4.05E-75"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PF13484","_",692,760,0.0579216,2.6e-10,"_","_","_","-"]
[null,"_","_","SSF54862","_",671,778,0.0911414,{"v":3.77e-17,"d":"3.77E-17"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",672,788,0.0988075,{"v":1.3e-38,"d":"1.30E-38"},"_","_","_","-"]
[null,"_","_","cd07034","_",10,173,0.138842,{"v":1.68802e-45,"d":"1.69E-45"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",2,258,0.218058,{"v":5.6e-102,"d":"5.60E-102"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",791,1174,0.326235,{"v":1.8e-151,"d":"1.80E-151"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",1,1170,0.995741,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",1,1170,0.995741,0,"_","_","_","-"]
[null,"_","_","cd03377","_",809,1172,0.309199,0,"_","_","_","-"]
[]
["ACT01_00545","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",268,373,0.0896669,{"v":3.6e-16,"d":"3.60E-16"},"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",3,257,0.216909,{"v":4.71e-76,"d":"4.71E-76"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",784,1164,0.324509,3.17E-125,"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",424,607,0.156277,{"v":1.1E-28,"d":"1.10E-28"},"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",630,673,0.0367208,2.7e-14,"Pyrv-flavodox_OxRtase_EKR","Domain","Pyruvate-flavodoxin oxidoreductase, EKR domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR019456","SMART","SM00890","EKR",620,678,0.0495303,3.2e-11,"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",743,754,0.00939368,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",734,763,0.0247652,10.356,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",679,708,0.0247652,9.861,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011895","PIRSF","PIRSF000159","NifJ",1,1170,0.998292,0,"Pyrv_flavodox_OxRed","Family","Pyruvate-flavodoxin oxidoreductase","Molecular Function: iron ion binding (GO:0005506); Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: electron transport chain (GO:0022900); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011895","TIGRFAMs","TIGR02176","pyruv_ox_red",4,1165,0.99146,0,"Pyrv_flavodox_OxRed","Family","Pyruvate-flavodoxin oxidoreductase","Molecular Function: iron ion binding (GO:0005506); Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: electron transport chain (GO:0022900); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011766","PFAM","PF02775","TPP_enzyme_C",953,1064,0.0947908,1.1e-08,"TPP_enzyme-bd_C","Domain","Thiamine pyrophosphate enzyme, C-terminal TPP-binding","Molecular Function: catalytic activity (GO:0003824); Molecular Function: thiamine pyrophosphate binding (GO:0030976)"]
[null,"IPR009014","CATHGENE3D","G3DSA:3.40.50.920","G3DSA:3.40.50.920",258,413,0.132365,{"v":3.3E-52,"d":"3.30E-52"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR009014","SSF","SSF52922","SSF52922",258,409,0.12895,{"v":8.38e-44,"d":"8.38E-44"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002880","PFAM","PF01855","POR_N",18,246,0.194705,{"v":7.4e-79,"d":"7.40E-79"},"Pyrv_Fd/Flavodoxin_OxRdtase_N","Domain","Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","CATHGENE3D","G3DSA:3.40.920.10","G3DSA:3.40.920.10",414,624,0.179334,{"v":7e-90,"d":"7.00E-90"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","SSF","SSF53323","SSF53323",415,667,0.215201,{"v":5.1e-82,"d":"5.10E-82"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PF13484","_",687,755,0.05807,2.6E-7,"_","_","_","-"]
[null,"_","_","SSF54862","_",665,829,0.140051,{"v":9.77e-22,"d":"9.77E-22"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",668,780,0.0956447,{"v":1.5e-31,"d":"1.50E-31"},"_","_","_","-"]
[null,"_","_","cd07034","_",9,172,0.139197,{"v":9.03194E-50,"d":"9.03E-50"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",2,257,0.217763,{"v":3.9e-105,"d":"3.90E-105"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",784,1168,0.327925,{"v":9.3E-168,"d":"9.30E-168"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",1,1165,0.994022,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",1,1165,0.994022,0,"_","_","_","-"]
[null,"_","_","cd03377","_",801,1164,0.309991,0,"_","_","_","-"]
[]
["ACT01_02090","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",270,373,0.0875106,8.1e-15,"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",7,259,0.214104,{"v":4.71e-71,"d":"4.71E-71"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",786,1176,0.331351,4.21E-121,"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",425,609,0.15633,{"v":1.4e-31,"d":"1.40E-31"},"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",628,680,0.0441801,{"v":6.9e-20,"d":"6.90E-20"},"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",622,681,0.0501274,{"v":5.6e-22,"d":"5.60E-22"},"Pyrv-flavodox_OxRtase_EKR","Domain","Pyruvate-flavodoxin oxidoreductase, EKR domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",747,758,0.00934579,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",738,767,0.0246389,10.054,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",682,711,0.0246389,9.323,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011895","PIRSF","PIRSF000159","NifJ",1,1177,0.99915,0,"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",6,1175,0.993203,0,"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",961,1073,0.0951572,5.5e-09,"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",260,412,0.129142,{"v":2.5E-53,"d":"2.50E-53"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR009014","SSF","SSF52922","SSF52922",260,405,0.123195,{"v":4.57e-43,"d":"4.57E-43"},"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",22,248,0.192014,{"v":1.5e-73,"d":"1.50E-73"},"Pyrv_Fd/Flavodoxin_OxRdtase_N","Domain","Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","CATHGENE3D","G3DSA:3.40.920.10","G3DSA:3.40.920.10",415,626,0.179269,{"v":3.7e-87,"d":"3.70E-87"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","SSF","SSF53323","SSF53323",415,670,0.216653,{"v":2.09e-80,"d":"2.09E-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,"_","_","PF13484","_",690,759,0.0586236,2.2e-09,"_","_","_","-"]
[null,"_","_","SSF54862","_",667,828,0.136788,{"v":2.09e-21,"d":"2.09E-21"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",671,784,0.0960068,{"v":1.1E-40,"d":"1.10E-40"},"_","_","_","-"]
[null,"_","_","cd07034","_",11,174,0.138488,{"v":1.38973e-48,"d":"1.39E-48"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",4,259,0.216653,{"v":3.9e-97,"d":"3.90E-97"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",785,1177,0.33305,{"v":1.2e-155,"d":"1.20E-155"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",6,1175,0.993203,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",6,1175,0.993203,0,"_","_","_","-"]
[null,"_","_","cd03377","_",803,1175,0.316058,0,"_","_","_","-"]
[]
["ACT01_02810","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",270,365,0.0811966,2.8e-13,"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",7,259,0.215385,1.12E-67,"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",783,1166,0.32735,{"v":4.16e-119,"d":"4.16E-119"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",426,609,0.15641,{"v":3.5e-30,"d":"3.50E-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",626,679,0.0452991,5E-15,"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",622,680,0.0495727,{"v":1.2e-17,"d":"1.20E-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",744,755,0.00940171,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",690,701,0.00940171,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF12838","Fer4_7",689,758,0.0589744,2.6e-09,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",681,710,0.0247863,10.155,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",735,764,0.0247863,9.97,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011895","PIRSF","PIRSF000159","NifJ",1,1170,0.999145,0,"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",6,1164,0.989744,0,"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",952,1062,0.0940171,4.9E-9,"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",260,412,0.129915,{"v":4.7e-53,"d":"4.70E-53"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR009014","SSF","SSF52922","SSF52922",260,408,0.126496,2.57E-40,"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002880","PFAM","PF01855","POR_N",20,249,0.195726,{"v":7.1e-67,"d":"7.10E-67"},"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",416,626,0.179487,{"v":4.2e-91,"d":"4.20E-91"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","SSF","SSF53323","SSF53323",418,669,0.21453,{"v":2.22e-84,"d":"2.22E-84"},"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","_",667,828,0.137607,3.91E-21,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",670,781,0.0948718,{"v":2.1E-35,"d":"2.10E-35"},"_","_","_","-"]
[null,"_","_","cd07034","_",11,174,0.139316,{"v":4.88981e-41,"d":"4.89E-41"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",3,259,0.218803,{"v":7.6e-92,"d":"7.60E-92"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",782,1167,0.32906,{"v":4.3e-163,"d":"4.30E-163"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",5,1163,0.989744,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",5,1163,0.989744,0,"_","_","_","-"]
[null,"_","_","cd03377","_",800,1163,0.310256,0,"_","_","_","-"]
[]
["ACT01_03520","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",273,366,0.0788136,2.5E-15,"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",9,262,0.214407,{"v":6.67e-70,"d":"6.67E-70"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",789,1179,0.330508,{"v":2.86e-118,"d":"2.86E-118"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",428,611,0.155085,{"v":1.9E-32,"d":"1.90E-32"},"Pyrv/ketoisovalerate_OxRed_cat","Domain","Pyruvate/ketoisovalerate oxidoreductase, catalytic domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR019456","PFAM","PF10371","EKR",628,683,0.0466102,{"v":8.6e-19,"d":"8.60E-19"},"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",625,684,0.05,{"v":9.8e-18,"d":"9.80E-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,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",694,705,0.00932203,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",750,761,0.00932203,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF12838","Fer4_7",693,764,0.0601695,8.9e-09,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",741,770,0.0245763,9.567,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",685,714,0.0245763,9.415,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011895","PIRSF","PIRSF000159","NifJ",4,1180,0.99661,0,"Pyrv_flavodox_OxRed","Family","Pyruvate-flavodoxin oxidoreductase","Molecular Function: iron ion binding (GO:0005506); Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: electron transport chain (GO:0022900); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011895","TIGRFAMs","TIGR02176","pyruv_ox_red",9,1177,0.98983,0,"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",945,1075,0.110169,1.1E-14,"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",263,416,0.129661,{"v":2.5e-58,"d":"2.50E-58"},"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",263,409,0.123729,1.36E-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",22,251,0.194068,{"v":3.2E-69,"d":"3.20E-69"},"Pyrv_Fd/Flavodoxin_OxRdtase_N","Domain","Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","CATHGENE3D","G3DSA:3.40.920.10","G3DSA:3.40.920.10",418,628,0.177966,{"v":3.7e-88,"d":"3.70E-88"},"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",419,664,0.207627,{"v":4.84e-82,"d":"4.84E-82"},"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","_",670,833,0.138136,{"v":7.39e-22,"d":"7.39E-22"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",674,787,0.0957627,{"v":1.9e-39,"d":"1.90E-39"},"_","_","_","-"]
[null,"_","_","cd07034","_",14,177,0.138136,{"v":3.66161e-41,"d":"3.66E-41"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",6,262,0.216949,{"v":1.1E-99,"d":"1.10E-99"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",788,1180,0.332203,{"v":1.4E-155,"d":"1.40E-155"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",9,1177,0.98983,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",9,1177,0.98983,0,"_","_","_","-"]
[null,"_","_","cd03377","_",806,1178,0.315254,0,"_","_","_","-"]
[null,"_","_","Coil","_",885,905,0.0169492,"_","_","_","_","-"]
[]
["ACT01_06665","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037112","CATHGENE3D","G3DSA:4.10.780.10","G3DSA:4.10.780.10",628,668,0.034188,7.9e-06,"Pyrv-flavodox_OxR_EKR_sf","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, EKR domain superfamily","-"]
[null,"IPR033412","PFAM","PF17147","PFOR_II",269,374,0.0897436,1.2e-14,"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",3,258,0.217949,{"v":4.71e-73,"d":"4.71E-73"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",784,1167,0.32735,{"v":2.65e-129,"d":"2.65E-129"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",425,608,0.15641,{"v":1.2e-30,"d":"1.20E-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",625,678,0.0452991,{"v":1.2E-22,"d":"1.20E-22"},"Pyrv-flavodox_OxRtase_EKR","Domain","Pyruvate-flavodoxin oxidoreductase, EKR domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR019456","SMART","SM00890","EKR",621,679,0.0495727,{"v":4.9e-28,"d":"4.90E-28"},"Pyrv-flavodox_OxRtase_EKR","Domain","Pyruvate-flavodoxin oxidoreductase, EKR domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",743,754,0.00940171,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",680,709,0.0247863,8.819,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",734,765,0.0264957,8.81,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011895","PIRSF","PIRSF000159","NifJ",1,1170,0.999145,0,"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",5,1167,0.993162,0,"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",955,1066,0.0948718,1.5E-9,"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",259,414,0.132479,{"v":1.3E-54,"d":"1.30E-54"},"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",259,413,0.131624,{"v":1.32e-45,"d":"1.32E-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",22,247,0.192308,{"v":6.7e-74,"d":"6.70E-74"},"Pyrv_Fd/Flavodoxin_OxRdtase_N","Domain","Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","CATHGENE3D","G3DSA:3.40.920.10","G3DSA:3.40.920.10",415,625,0.179487,{"v":1E-89,"d":"1.00E-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",416,667,0.21453,{"v":4.32e-85,"d":"4.32E-85"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PF13484","_",688,755,0.057265,4.4e-09,"_","_","_","-"]
[null,"_","_","SSF54862","_",665,829,0.140171,{"v":5.3e-19,"d":"5.30E-19"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",669,782,0.0965812,{"v":3.8e-40,"d":"3.80E-40"},"_","_","_","-"]
[null,"_","_","cd07034","_",10,173,0.139316,{"v":3.83057e-48,"d":"3.83E-48"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",2,258,0.218803,{"v":3.2e-104,"d":"3.20E-104"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",783,1170,0.330769,{"v":1.4e-172,"d":"1.40E-172"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",1,1167,0.996581,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",1,1167,0.996581,0,"_","_","_","-"]
[null,"_","_","cd03377","_",801,1166,0.311966,0,"_","_","_","-"]
[]
["ACT01_12570","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037112","CATHGENE3D","G3DSA:4.10.780.10","G3DSA:4.10.780.10",628,668,0.034188,7.9e-06,"Pyrv-flavodox_OxR_EKR_sf","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, EKR domain superfamily","-"]
[null,"IPR033412","PFAM","PF17147","PFOR_II",269,374,0.0897436,1.2e-14,"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",3,258,0.217949,{"v":2.8e-73,"d":"2.80E-73"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",784,1168,0.328205,{"v":1.33e-129,"d":"1.33E-129"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",425,608,0.15641,{"v":1.2e-30,"d":"1.20E-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",625,678,0.0452991,{"v":1.2E-22,"d":"1.20E-22"},"Pyrv-flavodox_OxRtase_EKR","Domain","Pyruvate-flavodoxin oxidoreductase, EKR domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR019456","SMART","SM00890","EKR",621,679,0.0495727,{"v":4.9e-28,"d":"4.90E-28"},"Pyrv-flavodox_OxRtase_EKR","Domain","Pyruvate-flavodoxin oxidoreductase, EKR domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",743,754,0.00940171,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",680,709,0.0247863,8.819,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",734,765,0.0264957,8.81,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011895","PIRSF","PIRSF000159","NifJ",1,1170,0.999145,0,"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",5,1168,0.994017,0,"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",955,1066,0.0948718,1.5E-9,"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",259,414,0.132479,{"v":5.6e-55,"d":"5.60E-55"},"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",259,413,0.131624,{"v":6.91e-46,"d":"6.91E-46"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002880","PFAM","PF01855","POR_N",22,247,0.192308,{"v":8.6e-74,"d":"8.60E-74"},"Pyrv_Fd/Flavodoxin_OxRdtase_N","Domain","Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","CATHGENE3D","G3DSA:3.40.920.10","G3DSA:3.40.920.10",415,625,0.179487,{"v":1E-89,"d":"1.00E-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",416,667,0.21453,{"v":4.32e-85,"d":"4.32E-85"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PF13484","_",688,755,0.057265,1.9e-09,"_","_","_","-"]
[null,"_","_","SSF54862","_",665,829,0.140171,{"v":1.88e-19,"d":"1.88E-19"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",669,782,0.0965812,{"v":6.7e-40,"d":"6.70E-40"},"_","_","_","-"]
[null,"_","_","cd07034","_",10,173,0.139316,{"v":7.21193e-48,"d":"7.21E-48"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",2,258,0.218803,{"v":1.4e-103,"d":"1.40E-103"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",783,1170,0.330769,{"v":5.9E-173,"d":"5.90E-173"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",1,1167,0.996581,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",1,1167,0.996581,0,"_","_","_","-"]
[null,"_","_","cd03377","_",801,1167,0.312821,0,"_","_","_","-"]
[]
["ACT01_05435","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",3,14,0.0277078,"_","Aliphatic_acid_kinase_CS","Conserved_site","Aliphatic acid kinase, short-chain, conserved site","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR023865","PROSITE","PS01076","ACETATE_KINASE_2",203,220,0.0428212,"_","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",1,397,0.997481,192.018,"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",1,397,0.997481,{"v":1.7e-154,"d":"1.70E-154"},"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",2,395,0.989924,{"v":1.5e-156,"d":"1.50E-156"},"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",1,396,0.994962,{"v":1.7E-164,"d":"1.70E-164"},"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",3,389,0.972292,{"v":2.2e-159,"d":"2.20E-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","PRINTS","PR00471","ACETATEKNASE",3,14,0.0277078,{"v":5.9e-43,"d":"5.90E-43"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",173,186,0.0327456,{"v":5.9e-43,"d":"5.90E-43"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",376,388,0.0302267,{"v":5.9e-43,"d":"5.90E-43"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",300,313,0.0327456,{"v":5.9e-43,"d":"5.90E-43"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",203,224,0.0528967,{"v":5.9e-43,"d":"5.90E-43"},"Aliphatic_acid_kin_short-chain","Family","Aliphatic acid kinase, short-chain","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PRINTS","PR00471","ACETATEKNASE",322,338,0.0403023,{"v":5.9e-43,"d":"5.90E-43"},"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","_",1,195,0.488665,4.23E-73,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",1,195,0.488665,{"v":5.1e-80,"d":"5.10E-80"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",196,397,0.506297,{"v":3.9e-81,"d":"3.90E-81"},"_","_","_","-"]
[null,"_","_","SSF53067","_",157,395,0.599496,{"v":1.07e-89,"d":"1.07E-89"},"_","_","_","-"]
[null,"_","_","PTHR21060:SF15","_",1,396,0.994962,{"v":1.7E-164,"d":"1.70E-164"},"_","_","_","-"]
[]
["ACT01_13325","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",9,331,0.936047,{"v":3E-124,"d":"3.00E-124"},"P_AcTrfase_dom1","Homologous_superfamily","Phosphate acetyltransferase, domain 1","-"]
[null,"IPR042112","CATHGENE3D","G3DSA:3.40.50.10750","G3DSA:3.40.50.10750",143,304,0.468023,{"v":3E-124,"d":"3.00E-124"},"P_AcTrfase_dom2","Homologous_superfamily","Phosphate acetyltransferase, domain 2","-"]
[null,"IPR012147","PIRSF","PIRSF000428","P_Ac_trans",1,334,0.968023,{"v":3.5e-108,"d":"3.50E-108"},"P_Ac_Bu_trans","Family","Phosphate acetyl/butyryltransferase","Molecular Function: transferase activity, transferring acyl groups (GO:0016746)"]
[null,"IPR004614","TIGRFAMs","TIGR00651","pta",18,326,0.895349,{"v":9.2e-105,"d":"9.20E-105"},"P_AcTrfase","Domain","Phosphate acetyltransferase","Molecular Function: acetyltransferase activity (GO:0016407)"]
[null,"IPR002505","PFAM","PF01515","PTA_PTB",3,327,0.94186,{"v":8.1e-116,"d":"8.10E-116"},"PTA_PTB","Domain","Phosphate acetyl/butaryl transferase","Molecular Function: transferase activity, transferring acyl groups (GO:0016746)"]
[null,"_","_","SSF53659","_",1,331,0.959302,1.15E-91,"_","_","_","-"]
[null,"_","_","PTHR43356","_",2,332,0.959302,{"v":1.6e-127,"d":"1.60E-127"},"_","_","_","-"]
[null,"_","_","PTHR43356:SF3","_",2,332,0.959302,{"v":1.6e-127,"d":"1.60E-127"},"_","_","_","-"]
[]
["ACT01_04870","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR016163","CATHGENE3D","G3DSA:3.40.309.10","G3DSA:3.40.309.10",223,406,0.369697,{"v":1.4e-177,"d":"1.40E-177"},"Ald_DH_C","Homologous_superfamily","Aldehyde dehydrogenase, C-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor (GO:0016620); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR016162","CATHGENE3D","G3DSA:3.40.605.10","G3DSA:3.40.605.10",17,445,0.864646,{"v":1.4e-177,"d":"1.40E-177"},"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",10,451,0.890909,{"v":1.18e-78,"d":"1.18E-78"},"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",9,273,0.533333,{"v":6.9e-25,"d":"6.90E-25"},"Aldehyde_DH_dom","Domain","Aldehyde dehydrogenase domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR013357","TIGRFAMs","TIGR02518","EutH_ACDH",5,488,0.975758,{"v":2e-223,"d":"2.00E-223"},"Acetaldehyde_DH_acetylating","Family","Acetaldehyde dehydrogenase, acetylating","-"]
[null,"_","_","PTHR11699","_",2,487,0.979798,{"v":6.2e-174,"d":"6.20E-174"},"_","_","_","-"]
[null,"_","_","PTHR11699:SF68","_",2,487,0.979798,{"v":6.2e-174,"d":"6.20E-174"},"_","_","_","-"]
[null,"_","_","cd07122","_",14,447,0.874747,0,"_","_","_","-"]
[]
["ACT01_02465","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",134,302,0.495575,{"v":1.91e-36,"d":"1.91E-36"},"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR020843","SMART","SM00829","PKS_ER",10,336,0.961652,1.6E-7,"PKS_ER","Domain","Polyketide synthase, enoylreductase domain","Molecular Function: oxidoreductase activity (GO:0016491)"]
[null,"IPR013154","PFAM","PF08240","ADH_N",25,131,0.312684,{"v":7.3e-36,"d":"7.30E-36"},"ADH_N","Domain","Alcohol dehydrogenase, N-terminal","Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR013149","PFAM","PF00107","ADH_zinc_N",171,298,0.374631,{"v":1.3E-24,"d":"1.30E-24"},"ADH_C","Domain","Alcohol dehydrogenase, C-terminal","Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011032","SSF","SSF50129","SSF50129",1,170,0.498525,{"v":4.87e-56,"d":"4.87E-56"},"GroES-like_sf","Homologous_superfamily","GroES-like superfamily","-"]
[null,"_","_","PTHR43401","_",1,338,0.9941,{"v":6.9E-96,"d":"6.90E-96"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.720","_",146,283,0.40413,{"v":7e-103,"d":"7.00E-103"},"_","_","_","-"]
[null,"_","_","G3DSA:3.90.180.10","_",13,321,0.908555,{"v":7e-103,"d":"7.00E-103"},"_","_","_","-"]
[null,"_","_","cd08261","_",1,338,0.9941,{"v":7.36673e-155,"d":"7.37E-155"},"_","_","_","-"]
[]
["ACT01_03450","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",138,306,0.491228,{"v":7.38e-32,"d":"7.38E-32"},"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR020843","SMART","SM00829","PKS_ER",11,340,0.961988,2e-05,"PKS_ER","Domain","Polyketide synthase, enoylreductase domain","Molecular Function: oxidoreductase activity (GO:0016491)"]
[null,"IPR013154","PFAM","PF08240","ADH_N",27,134,0.312865,{"v":6.1e-33,"d":"6.10E-33"},"ADH_N","Domain","Alcohol dehydrogenase, N-terminal","Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR013149","PFAM","PF00107","ADH_zinc_N",175,301,0.368421,{"v":6.3e-19,"d":"6.30E-19"},"ADH_C","Domain","Alcohol dehydrogenase, C-terminal","Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011032","SSF","SSF50129","SSF50129",2,173,0.5,{"v":7.61e-50,"d":"7.61E-50"},"GroES-like_sf","Homologous_superfamily","GroES-like superfamily","-"]
[null,"IPR002328","PROSITE","PS00059","ADH_ZINC",60,74,0.0409357,"_","ADH_Zn_CS","Conserved_site","Alcohol dehydrogenase, zinc-type, conserved site","Molecular Function: zinc ion binding (GO:0008270); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PTHR43401","_",1,342,0.997076,{"v":4.5e-80,"d":"4.50E-80"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.720","_",152,286,0.391813,{"v":5.2e-94,"d":"5.20E-94"},"_","_","_","-"]
[null,"_","_","G3DSA:3.90.180.10","_",16,327,0.909357,{"v":5.2e-94,"d":"5.20E-94"},"_","_","_","-"]
[]
["ACT01_04805","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",2,378,0.994709,{"v":1.8e-121,"d":"1.80E-121"},"Alcohol_dehydrogenase_Fe","Family","Iron-type alcohol dehydrogenase-like","-"]
[null,"IPR018211","PROSITE","PS00913","ADH_IRON_1",159,187,0.0740741,"_","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",9,370,0.955026,{"v":8e-103,"d":"8.00E-103"},"ADH_Fe/GldA","Domain","Alcohol dehydrogenase, iron-type/glycerol dehydrogenase GldA","Molecular Function: oxidoreductase activity (GO:0016491); Molecular Function: metal ion binding (GO:0046872); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","G3DSA:3.40.50.1970","_",1,170,0.44709,{"v":9.1e-40,"d":"9.10E-40"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.1090.10","_",172,378,0.544974,{"v":5.5e-64,"d":"5.50E-64"},"_","_","_","-"]
[null,"_","_","SSF56796","_",4,378,0.989418,{"v":2.75e-104,"d":"2.75E-104"},"_","_","_","-"]
[null,"_","_","PTHR11496:SF91","_",2,378,0.994709,{"v":1.8e-121,"d":"1.80E-121"},"_","_","_","-"]
[]
["ACT01_04800","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR016163","CATHGENE3D","G3DSA:3.40.309.10","G3DSA:3.40.309.10",226,410,0.360078,{"v":7.1e-153,"d":"7.10E-153"},"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",18,448,0.841487,{"v":7.1e-153,"d":"7.10E-153"},"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",13,454,0.863014,{"v":9.95e-63,"d":"9.95E-63"},"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",12,276,0.516634,{"v":1.8e-18,"d":"1.80E-18"},"Aldehyde_DH_dom","Domain","Aldehyde dehydrogenase domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PTHR11699","_",4,498,0.966732,{"v":7.8e-159,"d":"7.80E-159"},"_","_","_","-"]
[null,"_","_","PTHR11699:SF68","_",4,498,0.966732,{"v":7.8e-159,"d":"7.80E-159"},"_","_","_","-"]
[null,"_","_","cd07122","_",17,451,0.849315,0,"_","_","_","-"]
[]
["ACT01_05115","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR018211","PROSITE","PS00913","ADH_IRON_1",151,179,0.0767123,"_","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,"IPR016205","PANTHER","PTHR43616","PTHR43616",8,362,0.969863,{"v":6.2e-117,"d":"6.20E-117"},"Glycerol_DH","Family","Glycerol dehydrogenase","Molecular Function: oxidoreductase activity, acting on CH-OH group of donors (GO:0016614); Molecular Function: metal ion binding (GO:0046872); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR016205","PIRSF","PIRSF000112","Glycerol_dehydrogenase",2,363,0.989041,{"v":2.1e-76,"d":"2.10E-76"},"Glycerol_DH","Family","Glycerol dehydrogenase","Molecular Function: oxidoreductase activity, acting on CH-OH group of donors (GO:0016614); Molecular Function: metal ion binding (GO:0046872); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001670","PFAM","PF00465","Fe-ADH",10,350,0.931507,{"v":1.2E-61,"d":"1.20E-61"},"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","_",6,160,0.421918,{"v":3.3e-40,"d":"3.30E-40"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.1090.10","_",161,365,0.558904,{"v":1e-65,"d":"1.00E-65"},"_","_","_","-"]
[null,"_","_","SSF56796","_",8,359,0.961644,{"v":5.23e-80,"d":"5.23E-80"},"_","_","_","-"]
[null,"_","_","PTHR43616:SF5","_",8,362,0.969863,{"v":6.2e-117,"d":"6.20E-117"},"_","_","_","-"]
[null,"_","_","cd08170","_",9,360,0.961644,{"v":5.56047e-156,"d":"5.56E-156"},"_","_","_","-"]
[]
["ACT01_06790","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR039697","PANTHER","PTHR11496","PTHR11496",3,385,0.992208,{"v":4.8e-87,"d":"4.80E-87"},"Alcohol_dehydrogenase_Fe","Family","Iron-type alcohol dehydrogenase-like","-"]
[null,"IPR001670","PFAM","PF00465","Fe-ADH",4,359,0.922078,{"v":1.7e-98,"d":"1.70E-98"},"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","_",186,385,0.516883,{"v":3.4e-40,"d":"3.40E-40"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1970","_",1,184,0.475325,{"v":1.1e-53,"d":"1.10E-53"},"_","_","_","-"]
[null,"_","_","SSF56796","_",2,384,0.992208,{"v":2.62e-97,"d":"2.62E-97"},"_","_","_","-"]
[null,"_","_","cd08185","_",2,381,0.984416,0,"_","_","_","-"]
[]
["ACT01_11045","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",2,361,0.991713,{"v":9e-83,"d":"9.00E-83"},"Alcohol_dehydrogenase_Fe","Family","Iron-type alcohol dehydrogenase-like","-"]
[null,"IPR001670","PFAM","PF00465","Fe-ADH",7,312,0.842541,{"v":3.2e-88,"d":"3.20E-88"},"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","_",182,361,0.494475,{"v":8e-43,"d":"8.00E-43"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1970","_",1,179,0.491713,{"v":1.5e-53,"d":"1.50E-53"},"_","_","_","-"]
[null,"_","_","SSF56796","_",1,360,0.991713,{"v":1.96e-92,"d":"1.96E-92"},"_","_","_","-"]
[]
["ACT01_07765","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR020617","PFAM","PF02803","Thiolase_C",271,394,0.309824,{"v":5.1e-43,"d":"5.10E-43"},"Thiolase_C","Domain","Thiolase, C-terminal","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020616","PFAM","PF00108","Thiolase_N",4,262,0.649874,{"v":6.3e-101,"d":"6.30E-101"},"Thiolase_N","Domain","Thiolase, N-terminal","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020615","PROSITE","PS00098","THIOLASE_1",84,102,0.0453401,"_","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,"IPR020610","PROSITE","PS00099","THIOLASE_3",377,390,0.0327456,"_","Thiolase_AS","Active_site","Thiolase, active site","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR016039","CATHGENE3D","G3DSA:3.40.47.10","G3DSA:3.40.47.10",126,393,0.672544,{"v":4.9e-156,"d":"4.90E-156"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","CATHGENE3D","G3DSA:3.40.47.10","G3DSA:3.40.47.10",6,276,0.680101,{"v":4.9e-156,"d":"4.90E-156"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",271,394,0.309824,{"v":3.23e-37,"d":"3.23E-37"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",3,270,0.672544,{"v":6.26e-92,"d":"6.26E-92"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002155","CDD","cd00751","thiolase",5,393,0.97733,0,"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":2.4E-133,"d":"2.40E-133"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR002155","TIGRFAMs","TIGR01930","AcCoA-C-Actrans",6,393,0.974811,{"v":1.7E-147,"d":"1.70E-147"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"_","_","PTHR18919","_",2,394,0.987406,{"v":2e-158,"d":"2.00E-158"},"_","_","_","-"]
[null,"_","_","PTHR18919:SF107","_",2,394,0.987406,{"v":2e-158,"d":"2.00E-158"},"_","_","_","-"]
[]
["ACT01_10830","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR029045","SSF","SSF52096","SSF52096",1,259,0.992308,{"v":4.81e-92,"d":"4.81E-92"},"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",202,260,0.223077,{"v":4.6e-24,"d":"4.60E-24"},"Enoyl-CoA_hydra_C","Homologous_superfamily","Enoyl-CoA hydratase, C-terminal","-"]
[null,"IPR001753","PFAM","PF00378","ECH_1",11,259,0.953846,{"v":1.7E-76,"d":"1.70E-76"},"Enoyl-CoA_hydra/iso","Family","Enoyl-CoA hydratase/isomerase","Molecular Function: catalytic activity (GO:0003824)"]
[null,"_","_","G3DSA:3.90.226.10","_",1,201,0.769231,{"v":7.5e-75,"d":"7.50E-75"},"_","_","_","-"]
[null,"_","_","cd06558","_",6,199,0.742308,{"v":5.54776e-81,"d":"5.55E-81"},"_","_","_","-"]
[null,"_","_","PTHR11941","_",9,259,0.961538,{"v":1.6e-85,"d":"1.60E-85"},"_","_","_","-"]
[null,"_","_","PTHR11941:SF140","_",9,259,0.961538,{"v":1.6e-85,"d":"1.60E-85"},"_","_","_","-"]
[]
["ACT01_10835","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036291","SSF","SSF51735","SSF51735",1,186,0.649123,1.72E-57,"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR022694","PIRSF","PIRSF000105","HCDH",1,285,0.996491,{"v":1.3e-86,"d":"1.30E-86"},"3-OHacyl-CoA_DH","Family","3-hydroxyacyl-CoA dehydrogenase","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Biological Process: oxidation-reduction process (GO:0055114); Molecular Function: NAD+ binding (GO:0070403)"]
[null,"IPR013328","CATHGENE3D","G3DSA:1.10.1040.10","G3DSA:1.10.1040.10",194,279,0.298246,{"v":5.9E-36,"d":"5.90E-36"},"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",186,285,0.347368,{"v":4.17e-35,"d":"4.17E-35"},"6-PGluconate_DH-like_C_sf","Homologous_superfamily","6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily","Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006180","PROSITE","PS00067","3HCDH",184,209,0.0877193,"_","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",4,184,0.631579,{"v":4.9e-62,"d":"4.90E-62"},"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",187,283,0.336842,{"v":2.1E-35,"d":"2.10E-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","_",1,189,0.659649,{"v":6.6e-68,"d":"6.60E-68"},"_","_","_","-"]
[null,"_","_","PTHR43145","_",3,284,0.985965,{"v":3.7e-123,"d":"3.70E-123"},"_","_","_","-"]
[null,"_","_","PTHR43145:SF8","_",3,284,0.985965,{"v":3.7e-123,"d":"3.70E-123"},"_","_","_","-"]
[]
["ACT01_12410","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036291","SSF","SSF51735","SSF51735",3,185,0.587097,7.11E-44,"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR022694","PIRSF","PIRSF000105","HCDH",1,309,0.993548,{"v":1e-77,"d":"1.00E-77"},"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",192,309,0.377419,{"v":2.5e-33,"d":"2.50E-33"},"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",188,301,0.364516,{"v":1.28e-22,"d":"1.28E-22"},"6-PGluconate_DH-like_C_sf","Homologous_superfamily","6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily","Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006176","PFAM","PF02737","3HCDH_N",8,186,0.574194,{"v":6.8e-54,"d":"6.80E-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",189,287,0.316129,{"v":5.1E-21,"d":"5.10E-21"},"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","_",5,191,0.6,{"v":1.3E-56,"d":"1.30E-56"},"_","_","_","-"]
[null,"_","_","PTHR43145","_",6,292,0.922581,{"v":6.7e-86,"d":"6.70E-86"},"_","_","_","-"]
[null,"_","_","PTHR43145:SF4","_",6,292,0.922581,{"v":6.7e-86,"d":"6.70E-86"},"_","_","_","-"]
[]
["ACT01_02995","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR029069","SSF","SSF54637","SSF54637",7,136,0.934783,1.28E-36,"HotDog_dom_sf","Homologous_superfamily","HotDog domain superfamily","-"]
[null,"IPR002539","PFAM","PF01575","MaoC_dehydratas",19,111,0.666667,{"v":7.5e-22,"d":"7.50E-22"},"MaoC-like_dom","Domain","MaoC-like dehydratase domain","-"]
[null,"_","_","PTHR43437","_",5,136,0.949275,{"v":6.8e-30,"d":"6.80E-30"},"_","_","_","-"]
[null,"_","_","PTHR43437:SF5","_",5,136,0.949275,{"v":6.8e-30,"d":"6.80E-30"},"_","_","_","-"]
[null,"_","_","G3DSA:3.10.129.10","_",3,137,0.971014,{"v":2.8e-39,"d":"2.80E-39"},"_","_","_","-"]
[null,"_","_","cd03449","_",11,136,0.905797,{"v":1.88937e-54,"d":"1.89E-54"},"_","_","_","-"]
[]
["ACT01_00280","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",1,117,0.306069,{"v":7.7e-35,"d":"7.70E-35"},"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",228,376,0.390501,{"v":1.93e-57,"d":"1.93E-57"},"AcylCo_DH-like_C","Homologous_superfamily","Acyl-CoA dehydrogenase-like, C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR013786","PFAM","PF02771","Acyl-CoA_dh_N",6,109,0.271768,{"v":2.2e-27,"d":"2.20E-27"},"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",1,240,0.630607,{"v":2.36e-75,"d":"2.36E-75"},"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",229,376,0.387863,{"v":3.6e-47,"d":"3.60E-47"},"AcylCo_DH/oxidase_C","Domain","Acyl-CoA dehydrogenase/oxidase C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006091","PFAM","PF02770","Acyl-CoA_dh_M",120,217,0.255937,{"v":2.4e-28,"d":"2.40E-28"},"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",336,355,0.0501319,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PIRSF016578","_",4,368,0.960422,{"v":1.1E-20,"d":"1.10E-20"},"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",119,234,0.30343,{"v":1E-42,"d":"1.00E-42"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",235,379,0.379947,{"v":1E-56,"d":"1.00E-56"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",2,378,0.992084,{"v":1.3e-139,"d":"1.30E-139"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",2,378,0.992084,{"v":1.3e-139,"d":"1.30E-139"},"_","_","_","-"]
[]
["ACT01_02990","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":1.1E-41,"d":"1.10E-41"},"AcylCoA_DH/ox_N_sf","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR036250","SSF","SSF47203","SSF47203",227,378,0.398417,{"v":4.35e-62,"d":"4.35E-62"},"AcylCo_DH-like_C","Homologous_superfamily","Acyl-CoA dehydrogenase-like, C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR013786","PFAM","PF02771","Acyl-CoA_dh_N",6,117,0.292876,{"v":9.3e-36,"d":"9.30E-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",1,242,0.635884,{"v":3.27e-89,"d":"3.27E-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":1.9e-53,"d":"1.90E-53"},"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":8.5e-27,"d":"8.50E-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","PS00073","ACYL_COA_DH_2",336,355,0.0501319,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PIRSF016578","_",4,366,0.955145,{"v":4.7E-19,"d":"4.70E-19"},"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",121,234,0.298153,{"v":6.6e-48,"d":"6.60E-48"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",235,379,0.379947,{"v":7.2E-59,"d":"7.20E-59"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",2,378,0.992084,{"v":2e-157,"d":"2.00E-157"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",2,378,0.992084,{"v":2e-157,"d":"2.00E-157"},"_","_","_","-"]
[null,"_","_","cd01158","_",7,378,0.978892,0,"_","_","_","-"]
[]
["ACT01_10950","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",1,124,0.321149,{"v":1.2E-33,"d":"1.20E-33"},"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",231,383,0.396867,1.06E-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",7,122,0.300261,{"v":7.6e-29,"d":"7.60E-29"},"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",1,246,0.639687,{"v":2.09e-82,"d":"2.09E-82"},"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",233,376,0.373368,{"v":1.3e-50,"d":"1.30E-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",126,221,0.248042,{"v":3.5E-28,"d":"3.50E-28"},"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",340,359,0.0496084,"_","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","_",7,102,0.248042,6.3E-3,"_","_","_","-"]
[null,"_","_","PIRSF016578","_",131,381,0.652741,{"v":8.8E-16,"d":"8.80E-16"},"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",125,238,0.295039,{"v":5.5e-47,"d":"5.50E-47"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",239,383,0.375979,{"v":3.1e-56,"d":"3.10E-56"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",2,382,0.992167,{"v":2e-148,"d":"2.00E-148"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",2,382,0.992167,{"v":2e-148,"d":"2.00E-148"},"_","_","_","-"]
[null,"_","_","cd01158","_",7,383,0.981723,0,"_","_","_","-"]
[]
["ACT01_11040","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",1,128,0.31592,{"v":4.9e-26,"d":"4.90E-26"},"AcylCoA_DH/ox_N_sf","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR036250","SSF","SSF47203","SSF47203",243,401,0.393035,{"v":5.32e-50,"d":"5.32E-50"},"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",7,118,0.276119,{"v":3.7e-18,"d":"3.70E-18"},"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",3,256,0.629353,{"v":4.58e-67,"d":"4.58E-67"},"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",245,395,0.373134,{"v":9.6e-44,"d":"9.60E-44"},"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",138,233,0.236318,{"v":7.3e-27,"d":"7.30E-27"},"Acyl-CoA_Oxase/DH_cen-dom","Domain","Acyl-CoA oxidase/dehydrogenase, central domain","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00073","ACYL_COA_DH_2",357,376,0.0472637,"_","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","_",137,249,0.278607,{"v":3.8e-44,"d":"3.80E-44"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",250,400,0.373134,{"v":2e-49,"d":"2.00E-49"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",3,399,0.985075,{"v":2.4E-123,"d":"2.40E-123"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",3,399,0.985075,{"v":2.4E-123,"d":"2.40E-123"},"_","_","_","-"]
[]
["ACT01_09515","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",6,172,0.497006,{"v":2.64657e-34,"d":"2.65E-34"},"ETF_alpha_N","Domain","Electron transfer flavoprotein, alpha subunit, N-terminal","-"]
[null,"IPR029035","SSF","SSF52467","SSF52467",209,327,0.353293,{"v":6.27e-43,"d":"6.27E-43"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR018206","PROSITE","PS00696","ETF_ALPHA",272,298,0.0778443,"_","ETF_asu_C_CS","Conserved_site","Electron transfer flavoprotein subunit alpha, conserved site","-"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",210,291,0.242515,{"v":4e-30,"d":"4.00E-30"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",7,182,0.523952,{"v":3.1E-33,"d":"3.10E-33"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",7,194,0.55988,{"v":7.9e-25,"d":"7.90E-25"},"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",1,190,0.565868,{"v":5.3e-52,"d":"5.30E-52"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR001308","PIRSF","PIRSF000089","Electra_flavoP_a",3,333,0.988024,{"v":7.3e-91,"d":"7.30E-91"},"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","_",6,183,0.52994,{"v":3.84e-40,"d":"3.84E-40"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1220","_",204,334,0.389222,{"v":4.8e-49,"d":"4.80E-49"},"_","_","_","-"]
[null,"_","_","PTHR43153","_",2,332,0.988024,{"v":3e-100,"d":"3.00E-100"},"_","_","_","-"]
[null,"_","_","PTHR43153:SF9","_",2,332,0.988024,{"v":3e-100,"d":"3.00E-100"},"_","_","_","-"]
[]
["ACT01_09520","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033948","CDD","cd01714","ETF_beta",2,203,0.770115,{"v":5.98661e-77,"d":"5.99E-77"},"ETF_beta_N","Domain","Electron transfer flavoprotein, beta subunit, N-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",25,207,0.697318,{"v":5.1e-45,"d":"5.10E-45"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",22,212,0.727969,{"v":1e-49,"d":"1.00E-49"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014729","CATHGENE3D","G3DSA:3.40.50.620","G3DSA:3.40.50.620",1,261,0.996169,{"v":1.3E-87,"d":"1.30E-87"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR012255","PANTHER","PTHR21294","PTHR21294",1,260,0.992337,{"v":1.6e-82,"d":"1.60E-82"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"IPR012255","PIRSF","PIRSF000090","Beta-ETF",1,261,0.996169,{"v":5.1e-79,"d":"5.10E-79"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"_","_","SSF52402","_",1,251,0.957854,{"v":1.47e-69,"d":"1.47E-69"},"_","_","_","-"]
[null,"_","_","PTHR21294:SF17","_",1,260,0.992337,{"v":1.6e-82,"d":"1.60E-82"},"_","_","_","-"]
[]
["ACT01_10940","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033947","CDD","cd01715","ETF_alpha",8,185,0.528358,{"v":3.2441e-58,"d":"3.24E-58"},"ETF_alpha_N","Domain","Electron transfer flavoprotein, alpha subunit, N-terminal","-"]
[null,"IPR029035","SSF","SSF52467","SSF52467",209,329,0.358209,{"v":9.81e-46,"d":"9.81E-46"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR018206","PROSITE","PS00696","ETF_ALPHA",274,300,0.0776119,"_","ETF_asu_C_CS","Conserved_site","Electron transfer flavoprotein subunit alpha, conserved site","-"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",210,293,0.247761,{"v":2.3e-34,"d":"2.30E-34"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",11,187,0.525373,{"v":6.1e-48,"d":"6.10E-48"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",9,198,0.564179,{"v":4.2e-49,"d":"4.20E-49"},"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",5,204,0.59403,{"v":7.8e-77,"d":"7.80E-77"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR001308","PIRSF","PIRSF000089","Electra_flavoP_a",5,335,0.985075,{"v":4.3e-123,"d":"4.30E-123"},"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","_",205,335,0.38806,{"v":3.2e-56,"d":"3.20E-56"},"_","_","_","-"]
[null,"_","_","SSF52402","_",7,203,0.585075,{"v":6.63e-58,"d":"6.63E-58"},"_","_","_","-"]
[null,"_","_","PTHR43153","_",1,334,0.99403,{"v":2.9e-137,"d":"2.90E-137"},"_","_","_","-"]
[null,"_","_","PTHR43153:SF9","_",1,334,0.99403,{"v":2.9e-137,"d":"2.90E-137"},"_","_","_","-"]
[]
["ACT01_10945","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",2,212,0.774908,{"v":2.48794e-91,"d":"2.49E-91"},"ETF_beta_N","Domain","Electron transfer flavoprotein, beta subunit, N-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",24,215,0.704797,{"v":8.2e-51,"d":"8.20E-51"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",22,220,0.730627,{"v":1.8E-58,"d":"1.80E-58"},"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",1,271,0.99631,{"v":1.9e-95,"d":"1.90E-95"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR012255","PANTHER","PTHR21294","PTHR21294",1,270,0.99262,{"v":1.4E-95,"d":"1.40E-95"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"IPR012255","PIRSF","PIRSF000090","Beta-ETF",1,271,0.99631,{"v":5.2e-97,"d":"5.20E-97"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"_","_","SSF52402","_",1,266,0.97786,{"v":7.67e-79,"d":"7.67E-79"},"_","_","_","-"]
[null,"_","_","PTHR21294:SF17","_",1,270,0.99262,{"v":1.4E-95,"d":"1.40E-95"},"_","_","_","-"]
[]
["ACT01_02540","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR038460","CATHGENE3D","G3DSA:3.40.1080.20","G3DSA:3.40.1080.20",295,445,0.337079,{"v":6.8e-55,"d":"6.80E-55"},"AcetylCoA_hyd_C_sf","Homologous_superfamily","Acetyl-CoA hydrolase/transferase, C-terminal domain superfamily","-"]
[null,"IPR037171","SSF","SSF100950","SSF100950",5,225,0.494382,{"v":5.44e-36,"d":"5.44E-36"},"NagB/RpiA_transferase-like","Homologous_superfamily","NagB/RpiA transferase-like","-"]
[null,"IPR037171","SSF","SSF100950","SSF100950",190,440,0.561798,{"v":4.77e-57,"d":"4.77E-57"},"NagB/RpiA_transferase-like","Homologous_superfamily","NagB/RpiA transferase-like","-"]
[null,"IPR026888","PFAM","PF13336","AcetylCoA_hyd_C",277,433,0.350562,{"v":3.8e-56,"d":"3.80E-56"},"AcetylCoA_hyd_C","Domain","Acetyl-CoA hydrolase/transferase C-terminal domain","-"]
[null,"IPR003702","PFAM","PF02550","AcetylCoA_hydro",7,184,0.397753,{"v":7.2e-18,"d":"7.20E-18"},"ActCoA_hydro","Family","Acetyl-CoA hydrolase/transferase","Molecular Function: catalytic activity (GO:0003824); Biological Process: acetyl-CoA metabolic process (GO:0006084)"]
[null,"_","_","G3DSA:3.30.750.70","_",189,292,0.231461,{"v":6.2e-33,"d":"6.20E-33"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.1080.10","_",2,186,0.413483,{"v":5.7e-54,"d":"5.70E-54"},"_","_","_","-"]
[null,"_","_","PTHR21432","_",3,434,0.968539,{"v":1.7E-108,"d":"1.70E-108"},"_","_","_","-"]
[]
["ACT01_02765","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR038460","CATHGENE3D","G3DSA:3.40.1080.20","G3DSA:3.40.1080.20",300,451,0.334071,{"v":6.7E-58,"d":"6.70E-58"},"AcetylCoA_hyd_C_sf","Homologous_superfamily","Acetyl-CoA hydrolase/transferase, C-terminal domain superfamily","-"]
[null,"IPR037171","SSF","SSF100950","SSF100950",8,231,0.493363,{"v":5.23e-35,"d":"5.23E-35"},"NagB/RpiA_transferase-like","Homologous_superfamily","NagB/RpiA transferase-like","-"]
[null,"IPR037171","SSF","SSF100950","SSF100950",195,447,0.557522,{"v":2.79e-59,"d":"2.79E-59"},"NagB/RpiA_transferase-like","Homologous_superfamily","NagB/RpiA transferase-like","-"]
[null,"IPR026888","PFAM","PF13336","AcetylCoA_hyd_C",282,438,0.345133,{"v":2.8e-59,"d":"2.80E-59"},"AcetylCoA_hyd_C","Domain","Acetyl-CoA hydrolase/transferase C-terminal domain","-"]
[null,"IPR003702","PFAM","PF02550","AcetylCoA_hydro",9,196,0.413717,{"v":3.2e-17,"d":"3.20E-17"},"ActCoA_hydro","Family","Acetyl-CoA hydrolase/transferase","Molecular Function: catalytic activity (GO:0003824); Biological Process: acetyl-CoA metabolic process (GO:0006084)"]
[null,"_","_","G3DSA:3.30.750.70","_",194,297,0.227876,{"v":3.1E-31,"d":"3.10E-31"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.1080.10","_",3,190,0.413717,{"v":1.6E-47,"d":"1.60E-47"},"_","_","_","-"]
[null,"_","_","PTHR21432","_",4,441,0.966814,{"v":2.7E-107,"d":"2.70E-107"},"_","_","_","-"]
[]
["ACT01_03685","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR038460","CATHGENE3D","G3DSA:3.40.1080.20","G3DSA:3.40.1080.20",295,444,0.334831,{"v":2E-52,"d":"2.00E-52"},"AcetylCoA_hyd_C_sf","Homologous_superfamily","Acetyl-CoA hydrolase/transferase, C-terminal domain superfamily","-"]
[null,"IPR037171","SSF","SSF100950","SSF100950",5,225,0.494382,1.44E-37,"NagB/RpiA_transferase-like","Homologous_superfamily","NagB/RpiA transferase-like","-"]
[null,"IPR037171","SSF","SSF100950","SSF100950",190,442,0.566292,{"v":2.16e-58,"d":"2.16E-58"},"NagB/RpiA_transferase-like","Homologous_superfamily","NagB/RpiA transferase-like","-"]
[null,"IPR026888","PFAM","PF13336","AcetylCoA_hyd_C",277,433,0.350562,{"v":5.5e-53,"d":"5.50E-53"},"AcetylCoA_hyd_C","Domain","Acetyl-CoA hydrolase/transferase C-terminal domain","-"]
[null,"IPR003702","PFAM","PF02550","AcetylCoA_hydro",3,185,0.408989,{"v":3.5e-18,"d":"3.50E-18"},"ActCoA_hydro","Family","Acetyl-CoA hydrolase/transferase","Molecular Function: catalytic activity (GO:0003824); Biological Process: acetyl-CoA metabolic process (GO:0006084)"]
[null,"_","_","G3DSA:3.30.750.70","_",189,292,0.231461,{"v":4.1e-30,"d":"4.10E-30"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.1080.10","_",1,186,0.41573,{"v":4.6e-55,"d":"4.60E-55"},"_","_","_","-"]
[null,"_","_","PTHR21432","_",5,434,0.964045,{"v":3.6e-107,"d":"3.60E-107"},"_","_","_","-"]
[null,"_","_","PTHR21432:SF19","_",5,434,0.964045,{"v":3.6e-107,"d":"3.60E-107"},"_","_","_","-"]
[]
["ACT01_04510","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037225","CATHGENE3D","G3DSA:3.40.50.11540","G3DSA:3.40.50.11540",134,284,0.332594,3.7e-11,"Nuo51_FMN-bd_sf","Homologous_superfamily","NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily","-"]
[null,"IPR037225","SSF","SSF142019","SSF142019",85,293,0.461197,{"v":3.79e-58,"d":"3.79E-58"},"Nuo51_FMN-bd_sf","Homologous_superfamily","NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily","-"]
[null,"IPR026902","PFAM","PF13375","RnfC_N",7,104,0.215078,{"v":9.8e-33,"d":"9.80E-33"},"RnfC_N","Domain","RnfC Barrel sandwich hybrid domain","-"]
[null,"IPR019554","PFAM","PF10531","SLBB",288,335,0.104213,1.9E-12,"Soluble_ligand-bd","Domain","Soluble ligand binding domain","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",406,417,0.0243902,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",367,378,0.0243902,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF12800","Fer4_4",405,418,0.0288248,0.0032,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PFAM","PF00037","Fer4",366,381,0.0332594,1.1E-4,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",357,387,0.0665189,9.054,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",397,428,0.0687361,7.483,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011538","PFAM","PF01512","Complex1_51K",129,274,0.321508,{"v":3e-47,"d":"3.00E-47"},"Nuo51_FMN-bd","Domain","NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain","-"]
[null,"IPR010208","HAMAP","MF_00461","RsxC_RnfC",1,451,0.997783,144.466,"Ion_transpt_RnfC/RsxC","Family","Ion-translocating oxidoreductase complex, subunit RnfC/RsxC","Molecular Function: electron transfer activity (GO:0009055); Cellular Component: membrane (GO:0016020); Molecular Function: 4 iron, 4 sulfur cluster binding (GO:0051539)"]
[null,"IPR010208","PANTHER","PTHR43034","PTHR43034",1,447,0.988914,{"v":2.4E-156,"d":"2.40E-156"},"Ion_transpt_RnfC/RsxC","Family","Ion-translocating oxidoreductase complex, subunit RnfC/RsxC","Molecular Function: electron transfer activity (GO:0009055); Cellular Component: membrane (GO:0016020); Molecular Function: 4 iron, 4 sulfur cluster binding (GO:0051539)"]
[null,"IPR010208","TIGRFAMs","TIGR01945","rnfC",7,435,0.949002,{"v":5.2e-160,"d":"5.20E-160"},"Ion_transpt_RnfC/RsxC","Family","Ion-translocating oxidoreductase complex, subunit RnfC/RsxC","Molecular Function: electron transfer activity (GO:0009055); Cellular Component: membrane (GO:0016020); Molecular Function: 4 iron, 4 sulfur cluster binding (GO:0051539)"]
[null,"IPR009051","SSF","SSF46548","SSF46548",321,432,0.24612,{"v":1.57e-16,"d":"1.57E-16"},"Helical_ferredxn","Homologous_superfamily","Alpha-helical ferredoxin","Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"_","_","G3DSA:3.30.70.20","_",363,421,0.128603,4.4e-07,"_","_","_","-"]
[]
["ACT01_04515","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR011303","HAMAP","MF_00462","RsxD_RnfD",22,339,0.918841,24.648,"RnfD","Family","Ion-translocating oxidoreductase complex Rnf, subunit D","Cellular Component: integral component of membrane (GO:0016021); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR011303","PANTHER","PTHR30578:SF0","PTHR30578:SF0",21,342,0.930435,{"v":1.2e-103,"d":"1.20E-103"},"RnfD","Family","Ion-translocating oxidoreductase complex Rnf, subunit D","Cellular Component: integral component of membrane (GO:0016021); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR011303","TIGRFAMs","TIGR01946","rnfD",27,338,0.901449,{"v":2.1e-98,"d":"2.10E-98"},"RnfD","Family","Ion-translocating oxidoreductase complex Rnf, subunit D","Cellular Component: integral component of membrane (GO:0016021); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR004338","PANTHER","PTHR30578","PTHR30578",21,342,0.930435,{"v":1.2e-103,"d":"1.20E-103"},"NqrB/RnfD","Family","Ion-translocating oxidoreductase NqrB/RnfD","Cellular Component: membrane (GO:0016020); Biological Process: transmembrane transport (GO:0055085)"]
[null,"IPR004338","PFAM","PF03116","NQR2_RnfD_RnfE",23,337,0.910145,{"v":1.2e-109,"d":"1.20E-109"},"NqrB/RnfD","Family","Ion-translocating oxidoreductase NqrB/RnfD","Cellular Component: membrane (GO:0016020); Biological Process: transmembrane transport (GO:0055085)"]
[]
["ACT01_04520","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR010209","HAMAP","MF_00479","RsxG_RnfG",6,178,0.945055,19.982,"Ion_transpt_RnfG/RsxG","Family","Ion-translocating oxidoreductase complex, subunit RnfG/RsxG","Cellular Component: plasma membrane (GO:0005886); Molecular Function: electron transfer activity (GO:0009055); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR010209","PANTHER","PTHR36118","PTHR36118",8,177,0.928571,{"v":7.4e-35,"d":"7.40E-35"},"Ion_transpt_RnfG/RsxG","Family","Ion-translocating oxidoreductase complex, subunit RnfG/RsxG","Cellular Component: plasma membrane (GO:0005886); Molecular Function: electron transfer activity (GO:0009055); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR010209","PIRSF","PIRSF006091","E_trnsport_RnfG",1,181,0.989011,{"v":5.7e-33,"d":"5.70E-33"},"Ion_transpt_RnfG/RsxG","Family","Ion-translocating oxidoreductase complex, subunit RnfG/RsxG","Cellular Component: plasma membrane (GO:0005886); Molecular Function: electron transfer activity (GO:0009055); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR010209","TIGRFAMs","TIGR01947","rnfG",15,175,0.879121,{"v":1.3E-31,"d":"1.30E-31"},"Ion_transpt_RnfG/RsxG","Family","Ion-translocating oxidoreductase complex, subunit RnfG/RsxG","Cellular Component: plasma membrane (GO:0005886); Molecular Function: electron transfer activity (GO:0009055); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR007329","PFAM","PF04205","FMN_bind",88,173,0.467033,{"v":1.1e-19,"d":"1.10E-19"},"FMN-bd","Domain","FMN-binding","Molecular Function: FMN binding (GO:0010181); Cellular Component: membrane (GO:0016020)"]
[null,"IPR007329","SMART","SM00900","FMN_bind",88,176,0.483516,{"v":6.9e-27,"d":"6.90E-27"},"FMN-bd","Domain","FMN-binding","Molecular Function: FMN binding (GO:0010181); Cellular Component: membrane (GO:0016020)"]
[null,"_","_","PS51257","_",1,25,0.131868,5,"_","_","_","-"]
[]
["ACT01_04525","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR010968","HAMAP","MF_00478","RsxE_RnfE",1,196,0.942029,23.522,"RnfE","Family","Ion-translocating oxidoreductase complex subunit E","Cellular Component: membrane (GO:0016020); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR010968","TIGRFAMs","TIGR01948","rnfE",5,193,0.908213,{"v":2e-67,"d":"2.00E-67"},"RnfE","Family","Ion-translocating oxidoreductase complex subunit E","Cellular Component: membrane (GO:0016020); Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR003667","PFAM","PF02508","Rnf-Nqr",4,186,0.879227,{"v":1.3E-58,"d":"1.30E-58"},"NqrDE/RnfAE","Family","NqrDE/RnfAE","Cellular Component: membrane (GO:0016020)"]
[null,"IPR003667","PIRSF","PIRSF006102","NQR_DE",1,204,0.980676,{"v":4.6e-67,"d":"4.60E-67"},"NqrDE/RnfAE","Family","NqrDE/RnfAE","Cellular Component: membrane (GO:0016020)"]
[null,"_","_","PTHR30586","_",4,199,0.942029,{"v":1.2E-67,"d":"1.20E-67"},"_","_","_","-"]
[]
["ACT01_04530","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR011293","HAMAP","MF_00459","RsxA_RnfA",2,191,0.989529,24.036,"Ion_transpt_RnfA/RsxA","Family","Ion-translocating oxidoreductase complex, subunit  RnfA/RsxA","Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR011293","TIGRFAMs","TIGR01943","rnfA",4,191,0.979058,{"v":1.4e-74,"d":"1.40E-74"},"Ion_transpt_RnfA/RsxA","Family","Ion-translocating oxidoreductase complex, subunit  RnfA/RsxA","Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR003667","PFAM","PF02508","Rnf-Nqr",4,191,0.979058,{"v":1.5E-52,"d":"1.50E-52"},"NqrDE/RnfAE","Family","NqrDE/RnfAE","Cellular Component: membrane (GO:0016020)"]
[null,"IPR003667","PIRSF","PIRSF006102","NQR_DE",1,191,0.994764,{"v":3.1e-50,"d":"3.10E-50"},"NqrDE/RnfAE","Family","NqrDE/RnfAE","Cellular Component: membrane (GO:0016020)"]
[null,"_","_","PTHR30335","_",1,191,0.994764,{"v":1.2e-74,"d":"1.20E-74"},"_","_","_","-"]
[null,"_","_","PTHR30335:SF0","_",1,191,0.994764,{"v":1.2e-74,"d":"1.20E-74"},"_","_","_","-"]
[]
["ACT01_04535","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",175,186,0.0383275,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF00037","Fer4",168,191,0.0801394,1.8E-7,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",166,195,0.101045,10.969,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",243,275,0.111498,8.281,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",136,165,0.101045,8.105,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",209,240,0.108014,6.685,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011005","CATHGENE3D","G3DSA:3.20.20.20","G3DSA:3.20.20.20",40,136,0.334495,1.2e-07,"Dihydropteroate_synth-like","Homologous_superfamily","Dihydropteroate synthase-like","Biological Process: cellular metabolic process (GO:0044237)"]
[null,"IPR010207","HAMAP","MF_00463","RsxB_RnfB",7,197,0.662021,27.941,"Elect_transpt_cplx_RnfB/RsxB","Family","Ion-translocating oxidoreductase complex, RnfB/RsxB","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"IPR010207","TIGRFAMs","TIGR01944","rnfB",6,100,0.327526,{"v":2e-21,"d":"2.00E-21"},"Elect_transpt_cplx_RnfB/RsxB","Family","Ion-translocating oxidoreductase complex, RnfB/RsxB","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"IPR007202","PFAM","PF04060","FeS",47,80,0.114983,4.8E-10,"4Fe-4S_dom","Domain","4Fe-4S domain","Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"IPR007202","PROFILE","PS51656","4FE4S",35,95,0.209059,23.614,"4Fe-4S_dom","Domain","4Fe-4S domain","Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"_","_","G3DSA:3.30.70.20","_",212,280,0.236934,5.1e-07,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",137,197,0.209059,4.3E-14,"_","_","_","-"]
[null,"_","_","SSF54862","_",143,269,0.439024,1.7E-14,"_","_","_","-"]
[null,"_","_","cd10549","_",138,269,0.456446,{"v":2.90862E-21,"d":"2.91E-21"},"_","_","_","-"]
[null,"_","_","PTHR43560","_",7,269,0.912892,{"v":4.3E-50,"d":"4.30E-50"},"_","_","_","-"]

{"sheet":"Sheet1","index":13,"n_rows":0,"n_cols":0,"rows_kept":0,"hidden":true}

{"sheet":"PSortB","index":14,"n_rows":48,"n_cols":4,"rows_kept":48}
["CDS","PsortB Localization","Score","Gram"]
["ACT01_13720","Cytoplasmic",7.5,"+"]
["ACT01_13730","CytoplasmicMembrane",10,"+"]
["ACT01_00410","Cytoplasmic",9.97,"+"]
["ACT01_04310","Cytoplasmic",7.5,"+"]
["ACT01_03310","Unknown",2.5,"+"]
["ACT01_03315","Cytoplasmic",7.5,"+"]
["ACT01_03320","Cytoplasmic",7.5,"+"]
["ACT01_03325","Unknown",2.5,"+"]
["ACT01_00445","Unknown",2.5,"+"]
["ACT01_00545","Unknown",2.5,"+"]
["ACT01_02090","Unknown",2.5,"+"]
["ACT01_02810","Unknown",2.5,"+"]
["ACT01_03520","Unknown",2.5,"+"]
["ACT01_06665","Cytoplasmic",7.5,"+"]
["ACT01_12570","Cytoplasmic",7.5,"+"]
["ACT01_05435","Cytoplasmic",9.97,"+"]
["ACT01_13325","Cytoplasmic",7.5,"+"]
["ACT01_04870","Cytoplasmic",7.5,"+"]
["ACT01_02465","Cytoplasmic",9.97,"+"]
["ACT01_03450","Cytoplasmic",9.97,"+"]
["ACT01_04805","Cytoplasmic",9.97,"+"]
["ACT01_04800","Cytoplasmic",7.5,"+"]
["ACT01_05115","Cytoplasmic",9.97,"+"]
["ACT01_06790","Cytoplasmic",9.97,"+"]
["ACT01_11045","Cytoplasmic",9.97,"+"]
["ACT01_07765","Cytoplasmic",9.97,"+"]
["ACT01_10830","Cytoplasmic",7.5,"+"]
["ACT01_10835","Cytoplasmic",7.5,"+"]
["ACT01_12410","Cytoplasmic",7.5,"+"]
["ACT01_02995","Cytoplasmic",7.5,"+"]
["ACT01_00280","Cytoplasmic",9.97,"+"]
["ACT01_02990","Cytoplasmic",9.97,"+"]
["ACT01_10950","Cytoplasmic",9.97,"+"]
["ACT01_11040","Cytoplasmic",9.97,"+"]
["ACT01_09515","Cytoplasmic",7.5,"+"]
["ACT01_09520","Cytoplasmic",7.5,"+"]
["ACT01_10940","Cytoplasmic",7.5,"+"]
["ACT01_10945","Cytoplasmic",7.5,"+"]
["ACT01_02540","Cytoplasmic",7.5,"+"]
["ACT01_02765","Unknown",2.5,"+"]
["ACT01_03685","Cytoplasmic",7.5,"+"]
["ACT01_04510","Cytoplasmic",7.5,"+"]
["ACT01_04515","CytoplasmicMembrane",10,"+"]
["ACT01_04520","Unknown",3.33,"+"]
["ACT01_04525","CytoplasmicMembrane",10,"+"]
["ACT01_04530","CytoplasmicMembrane",10,"+"]
["ACT01_04535","Cytoplasmic",9.97,"+"]