{"text_format":"3","workbook":"xlsx","n_sheets":14,"sheets":["reactions","instruction","start","gene features","protein features","MaGe-Curated annotations","SwissProt","UniFIRE ","PRIAM EC number","COG","EGGNOG","FigFam","InterProScan","PSortB"],"not_rendered":{"defined_names":1},"read":"whole","date_system":"1900"}

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

{"sheet":"instruction","index":1,"n_rows":14,"n_cols":2,"rows_kept":14,"merged":[[0,0,0,1]]}
["Additional file 8. Functional annotations of strain Megasphaera elsdenii 14-14"]
["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":38,"n_cols":13,"rows_kept":38}
["CDS","Strand","length","Begin","End","AMIGene Start","AMIGene Lpcod","AMIGene Apcod","Matrix","Prodigal Begin","Prodigal End","Glimmer Begin","Glimmer End"]
["AZ49_00320","R",1284,68255,69562,69562,0.953022,0.953022,1,68255,69538,68255,69538]
["AZ49_00330","R",1566,71585,73183,72958,0.860512,0.988403,1,71585,73132,71585,73003]
["AZ49_04210","D",1521,897578,899098,897578,0.944394,0.944394,1,897578,899098,897578,899098]
["AZ49_00515","R",996,115641,116711,116627,0.898542,0.975243,1,115641,116636,115641,116627]
["AZ49_11470","R",957,2401201,2402157,2402157,0.956509,0.956509,1,2401201,2402157,2401201,2402157]
["AZ49_01710","R",3513,356796,360308,360308,0.976397,0.976397,1,356796,360308,356796,360308]
["AZ49_05490","D",3531,1178774,1182409,1178774,0.959421,0.959421,1,1178879,1182409,1178879,1182409]
["AZ49_06970","D",3516,1481217,1484975,1481562,0.874066,0.951269,1,1481460,1484975,1481460,1484975]
["AZ49_06950","D",1197,1477718,1478914,1477718,0.968603,0.968603,1,1477718,1478914,1477718,1478914]
["AZ49AM_0981","D",756,1062156,1062926,1062156,0.832101,0.832101,2,1062171,1062926,1062156,1062926]
["AZ49_00050","R",1098,14876,16018,16018,0.935633,0.935633,1,14876,15973,14876,15973]
["AZ49_02525","R",1170,531810,533012,533012,0.923226,0.923226,1,531810,532979,531810,532979]
["AZ49_03535","D",2691,759104,761794,759104,0.95945,0.95945,1,759104,761794,759104,761794]
["AZ49_05685","R",1182,1213468,1214658,1214658,0.898635,0.898635,1,1213468,1214649,1213468,1214649]
["AZ49_05690","R",1185,1214853,1216196,1216037,0.805526,0.895968,2,1214853,1216037,1214853,1216037]
["AZ49_10655","R",855,2239932,2240786,2240786,0.95933,0.95933,1,2239932,2240786,2239932,2240786]
["AZ49_00555","R",795,129635,130429,130429,0.954939,0.954939,1,129635,130429,129635,130429]
["AZ49_00545","R",663,128202,129068,128840,0.68497,0.930514,1,128202,128840,128202,128864]
["AZ49_00550","R",738,128869,129615,129543,0.835129,0.914309,1,128869,129606,128869,129606]
["AZ49_02170","R",417,462552,462968,462968,0.831462,0.831462,2,462552,462968,462552,462968]
["AZ49_02175","R",1542,462995,464545,464545,0.943908,0.943908,2,462995,464536,462995,464536]
["AZ49_00650","R",1161,149494,150741,150642,0.904001,0.974284,1,149494,150654,149494,150654]
["AZ49_02755","R",1149,586996,588144,588144,0.977347,0.977347,1,586996,588144,586996,588144]
["AZ49_02760","R",783,588268,589050,589050,0.967782,0.967782,1,588268,589050,588268,589050]
["AZ49_04240","D",1149,905707,906855,905707,0.979975,0.979975,1,905707,906855,905707,906855]
["AZ49_06245","D",1140,1315202,1316341,1315202,0.960952,0.960952,1,1315202,1316341,1315202,1316341]
["AZ49_06555","D",1152,1382659,1383810,1382659,0.974328,0.974328,1,1382659,1383810,1382659,1383810]
["AZ49_06560","D",813,1383884,1384696,1383884,0.904902,0.904902,2,1383884,1384696,1383884,1384696]
["AZ49_06565","D",1017,1384711,1385733,1384711,0.944723,0.944723,1,1384717,1385733,1384717,1385733]
["AZ49_07320","D",783,1562923,1563705,1562923,0.95406,0.95406,2,1562923,1563705,1562923,1563705]
["AZ49_07325","D",1002,1563719,1564720,1563719,0.950187,0.950187,1,1563719,1564720,1563719,1564720]
["AZ49_01090","R",855,235264,236118,236118,0.944708,0.944708,1,235264,236118,235264,236118]
["AZ49_01095","R",576,236142,236714,236714,0.910295,0.910295,1,236142,236714,236142,236714]
["AZ49_01100","R",624,236714,237337,237220,0.725932,0.797988,1,236714,237337,236714,237337]
["AZ49_01105","R",552,237340,237891,237831,0.895186,0.975319,1,237340,237891,237340,237891]
["AZ49_01110","R",1035,237893,238927,238927,0.921778,0.921778,1,237893,238927,237893,238927]
["AZ49_01115","R",1356,238945,240303,240303,0.93492,0.93492,1,238945,240300,238945,240300]

{"sheet":"gene features","index":3,"n_rows":38,"n_cols":8,"rows_kept":38}
["CDS","GC Content","GC1 Content","GC2 Content","GC3 Content","CAI","GCskew","R/Y ratio"]
["AZ49_00320",53.66,57.71,36.68,66.59,0.73,0.077,1.061]
["AZ49_00330",53.13,51.92,43.68,63.79,0.68,0.06,0.768]
["AZ49_04210",54.44,51.68,42.6,69.03,0.69,0.094,0.748]
["AZ49_00515",63.25,66.27,43.98,79.52,0.61,0.025,0.923]
["AZ49_11470",54.75,55.17,37.3,71.79,0.72,0.034,1.036]
["AZ49_01710",54.4,56.62,40.48,66.1,0.78,0.046,1.031]
["AZ49_05490",54.23,55.14,39.76,67.8,0.74,0.087,0.998]
["AZ49_06970",51.82,58.45,40.19,56.83,0.81,0.087,0.941]
["AZ49_06950",53.63,58.9,36.59,65.41,0.83,0.087,1.008]
["AZ49AM_0981",57.28,63.89,44.44,63.49,0.52,-0.067,1.032]
["AZ49_00050",54.46,55.46,42.62,65.3,0.59,-0.077,1.033]
["AZ49_02525",54.44,57.69,39.74,65.9,0.61,0.008,1.028]
["AZ49_03535",58.53,62.21,44.59,68.78,0.62,0.008,1.045]
["AZ49_05685",52.62,62.94,42.89,52.03,0.81,-0.006,1.038]
["AZ49_05690",54.77,61.77,42.78,59.75,0.8,0.048,0.978]
["AZ49_10655",49.82,54.04,34.39,61.05,0.83,0.066,1.055]
["AZ49_00555",54.47,60.75,36.98,65.66,0.66,-0.012,1.044]
["AZ49_00545",58.37,59.28,44.34,71.49,0.59,-0.013,1.04]
["AZ49_00550",58.54,65.85,41.06,68.7,0.59,-0.056,1.164]
["AZ49_02170",41.25,51.08,36.69,35.97,0.42,-0.105,1.195]
["AZ49_02175",45.27,56.42,40.08,39.3,0.46,-0.18,1.181]
["AZ49_00650",55.47,60.72,36.69,68.99,0.74,0.009,1.084]
["AZ49_02755",51.26,58.22,39.16,56.4,0.83,0.029,1.085]
["AZ49_02760",50.32,57.47,38.7,54.79,0.8,0.035,1.044]
["AZ49_04240",50.57,58.75,39.16,53.79,0.81,0.071,1.063]
["AZ49_06245",55.09,59.47,40.79,65,0.74,0.035,1.011]
["AZ49_06555",50.26,55.73,38.28,56.77,0.79,0.033,1.043]
["AZ49_06560",49.08,61.99,36.16,49.08,0.73,0.023,1.064]
["AZ49_06565",50.15,60.18,38.05,52.21,0.79,0.023,1.022]
["AZ49_07320",57.34,63.22,44.06,64.75,0.67,-0.06,1.122]
["AZ49_07325",57.19,61.98,42.81,66.77,0.75,-2E-3,1.045]
["AZ49_01090",53.1,54.04,44.21,61.05,0.74,0.022,1.002]
["AZ49_01095",49.48,43.23,35.42,69.79,0.7,0.095,0.74]
["AZ49_01100",49.36,49.04,37.02,62.02,0.68,0.058,0.846]
["AZ49_01105",50.54,55.43,39.13,57.07,0.75,0.004,1.14]
["AZ49_01110",53.33,53.33,42.32,64.35,0.71,0.076,0.829]
["AZ49_01115",54.57,57.3,42.04,64.38,0.73,0.035,1.08]

{"sheet":"protein features","index":4,"n_rows":38,"n_cols":14,"rows_kept":38}
["CDS","Mw (Da)","Hydrophobicity","Tiny","Small","Aliphatic","Aromatic","Non Polar","Polar","Charged","Basic","Acidic","pI","Oxyphobic Index"]
["AZ49_00320",46200.34,-0.06,29.27,51.99,23.42,8.67,56.67,43.33,27.4,14.29,13.11,5.86,9.13]
["AZ49_00330",54075.92,1.15,36.66,55.85,32.44,9.6,75.43,24.57,9.02,5.18,3.84,8.84,8.32]
["AZ49_04210",53253.88,1.06,34.98,52.96,32.61,9.88,73.32,26.68,9.29,5.73,3.56,8.91,8.29]
["AZ49_00515",35666.58,0.13,32.63,54.98,23.87,10.88,64.65,35.35,22.36,11.78,10.57,5.99,9.81]
["AZ49_11470",34650.21,-0.05,30.19,53.14,22.64,11.01,57.86,42.14,25.47,12.89,12.58,5.59,9.38]
["AZ49_01710",128794.7,-0.24,31.37,51.88,17.95,12.05,57.01,42.99,25.56,12.91,12.65,5.7,9.54]
["AZ49_05490",130038.34,-0.22,30.78,51.28,19.98,12.07,55.7,44.3,25.51,13.35,12.16,5.92,9.44]
["AZ49_06970",128078.52,-0.23,31.51,53.29,18.79,11.78,57.3,42.7,25.45,12.72,12.72,5.57,9.41]
["AZ49_06950",43091.82,-0.06,29.65,53.02,23.62,8.29,57.29,42.71,26.38,13.57,12.81,5.77,9.53]
["AZ49AM_0981",26625.4,0.21,34.26,60.96,24.3,6.77,62.15,37.85,22.71,9.56,13.15,4.61,9.86]
["AZ49_00050",39220.53,0.09,34.52,56.44,22.74,9.86,58.9,41.1,21.64,10.14,11.51,5.07,9.16]
["AZ49_02525",41956.37,-0.04,32.39,52.7,20.57,10.28,58.87,41.13,23.39,11.57,11.83,5.37,9.42]
["AZ49_03535",96035,-0.08,34.38,56.92,22.32,9.15,59.26,40.74,24.89,13.17,11.72,6.15,9.74]
["AZ49_05685",40789.37,0.12,35.88,58.78,22.65,5.85,63.1,36.9,22.65,11.96,10.69,7.66,9.56]
["AZ49_05690",41596.16,0.09,34.26,56.35,23.86,5.84,60.91,39.09,22.59,11.68,10.91,6.14,9.8]
["AZ49_10655",30946.6,-0.07,28.17,51.76,23.59,8.45,57.04,42.96,27.11,14.08,13.03,6.27,8.99]
["AZ49_00555",28614.9,0.03,30.3,51.52,22.73,9.47,61.36,38.64,24.62,12.5,12.12,6.01,9.47]
["AZ49_00545",23580.12,0.16,33.64,56.82,24.55,9.55,62.27,37.73,22.27,10,12.27,4.89,9.71]
["AZ49_00550",26484.41,-0.02,30.61,50.2,24.49,8.57,60,40,26.53,13.47,13.06,5.75,9.54]
["AZ49_02170",15284.82,-0.17,29.71,52.9,23.19,10.87,51.45,48.55,27.54,15.22,12.32,6.57,9.38]
["AZ49_02175",55196.72,-0.07,31.38,53.41,22.81,9.36,58.48,41.52,23.98,11.5,12.48,5.24,9.34]
["AZ49_00650",41875.34,-0.02,31.09,51.3,22.54,10.1,59.84,40.16,24.87,12.18,12.69,5.47,9.57]
["AZ49_02755",41458.75,-0.17,32.72,51.05,19.37,9.16,57.33,42.67,25.13,12.04,13.09,5.37,9.37]
["AZ49_02760",28023.94,-0.12,31.15,54.23,21.54,7.31,57.69,42.31,25,12.31,12.69,5.63,9.96]
["AZ49_04240",41424.72,-0.15,32.72,51.05,19.63,9.16,57.33,42.67,25.13,12.04,13.09,5.38,9.32]
["AZ49_06245",40975.43,0.01,33.25,52.77,20.84,8.97,60.42,39.58,24.54,11.87,12.66,5.4,9.98]
["AZ49_06555",41406.47,-0.16,33.42,50.91,20.1,9.92,56.66,43.34,25.33,11.75,13.58,5.06,9.21]
["AZ49_06560",29084.22,-0.12,27.41,53.33,25.56,4.07,56.3,43.7,27.41,12.22,15.19,4.85,9.13]
["AZ49_06565",36163.02,0.01,30.77,53.85,24.56,8.28,60.06,39.94,26.92,12.72,14.2,5.12,9.2]
["AZ49_07320",26687.56,0.19,36.15,63.46,26.15,2.69,59.23,40.77,21.54,10.38,11.15,5.32,9.11]
["AZ49_07325",35186.93,0.08,34.53,54.35,24.32,7.81,60.96,39.04,24.32,11.41,12.91,5.13,8.81]
["AZ49_01090",29670.5,0.24,38.38,59.15,20.07,7.75,65.14,34.86,20.42,11.97,8.45,8.11,9.88]
["AZ49_01095",20845.38,1.25,30.37,48.69,35.08,13.61,73.82,26.18,8.38,4.71,3.66,7.83,8.4]
["AZ49_01100",22684.19,0.81,28.99,49.76,30.92,12.56,70.05,29.95,13.04,7.73,5.31,8.72,9.14]
["AZ49_01105",19398.72,-0.14,33.88,53.55,20.22,6.56,56.83,43.17,24.59,14.21,10.38,9.23,8.66]
["AZ49_01110",36832.14,0.69,33.72,54.65,28.2,11.63,70.35,29.65,11.92,7.27,4.65,8.85,9.09]
["AZ49_01115",48482.51,-0.05,32.59,54.99,21.29,6.65,59.87,40.13,23.5,12.86,10.64,7.94,9.77]

{"sheet":"MaGe-Curated annotations","index":5,"n_rows":1100,"n_cols":26,"rows_kept":1100}
["AZ49_00320","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","_",1.00234,1.00943,57.94,{"v":2E-175,"d":"2.00E-175"},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 ;",1,1.00708,57.85,{"v":2e-173,"d":"2.00E-173"},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":3E-157,"d":"3.00E-157"},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]
[]
["AZ49_00330","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","_",0.98656,1.01181,46.11,{"v":3E-158,"d":"3.00E-158"},1,2,"4.S.98 : lactate ;","_","11 : Membrane","_","t : transporter",10508058,"2a : Function from experimental evidences in other organisms",5,518,521,4,507,508]
[null,"CLOSTRIBL6_v1_3223",null,"Clostridiales BL-6","lctP","L-lactate permease","_",0.97313,0.98066,47.14,{"v":1E-146,"d":"1.00E-146"},1,2,"_","_","11 : Membrane","_","t : transporter",10508058,"2a : Function from experimental evidences in other organisms",10,505,521,6,504,517]
[]
["AZ49_04210","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","_","Clostridiaceae BL-3","lctP","L-lactate permease","_",0.99803,1.00198,49.7,{"v":7e-178,"d":"7.00E-178"},1,1,"4.S.98 : lactate ;","_","11 : Membrane","_","t : transporter",10508058,"2a : Function from experimental evidences in other organisms",1,506,506,5,506,508]
[null,"CLOSTRIBL6_v1_3223","_","Clostridiales BL-6","lctP","L-lactate permease","_",0.97872,1,50.4,{"v":8e-162,"d":"8.00E-162"},1,1,"_","_","11 : Membrane","_","t : transporter",10508058,"2a : Function from experimental evidences in other organisms",5,501,506,6,511,517]
[null,"ECED1_5018","_","Escherichia coli ED1a","_","L-lactate permease","_",0.96911,0.99209,43.23,{"v":1e-131,"d":"1.00E-131"},1,1,"_","_","1 : Unknown","7 : Transport and binding proteins ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,495,506,5,506,518]
[]
["AZ49_00515","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 ;",0.68116,0.85196,42.91,{"v":1e-67,"d":"1.00E-67"},1,1,"_","1.1.1.27","2 : Cytoplasmic","_","e : enzyme",18356528,"3 : Putative function from multiple computational evidences",30,307,331,120,390,414]
[]
["AZ49_11470","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 ;",0.96855,0.97468,50.32,{"v":3e-112,"d":"3.00E-112"},1,1,"_","1.1.1.27","2 : Cytoplasmic","_","e : enzyme",11889109,"2a : Function from experimental evidences in other organisms",4,309,318,2,309,316]
[null,"CD630_21640","_","Clostridium difficile 630","ldh","L-lactate dehydrogenase (L-LDH)","_",0.98447,0.99686,37.54,{"v":1E-78,"d":"1.00E-78"},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)","_",0.91202,0.97799,35.69,{"v":7e-64,"d":"7.00E-64"},1,1,"_","1.1.1.27","2 : Cytoplasmic","6.8 : Glycolysis/gluconeogenesis ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,310,318,28,338,341]
[]
["AZ49_01710","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 ;",0.58974,0.97872,57.54,0,3,2,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",1,685,1170,1,688,705]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.38974,0.97021,55.92,{"v":9E-176,"d":"9.00E-176"},2,3,"_","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 ;",0.39316,0.98501,54.13,{"v":2E-170,"d":"2.00E-170"},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",710,1163,1170,1,460,467]
[]
["AZ49_05490","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,"CLOAM0324","_","Candidatus Cloacamonas acidaminovorans Evry","_","putative pyruvate-ferredoxin oxidoreductase (por-like) or pyruvate-flavodoxin oxidoreductase (ydbK-like), 4Fe-4S domain","_",1.0068,1.00938,50.59,0,1,1,"1.7.1 : Unassigned reversible reactions ; 1.1.2.3 : Propionate degradation ; 1.3.5 : Fermentation ;","1.2.7.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,1175,1176,1,1172,1173]
[null,"Ent638_2136","_","Enterobacter sp. 638","ydbK","Putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; 4Fe-4S cluster binding protein","_",1.0068,1.00852,46.03,0,1,1,"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)",8,1174,1176,3,1165,1174]
[null,"ECK1374","_","Escherichia coli K12","ydbK","putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; 4Fe-4S cluster binding protein","PYRUFLAVREDUCT-RXN ;",1.0068,1.00852,46.28,0,1,1,"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",8,1174,1176,3,1165,1174]
[null,"Spro_2604","_","Serratia proteamaculans 568","_","Putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; 4Fe-4S cluster binding protein (NifJ)","_",1.00595,1.0068,45.35,0,1,1,"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",8,1174,1176,3,1168,1177]
[null,"AZOLI_p30297","_","Azospirillum lipoferum 4B","_","putative pyruvate-ferredoxin/flavodoxin oxidoreductase","_",1.01105,1.01451,46.59,0,1,1,"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",9,1174,1176,1,1168,1172]
[null,"BN874v1_1210009","_","Candidatus Contendobacter odensis Run_B_J11","_","putative pyruvate-flavodoxin oxidoreductase (nifJ)","_",1.00586,1.02126,45.38,0,1,1,"_","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",1,1174,1176,1,1181,1194]
[null,"FRAAL3253","_","Frankia alni ACN14a","_","Pyruvate-flavodoxin oxidoreductase","_",1.01616,1.01702,43.93,0,1,1,"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)",7,1174,1176,4,1163,1175]
[null,"SBF1_v1_1030024",null,"Desulfosporosinus sp. SbF1","pfoA_3a","fragment of pyruvate synthase (part 1/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.58418,0.97447,54.44,0,3,3,"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",6,687,1176,4,688,705]
[null,"VCA0530","_","Vibrio cholerae N16961","_","putative Pyruvate-flavodoxin oxidoreductase","_",0.94558,1.03058,38.31,0,1,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",10,1106,1176,6,1072,1079]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.38776,0.97021,58.99,0,2,2,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"2a : Function from experimental evidences in other organisms",4,458,1176,3,458,470]
[null,"SBF1_v1_1030023",null,"Desulfosporosinus sp. SbF1","pfoA_3b","fragment of pyruvate synthase (part 2/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.39796,1.00214,55.98,{"v":1E-175,"d":"1.00E-175"},5,1,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",715,1176,1176,4,463,467]
[]
["AZ49_06970","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 ;",0.99744,1,64.64,0,1,1,"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",1,1165,1171,1,1164,1168]
[null,"CD630_26820","_","Clostridium difficile 630","pfo","Pyruvate-ferredoxin oxidoreductase","_",1.00424,1.0111,59.54,0,1,1,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"1c : Function from experimental evidences in the studied genus",1,1165,1171,1,1177,1179]
[null,"SBF1_v1_1620011","_","Desulfosporosinus sp. SbF1","pfoA_2","pyruvate synthase","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.9983,1.00085,59.73,0,1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,1165,1171,1,1169,1174]
[null,"CLOSTRIBL4_v1_0841","_","Clostridiales BL-4","PFOF","Pyruvate:ferredoxin oxidoreductase","PYRUFLAVREDUCT-RXN ; RHEA:12768 ;",0.99831,1.00939,57.19,0,1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme",18631365,"2a : Function from experimental evidences in other organisms",3,1167,1171,5,1179,1184]
[null,"CLOSTRIBL6_v1_0279","_","Clostridiales BL-6","PFOF","Pyruvate:ferredoxin oxidoreductase","PYRUFLAVREDUCT-RXN ; RHEA:12768 ;",1.00084,1.01281,56.16,0,1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme","8620891, 7608066, 9495749","2a : Function from experimental evidences in other organisms",3,1167,1171,4,1184,1185]
[null,"CLOAM0324",null,"Candidatus Cloacamonas acidaminovorans Evry","_","putative pyruvate-ferredoxin oxidoreductase (por-like) or pyruvate-flavodoxin oxidoreductase (ydbK-like), 4Fe-4S domain","_",1.00256,1.00427,52.81,0,1,2,"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,"BN873v1_150048","_","Candidatus Competibacter denitrificans Run_A_D11","_","putative pyruvate-flavodoxin oxidoreductase (nifJ)","_",0.9824,1.00085,47.35,0,1,1,"_","1.2.7.-","1 : Unknown","5 : Central intermediary metabolism ; 5.6 : Nitrogen fixation ;","e : enzyme","11167002, 21317262, 8415612","3 : Putative function from multiple computational evidences",3,1147,1171,5,1162,1193]
[null,"BN11v3_340013","_","Tetrasphaera australiensis Ben110","_","putative pyruvate-flavodoxin oxidoreductase","_",0.9891,1.00769,46.86,0,1,1,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",8352652,"3 : Putative function from multiple computational evidences",6,1162,1171,8,1174,1193]
[null,"SBF1_v1_1030024",null,"Desulfosporosinus sp. SbF1","pfoA_3a","fragment of pyruvate synthase (part 1/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.58753,0.97589,61.05,0,3,1,"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",1,683,1171,1,688,705]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.39197,0.9766,64.49,0,2,1,"_","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 ;",0.39453,0.98929,54.98,{"v":2e-164,"d":"2.00E-164"},4,3,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",710,1165,1171,3,460,467]
[null,"NBG4_v1_230036","_","Candidatus Sulfobium mesophilum","nifJ","Pyruvate:ferredoxin oxidoreductase","PYRUFLAVREDUCT-RXN ;",0.22801,0.98162,56.93,{"v":1e-94,"d":"1.00E-94"},1,1,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","1 : Unknown","6 : Energy metabolism ;","e : enzyme",11167002,"2a : Function from experimental evidences in other organisms",3,269,1171,4,270,272]
[]
["AZ49_06950","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 ;",0.98997,0.99246,63.29,0,1,1,"_","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",1,395,398,1,395,399]
[null,"CD630_11750",null,"Clostridium difficile 630","ackA","Acetate kinase (Acetokinase)","_",0.99749,0.99749,59.45,{"v":1E-169,"d":"1.00E-169"},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",1,395,398,1,397,398]
[null,"SBF1_v1_800074","_","Desulfosporosinus sp. SbF1","ackA","acetate kinase","ACETATEKIN-RXN ; RHEA:11355 ;",0.99246,0.99496,57.47,{"v":2E-165,"d":"2.00E-165"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,394,398,1,395,397]
[null,"BSU29470","_","Bacillus subtilis 168","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ; RHEA:11352 ;",0.97487,0.98228,55.67,{"v":4e-156,"d":"4.00E-156"},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",3,390,398,4,389,395]
[null,"CLOSTRIBL6_v1_2260",null,"Clostridiales BL-6","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ; RHEA:11352 ;",0.99252,1,52.01,{"v":1e-143,"d":"1.00E-143"},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",1,395,398,1,398,401]
[null,"CLOSTRIBL4_v1_2217",null,"Clostridiales BL-4","ackA","Acetate kinase","ACETATEKIN-RXN ; RHEA:11355 ;",0.95923,1.00503,52,{"v":5e-140,"d":"5.00E-140"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","10360571, 10074080","2a : Function from experimental evidences in other organisms",1,396,398,1,399,417]
[null,"BTCD_v1_0691","_","Brochothrix thermosphacta CD337","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ;",0.99751,1.00503,50.25,{"v":6e-135,"d":"6.00E-135"},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",3,398,398,4,401,401]
[null,"EFER_2027","_","Escherichia fergusonii ATCC 35469T","_","putative acetate/propionate kinase pduW","_",0.9703,0.98492,48.21,{"v":3E-132,"d":"3.00E-132"},1,1,"_","2.7.2.1","1 : Unknown","_","e : enzyme",10498708,"3 : Putative function from multiple computational evidences",3,394,398,5,392,404]
[null,"SSV_v1_0105","_","Streptococcus sanguinis 2908","ackA","acetate kinase","ACETATEKIN-RXN ; PROPKIN-RXN ;",0.97739,0.97985,49.87,{"v":2E-131,"d":"2.00E-131"},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",6,392,398,7,392,397]
[null,"NMA2050","_","Neisseria meningitidis Z2491","ackA2","acetate kinase 2 (acetokinase 2)","_",0.99499,0.99749,46.85,{"v":1e-118,"d":"1.00E-118"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,395,398,5,396,399]
[null,"NMV_0478",null,"Neisseria meningitidis NEM8013","ackA2","acetate kinase 2 (acetokinase 2)","_",0.99248,0.99497,45.96,{"v":4e-117,"d":"4.00E-117"},1,1,"1.3.5 : Fermentation ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,394,398,5,395,399]
[null,"VC1098","_","Vibrio cholerae N16961","ackA","acetate kinase","_",1,1,44.22,{"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",2,396,398,4,397,398]
[null,"VIBNIv4_A2401","_","Vibrio nigripulchritudo SFn1","ackA","acetate kinase","_",0.99497,0.99497,43.43,{"v":4e-110,"d":"4.00E-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",2,394,398,4,395,398]
[null,"VIBNIv4_B1211","_","Vibrio nigripulchritudo SFn1","ackA","Acetate kinase","_",1,1.00252,44.47,{"v":2E-109,"d":"2.00E-109"},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",3,395,398,6,397,397]
[null,"ECS88_4678","_","Escherichia coli S88","_","Putative Acetate/propionate kinase","_",0.90805,0.99246,42.53,{"v":3e-108,"d":"3.00E-108"},1,1,"_","2.7.2.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,394,398,43,431,435]
[null,"BN12v2_1100005","_","Tetrasphaera japonica T1-X7","ackA","Acetate kinase","_",0.99497,0.99748,43.94,{"v":3e-108,"d":"3.00E-108"},1,1,"_","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",2,397,398,5,397,397]
[null,"ECED1_3455","_","Escherichia coli ED1a","_","Putative Acetate/propionate kinase","_",0.90805,0.99246,42.53,{"v":4e-108,"d":"4.00E-108"},1,1,"_","2.7.2.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,394,398,43,431,435]
[null,"VS_II1135","_","Vibrio tasmaniensis LGP32","ackA-2","Acetate kinase","ACETATEKIN-RXN ; RXN-7958 ;",1.00251,1.00504,44.11,{"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",3,395,398,6,397,397]
[null,"BN13v1_910016",null,"Tetrasphaera jenkinsii Ben74","ackA","Acetate kinase","_",0.99497,1.00508,43.18,{"v":4e-103,"d":"4.00E-103"},1,1,"_","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","7883769, 7918659","2a : Function from experimental evidences in other organisms",3,397,398,4,394,394]
[null,"MARHY2148","_","Marinobacter hydrocarbonoclasticus ATCC 49840","ackA","acetate kinase A and propionate kinase 2","_",0.99002,0.99749,41.56,{"v":5e-103,"d":"5.00E-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",3,396,398,5,393,401]
[null,"BN11v3_1350008","_","Tetrasphaera australiensis Ben110","ackA","acetate kinase A and propionate kinase 2","_",0.98496,0.98744,44.53,{"v":4e-102,"d":"4.00E-102"},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",3,393,398,8,394,399]
[null,"BN45v3_10447","_","Mycobacterium canettii STB-J","ackA","Putative acetate kinase AckA (acetokinase)","_",0.98995,1.02338,42.89,{"v":9e-101,"d":"9.00E-101"},1,1,"7 : intermediary metabolism and respiration ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",3,395,398,5,380,385]
[null,"BN42v3_20130","_","Mycobacterium canettii STB-K","ackA","Putative acetate kinase AckA (acetokinase)","_",0.98995,1.02338,42.64,{"v":7e-100,"d":"7.00E-100"},1,1,"7 : intermediary metabolism and respiration ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",3,395,398,5,380,385]
[null,"BN44v3_10450","_","Mycobacterium canettii STB-D","ackA","Putative acetate kinase AckA (acetokinase)","_",0.98995,1.02338,42.89,{"v":9e-100,"d":"9.00E-100"},1,1,"7 : intermediary metabolism and respiration ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",3,395,398,5,380,385]
[null,"BN43v3_10442","_","Mycobacterium canettii STB-L","ackA","Putative acetate kinase AckA (acetokinase)","_",0.98995,1.02338,42.64,{"v":4e-99,"d":"4.00E-99"},1,1,"7 : intermediary metabolism and respiration ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",3,395,398,5,380,385]
[null,"BN10v3_560037","_","Tetrasphaera elongata Lp2","ackA","Acetate kinase","_",0.99497,1.05319,41.41,{"v":6e-96,"d":"6.00E-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",2,396,398,4,371,376]
[null,"ABAYE3282","_","Acinetobacter baumannii AYE","ack","acetate kinase (propionate kinase)","_",0.99,0.99497,40.66,{"v":1e-94,"d":"1.00E-94"},1,1,"1.1.1 : carbon compounds ; 1.1.3 : amino acids ; 1.7.28 : pyruvate oxidation ; 1.7.29 : acetate catabolism ; 1.7.30 : threonine catabolism ;","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,395,398,5,387,400]
[null,"ACIAD0541","_","Acinetobacter baylyi ADP1","ack","acetate kinase (propionate kinase)","ACETATEKIN-RXN ; PROPKIN-RXN ; RXN-7958 ; RHEA:11355 ; RHEA:23151 ;",0.99002,0.99749,41.31,{"v":2e-93,"d":"2.00E-93"},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",3,395,398,5,388,401]
[null,"BN77v1_3277","_","Rhizobium mesoamericanum STM3625","ackA","Acetate kinase","_",1.00251,1.02308,39.85,{"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",3,396,398,4,389,390]
[null,"BRADO1872","_","Bradyrhizobium sp. ORS278","tdcD","propionate kinase/acetate kinase C, anaerobic","_",1.01005,1.01772,38.56,{"v":1E-89,"d":"1.00E-89"},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",3,398,398,6,394,395]
[null,"NIDE3516","_","Candidatus Nitrospira defluvii","ackA","Acetate kinase","_",0.98515,1,40.7,{"v":3e-89,"d":"3.00E-89"},1,1,"1.3.5 : Fermentation ; 1.7.28 : Pyruvate catabolism ; 1.7.29 : Acetate catabolism ; 7.1 : Cytoplasm ; 1.1.3.7 : Threonine catabolism ;","2.7.2.1","2 : Cytoplasmic","6.2 : Amino acids and amines ; 6.7 : Fermentation ; 6.8 : Glycolysis/gluconeogenesis ;","e : enzyme","10074080, 10075432, 10094701, 11133963, 7883769, 8226623, 8226682, 8702268, 9805396","2a : Function from experimental evidences in other organisms",3,396,398,11,399,404]
[null,"p2METDI0002","_","Methylobacterium extorquens DM4","ackA","acetate kinase","_",0.98744,1.00512,39.69,{"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",2,392,398,5,388,391]
[null,"HELPY_0888",null,"Helicobacter pylori B38","_","Fragment of putative acetate kinase AckA (Part 1)","_",0.72362,0.96,47.92,{"v":2E-87,"d":"2.00E-87"},1,1,"1.3.5 : Fermentation ;","2.7.2.1","1 : Unknown","6.7 : Fermentation ;","e : enzyme","12634340, 15755952, 17465479, 18223085","5 : Unknown function",1,284,398,1,286,300]
[null,"AZOLI_p20461","_","Azospirillum lipoferum 4B","ackA2","Acetate kinase","_",0.9902,1.01508,40.35,{"v":4e-87,"d":"4.00E-87"},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",4,398,398,13,402,408]
[null,"BN874v1_640030","_","Candidatus Contendobacter odensis Run_B_J11","ackA","Acetate/propionate kinase","_",1.00754,1.02296,39.4,{"v":6e-87,"d":"6.00E-87"},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",3,395,398,5,391,392]
[null,"MGMSRv2_1019","_","Magnetospirillum gryphiswaldense MSR-1 v2","ackA","Acetate kinase","_",0.96163,1.00754,37.91,{"v":1e-86,"d":"1.00E-86"},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",3,394,398,22,408,417]
[null,"METDI0790","_","Methylobacterium extorquens DM4","_","putative acetate kinase (ackA)","_",1.00251,1.01269,39.6,{"v":1e-86,"d":"1.00E-86"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,395,398,9,391,394]
[null,"HP0903",null,"Helicobacter pylori 26695","ackA","Fragment of putative acetate kinase (Part 1)","_",0.72362,0.9863,47.92,{"v":5e-86,"d":"5.00E-86"},1,1,"6.7 : Fermentation ;","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,284,398,1,286,292]
[null,"RM41v1_pld1870123",null,"Sinorhizobium sp. Rm41","ackA","Acetate kinase","_",1.00251,1.01786,39.6,{"v":1e-85,"d":"1.00E-85"},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",3,395,398,4,389,392]
[null,"BN873v1_460010","_","Candidatus Competibacter denitrificans Run_A_D11","ackA","Acetate/propionate kinase","_",1.01425,1.07286,35.6,{"v":1e-85,"d":"1.00E-85"},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",3,395,398,5,419,421]
[null,"RCFBPv5_mp0810","_","Ralstonia solanacearum CFBP2957","ackA","acetate kinase","_",0.98995,1.0051,38.83,{"v":4e-83,"d":"4.00E-83"},1,1,"_","2.7.2.1","2 : Cytoplasmic","6.2 : Amino acids and amines ; 5 : Central intermediary metabolism ;","e : enzyme",10094701,"2a : Function from experimental evidences in other organisms",2,389,398,3,384,392]
[null,"RPSI07_mp1366","_","Ralstonia solanacearum PSI07","ackA","Acetate kinase","_",0.99246,1.00765,39.24,{"v":3e-81,"d":"3.00E-81"},1,1,"_","2.7.2.1","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",10094701,"2a : Function from experimental evidences in other organisms",2,389,398,3,384,392]
[null,"AZOLI_0599","_","Azospirillum lipoferum 4B","ackA1","Acetate kinase","_",1.01256,1.02284,36.72,{"v":5E-80,"d":"5.00E-80"},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",3,396,398,5,392,394]
[null,"MT37II_v2_a0110","_","Ca. Spiroplasma holothuricola MT37","ackA","acetate kinase (possibly promiscuous)","RXN-7958 ; ACETATEKIN-RXN ; RHEA:11352 ;",0.98272,1,37.44,{"v":2E-79,"d":"2.00E-79"},1,1,"_","2.7.2.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,391,398,5,394,405]
[null,"RALTA_A1397","_","Cupriavidus taiwanensis LMG19424","_","Acetate kinase","_",1.01256,1.01768,36.23,{"v":5E-79,"d":"5.00E-79"},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)",2,398,398,4,394,396]
[null,"THI_1474","_","Thiomonas sp. 3As","ackA","Acetate kinase AckA","_",1.0175,1.02261,35.87,{"v":5e-73,"d":"5.00E-73"},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)",3,396,398,6,400,400]
[null,"Rmet_0562","_","Cupriavidus metallidurans CH34","ackA2","acetate kinase","_",1.00741,1.02513,37.75,{"v":2e-72,"d":"2.00E-72"},1,1,"_","2.7.2.1","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,395,398,7,401,405]
[null,"HEAR1515","_","Herminiimonas arsenicoxydans","ackA","Acetate kinase (Acetokinase)","_",0.98786,1.02261,36.36,{"v":6e-69,"d":"6.00E-69"},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)",2,395,398,20,407,412]
[null,"HPP12_0900",null,"Helicobacter pylori P12","ackA-2","Fragment of acetate kinase (Part 2)","_",0.4799,0.94554,50.79,{"v":1e-63,"d":"1.00E-63"},1,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",94,284,398,5,195,202]
[null,"HPB8_649",null,"Helicobacter pylori B8","_","Fragment of acetate kinase AckA (Part 2)","_",0.44221,0.96175,53.98,{"v":7e-62,"d":"7.00E-62"},1,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",109,284,398,1,176,183]
[null,"HPAG1_0884",null,"Helicobacter pylori HPAG1","_","Fragment of acetate kinase (Part 1)","_",0.42211,0.9711,41.07,{"v":2e-33,"d":"2.00E-33"},1,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,162,398,2,167,173]
[null,"HPP12_0899",null,"Helicobacter pylori P12","ackA-3","Fragment of acetate kinase (Part 3)","_",0.28141,0.94915,43.75,{"v":7e-21,"d":"7.00E-21"},2,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",288,397,398,5,116,118]
[null,"HPB8_650",null,"Helicobacter pylori B8","_","Fragment of acetate kinase AckA (Part 3)","_",0.28894,0.97458,41.74,{"v":1e-20,"d":"1.00E-20"},2,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",284,397,398,2,116,118]
[null,"HPG27_856","_","Helicobacter pylori G27","_","Fragment of putative acetate kinase AckA (Part 2)","_",0.28141,0.92562,41.96,{"v":1e-19,"d":"1.00E-19"},1,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",288,397,398,8,119,121]
[null,"HP0903",null,"Helicobacter pylori 26695","ackA","Fragment of putative acetate kinase (Part 2)","_",0.28141,0.94915,41.07,{"v":2E-19,"d":"2.00E-19"},2,1,"6.7 : Fermentation ;","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",288,397,398,5,116,118]
[null,"HPB8_648",null,"Helicobacter pylori B8","_","Fragment of acetate kinase AckA (Part 1)","_",0.24874,0.95192,42.42,{"v":7e-16,"d":"7.00E-16"},3,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,95,398,1,97,104]
[null,"HPP12_0901",null,"Helicobacter pylori P12","ackA-1","Fragment of acetate kinase (Part 1)","_",0.24874,1.0102,42.42,{"v":7e-16,"d":"7.00E-16"},3,1,"_","_","1 : Unknown","_","u : unknown","_","5 : Unknown function",1,95,398,1,97,98]
[null,"HELPY_0887",null,"Helicobacter pylori B38","_","Fragment of putative acetate kinase AckA (Part 2)","_",0.19095,0.86364,44.74,1e-12,2,1,"1.3.5 : Fermentation ;","2.7.2.1","1 : Unknown","6.7 : Fermentation ;","e : enzyme","12634340, 15755952, 17465479, 18223085","5 : Unknown function",288,362,398,8,83,88]
[null,"HPAG1_0883",null,"Helicobacter pylori HPAG1","_","Fragment of actetate kinase (Part 3)","_",0.19095,0.86364,44.74,2E-12,2,1,"_","2.7.2.1","1 : Unknown","_","u : unknown","_","5 : Unknown function",288,362,398,8,83,88]
[]
["AZ49AM_0981","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"RALTA_B1570",null,"Cupriavidus taiwanensis LMG19424","pta","phosphate acetyltransferase (taurine catabolism pathway)","_",0.7093,0.97211,40.57,{"v":2e-47,"d":"2.00E-47"},1,2,"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",8,251,251,88,329,344]
[]
["AZ49_02525","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","_",0.99231,0.99486,57.62,{"v":4e-153,"d":"4.00E-153"},1,1,"_","1.1.1.1","2 : Cytoplasmic","_","e : enzyme",2673928,"2a : Function from experimental evidences in other organisms",3,389,389,4,390,390]
[null,"CLOSTRIBL4_v1_2290","_","Clostridiales BL-4","adh","Alcohol dehydrogenase","RXN-12448 ;",1,1.01302,50.9,{"v":1e-130,"d":"1.00E-130"},1,1,"_","1.1.1.1","2 : Cytoplasmic","_","e : enzyme",2673928,"2a : Function from experimental evidences in other organisms",1,389,389,1,384,384]
[]
["AZ49_03535","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_31770",null,"Clostridium difficile 630","_","Putative xanthine dehydrogenase","_",0.99107,1.04103,59.12,0,1,1,"_","1.17.1.4","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",9,895,896,6,853,853]
[null,"RALTA_B0582","_","Cupriavidus taiwanensis LMG19424","hbaB","4-hydroxybenzoyl-CoA reductase HbaB subunit","_",0.16741,0.94937,38.67,{"v":3e-33,"d":"3.00E-33"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","1.3.99.20","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",9006014,"2a : Function from experimental evidences in other organisms",6,152,896,7,156,158]
[null,"CD630_20880",null,"Clostridium difficile 630","xdhC2","Xanthine dehydrogenase iron-sulfur binding subunit XdhC2","_",0.16629,0.95513,42.28,{"v":2e-32,"d":"2.00E-32"},6,1,"1.7.33.1 : Salvage pathways of adenine, hypoxanthine, and their nucleosides ;","1.17.1.4","1 : Unknown","2.2 : Nucleotide and nucleoside interconversions ;","c : carrier","17686778, 16597619, 10217763","2a : Function from experimental evidences in other organisms",3,148,896,2,150,156]
[null,"Gobs_3388",null,"Geodermatophilus obscurus DSM 43160","xdhC","xanthine dehydrogenase, Fe-S binding subunit","_",0.1596,0.91667,44.06,{"v":2e-30,"d":"2.00E-30"},5,1,"_","_","1 : Unknown","2.6 : Sugar-nucleotide biosynthesis and conversions ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,147,896,7,149,156]
[null,"PP_3947","_","Pseudomonas putida KT2440","nicA","nicotinate dehydrogenase subunit A","NICOTINATE-DEHYDROGENASE-RXN ;",0.17299,0.98726,39.35,{"v":2e-28,"d":"2.00E-28"},1,1,"1.1 : Carbon compound utilization ;","1.17.2.1","1 : Unknown","3.2 : Degradation ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","12534466, 18678916","1a : Function from experimental evidences in the studied strain",1,152,896,1,155,157]
[null,"BSU32470",null,"Bacillus subtilis 168","pucE","xanthine dehydrogenase, iron-sulfur subunit","RXN-7682 ; RXN0-901 ; RHEA:24670 ; RHEA:16669 ;",0.15737,0.81503,38.3,{"v":2e-27,"d":"2.00E-27"},2,1,"2.3 : Metabolism of nucleotides and nucleic acids ;","1.17.1.4","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","9098051, 11344136, 18569337","2a : Function from experimental evidences in other organisms",3,141,896,14,154,173]
[null,"MARHY2383","_","Marinobacter hydrocarbonoclasticus ATCC 49840","_","conserved hypothetical protein, putative 2Fe-2S Iron-sulfur Metal-binding Oxidoreductase","_",0.16183,0.89506,37.93,{"v":3e-26,"d":"3.00E-26"},1,1,"_","_","1 : Unknown","_","u : unknown","_","4 : Unknown function but conserved in other organisms",7,148,896,5,149,162]
[null,"RPSI07_mp0937","_","Ralstonia solanacearum PSI07","iorA","Isoquinoline 1-oxidoreductase alpha subunit","_",0.15513,0.91447,37.41,{"v":3e-25,"d":"3.00E-25"},1,1,"1 : Metabolism ;","1.3.99.16","1 : Unknown","6 : Energy metabolism ;","e : enzyme","7782304, 8157655","2b : Function from indirect experimental evidences (e.g. phenotypes)",14,151,896,13,151,152]
[null,"META2_0884","_","Methylobacterium extorquens AM1","_","Putative dehydrogenase subunit","_",0.16518,0.96732,35.81,{"v":7e-25,"d":"7.00E-25"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",9,154,896,6,153,153]
[null,"AZOLI_p50066","_","Azospirillum lipoferum 4B","iorA","Isoquinoline 1-oxidoreductase subunit alpha","_",0.1596,0.93464,35.66,{"v":7e-25,"d":"7.00E-25"},1,1,"1.1 : Carbon compound utilization ;","1.3.99.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","7782304, 8157655","2a : Function from experimental evidences in other organisms",11,152,896,10,152,153]
[null,"METDI1056","_","Methylobacterium extorquens DM4","iorA","isoquinoline 1-oxidoreductase, alpha subunit","_",0.15625,0.92715,35.71,{"v":3E-24,"d":"3.00E-24"},1,1,"_","_","1 : Unknown","_","e : enzyme","9238099, 7782304, 8157655","2b : Function from indirect experimental evidences (e.g. phenotypes)",12,151,896,11,150,151]
[null,"HEAR1179","_","Herminiimonas arsenicoxydans","iorA","Isoquinoline 1-oxidoreductase alpha subunit","_",0.1529,0.90132,37.23,{"v":3E-24,"d":"3.00E-24"},1,1,"1.4.3 : Electron carrier ;","1.3.99.16","1 : Unknown","6 : Energy metabolism ;","e : enzyme",7782304,"2a : Function from experimental evidences in other organisms",13,148,896,12,148,152]
[null,"CD630_20810",null,"Clostridium difficile 630","xdhC1","Xanthine dehydrogenase iron-sulfur binding subunit XdhC1","_",0.1596,0.92258,38.46,{"v":6e-24,"d":"6.00E-24"},7,2,"1.7.33.1 : Salvage pathways of adenine, hypoxanthine, and their nucleosides ;","1.17.1.4","1 : Unknown","2.2 : Nucleotide and nucleoside interconversions ;","c : carrier","17686778, 16597619, 10217763","2a : Function from experimental evidences in other organisms",4,144,896,9,149,155]
[null,"Mchl_2065",null,"Methylobacterium extorquens CM4","_","putative oxidoreductase, Fe-S binding domain, related to xanthine dehydrogenase","_",0.15625,0.82353,37.14,{"v":1e-23,"d":"1.00E-23"},9,1,"_","1.17.1.4","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",17,155,896,18,157,170]
[null,"PSEEN2172","_","Pseudomonas entomophila L48","_","putative isoquinoline 1-oxidoreductase, alpha subunit","_",0.14844,0.88079,38.35,{"v":4e-23,"d":"4.00E-23"},1,1,"_","1.3.99.16","Unknown","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",13,144,896,11,142,151]
[null,"FRAAL1458",null,"Frankia alni ACN14a","xdhC","Xanthine dehydrogenase, 2Fe-2S ferredoxin-like, small subunit","_",0.15067,0.92466,40,{"v":1E-22,"d":"1.00E-22"},5,2,"1.2.2 : DNA ;","1.17.1.4","1 : Unknown","8.3 : Degradation of DNA ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",34,164,896,3,137,146]
[null,"NT26v4_p10157","_","Rhizobium sp. NT-26","_","Putative oxidoreductase (Aldehyde oxidase/Xanthine dehydrogenase-like) subunit alpha; [2Fe-2S]-binding subunit","_",0.15067,0.87097,37.04,{"v":1E-22,"d":"1.00E-22"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",19,152,896,18,152,155]
[]
["AZ49_05685","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_12838",null,"Clostridiaceae BL-3","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99491,0.99745,67.52,0,1,1,"_","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","7867955, 11075929, 11466286, 1685080","2a : Function from experimental evidences in other organisms",1,390,393,1,391,392]
[null,"CLOSTRIBL4_v1_1867",null,"Clostridiales BL-4","thlA","acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.92417,0.99237,63.33,{"v":4e-177,"d":"4.00E-177"},1,1,"_","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","7867955, 11075929","2a : Function from experimental evidences in other organisms",2,390,393,29,418,422]
[null,"CD630_10590",null,"Clostridium difficile 630","thlA1","Acetoacetyl-CoA thiolase 1","_",0.99237,0.99744,62.05,{"v":2E-171,"d":"2.00E-171"},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",1,390,393,1,390,391]
[null,"RALTA_A1351",null,"Cupriavidus taiwanensis LMG19424","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.99491,0.99491,63.43,{"v":5e-171,"d":"5.00E-171"},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",1,390,393,1,391,393]
[null,"Rmet_1357",null,"Cupriavidus metallidurans CH34","phaA","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.99491,0.99491,62.66,{"v":9e-171,"d":"9.00E-171"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,390,393,1,391,393]
[null,"CD630_26760",null,"Clostridium difficile 630","thlA2","Acetoacetyl-CoA thiolase 2","_",0.99237,0.9949,62.56,{"v":2E-170,"d":"2.00E-170"},2,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","11075929, 2191949","1c : Function from experimental evidences in the studied genus",1,389,393,1,390,392]
[null,"PSEEN4635",null,"Pseudomonas entomophila L48","phbA","acetyl-CoA acetyltransferase","_",0.96069,0.99491,61.64,{"v":1E-169,"d":"1.00E-169"},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",1,390,393,15,405,407]
[null,"MARHY3102",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","phbA","acetyl-CoA acetyltransferase with thiolase domain, PHB biosynthesis","_",0.99491,0.99745,60.87,{"v":3e-169,"d":"3.00E-169"},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",1,390,393,1,391,392]
[null,"CLOSTRIBL6_v1_0127",null,"Clostridiales BL-6","phaA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99241,0.99746,62.5,{"v":1E-166,"d":"1.00E-166"},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",2,390,393,3,394,395]
[null,"PP_4636",null,"Pseudomonas putida KT2440","yqeF","acetyl-CoA acetyltransferase","METHYLACETOACETYLCOATHIOL-RXN ; RXN-12561 ; ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",0.99491,0.99745,60.61,{"v":7e-166,"d":"7.00E-166"},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",1,390,393,1,391,392]
[null,"CMR15v5_2547",null,"Ralstonia solanacearum CMR15","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.99491,0.99491,61.38,{"v":1E-165,"d":"1.00E-165"},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",1,390,393,1,391,393]
[null,"METDI4272",null,"Methylobacterium extorquens DM4","phaA","beta-ketothiolase","_",0.99239,0.99491,61.89,{"v":2E-165,"d":"2.00E-165"},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",2,392,393,5,394,394]
[null,"AZOLI_2388",null,"Azospirillum lipoferum 4B","phbA3","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.99237,0.99744,60.51,{"v":8e-164,"d":"8.00E-164"},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",1,390,393,1,389,391]
[null,"THI_1641",null,"Thiomonas sp. 3As","phbA1","acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.99491,0.99745,60.87,{"v":3e-163,"d":"3.00E-163"},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",1,390,393,1,391,392]
[null,"BRADO0562",null,"Bradyrhizobium sp. ORS278","phbA","acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98223,0.98473,61.5,{"v":4e-163,"d":"4.00E-163"},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)",3,389,393,6,391,394]
[null,"HEAR0577",null,"Herminiimonas arsenicoxydans","phbA","acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.97744,0.99237,57.95,{"v":1E-161,"d":"1.00E-161"},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)",1,390,393,9,398,399]
[null,"BN874v1_850028",null,"Candidatus Contendobacter odensis Run_B_J11","phaA","Acetyl-CoA acetyltransferase","_",0.99491,0.99491,59.08,{"v":7E-159,"d":"7.00E-159"},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)",1,390,393,1,391,393]
[null,"BN873v1_100077",null,"Candidatus Competibacter denitrificans Run_A_D11","phaA","Acetyl-CoA acetyltransferase","_",0.99491,0.99491,58.57,{"v":1e-157,"d":"1.00E-157"},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",1,390,393,1,391,393]
[null,"NT26v4_3604",null,"Rhizobium sp. NT-26","phbA","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98473,0.98473,59.69,{"v":3E-157,"d":"3.00E-157"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 1.3 : Energy metabolism (carbon) ; 7.1 : Cytoplasm ;","2.3.1.9","1 : Unknown","16.2 : Construct biomass (Anabolism) ; 6 : Energy metabolism ;","e : enzyme",7582015,"2b : Function from indirect experimental evidences (e.g. phenotypes)",4,390,393,6,391,393]
[null,"RM41v1_110012",null,"Sinorhizobium sp. Rm41","phbA","acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98982,0.98982,59.38,{"v":2E-155,"d":"2.00E-155"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 1.7 : Central intermediary metabolism ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ; 16.2 : Construct biomass (Anabolism) ;","e : enzyme",7582015,"1b : Function from experimental evidences in the studied species",4,392,393,6,393,393]
[null,"Spro_0592",null,"Serratia proteamaculans 568","atoB","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.97506,0.99491,57.03,{"v":8e-153,"d":"8.00E-153"},1,1,"1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,390,393,9,399,401]
[null,"MGMSRv2_1838",null,"Magnetospirillum gryphiswaldense MSR-1 v2","phbA","acetyl-CoA acetyltransferase containing thiolase domain (Acetoacetyl-CoA thiolase)","_",0.99237,1,56.92,{"v":4e-151,"d":"4.00E-151"},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)",1,390,393,1,389,390]
[null,"ECIAI1_1489",null,"Escherichia coli IAI1","_","putative acetyl-CoA acetyltransferase","_",0.97756,0.99746,55.1,{"v":8e-147,"d":"8.00E-147"},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",1,390,393,1,392,401]
[null,"ECK2842",null,"Escherichia coli K12","yqeF","Acetyl-CoA acetyltransferase","_",0.99237,0.99237,53.59,{"v":3e-145,"d":"3.00E-145"},2,1,"1.7 : Central intermediary metabolism ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",7763384,"2a : Function from experimental evidences in other organisms",1,390,393,1,390,393]
[null,"CLOSTRIBL6_v1_0556",null,"Clostridiales BL-6","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",1,1.01018,53.4,{"v":2e-141,"d":"2.00E-141"},2,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","7867955, 11075929, 11466286, 1685080","2a : Function from experimental evidences in other organisms",1,392,393,3,397,397]
[null,"Rmet_1362",null,"Cupriavidus metallidurans CH34","bktB","acetyl-CoA acetyltransferase","_",0.99746,1,54.45,{"v":4e-141,"d":"4.00E-141"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,392,393,3,394,394]
[null,"NBG4_v1_200004",null,"Candidatus Sulfobium mesophilum","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.98481,0.98982,52.7,{"v":4e-141,"d":"4.00E-141"},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",2,390,393,9,394,395]
[null,"AZOLI_p10676",null,"Azospirillum lipoferum 4B","phbA2","Acetyl-CoA acetyltransferase with thiolase domain (Beta-ketothiolase)","_",0.99491,0.99491,53.45,{"v":8e-141,"d":"8.00E-141"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.9","1 : Unknown","3.1 : Biosynthesis ; 3 : Fatty acid and phospholipid metabolism ;","e : enzyme","12534463, 9851987","2a : Function from experimental evidences in other organisms",3,392,393,4,393,393]
[null,"RCFBPv4_1653",null,"Ralstonia solanacearum CFBP2957","phaA","acetyl-CoA acetyltransferase, thiolase-like","_",0.99746,1,53.44,{"v":2E-140,"d":"2.00E-140"},2,1,"1.7 : Central intermediary metabolism ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",1685080,"2b : Function from indirect experimental evidences (e.g. phenotypes)",2,392,393,3,394,394]
[null,"RPSI07_1730",null,"Ralstonia solanacearum PSI07","phaA","acetyl-CoA acetyltransferase, thiolase-like","_",0.99746,1,53.94,{"v":8e-140,"d":"8.00E-140"},2,1,"1.7 : Central intermediary metabolism ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,392,393,3,394,394]
[null,"METUNv2_520573",null,"Methyloversatilis universalis FAM5","phbA","Acetyl-CoA acetyltransferase","_",0.99241,0.99746,53.32,{"v":4e-139,"d":"4.00E-139"},1,1,"1 : Metabolism ; 1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.9","2 : Cytoplasmic","15.11 : Biosynthesis of natural products ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,392,393,5,395,395]
[null,"SCFA_v1_120020",null,"Ca. Phosphitivorax anaerolimi F81","yqeF","Acetyl-CoA acetyltransferase","_",0.99491,0.99745,54.48,{"v":2e-138,"d":"2.00E-138"},3,1,"1.7 : Central intermediary metabolism ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",7763384,"2a : Function from experimental evidences in other organisms",1,390,393,1,390,392]
[null,"VIBNIv4_B1306",null,"Vibrio nigripulchritudo SFn1","phbA","acetyl-CoA acetyltransferase","_",0.99501,1.01527,51.38,{"v":8E-136,"d":"8.00E-136"},1,1,"1.1.2.7 : Acetoacetate degradation ; 7.1 : Cytoplasm ; 1.3 : Energy metabolism (carbon) ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ; 6 : Energy metabolism ;","e : enzyme","2670935, 16964242, 2670936","2a : Function from experimental evidences in other organisms",1,390,393,1,399,401]
[null,"RALTA_A1359",null,"Cupriavidus taiwanensis LMG19424","bktB","acetyl-CoA acetyltransferase, thiolase","_",0.99746,1,53.44,{"v":1E-135,"d":"1.00E-135"},2,1,"1.7 : Central intermediary metabolism ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",1685080,"2b : Function from indirect experimental evidences (e.g. phenotypes)",2,392,393,3,394,394]
[null,"CLOSTRIBL3_v1_13111",null,"Clostridiaceae BL-3","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",1.00509,1.01023,49.62,{"v":2e-135,"d":"2.00E-135"},2,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","7867955, 11075929, 11466286, 1685080","1c : Function from experimental evidences in the studied genus",1,390,393,1,390,391]
[null,"CLOSTRIBL4_v1_1159",null,"Clostridiales BL-4","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",0.99748,1.00763,51.01,{"v":2e-135,"d":"2.00E-135"},2,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","7867955, 11075929, 11466286, 1685080","2a : Function from experimental evidences in other organisms",2,392,393,4,397,397]
[null,"HELPY_0683",null,"Helicobacter pylori B38","atoB","Acetyl coenzyme A acetyltransferase","_",0.99237,0.99744,52.05,{"v":2e-135,"d":"2.00E-135"},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",1,390,393,1,389,391]
[null,"BSU24170",null,"Bacillus subtilis 168","mmgA","degradative acetoacetyl-CoA thiolase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99491,0.99491,50.9,{"v":6e-133,"d":"6.00E-133"},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",1,390,393,1,391,393]
[null,"VS_II0585",null,"Vibrio tasmaniensis LGP32","_","Acetyl-CoA C acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99752,1.0229,50.5,{"v":3E-132,"d":"3.00E-132"},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",1,393,393,1,402,403]
[null,"NIDE3116",null,"Candidatus Nitrospira defluvii","atoB","Acetyl-CoA acetyltransferase","_",0.9797,0.98219,50.52,{"v":3e-129,"d":"3.00E-129"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.7 : Acetoacetate degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","15229654, 1685080, 1755959, 7867955, 9904","2a : Function from experimental evidences in other organisms",5,390,393,8,393,394]
[null,"PSEEN3197",null,"Pseudomonas entomophila L48","_","putative Acetoacetyl-CoA thiolase","_",0.99239,0.99491,49.62,{"v":4e-127,"d":"4.00E-127"},2,1,"1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.9","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,392,393,5,394,394]
[null,"BN424_3179",null,"Carnobacterium maltaromaticum LMA28 v1","thlA","Acetoacetyl-CoA thiolase","METHYLACETOACETYLCOATHIOL-RXN ; RXN-12561 ; ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99237,1.00257,49.23,{"v":9e-127,"d":"9.00E-127"},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)",1,390,393,1,387,389]
[null,"VIBNIv4_A1234",null,"Vibrio nigripulchritudo SFn1","phbA","Acetyl-CoA acetyltransferase","_",0.99239,0.99491,48.08,{"v":3e-126,"d":"3.00E-126"},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",3,393,393,5,394,394]
[null,"ACIAD0694",null,"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 ;",0.99746,1.00256,49.23,{"v":8e-126,"d":"8.00E-126"},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",1,392,393,1,391,391]
[null,"LFAv2_0052",null,"Legionella-Like Amoebal Pathogens 10","thlA","Acetyl-CoA acetyltransferase","_",0.98985,0.99237,46.67,{"v":2e-123,"d":"2.00E-123"},1,1,"_","2.3.1.9","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,392,393,5,394,394]
[null,"PSHAa1586",null,"Pseudoalteromonas haloplanktis TAC125","atoB","acetyl-CoA acetyltransferase with thiolase domain, Acetoacetyl-CoA thiolase","_",0.94866,0.98728,48.45,{"v":3e-123,"d":"3.00E-123"},1,1,"_","2.3.1.9","cytoplasm (undefined)","_","e : enzyme",7867955,"2a : Function from experimental evidences in other organisms",4,390,393,21,407,409]
[null,"VIBNIv4_B0465",null,"Vibrio nigripulchritudo SFn1","phbA","acetyl-CoA acetyltransferase","_",0.99254,1.01527,47.37,{"v":2e-122,"d":"2.00E-122"},2,2,"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",1,390,393,1,399,402]
[null,"RCFBPv4_3139",null,"Ralstonia solanacearum CFBP2957","_","putative acetyl-CoA acetyltransferase with thiolase domain","_",0.98728,0.98728,48.45,{"v":2E-120,"d":"2.00E-120"},3,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,390,393,5,391,393]
[null,"THI_0462",null,"Thiomonas sp. 3As","pcaF1","Beta-ketoadipyl CoA thiolase","_",1.0025,1.02036,47.38,{"v":2E-119,"d":"2.00E-119"},2,1,"1 : Metabolism ;","2.3.1.-","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",7961399,"2a : Function from experimental evidences in other organisms",1,392,393,1,400,400]
[null,"RPSI07_3138",null,"Ralstonia solanacearum PSI07","_","putative acetyl-CoA acetyltransferase with thiolase domain","_",0.98728,0.98728,47.94,{"v":2E-119,"d":"2.00E-119"},3,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,390,393,5,391,393]
[null,"LEPBIa0355",null,"Leptospira biflexa serovar Patoc Patoc 1","thiL1","Putative acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.99746,0.99746,48.21,{"v":3e-119,"d":"3.00E-119"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme",15733928,"2a : Function from experimental evidences in other organisms",1,391,393,1,390,393]
[null,"AZOLI_p10029",null,"Azospirillum lipoferum 4B","atoB","acetyl-CoA acetyltransferase with thiolase domain","_",0.99237,0.99237,48.46,{"v":6e-119,"d":"6.00E-119"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1 : Carbon compound utilization ; 1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ; 6.2 : Amino acids and amines ;","e : enzyme",7867955,"2a : Function from experimental evidences in other organisms",4,392,393,5,393,393]
[null,"BN12v2_3170003",null,"Tetrasphaera japonica T1-X7","phaA","acetyl-CoA acetyltransferase (fadA) (Acetoacetyl-CoA thiolase) (beta-ketothiolase)","_",0.97739,0.98982,49.61,{"v":1e-118,"d":"1.00E-118"},1,1,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",5,389,393,7,393,398]
[null,"CMR15v5_0670",null,"Ralstonia solanacearum CMR15","_","putative acetyl-CoA acetyltransferase with thiolase domain","_",0.98728,0.98728,47.68,{"v":6e-118,"d":"6.00E-118"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,390,393,5,391,393]
[null,"MARHY2580",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","atoB","acetyl-CoA acetyltransferase","_",0.98477,0.98728,48.71,{"v":7e-118,"d":"7.00E-118"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,390,393,6,392,394]
[null,"BTCD_v1_1714",null,"Brochothrix thermosphacta CD337","mevB","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99237,1.00515,50.26,{"v":7e-118,"d":"7.00E-118"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme",7763384,"2a : Function from experimental evidences in other organisms",1,389,393,1,385,388]
[null,"RALTA_A0113",null,"Cupriavidus taiwanensis LMG19424","_","putative acetyl-CoA acetyltransferase with thiolase domain","_",0.99491,0.99745,47.57,{"v":1E-117,"d":"1.00E-117"},3,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,390,393,1,390,392]
[null,"BN381v2_150043",null,"Candidatus Microthrix parvicella RN1","phaA","acetyl-CoA acetyltransferase","_",0.99237,0.99237,48.21,{"v":1e-116,"d":"1.00E-116"},1,2,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","18246303, 10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",5,392,393,5,393,393]
[null,"Rmet_0106",null,"Cupriavidus metallidurans CH34","atoB","acetyl-CoA acetyltransferase","_",0.98477,0.98728,48.97,{"v":1e-116,"d":"1.00E-116"},3,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",4,390,393,6,392,394]
[null,"BN874v1_1120001",null,"Candidatus Contendobacter odensis Run_B_J11","phaA","Acetyl-CoA acetyltransferase","_",0.9775,0.99491,46.8,{"v":6e-116,"d":"6.00E-116"},2,2,"_","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",1,386,393,3,393,400]
[null,"MARHY1170",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","thlA","acetyl-CoA acetyltransferase, Acetoacetyl-CoA thiolase","_",0.99237,0.99237,46.92,{"v":2e-115,"d":"2.00E-115"},3,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",7867955,"2a : Function from experimental evidences in other organisms",3,392,393,5,393,393]
[null,"PSEEN3547",null,"Pseudomonas entomophila L48","fadAx","acetyl-CoA acetyltransferase with thiolase domain FadAx","_",0.97733,0.98728,47.68,{"v":3e-115,"d":"3.00E-115"},3,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",11251808,"2b : Function from indirect experimental evidences (e.g. phenotypes)",4,390,393,8,394,397]
[null,"pRALTA_0081",null,"Cupriavidus taiwanensis LMG19424","_","acetyl-CoA acetyltransferase","_",0.9775,0.99491,46.8,{"v":3e-115,"d":"3.00E-115"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,390,393,9,398,400]
[null,"MGMSRv2_3177",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaE","beta-ketoadipyl CoA thiolase","_",1,1.02036,46.38,{"v":7e-115,"d":"7.00E-115"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","10766858, 12846838, 17259607, 9748275","2a : Function from experimental evidences in other organisms",1,392,393,1,401,401]
[null,"ACIAD2516",null,"Acinetobacter baylyi ADP1","atoB","acetyl-CoA acetyltransferase with thiolase domain","ACETYL-COA-ACETYLTRANSFER-RXN ; METHYLACETOACETYLCOATHIOL-RXN ; RXN-12561 ; RHEA:21039 ;",0.99746,1,45.04,{"v":5e-114,"d":"5.00E-114"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.9","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","11075929, 18246303, 21209787","2a : Function from experimental evidences in other organisms",1,393,393,3,394,394]
[null,"PP_2215",null,"Pseudomonas putida KT2440","_","acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",0.97733,0.98728,47.42,{"v":6e-114,"d":"6.00E-114"},3,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","4150713, 773366, 236278, 9904, 2883931","2a : Function from experimental evidences in other organisms",4,390,393,8,394,397]
[null,"ABSDF1999",null,"Acinetobacter baumannii SDF","catF","beta-ketoadipyl CoA thiolase","_",0.99015,1.0229,45.27,{"v":6e-114,"d":"6.00E-114"},2,1,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme",8125318,"2a : Function from experimental evidences in other organisms",1,393,393,3,404,406]
[null,"ACIAD1612",null,"Acinetobacter baylyi ADP1","_","putative acetyl-CoA C-acetyltransferase with thiolase domain","_",0.98982,0.98982,46.27,{"v":9e-114,"d":"9.00E-114"},3,1,"1.1.1 : carbon compounds ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,390,393,4,391,393]
[null,"ABAYE1675",null,"Acinetobacter baumannii AYE","pcaF","beta-ketoadipyl CoA thiolase","_",0.99504,1.02036,45.39,{"v":1e-113,"d":"1.00E-113"},3,1,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme",8125318,"2a : Function from experimental evidences in other organisms",1,392,393,3,403,403]
[null,"ABSDF2022",null,"Acinetobacter baumannii SDF","pcaF","beta-ketoadipyl CoA thiolase","_",0.99504,1.02036,45.14,{"v":2E-113,"d":"2.00E-113"},3,1,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme",8125318,"2a : Function from experimental evidences in other organisms",1,392,393,3,403,403]
[null,"BN13v1_460011",null,"Tetrasphaera jenkinsii Ben74","_","putative Acetyl-CoA acetyltransferase (beta-ketothiolase) (phaA)","_",0.97487,0.98728,48.71,{"v":2E-113,"d":"2.00E-113"},1,1,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","3 : Putative function from multiple computational evidences",5,389,393,7,393,398]
[null,"AZOLI_p40026",null,"Azospirillum lipoferum 4B","pcaF","Beta-ketoadipyl CoA thiolase","_",0.98522,1.01781,46,{"v":4e-113,"d":"4.00E-113"},1,1,"1.1 : Carbon compound utilization ;","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",9582432,"2a : Function from experimental evidences in other organisms",1,392,393,8,406,406]
[null,"ABAYE1715",null,"Acinetobacter baumannii AYE","catF","beta-ketoadipyl CoA thiolase","_",0.99505,1.0229,45.02,{"v":6e-113,"d":"6.00E-113"},4,1,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme",8125318,"2a : Function from experimental evidences in other organisms",1,393,393,1,402,404]
[null,"ACIAD1706",null,"Acinetobacter baylyi ADP1","pcaF","beta-ketoadipyl CoA thiolase","2.3.1.155-RXN ; KETOACYLCOATHIOL-RXN ; RXN-3641 ;",1,1.02036,46.38,{"v":1e-112,"d":"1.00E-112"},4,1,"_","2.3.1.-","1 : Unknown","_","e : enzyme","8125318, 7883173, 8063101, 3036773","1a : Function from experimental evidences in the studied strain",1,392,393,1,401,401]
[null,"NIDE3104",null,"Candidatus Nitrospira defluvii","fadA","3-ketoacyl-CoA thiolase","_",1.00253,1.01018,45.09,{"v":1e-112,"d":"1.00E-112"},2,1,"1.1.2.4 : Anaerobic fatty acid oxidation pathway ; 7.1 : Cytoplasm ;","2.3.1.16","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","12535077, 1354266, 15229654, 2191949, 6350283","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,393,1,396,396]
[null,"METUNv2_320010",null,"Methyloversatilis universalis FAM5","phbA2","Putative acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.97494,0.98982,48.33,{"v":1e-112,"d":"1.00E-112"},2,1,"1.3 : Energy metabolism (carbon) ;","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ; 15 : Cellular processes ;","e : enzyme","2670935, 2670936","2a : Function from experimental evidences in other organisms",4,390,393,8,395,399]
[null,"SCFA_v1_300017",null,"Ca. Phosphitivorax anaerolimi F81","thlA","Acetyl-CoA acetyltransferase","_",0.9952,1.05598,46.99,{"v":3e-112,"d":"3.00E-112"},4,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,390,393,1,415,417]
[null,"BN873v1_610042",null,"Candidatus Competibacter denitrificans Run_A_D11","phaA","Acetyl-CoA acetyltransferase","_",0.97756,0.99746,45.66,{"v":6e-112,"d":"6.00E-112"},2,2,"_","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",1,386,393,3,394,401]
[null,"BRADO0538",null,"Bradyrhizobium sp. ORS278","_","putative acetyl-CoA acetyltransferase (phbA/atoB/paaJ-like)","_",1,1.0229,46.52,{"v":1e-111,"d":"1.00E-111"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,393,393,1,402,402]
[null,"Pars_0309",null,"Pyrobaculum arsenaticum DSM 13514","thlA","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.96806,1.00254,48.73,{"v":1e-111,"d":"1.00E-111"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11075929, 11466286, 1685080, 7867955","2a : Function from experimental evidences in other organisms",3,392,393,15,407,407]
[null,"Atu3475",null,"Agrobacterium tumefaciens C58","fadAx","acetyl-CoA C-acetyltransferase","_",0.94175,0.98728,48.2,{"v":1e-111,"d":"1.00E-111"},1,1,"1 : Metabolism ;","_","2 : Cytoplasmic","_","e : enzyme",11251808,"2b : Function from indirect experimental evidences (e.g. phenotypes)",4,390,393,32,410,412]
[null,"ACIAD1450",null,"Acinetobacter baylyi ADP1","catF","beta-ketoadipyl CoA thiolase","2.3.1.155-RXN ; KETOACYLCOATHIOL-RXN ; RXN-3641 ;",1,1.02036,46.13,{"v":2e-111,"d":"2.00E-111"},5,1,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme",8125318,"1a : Function from experimental evidences in the studied strain",1,392,393,1,401,401]
[null,"ABAYE2367",null,"Acinetobacter baumannii AYE","paaJ","beta-ketoadipyl CoA thiolase with thiolase-like domain, phenylacetic acid degradation","_",1.00249,1.02545,46.4,{"v":3e-111,"d":"3.00E-111"},5,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","1 : Unknown","_","e : enzyme",9748275,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,393,393,1,402,402]
[null,"BN11v3_1860009",null,"Tetrasphaera australiensis Ben110","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.97243,0.98728,47.16,{"v":4e-110,"d":"4.00E-110"},1,1,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",5,389,393,8,394,399]
[null,"Rmet_3669",null,"Cupriavidus metallidurans CH34","pcaF","acetyl-CoA acetyltransferase","_",1.0025,1.02036,44.64,{"v":7e-110,"d":"7.00E-110"},1,1,"1.1.2.7 : Acetoacetate degradation ;","_","1 : Unknown","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,392,393,1,400,400]
[null,"PSEEN1165",null,"Pseudomonas entomophila L48","pcaF","beta-ketoadipyl CoA thiolase","_",1.0025,1.02036,45.14,{"v":3e-109,"d":"3.00E-109"},4,2,"1.1.1 : carbon compounds ;","2.3.1.9","Unknown","6 : Energy metabolism ;","e : enzyme",12534466,"2a : Function from experimental evidences in other organisms",1,392,393,1,400,400]
[null,"MARHY0270",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","paaJ","beta-ketoadipyl CoA thiolase with thiolase-like domain, phenylacetic acid degradation","_",1.005,1.0229,45.02,{"v":4E-109,"d":"4.00E-109"},4,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","1 : Unknown","_","e : enzyme",7961399,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,393,1,400,400]
[null,"RALTA_B0208",null,"Cupriavidus taiwanensis LMG19424","pcaF","Beta-ketoadipyl CoA thiolase","_",1.0025,1.02036,44.64,{"v":5e-109,"d":"5.00E-109"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.16","1 : Unknown","6 : Energy metabolism ;","e : enzyme",7961399,"2a : Function from experimental evidences in other organisms",1,392,393,1,400,400]
[null,"PP_3280",null,"Pseudomonas putida KT2440","paaJ","3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase","RXN0-6512 ; RXN-3641 ; RHEA:34441 ; RHEA:19483 ;",0.98276,1.01527,44.36,{"v":8e-109,"d":"8.00E-109"},4,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-, 2.3.1.174","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","20660314, 17259607","2a : Function from experimental evidences in other organisms",3,392,393,8,406,406]
[null,"BRADO3134",null,"Bradyrhizobium sp. ORS278","atoB","acetyl-CoA acetyltransferase with thiolase domain","_",0.98228,0.98728,45.88,{"v":9e-109,"d":"9.00E-109"},3,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1 : Carbon compound utilization ; 1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,390,393,7,393,395]
[null,"PSEEN2795",null,"Pseudomonas entomophila L48","pcaF-2","beta-ketoadipyl CoA thiolase","_",0.99015,1.0229,45.52,{"v":1E-108,"d":"1.00E-108"},5,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.9","Cytoplasmic","6 : Energy metabolism ;","e : enzyme","12534466, 15474299, 9600981","2a : Function from experimental evidences in other organisms",1,392,393,6,406,406]
[null,"CMR15v5_2038",null,"Ralstonia solanacearum CMR15","pcaF","Beta-ketoadipyl-CoA thiolase","_",1.005,1.0229,44.28,{"v":1E-108,"d":"1.00E-108"},3,1,"_","2.3.1.-","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,393,1,400,400]
[null,"FRAAL5910",null,"Frankia alni ACN14a","atoB","acetyl-CoA acetyltransferase with thiolase domain","_",0.97975,0.98473,47.8,{"v":5E-108,"d":"5.00E-108"},1,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,389,393,5,390,395]
[null,"MGMSRv2_0194",null,"Magnetospirillum gryphiswaldense MSR-1 v2","atoB","acetyl-CoA acetyltransferase with thiolase domain","_",0.99237,0.9949,46.92,{"v":8e-108,"d":"8.00E-108"},3,1,"1.1 : Carbon compound utilization ; 1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.3 : Amino acids ;","2.3.1.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","2670935, 2670936","2a : Function from experimental evidences in other organisms",4,392,393,6,391,392]
[null,"BDBv6_10148",null,"Blood disease bacterium R229","pcaF","Beta-ketoadipyl-CoA thiolase","_",1.005,1.0229,44.53,{"v":9e-107,"d":"9.00E-107"},4,1,"_","2.3.1.-","1 : Unknown","6 : Energy metabolism ;","e : enzyme",7961399,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,393,1,400,400]
[null,"AZOLI_p40258",null,"Azospirillum lipoferum 4B","paaJ","beta-ketoadipyl CoA thiolase","_",1,1.0229,45.02,{"v":1e-106,"d":"1.00E-106"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",1,392,393,1,402,402]
[null,"SCFA_v1_3830001",null,"Ca. Phosphitivorax butyraticus R76","atoB","fragment of acetyl-CoA acetyltransferase (part 2)","ACETYL-COA-ACETYLTRANSFER-RXN ;",0.93911,1.02036,45.89,{"v":3e-106,"d":"3.00E-106"},4,1,"1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,375,393,27,427,427]
[null,"BN873v1_20049",null,"Candidatus Competibacter denitrificans Run_A_D11","_","putative acetyl-CoA acetyltransferase","_",1.01005,1.0229,44.78,{"v":3e-105,"d":"3.00E-105"},3,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.16","2 : Cytoplasmic","_","e : enzyme","1699931, 2191949, 2204034","3 : Putative function from multiple computational evidences",1,390,393,5,396,398]
[null,"THI_3278",null,"Thiomonas sp. 3As","phbA2","acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.98728,0.9898,46.39,{"v":3e-105,"d":"3.00E-105"},3,2,"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",4,390,393,5,390,392]
[null,"ECK1394",null,"Escherichia coli K12","paaE","beta-ketoadipyl CoA thiolase","RXN-3641 ; RXN0-6512 ;",1,1.02036,43.89,{"v":5e-105,"d":"5.00E-105"},3,1,"1.1.5.1 : Phenylacetic acid degradation ;","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 17259607, 9748275","1a : Function from experimental evidences in the studied strain",1,392,393,1,401,401]
[null,"THI_3549",null,"Thiomonas sp. 3As","pcaF2","Beta-ketoadipyl CoA thiolase","_",0.98515,1.01272,43.72,{"v":2e-104,"d":"2.00E-104"},4,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","10766858, 12846838, 7961399, 9748275","2a : Function from experimental evidences in other organisms",2,390,393,5,402,404]
[null,"BN45v3_30404",null,"Mycobacterium canettii STB-J","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98219,0.99229,45.6,{"v":8e-104,"d":"8.00E-104"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,389,393,1,386,389]
[null,"VCRLGP8v1_930035",null,"Vibrio crassostreae LGP8","paaE","beta-ketoadipyl CoA thiolase","RXN0-6512 ; RXN-3641 ;",1,1.0229,45.02,{"v":1e-103,"d":"1.00E-103"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","_","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","10766858, 12846838, 17259607, 9748275","2a : Function from experimental evidences in other organisms",2,390,393,4,400,402]
[null,"XDD1v4_3927",null,"Xenorhabdus doucetiae FRM16","paaJ","protein PaaJ; Beta-ketoadipyl-CoA thiolase","_",1,1.02799,42.57,{"v":2e-103,"d":"2.00E-103"},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",1,393,393,1,404,404]
[null,"BN42v3_21228",null,"Mycobacterium canettii STB-K","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98219,0.99229,45.6,{"v":3E-103,"d":"3.00E-103"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,389,393,1,386,389]
[null,"ABAYE2307",null,"Acinetobacter baumannii AYE","dcaF","beta-ketoadipyl CoA thiolase","_",1.00249,1.0229,42.29,{"v":1e-102,"d":"1.00E-102"},6,1,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",1,392,393,1,400,401]
[null,"BN44v3_11488",null,"Mycobacterium canettii STB-D","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98219,0.99229,45.34,{"v":1e-102,"d":"1.00E-102"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,389,393,1,386,389]
[null,"BN43v3_30420",null,"Mycobacterium canettii STB-L","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98219,0.99229,45.34,{"v":1e-102,"d":"1.00E-102"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,389,393,1,386,389]
[null,"ACIAD1689",null,"Acinetobacter baylyi ADP1","dcaF","beta-ketoadipyl CoA thiolase","2.3.1.155-RXN ; KETOACYLCOATHIOL-RXN ; RXN-3641 ;",1.00249,1.0229,42.29,{"v":2e-102,"d":"2.00E-102"},6,1,"_","2.3.1.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921, 11571189","1a : Function from experimental evidences in the studied strain",1,392,393,1,400,401]
[null,"ABSDF1531",null,"Acinetobacter baumannii SDF","_","fragment of putative Beta-ketoadipyl CoA thiolase (part 2)","_",0.9597,0.96947,43.83,{"v":2e-102,"d":"2.00E-102"},4,1,"1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.9","1 : Unknown","_","e : enzyme","_","5 : Unknown function",20,392,393,18,397,397]
[null,"BN874v1_1250003",null,"Candidatus Contendobacter odensis Run_B_J11","_","putative acetyl-CoA acetyltransferase","_",1.01005,1.0229,43.53,{"v":1e-101,"d":"1.00E-101"},3,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.16","2 : Cytoplasmic","_","e : enzyme","1699931, 2191949, 2204034","3 : Putative function from multiple computational evidences",1,390,393,5,396,398]
[null,"VIBNIv4_A0031",null,"Vibrio nigripulchritudo SFn1","fadA","3-ketoacyl-CoA thiolase","_",1.02036,1.03351,44.64,{"v":2e-101,"d":"2.00E-101"},2,1,"1.1.2.6 : Aerobic fatty acid oxidation pathway ; 7.1 : Cytoplasm ;","2.3.1.16","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","1699931, 2191949, 2204034","2a : Function from experimental evidences in other organisms",1,393,393,1,388,388]
[null,"EFER_1634",null,"Escherichia fergusonii ATCC 35469T","paaJ","Beta-ketoadipyl CoA thiolase","_",1.005,1.0229,43.03,{"v":8e-101,"d":"8.00E-101"},4,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.9","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9748275,"2a : Function from experimental evidences in other organisms",1,392,393,1,400,400]
[null,"BSU32830",null,"Bacillus subtilis 168","fadA","acetyl-CoA C-acyltransferase","KETOACYLCOATHIOL-RXN ; RHEA:21564 ;",1.02036,1.02558,43.14,{"v":2E-100,"d":"2.00E-100"},2,2,"2.4 : Metabolism of lipids ;","2.3.1.16","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","1a : Function from experimental evidences in the studied strain",1,390,393,1,389,391]
[null,"BN381v2_70026",null,"Candidatus Microthrix parvicella RN1","_","Acetyl-CoA acetyltransferase","_",1.00995,1.03308,43.84,{"v":6e-100,"d":"6.00E-100"},2,1,"_","2.3.1.16","2 : Cytoplasmic","_","e : enzyme","1699931, 2191949, 2204034","2a : Function from experimental evidences in other organisms",1,392,393,1,401,402]
[null,"Spro_3039",null,"Serratia proteamaculans 568","pcaF","Beta-ketoadipyl-CoA thiolase","_",0.99,1.00763,42.93,{"v":1E-99,"d":"1.00E-99"},3,1,"1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.-","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,392,393,6,400,400]
[null,"RALTA_B1528",null,"Cupriavidus taiwanensis LMG19424","_","putative acetyl-CoA acetyltransferase with thiolase domain","_",1.00249,1.02545,42.93,{"v":1E-99,"d":"1.00E-99"},2,1,"1.7 : Central intermediary metabolism ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,390,393,1,400,402]
[null,"AZOLI_p30161",null,"Azospirillum lipoferum 4B","phbA4","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",1.01272,1.02314,43.97,{"v":3e-97,"d":"3.00E-97"},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",2,392,393,3,389,389]
[null,"XPG1v4_0713",null,"Xenorhabdus poinarii G6","pcaF","Beta-ketoadipyl-CoA thiolase","_",1.005,1.0229,42.04,{"v":2e-96,"d":"2.00E-96"},1,2,"_","2.3.1.174","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,393,1,400,400]
[null,"MARHY2135",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","fadA","3-ketoacyl-CoA thiolase; (thiolase I, acetyl-CoA transferase), in complex with FadB catalyzes Catalyzes the final step of fatty acid oxidation","_",1.01527,1.02046,45.11,{"v":3e-96,"d":"3.00E-96"},5,2,"1.1.2.1 : Degradation of short-chain fatty acids ; 7.1 : Cytoplasm ;","2.3.1.16","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",12115060,"2a : Function from experimental evidences in other organisms",2,392,393,6,391,391]
[null,"Pars_1071",null,"Pyrobaculum arsenaticum DSM 13514","_","putative acetyl-CoA acetyltransferase","_",1.00249,1.02545,41.19,{"v":1e-95,"d":"1.00E-95"},2,1,"1.3 : Energy metabolism (carbon) ;","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ; 15 : Cellular processes ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,392,393,8,402,402]
[null,"BN12v2_1200011",null,"Tetrasphaera japonica T1-X7","_","Putative 3-ketoacyl-CoA thiolase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",1.01235,1.04326,42.2,{"v":3e-95,"d":"3.00E-95"},2,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","3 : Putative function from multiple computational evidences",1,392,393,1,404,405]
[null,"BN42v3_20922",null,"Mycobacterium canettii STB-K","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",1.03704,1.0687,42.38,{"v":5e-95,"d":"5.00E-95"},2,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",1,392,393,1,404,405]
[null,"PSEEN3727",null,"Pseudomonas entomophila L48","fadA","3-ketoacyl-CoA thiolase (Fatty oxidation complex beta subunit) (Beta-ketothiolase) (Acetyl-CoA acyltransferase)","_",1.01527,1.02046,46.12,{"v":5e-95,"d":"5.00E-95"},6,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16","Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,392,393,6,391,391]
[null,"BN45v3_30114",null,"Mycobacterium canettii STB-J","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",1.02439,1.0687,42.38,{"v":1e-94,"d":"1.00E-94"},2,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",1,392,393,6,409,410]
[null,"BN44v3_11190",null,"Mycobacterium canettii STB-D","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",1,1.04326,42.93,{"v":1e-94,"d":"1.00E-94"},2,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",1,392,393,6,409,410]
[null,"BN43v3_30127",null,"Mycobacterium canettii STB-L","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",1,1.04326,42.93,{"v":1e-94,"d":"1.00E-94"},2,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",1,392,393,6,409,410]
[null,"Rmet_1853",null,"Cupriavidus metallidurans CH34","atoB","acetyl-CoA acetyltransferase / thiolase","_",1.0229,1.02551,42.04,{"v":6e-94,"d":"6.00E-94"},4,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","_","c : carrier","_","3 : Putative function from multiple computational evidences",1,390,393,1,390,392]
[null,"RALTA_A1469",null,"Cupriavidus taiwanensis LMG19424","_","putative 3-ketoacyl-CoA thiolase / acetyl-CoA acetyltransferase","_",1.0229,1.02551,42.54,{"v":1e-93,"d":"1.00E-93"},4,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16, 2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,390,393,1,390,392]
[null,"BN13v1_250034",null,"Tetrasphaera jenkinsii Ben74","_","Putative 3-ketoacyl-CoA thiolase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",1.01238,1.04071,41.56,{"v":6e-93,"d":"6.00E-93"},2,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","3 : Putative function from multiple computational evidences",1,392,393,1,403,404]
[null,"PSHAa0010",null,"Pseudoalteromonas haloplanktis TAC125","fadA","3-ketoacyl-CoA thiolase; (thiolase I, acetyl-CoA transferase), in complex with FadB catalyzes EC 2.3.1.16","_",0.96154,1.01781,43.25,{"v":6e-92,"d":"6.00E-92"},3,1,"2.4.1.1 : Biosynthesis ;","2.3.1.16","cytoplasm (undefined)","16.2 : Construct biomass (Anabolism) ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",8446033,"2a : Function from experimental evidences in other organisms",1,392,393,28,414,416]
[null,"CMR15v5_2683",null,"Ralstonia solanacearum CMR15","_","acetyl-CoA acetyltransferase","_",1.0229,1.02551,42.29,{"v":9e-92,"d":"9.00E-92"},4,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,390,393,1,390,392]
[null,"BN10v3_920035",null,"Tetrasphaera elongata Lp2","_","Putative 3-ketoacyl-CoA thiolase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",1.00737,1.04326,40.49,{"v":4e-91,"d":"4.00E-91"},1,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,392,393,3,406,407]
[null,"BN11v3_1350015",null,"Tetrasphaera australiensis Ben110","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",1.01232,1.0458,40.88,{"v":2E-90,"d":"2.00E-90"},2,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",1,392,393,1,405,406]
[null,"RALTA_A0405",null,"Cupriavidus taiwanensis LMG19424","_","putative 3-ketoacyl-CoA thiolase","_",1.01759,1.03053,39.26,{"v":5e-89,"d":"5.00E-89"},5,1,"1 : Metabolism ;","2.3.1.16","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,392,393,4,398,398]
[null,"BBta_5147",null,"Bradyrhizobium sp. BTAi1","pimB","Acetyl-CoA acetyltransferase with thiolase domain","_",1.01266,1.01781,41,{"v":7e-89,"d":"7.00E-89"},4,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,390,393,3,392,395]
[null,"BN381v2_90096",null,"Candidatus Microthrix parvicella RN1","_","Thiolase","_",1.015,1.03308,41.63,{"v":9e-89,"d":"9.00E-89"},3,2,"_","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","1699931, 2191949, 2204034","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,393,1,399,400]
[null,"CMR15v5_0432",null,"Ralstonia solanacearum CMR15","fadA","3-ketoacyl-CoA thiolase (Fatty acid oxidation complex beta subunit) (Beta-ketothiolase) (Acetyl-CoA acyltransferase)","_",1.01504,1.03053,39.51,{"v":8e-88,"d":"8.00E-88"},5,1,"1 : Metabolism ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.16","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","11356168, 11696182, 14630959, 15979881, 9490742","2a : Function from experimental evidences in other organisms",1,392,393,5,399,399]
[null,"AZOLI_p30357",null,"Azospirillum lipoferum 4B","phbA1","acetyl-CoA acetyltransferase with thiolase domain (Beta-ketothiolase)","_",1.00254,1.04233,40.61,{"v":9e-88,"d":"9.00E-88"},2,1,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.-","2 : Cytoplasmic","3.1 : Biosynthesis ;","e : enzyme","12039753, 7582015","1c : Function from experimental evidences in the studied genus",1,392,393,1,378,378]
[null,"Rmet_0387",null,"Cupriavidus metallidurans CH34","fadA","acetyl-CoA C-acyltransferase","_",1.01759,1.03053,39.51,{"v":2E-87,"d":"2.00E-87"},5,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.16","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,393,4,398,398]
[null,"BRADO2393",null,"Bradyrhizobium sp. ORS278","_","putative acetyl-CoA acyltransferase","_",1.02927,1.07379,40.76,{"v":3e-87,"d":"3.00E-87"},4,1,"_","2.3.1.16","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,392,393,1,410,410]
[null,"BN11v3_1360003",null,"Tetrasphaera australiensis Ben110","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase)","_",0.99491,1.01034,39.9,{"v":6e-87,"d":"6.00E-87"},3,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",17189250,"3 : Putative function from multiple computational evidences",2,390,393,4,385,387]
[null,"AZCBGv1_p150132",null,"Azospirillum brasilense CBG497","phaA","Beta-ketothiolase (acetyl-CoA acetyltransferase with thiolase domain)(Acetyl-CoA C-acyltransferase)","_",0.9313,0.94574,42.08,{"v":8e-87,"d":"8.00E-87"},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",28,392,393,38,387,387]
[null,"BN13v1_370004",null,"Tetrasphaera jenkinsii Ben74","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase)","_",0.99746,1.01818,40.05,{"v":9e-87,"d":"9.00E-87"},3,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",17189250,"3 : Putative function from multiple computational evidences",2,390,393,4,383,385]
[null,"ACIAD0334",null,"Acinetobacter baylyi ADP1","fadA","3-ketoacyl-CoA thiolase (Fatty oxidation complex beta subunit) (Beta-ketothiolase) (Acetyl-CoA acyltransferase)","2.3.1.155-RXN ; KETOACYLCOATHIOL-RXN ; METHYLACETOACETYLCOATHIOL-RXN ;",1.01018,1.01795,41.06,{"v":4e-86,"d":"4.00E-86"},7,2,"1.1.2 : fatty acids ;","2.3.1.16","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,392,393,7,390,390]
[null,"RALTA_B0510",null,"Cupriavidus taiwanensis LMG19424","_","putative beta-ketoadipyl CoA thiolase with thiolase-like domain, phenylacetic acid degradation","_",1.02,1.03817,39.46,{"v":1e-85,"d":"1.00E-85"},3,1,"1.1.5.1 : Phenylacetic acid degradation ;","_","1 : Unknown","6 : Energy metabolism ;","e : enzyme","12846838, 9748275","3 : Putative function from multiple computational evidences",1,390,393,1,398,400]
[null,"BN10v3_1170012",null,"Tetrasphaera elongata Lp2","_","putative acetyl-CoA acetyltransferase (phaA)","_",0.81425,0.94675,46.88,{"v":1e-85,"d":"1.00E-85"},2,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,321,393,7,325,338]
[null,"HEAR2836",null,"Herminiimonas arsenicoxydans","fadA","3-ketoacyl-CoA thiolase (Fatty acid oxidation complex beta subunit) (Beta-ketothiolase) (Acetyl-CoA acyltransferase)","_",1.01759,1.03053,38.52,{"v":5e-85,"d":"5.00E-85"},2,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.16","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","11356168, 11696182, 14630959, 15979881, 9490742","2a : Function from experimental evidences in other organisms",1,392,393,5,398,398]
[null,"ACIAD2988",null,"Acinetobacter baylyi ADP1","_","putative thiolase; putative acyl-CoA thiolase","_",1.03234,1.05598,40.48,{"v":6e-85,"d":"6.00E-85"},8,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,392,393,2,402,402]
[null,"MARHY2410",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","paaJ","ketoadipyl CoA thiolase subunit","_",1.02736,1.05089,40.92,{"v":5e-84,"d":"5.00E-84"},6,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.16","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,392,393,4,402,402]
[null,"FRAAL4934",null,"Frankia alni ACN14a","fadA","3-ketoacyl-CoA thiolase; (thiolase I, acetyl-CoA transferase)","_",1.03526,1.0458,39.42,{"v":8e-84,"d":"8.00E-84"},3,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16","1 : Unknown","3.2 : Degradation ;","e : enzyme",2191949,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,393,1,397,397]
[null,"THI_3002",null,"Thiomonas sp. 3As","PED1","3-ketoacyl-CoA thiolase 2 (Beta- ketothiolase 2) (Acetyl-CoA acyltransferase 2)","_",1.01754,1.03308,38.67,{"v":9e-84,"d":"9.00E-84"},5,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.16","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","11356168, 11696182, 14630959, 15979881, 9490742","2a : Function from experimental evidences in other organisms",1,392,393,5,399,399]
[null,"SCFA_v1_1130010",null,"Ca. Phosphitivorax anaerolimi F81","fadA","acetyl-CoA C-acyltransferase","_",1.02993,1.05089,39.71,{"v":2e-83,"d":"2.00E-83"},5,1,"_","2.3.1.16","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,393,393,1,401,401]
[null,"RALTA_A1580",null,"Cupriavidus taiwanensis LMG19424","fadA","3-ketoacyl-CoA thiolase; (thiolase I, acetyl-CoA transferase)","_",1.03053,1.03316,39.51,{"v":5e-83,"d":"5.00E-83"},6,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 7.1 : Cytoplasm ;","2.3.1.16","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,392,393,1,392,392]
[null,"BRADO0983",null,"Bradyrhizobium sp. ORS278","pimB","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",1.01772,1.0229,38.31,{"v":1e-81,"d":"1.00E-81"},5,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",2883171,"2a : Function from experimental evidences in other organisms",1,390,393,1,392,395]
[null,"Spro_4857",null,"Serratia proteamaculans 568","atoB","3-ketoacyl-CoA thiolase / acetyl-CoA acetyltransferase","_",1.03562,1.03827,39.56,{"v":1e-81,"d":"1.00E-81"},6,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16","2 : Cytoplasmic","3.2 : Degradation ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,390,393,1,390,392]
[null,"BN42v3_90051",null,"Mycobacterium canettii STB-K","fadA","Putative Acetyl-CoA Acetyltransferase FadA6 (Acetoacetyl-CoA Thiolase)","_",1.01018,1.0285,39.04,{"v":7e-81,"d":"7.00E-81"},3,1,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","11929527, 12657046, 12775759, 15928073","3 : Putative function from multiple computational evidences",1,392,393,1,386,386]
[null,"BBta_7072",null,"Bradyrhizobium sp. BTAi1","pimB","Acetyl-CoA acetyltransferase with thiolase domain","_",1.01772,1.0229,38.31,{"v":8e-81,"d":"8.00E-81"},6,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,390,393,1,392,395]
[null,"BN44v3_110048",null,"Mycobacterium canettii STB-D","fadA","Putative Acetyl-CoA Acetyltransferase FadA6 (Acetoacetyl-CoA Thiolase)","_",1.01018,1.0285,38.79,{"v":1e-80,"d":"1.00E-80"},3,1,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","11929527, 12657046, 12775759, 15928073","3 : Putative function from multiple computational evidences",1,392,393,1,386,386]
[null,"BN43v3_90054",null,"Mycobacterium canettii STB-L","fadA","Putative Acetyl-CoA Acetyltransferase FadA6 (Acetoacetyl-CoA Thiolase)","_",1.01018,1.0285,38.79,{"v":1e-80,"d":"1.00E-80"},3,1,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","11929527, 12657046, 12775759, 15928073","3 : Putative function from multiple computational evidences",1,392,393,1,386,386]
[null,"BN45v3_100051",null,"Mycobacterium canettii STB-J","fadA","Putative Acetyl-CoA Acetyltransferase FadA6 (Acetoacetyl-CoA Thiolase)","_",1.01018,1.0285,39.04,{"v":2e-80,"d":"2.00E-80"},3,1,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","11929527, 12657046, 12775759, 15928073","3 : Putative function from multiple computational evidences",1,392,393,1,386,386]
[null,"BN12v2_800001",null,"Tetrasphaera japonica T1-X7","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase)","_",1.03308,1.04103,38.92,{"v":2e-77,"d":"2.00E-77"},3,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",17189250,"3 : Putative function from multiple computational evidences",1,392,393,1,390,390]
[null,"BN42v3_20639",null,"Mycobacterium canettii STB-K","fadA","Putative acyl-CoA thiolase FadA","_",1.02978,1.05598,38.31,{"v":8e-77,"d":"8.00E-77"},4,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",2,392,393,3,403,403]
[null,"BN43v3_20310",null,"Mycobacterium canettii STB-L","fadA","Putative acyl-CoA thiolase FadA","_",1.01467,1.05598,38.07,{"v":1e-76,"d":"1.00E-76"},4,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",2,392,393,9,409,409]
[null,"Rmet_5432",null,"Cupriavidus metallidurans CH34","_","acetyl-CoA acetyltransferase","_",1.00763,1.0102,35.61,{"v":3e-76,"d":"3.00E-76"},2,1,"_","2.3.1.16","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,393,1,392,392]
[null,"BN44v3_10940",null,"Mycobacterium canettii STB-D","fadA","Putative acyl-CoA thiolase FadA","_",1.01467,1.05598,38.07,{"v":4e-76,"d":"4.00E-76"},4,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",2,392,393,9,409,409]
[null,"BN45v3_20150",null,"Mycobacterium canettii STB-J","fadA","Putative acyl-CoA thiolase FadA","_",1.00728,1.05598,37.83,{"v":6e-76,"d":"6.00E-76"},4,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",2,392,393,12,412,412]
[null,"BN10v3_810005",null,"Tetrasphaera elongata Lp2","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",0.99256,1.01781,39.5,{"v":1e-74,"d":"1.00E-74"},3,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,391,393,5,393,403]
[null,"BN45v3_100041",null,"Mycobacterium canettii STB-J","fadA","Putative acetyl-CoA acetyltransferase FadA5 (acetoacetyl-CoA thiolase)","_",1.04071,1.04604,39.36,{"v":1e-74,"d":"1.00E-74"},5,1,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","12657046, 17635188","3 : Putative function from multiple computational evidences",1,392,393,1,391,391]
[null,"FRAAL2097",null,"Frankia alni ACN14a","fadA","3-ketoadipyl CoA thiolase","_",1.00253,1.00763,38.64,{"v":9e-74,"d":"9.00E-74"},9,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.16","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,391,393,1,384,395]
[null,"METDI4034",null,"Methylobacterium extorquens DM4","_","putative acetyl-CoA acyltransferase (Fatty oxidation complex beta subunit) (3-ketoacyl-CoA thiolase) (Beta-ketothiolase) (fadA-like)","_",1.00964,1.06616,36.04,{"v":1E-73,"d":"1.00E-73"},2,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.16","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","1699931, 7961399","3 : Putative function from multiple computational evidences",1,392,393,14,415,415]
[null,"BN43v3_90044",null,"Mycobacterium canettii STB-L","fadA","Putative acetyl-CoA acetyltransferase FadA5 (acetoacetyl-CoA thiolase)","_",1.03053,1.03581,39.26,{"v":1E-73,"d":"1.00E-73"},5,1,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","12657046, 17635188","3 : Putative function from multiple computational evidences",5,392,393,5,391,391]
[null,"Rmet_5156",null,"Cupriavidus metallidurans CH34","paaE","beta-ketoadipyl CoA thiolase","_",1.03053,1.03316,36.05,{"v":2E-73,"d":"2.00E-73"},3,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.16","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,393,1,392,392]
[null,"BN42v3_90041",null,"Mycobacterium canettii STB-K","fadA","Putative acetyl-CoA acetyltransferase FadA5 (acetoacetyl-CoA thiolase)","_",1.04071,1.04604,39.36,{"v":8E-73,"d":"8.00E-73"},5,1,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","12657046, 17635188","3 : Putative function from multiple computational evidences",1,392,393,1,391,391]
[null,"ACIAD1569",null,"Acinetobacter baylyi ADP1","_","putative 3-ketoacyl-CoA thiolase/acetyl-CoA acetyltransferase","_",0.99746,1.01292,36.73,{"v":3e-72,"d":"3.00E-72"},9,1,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,390,393,1,384,387]
[null,"BN11v3_4910007",null,"Tetrasphaera australiensis Ben110","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",0.99504,1.02036,38.15,{"v":4e-72,"d":"4.00E-72"},4,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,391,393,5,393,403]
[null,"BRADO6724",null,"Bradyrhizobium sp. ORS278","_","putative acyl-CoA thiolase","_",1.06219,1.08651,36.07,{"v":6e-72,"d":"6.00E-72"},7,2,"_","2.3.1.16","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,392,393,1,402,402]
[null,"BN44v3_110038",null,"Mycobacterium canettii STB-D","fadA","Putative acetyl-CoA acetyltransferase FadA5 (acetoacetyl-CoA thiolase)","_",1.03053,1.03581,39.01,{"v":3e-71,"d":"3.00E-71"},5,1,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","12657046, 17635188","3 : Putative function from multiple computational evidences",5,392,393,5,391,391]
[null,"BN13v1_130025",null,"Tetrasphaera jenkinsii Ben74","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",0.99752,1.0229,38.06,{"v":4e-71,"d":"4.00E-71"},4,2,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",2,393,393,6,395,403]
[null,"Rmet_5510",null,"Cupriavidus metallidurans CH34","_","beta-ketoadipyl CoA thiolase","_",1.03731,1.06107,36.21,{"v":4E-70,"d":"4.00E-70"},4,2,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,393,1,402,402]
[null,"BSU10350",null,"Bacillus subtilis 168","yhfS","acetyl-CoA C-acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.98982,1.06868,36.25,{"v":3e-67,"d":"3.00E-67"},3,2,"2.4 : Metabolism of lipids ;","2.3.1.9","1 : Unknown","_","e : enzyme","12368242, 23840410","1a : Function from experimental evidences in the studied strain",5,390,393,4,361,364]
[null,"BN381v2_330040",null,"Candidatus Microthrix parvicella RN1","_","putative acetyl-CoA acetyltransferase","_",1.00763,1.02857,37.12,{"v":4e-67,"d":"4.00E-67"},5,2,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","18246303, 10416645, 1987116, 2670936","3 : Putative function from multiple computational evidences",1,392,393,1,385,385]
[null,"RALSYv5_mp0378",null,"Ralstonia syzygii R24","_","putative 3-ketoacyl-CoA thiolase / acetyl-CoA acetyltransferase (fragment)","_",0.43511,0.93443,38.6,{"v":5e-35,"d":"5.00E-35"},1,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16, 2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",220,390,393,12,181,183]
[null,"RALSYv5_0673",null,"Ralstonia syzygii R24","fadI","fragment of 3-ketoacyl-CoA thiolase (Fatty acid oxidation complex subunit beta) (Beta-ketothiolase) (Acetyl-CoA acyltransferase) (Acyl- CoA ligase) (ACSs) (part 2)","_",0.13232,0.88136,38.46,3e-08,8,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",339,390,393,1,52,59]
[]
["AZ49_05690","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",null,"Clostridium difficile 630","thlA1","Acetoacetyl-CoA thiolase 1","_",0.99746,1.00512,61.07,{"v":3e-169,"d":"3.00E-169"},1,2,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","11075929, 2191949","1c : Function from experimental evidences in the studied genus",1,393,394,1,391,391]
[null,"CLOSTRIBL3_v1_12838",null,"Clostridiaceae BL-3","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",1,1.0051,60.41,{"v":1e-164,"d":"1.00E-164"},1,2,"_","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","7867955, 11075929, 11466286, 1685080","2a : Function from experimental evidences in other organisms",1,393,394,1,392,392]
[null,"CD630_26760",null,"Clostridium difficile 630","thlA2","Acetoacetyl-CoA thiolase 2","_",1,1.0051,55.33,{"v":1E-153,"d":"1.00E-153"},2,2,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","11075929, 2191949","1c : Function from experimental evidences in the studied genus",1,393,394,1,392,392]
[null,"HEAR0577",null,"Herminiimonas arsenicoxydans","phbA","acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.98496,0.99746,55.22,{"v":2e-153,"d":"2.00E-153"},1,2,"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)",1,393,394,9,399,399]
[null,"MARHY3102",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","phbA","acetyl-CoA acetyltransferase with thiolase domain, PHB biosynthesis","_",1,1.0051,55.84,{"v":1E-150,"d":"1.00E-150"},1,2,"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",1,393,394,1,392,392]
[null,"AZOLI_2388",null,"Azospirillum lipoferum 4B","phbA3","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.99746,1.00512,56.23,{"v":2e-148,"d":"2.00E-148"},1,2,"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",1,393,394,1,390,391]
[null,"METDI4272",null,"Methylobacterium extorquens DM4","phaA","beta-ketothiolase","_",0.99492,0.99492,55.1,{"v":1e-147,"d":"1.00E-147"},1,2,"1.1 : Carbon compound utilization ; 1.7.37 : C1 assimilation, serine pathway ;","2.3.1.16","2 : Cytoplasmic","_","e : enzyme",11208803,"1b : Function from experimental evidences in the studied species",3,394,394,6,394,394]
[null,"Rmet_1357",null,"Cupriavidus metallidurans CH34","phaA","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",1,1.00254,54.57,{"v":1e-147,"d":"1.00E-147"},1,2,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,393,394,1,392,393]
[null,"CLOSTRIBL4_v1_1867",null,"Clostridiales BL-4","thlA","acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.9218,0.98731,56.04,{"v":2e-147,"d":"2.00E-147"},1,2,"_","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","7867955, 11075929","2a : Function from experimental evidences in other organisms",5,392,394,32,418,422]
[null,"RALTA_A1351",null,"Cupriavidus taiwanensis LMG19424","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",1,1.00254,54.82,{"v":2e-147,"d":"2.00E-147"},1,2,"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",1,393,394,1,392,393]
[null,"Spro_0592",null,"Serratia proteamaculans 568","atoB","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.98254,1,55.08,{"v":6e-147,"d":"6.00E-147"},1,2,"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)",1,393,394,9,400,401]
[null,"THI_1641",null,"Thiomonas sp. 3As","phbA1","acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",1,1.0051,54.82,{"v":4e-146,"d":"4.00E-146"},1,2,"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",1,393,394,1,392,392]
[null,"BN874v1_850028",null,"Candidatus Contendobacter odensis Run_B_J11","phaA","Acetyl-CoA acetyltransferase","_",1,1.00254,54.31,{"v":8e-145,"d":"8.00E-145"},1,2,"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)",1,393,394,1,392,393]
[null,"CMR15v5_2547",null,"Ralstonia solanacearum CMR15","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",1,1.00254,53.55,{"v":1e-144,"d":"1.00E-144"},1,2,"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",1,393,394,1,392,393]
[null,"PP_4636",null,"Pseudomonas putida KT2440","yqeF","acetyl-CoA acetyltransferase","METHYLACETOACETYLCOATHIOL-RXN ; RXN-12561 ; ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",1,1.0051,53.55,{"v":2e-144,"d":"2.00E-144"},1,2,"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",1,393,394,1,392,392]
[null,"RM41v1_110012",null,"Sinorhizobium sp. Rm41","phbA","acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98985,0.99237,54.36,{"v":3e-144,"d":"3.00E-144"},1,2,"1.5.4 : Fatty acid and phosphatidic acid ; 1.7 : Central intermediary metabolism ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ; 16.2 : Construct biomass (Anabolism) ;","e : enzyme",7582015,"1b : Function from experimental evidences in the studied species",5,394,394,7,393,393]
[null,"BRADO0562",null,"Bradyrhizobium sp. ORS278","phbA","acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.99239,0.99239,54.99,{"v":1e-143,"d":"1.00E-143"},1,2,"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)",3,393,394,6,393,394]
[null,"PSEEN4635",null,"Pseudomonas entomophila L48","phbA","acetyl-CoA acetyltransferase","_",0.96806,1,53.55,{"v":4e-143,"d":"4.00E-143"},1,2,"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",1,393,394,15,406,407]
[null,"NT26v4_3604",null,"Rhizobium sp. NT-26","phbA","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98985,0.99237,53.59,{"v":5e-142,"d":"5.00E-142"},1,2,"1.5.4 : Fatty acid and phosphatidic acid ; 1.3 : Energy metabolism (carbon) ; 7.1 : Cytoplasm ;","2.3.1.9","1 : Unknown","16.2 : Construct biomass (Anabolism) ; 6 : Energy metabolism ;","e : enzyme",7582015,"2b : Function from indirect experimental evidences (e.g. phenotypes)",5,394,394,7,393,393]
[null,"BN873v1_100077",null,"Candidatus Competibacter denitrificans Run_A_D11","phaA","Acetyl-CoA acetyltransferase","_",1,1.00254,52.28,{"v":7e-142,"d":"7.00E-142"},1,2,"_","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",1,393,394,1,392,393]
[null,"CLOSTRIBL6_v1_0127",null,"Clostridiales BL-6","phaA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99747,1,53.05,{"v":2e-139,"d":"2.00E-139"},1,2,"_","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","16352833, 18246303, 19016856, 28956599","2a : Function from experimental evidences in other organisms",2,392,394,3,394,395]
[null,"MGMSRv2_1838",null,"Magnetospirillum gryphiswaldense MSR-1 v2","phbA","acetyl-CoA acetyltransferase containing thiolase domain (Acetoacetyl-CoA thiolase)","_",0.99746,1.00769,51.15,{"v":2e-135,"d":"2.00E-135"},1,2,"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)",1,393,394,1,390,390]
[null,"ECIAI1_1489",null,"Escherichia coli IAI1","_","putative acetyl-CoA acetyltransferase","_",0.98504,1.00254,51.14,{"v":3E-132,"d":"3.00E-132"},1,2,"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",1,393,394,1,393,401]
[null,"AZOLI_p10676",null,"Azospirillum lipoferum 4B","phbA2","Acetyl-CoA acetyltransferase with thiolase domain (Beta-ketothiolase)","_",0.99746,1,51.4,{"v":2e-130,"d":"2.00E-130"},1,2,"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",3,394,394,4,393,393]
[null,"VIBNIv4_B0465",null,"Vibrio nigripulchritudo SFn1","phbA","acetyl-CoA acetyltransferase","_",0.99751,1.01777,48.13,{"v":3e-130,"d":"3.00E-130"},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",1,392,394,1,399,402]
[null,"NBG4_v1_200004",null,"Candidatus Sulfobium mesophilum","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.98987,0.99239,47.83,{"v":2e-129,"d":"2.00E-129"},1,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.9","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",23468890,"2a : Function from experimental evidences in other organisms",3,393,394,10,395,395]
[null,"CLOSTRIBL4_v1_1159",null,"Clostridiales BL-4","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",0.99748,1.00508,50,{"v":2e-126,"d":"2.00E-126"},2,2,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","7867955, 11075929, 11466286, 1685080","2a : Function from experimental evidences in other organisms",6,394,394,8,397,397]
[null,"ECK2842",null,"Escherichia coli K12","yqeF","Acetyl-CoA acetyltransferase","_",0.99746,1,49.36,{"v":8e-126,"d":"8.00E-126"},2,2,"1.7 : Central intermediary metabolism ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",7763384,"2a : Function from experimental evidences in other organisms",1,393,394,1,391,393]
[null,"NIDE3116",null,"Candidatus Nitrospira defluvii","atoB","Acetyl-CoA acetyltransferase","_",0.98985,0.98985,46.92,{"v":3E-124,"d":"3.00E-124"},1,2,"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",4,393,394,7,394,394]
[null,"BSU24170",null,"Bacillus subtilis 168","mmgA","degradative acetoacetyl-CoA thiolase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99746,1,48.35,{"v":3E-124,"d":"3.00E-124"},1,2,"2.4 : Metabolism of lipids ;","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","16352833, 18246303, 19016856, 28956599","1a : Function from experimental evidences in the studied strain",1,392,394,1,391,393]
[null,"CLOSTRIBL6_v1_0556",null,"Clostridiales BL-6","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",1.00504,1.01269,49.62,{"v":4e-124,"d":"4.00E-124"},2,2,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","7867955, 11075929, 11466286, 1685080","2a : Function from experimental evidences in other organisms",1,394,394,3,397,397]
[null,"RPSI07_1730",null,"Ralstonia solanacearum PSI07","phaA","acetyl-CoA acetyltransferase, thiolase-like","_",1.00254,1.00254,48.35,{"v":1e-123,"d":"1.00E-123"},2,2,"1.7 : Central intermediary metabolism ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,394,394,3,394,394]
[null,"HELPY_0683",null,"Helicobacter pylori B38","atoB","Acetyl coenzyme A acetyltransferase","_",0.99746,1.00512,47.84,{"v":3e-123,"d":"3.00E-123"},1,2,"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",1,393,394,1,390,391]
[null,"ACIAD0694",null,"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 ;",0.99746,1.00512,48.35,{"v":4e-123,"d":"4.00E-123"},1,2,"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",1,392,394,1,389,391]
[null,"BN381v2_150043",null,"Candidatus Microthrix parvicella RN1","phaA","acetyl-CoA acetyltransferase","_",0.99492,0.99746,48.72,{"v":5e-123,"d":"5.00E-123"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","18246303, 10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",1,391,394,1,390,393]
[null,"RCFBPv4_1653",null,"Ralstonia solanacearum CFBP2957","phaA","acetyl-CoA acetyltransferase, thiolase-like","_",1.00254,1.00254,47.59,{"v":1e-122,"d":"1.00E-122"},2,2,"1.7 : Central intermediary metabolism ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",1685080,"2b : Function from indirect experimental evidences (e.g. phenotypes)",2,394,394,3,394,394]
[null,"BN424_3179",null,"Carnobacterium maltaromaticum LMA28 v1","thlA","Acetoacetyl-CoA thiolase","METHYLACETOACETYLCOATHIOL-RXN ; RXN-12561 ; ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99746,1.01028,49.62,{"v":2e-122,"d":"2.00E-122"},1,2,"_","2.3.1.9","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,393,394,1,388,389]
[null,"SCFA_v1_120020",null,"Ca. Phosphitivorax anaerolimi F81","yqeF","Acetyl-CoA acetyltransferase","_",1,1.0051,47.21,{"v":5e-121,"d":"5.00E-121"},3,2,"1.7 : Central intermediary metabolism ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",7763384,"2a : Function from experimental evidences in other organisms",1,393,394,1,391,392]
[null,"Rmet_1362",null,"Cupriavidus metallidurans CH34","bktB","acetyl-CoA acetyltransferase","_",1.00254,1.00254,47.85,{"v":7e-121,"d":"7.00E-121"},2,2,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,394,394,3,394,394]
[null,"METUNv2_520573",null,"Methyloversatilis universalis FAM5","phbA","Acetyl-CoA acetyltransferase","_",0.99747,1,46.7,{"v":4e-120,"d":"4.00E-120"},1,2,"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",2,394,394,5,395,395]
[null,"VIBNIv4_B1306",null,"Vibrio nigripulchritudo SFn1","phbA","acetyl-CoA acetyltransferase","_",1.00249,1.0203,45.27,{"v":7e-120,"d":"7.00E-120"},2,2,"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",1,393,394,1,400,401]
[null,"CLOSTRIBL3_v1_13111",null,"Clostridiaceae BL-3","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99746,1.00512,47.07,{"v":9E-120,"d":"9.00E-120"},2,2,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","7867955, 11075929, 11466286, 1685080","1c : Function from experimental evidences in the studied genus",1,392,394,1,390,391]
[null,"VS_II0585",null,"Vibrio tasmaniensis LGP32","_","Acetyl-CoA C acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99504,1.01777,44.14,{"v":6e-119,"d":"6.00E-119"},1,2,"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",1,392,394,1,399,403]
[null,"VIBNIv4_A1234",null,"Vibrio nigripulchritudo SFn1","phbA","Acetyl-CoA acetyltransferase","_",0.98985,0.98985,44.87,{"v":3e-118,"d":"3.00E-118"},1,2,"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",3,392,394,5,391,394]
[null,"AZOLI_p10029",null,"Azospirillum lipoferum 4B","atoB","acetyl-CoA acetyltransferase with thiolase domain","_",1.00761,1.01018,47.86,{"v":3e-118,"d":"3.00E-118"},2,2,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1 : Carbon compound utilization ; 1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ; 6.2 : Amino acids and amines ;","e : enzyme",7867955,"2a : Function from experimental evidences in other organisms",1,394,394,1,393,393]
[null,"PSEEN3197",null,"Pseudomonas entomophila L48","_","putative Acetoacetyl-CoA thiolase","_",1.01015,1.01015,46.73,{"v":7e-118,"d":"7.00E-118"},2,2,"1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.9","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,394,394,8,394,394]
[null,"BN874v1_1120001",null,"Candidatus Contendobacter odensis Run_B_J11","phaA","Acetyl-CoA acetyltransferase","_",0.995,1.01015,47.24,{"v":7e-118,"d":"7.00E-118"},2,1,"_","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",1,393,394,3,398,400]
[null,"MARHY2580",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","atoB","acetyl-CoA acetyltransferase","_",1,1,48.73,{"v":1E-117,"d":"1.00E-117"},2,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,394,394,5,394,394]
[null,"RPSI07_3138",null,"Ralstonia solanacearum PSI07","_","putative acetyl-CoA acetyltransferase with thiolase domain","_",0.99239,0.99491,48.59,{"v":2e-117,"d":"2.00E-117"},3,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,394,394,6,393,393]
[null,"RALTA_A0113",null,"Cupriavidus taiwanensis LMG19424","_","putative acetyl-CoA acetyltransferase with thiolase domain","_",1.00254,1.00765,47.34,{"v":2e-117,"d":"2.00E-117"},2,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,394,394,1,392,392]
[null,"PSHAa1586",null,"Pseudoalteromonas haloplanktis TAC125","atoB","acetyl-CoA acetyltransferase with thiolase domain, Acetoacetyl-CoA thiolase","_",0.95599,0.99239,47.83,{"v":1e-116,"d":"1.00E-116"},1,2,"_","2.3.1.9","cytoplasm (undefined)","_","e : enzyme",7867955,"2a : Function from experimental evidences in other organisms",5,394,394,22,409,409]
[null,"RCFBPv4_3139",null,"Ralstonia solanacearum CFBP2957","_","putative acetyl-CoA acetyltransferase with thiolase domain","_",0.99239,0.99491,48.59,{"v":1e-116,"d":"1.00E-116"},3,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,394,394,6,393,393]
[null,"BTCD_v1_1714",null,"Brochothrix thermosphacta CD337","mevB","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99746,1.01289,47.84,{"v":6e-116,"d":"6.00E-116"},1,2,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme",7763384,"2a : Function from experimental evidences in other organisms",1,393,394,1,387,388]
[null,"CMR15v5_0670",null,"Ralstonia solanacearum CMR15","_","putative acetyl-CoA acetyltransferase with thiolase domain","_",0.99239,0.99491,48.59,{"v":1e-115,"d":"1.00E-115"},2,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,394,394,6,393,393]
[null,"RALTA_A1359",null,"Cupriavidus taiwanensis LMG19424","bktB","acetyl-CoA acetyltransferase, thiolase","_",1.00254,1.00254,46.58,{"v":2e-115,"d":"2.00E-115"},3,2,"1.7 : Central intermediary metabolism ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",1685080,"2b : Function from indirect experimental evidences (e.g. phenotypes)",2,394,394,3,394,394]
[null,"Rmet_0106",null,"Cupriavidus metallidurans CH34","atoB","acetyl-CoA acetyltransferase","_",0.98731,0.98731,47.3,{"v":2e-114,"d":"2.00E-114"},3,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",5,392,394,7,392,394]
[null,"BN873v1_610042",null,"Candidatus Competibacter denitrificans Run_A_D11","phaA","Acetyl-CoA acetyltransferase","_",0.99751,1.01523,46.5,{"v":3e-114,"d":"3.00E-114"},2,1,"_","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",1,393,394,3,399,401]
[null,"pRALTA_0081",null,"Cupriavidus taiwanensis LMG19424","_","acetyl-CoA acetyltransferase","_",0.9875,1.00254,46.84,{"v":4e-114,"d":"4.00E-114"},1,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,392,394,10,398,400]
[null,"LEPBIa0355",null,"Leptospira biflexa serovar Patoc Patoc 1","thiL1","Putative acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.99746,1,47.07,{"v":1e-113,"d":"1.00E-113"},1,2,"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",1,392,394,1,389,393]
[null,"LFAv2_0052",null,"Legionella-Like Amoebal Pathogens 10","thlA","Acetyl-CoA acetyltransferase","_",0.98985,0.98985,42.56,{"v":3e-113,"d":"3.00E-113"},2,2,"_","2.3.1.9","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,392,394,5,392,394]
[null,"METUNv2_320010",null,"Methyloversatilis universalis FAM5","phbA2","Putative acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.98246,0.99492,47.96,{"v":2e-112,"d":"2.00E-112"},2,2,"1.3 : Energy metabolism (carbon) ;","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ; 15 : Cellular processes ;","e : enzyme","2670935, 2670936","2a : Function from experimental evidences in other organisms",5,394,394,9,397,399]
[null,"Atu3475",null,"Agrobacterium tumefaciens C58","fadAx","acetyl-CoA C-acetyltransferase","_",0.95388,0.99746,48.6,{"v":5e-111,"d":"5.00E-111"},1,2,"1 : Metabolism ;","_","2 : Cytoplasmic","_","e : enzyme",11251808,"2b : Function from indirect experimental evidences (e.g. phenotypes)",5,393,394,33,411,412]
[null,"PSEEN1165",null,"Pseudomonas entomophila L48","pcaF","beta-ketoadipyl CoA thiolase","_",1.0075,1.02284,48.14,{"v":7e-111,"d":"7.00E-111"},3,1,"1.1.1 : carbon compounds ;","2.3.1.9","Unknown","6 : Energy metabolism ;","e : enzyme",12534466,"2a : Function from experimental evidences in other organisms",1,394,394,1,400,400]
[null,"FRAAL5910",null,"Frankia alni ACN14a","atoB","acetyl-CoA acetyltransferase with thiolase domain","_",0.99241,0.99492,46.43,{"v":1e-110,"d":"1.00E-110"},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)",1,391,394,1,390,395]
[null,"ABSDF1999",null,"Acinetobacter baumannii SDF","catF","beta-ketoadipyl CoA thiolase","_",1.01478,1.04569,47.09,{"v":1e-110,"d":"1.00E-110"},2,2,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme",8125318,"2a : Function from experimental evidences in other organisms",1,394,394,3,403,406]
[null,"PSEEN3547",null,"Pseudomonas entomophila L48","fadAx","acetyl-CoA acetyltransferase with thiolase domain FadAx","_",0.99244,1,47.46,{"v":2e-110,"d":"2.00E-110"},4,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",11251808,"2b : Function from indirect experimental evidences (e.g. phenotypes)",5,394,394,9,396,397]
[null,"ABAYE1715",null,"Acinetobacter baumannii AYE","catF","beta-ketoadipyl CoA thiolase","_",1.0198,1.04569,46.84,{"v":2e-110,"d":"2.00E-110"},3,2,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme",8125318,"2a : Function from experimental evidences in other organisms",1,394,394,1,401,404]
[null,"ACIAD1706",null,"Acinetobacter baylyi ADP1","pcaF","beta-ketoadipyl CoA thiolase","2.3.1.155-RXN ; KETOACYLCOATHIOL-RXN ; RXN-3641 ;",1.00748,1.02538,48.02,{"v":2e-110,"d":"2.00E-110"},2,2,"_","2.3.1.-","1 : Unknown","_","e : enzyme","8125318, 7883173, 8063101, 3036773","1a : Function from experimental evidences in the studied strain",1,394,394,1,401,401]
[null,"ABSDF2022",null,"Acinetobacter baumannii SDF","pcaF","beta-ketoadipyl CoA thiolase","_",1.02233,1.04569,46.84,{"v":2e-110,"d":"2.00E-110"},3,2,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme",8125318,"2a : Function from experimental evidences in other organisms",1,394,394,3,403,403]
[null,"ABAYE1675",null,"Acinetobacter baumannii AYE","pcaF","beta-ketoadipyl CoA thiolase","_",1.02233,1.04569,46.36,{"v":2E-109,"d":"2.00E-109"},4,2,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme",8125318,"2a : Function from experimental evidences in other organisms",1,394,394,3,403,403]
[null,"PP_2215",null,"Pseudomonas putida KT2440","_","acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",0.99244,1,47.46,{"v":3e-109,"d":"3.00E-109"},3,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","4150713, 773366, 236278, 9904, 2883931","2a : Function from experimental evidences in other organisms",5,394,394,9,396,397]
[null,"ABAYE2367",null,"Acinetobacter baumannii AYE","paaJ","beta-ketoadipyl CoA thiolase with thiolase-like domain, phenylacetic acid degradation","_",1.00498,1.02538,47.03,{"v":3e-109,"d":"3.00E-109"},5,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","1 : Unknown","_","e : enzyme",9748275,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,394,1,401,402]
[null,"ACIAD1450",null,"Acinetobacter baylyi ADP1","catF","beta-ketoadipyl CoA thiolase","2.3.1.155-RXN ; KETOACYLCOATHIOL-RXN ; RXN-3641 ;",1.00748,1.02538,47.77,{"v":3e-109,"d":"3.00E-109"},3,2,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme",8125318,"1a : Function from experimental evidences in the studied strain",1,394,394,1,401,401]
[null,"Rmet_3669",null,"Cupriavidus metallidurans CH34","pcaF","acetyl-CoA acetyltransferase","_",1.0075,1.02284,45.91,{"v":4E-109,"d":"4.00E-109"},1,2,"1.1.2.7 : Acetoacetate degradation ;","_","1 : Unknown","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,394,394,1,400,400]
[null,"SCFA_v1_300017",null,"Ca. Phosphitivorax anaerolimi F81","thlA","Acetyl-CoA acetyltransferase","_",1.00959,1.06853,45.61,{"v":6e-109,"d":"6.00E-109"},4,2,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,394,1,417,417]
[null,"MARHY1170",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","thlA","acetyl-CoA acetyltransferase, Acetoacetyl-CoA thiolase","_",0.99239,0.99491,45.78,{"v":2e-108,"d":"2.00E-108"},3,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",7867955,"2a : Function from experimental evidences in other organisms",3,392,394,5,391,393]
[null,"ACIAD2516",null,"Acinetobacter baylyi ADP1","atoB","acetyl-CoA acetyltransferase with thiolase domain","ACETYL-COA-ACETYLTRANSFER-RXN ; METHYLACETOACETYLCOATHIOL-RXN ; RXN-12561 ; RHEA:21039 ;",0.99746,0.99746,44.78,{"v":2e-108,"d":"2.00E-108"},4,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.9","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","11075929, 18246303, 21209787","2a : Function from experimental evidences in other organisms",1,392,394,3,391,394]
[null,"ACIAD1612",null,"Acinetobacter baylyi ADP1","_","putative acetyl-CoA C-acetyltransferase with thiolase domain","_",1.00254,1.00509,44.81,{"v":3e-108,"d":"3.00E-108"},5,2,"1.1.1 : carbon compounds ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,392,394,4,391,393]
[null,"RALTA_B0208",null,"Cupriavidus taiwanensis LMG19424","pcaF","Beta-ketoadipyl CoA thiolase","_",1.0075,1.02284,45.41,{"v":8e-108,"d":"8.00E-108"},1,2,"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",1,394,394,1,400,400]
[null,"THI_0462",null,"Thiomonas sp. 3As","pcaF1","Beta-ketoadipyl CoA thiolase","_",1.0175,1.03299,44.72,{"v":9e-108,"d":"9.00E-108"},2,2,"1 : Metabolism ;","2.3.1.-","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",7961399,"2a : Function from experimental evidences in other organisms",1,394,394,1,400,400]
[null,"BN12v2_3170003",null,"Tetrasphaera japonica T1-X7","phaA","acetyl-CoA acetyltransferase (fadA) (Acetoacetyl-CoA thiolase) (beta-ketothiolase)","_",0.97739,0.98731,45.5,{"v":2e-106,"d":"2.00E-106"},1,2,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",5,391,394,7,393,398]
[null,"CMR15v5_2038",null,"Ralstonia solanacearum CMR15","pcaF","Beta-ketoadipyl-CoA thiolase","_",1.015,1.03046,45.07,{"v":4e-106,"d":"4.00E-106"},3,2,"_","2.3.1.-","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,394,1,400,400]
[null,"THI_3278",null,"Thiomonas sp. 3As","phbA2","acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.99492,1,46.43,{"v":6e-106,"d":"6.00E-106"},3,1,"1.3 : Energy metabolism (carbon) ;","2.3.1.9","2 : Cytoplasmic","15 : Cellular processes ; 6 : Energy metabolism ;","e : enzyme","2670935, 2670936","2a : Function from experimental evidences in other organisms",5,394,394,6,392,392]
[null,"BDBv6_10148",null,"Blood disease bacterium R229","pcaF","Beta-ketoadipyl-CoA thiolase","_",1.01,1.02538,45.54,{"v":7E-106,"d":"7.00E-106"},4,2,"_","2.3.1.-","1 : Unknown","6 : Energy metabolism ;","e : enzyme",7961399,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,394,1,400,400]
[null,"MGMSRv2_0194",null,"Magnetospirillum gryphiswaldense MSR-1 v2","atoB","acetyl-CoA acetyltransferase with thiolase domain","_",1,1.0051,46.7,{"v":2e-104,"d":"2.00E-104"},2,2,"1.1 : Carbon compound utilization ; 1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.3 : Amino acids ;","2.3.1.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","2670935, 2670936","2a : Function from experimental evidences in other organisms",5,394,394,7,391,392]
[null,"MARHY0270",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","paaJ","beta-ketoadipyl CoA thiolase with thiolase-like domain, phenylacetic acid degradation","_",1.0125,1.02792,46.17,{"v":7e-104,"d":"7.00E-104"},4,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","1 : Unknown","_","e : enzyme",7961399,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,394,1,400,400]
[null,"SCFA_v1_3830001",null,"Ca. Phosphitivorax butyraticus R76","atoB","fragment of acetyl-CoA acetyltransferase (part 2)","ACETYL-COA-ACETYLTRANSFER-RXN ;",0.91803,0.99492,45.92,{"v":9e-104,"d":"9.00E-104"},4,2,"1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,365,394,27,417,427]
[null,"BN13v1_460011",null,"Tetrasphaera jenkinsii Ben74","_","putative Acetyl-CoA acetyltransferase (beta-ketothiolase) (phaA)","_",0.97739,0.98731,45.76,{"v":2e-103,"d":"2.00E-103"},1,2,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","3 : Putative function from multiple computational evidences",5,391,394,7,393,398]
[null,"ECK1394",null,"Escherichia coli K12","paaE","beta-ketoadipyl CoA thiolase","RXN-3641 ; RXN0-6512 ;",1.01247,1.03046,43.84,{"v":3E-103,"d":"3.00E-103"},3,2,"1.1.5.1 : Phenylacetic acid degradation ;","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 17259607, 9748275","1a : Function from experimental evidences in the studied strain",1,394,394,1,401,401]
[null,"AZOLI_p40026",null,"Azospirillum lipoferum 4B","pcaF","Beta-ketoadipyl CoA thiolase","_",0.99015,1.0203,43.53,{"v":6E-103,"d":"6.00E-103"},1,2,"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",1,394,394,8,406,406]
[null,"Pars_0309",null,"Pyrobaculum arsenaticum DSM 13514","thlA","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.96806,1,45.69,{"v":7e-103,"d":"7.00E-103"},1,2,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11075929, 11466286, 1685080, 7867955","2a : Function from experimental evidences in other organisms",3,392,394,15,405,407]
[null,"PP_3280",null,"Pseudomonas putida KT2440","paaJ","3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase","RXN0-6512 ; RXN-3641 ; RHEA:34441 ; RHEA:19483 ;",0.98768,1.01777,45.39,{"v":1e-102,"d":"1.00E-102"},5,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-, 2.3.1.174","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","20660314, 17259607","2a : Function from experimental evidences in other organisms",3,394,394,8,406,406]
[null,"THI_3549",null,"Thiomonas sp. 3As","pcaF2","Beta-ketoadipyl CoA thiolase","_",0.99257,1.01777,45.14,{"v":1e-102,"d":"1.00E-102"},4,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","10766858, 12846838, 7961399, 9748275","2a : Function from experimental evidences in other organisms",2,393,394,5,403,404]
[null,"MGMSRv2_3177",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaE","beta-ketoadipyl CoA thiolase","_",1.01496,1.03299,43.98,{"v":7e-102,"d":"7.00E-102"},3,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","10766858, 12846838, 17259607, 9748275","2a : Function from experimental evidences in other organisms",1,394,394,1,401,401]
[null,"PSEEN2795",null,"Pseudomonas entomophila L48","pcaF-2","beta-ketoadipyl CoA thiolase","_",0.98522,1.01523,45,{"v":8e-102,"d":"8.00E-102"},5,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.9","Cytoplasmic","6 : Energy metabolism ;","e : enzyme","12534466, 15474299, 9600981","2a : Function from experimental evidences in other organisms",4,394,394,9,406,406]
[null,"AZOLI_p40258",null,"Azospirillum lipoferum 4B","paaJ","beta-ketoadipyl CoA thiolase","_",1.01244,1.03299,43.24,{"v":1e-101,"d":"1.00E-101"},2,2,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.-","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",1,394,394,1,402,402]
[null,"BN45v3_30404",null,"Mycobacterium canettii STB-J","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98477,0.99743,44.59,{"v":8e-101,"d":"8.00E-101"},1,2,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,391,394,1,386,389]
[null,"BSU32830",null,"Bacillus subtilis 168","fadA","acetyl-CoA C-acyltransferase","KETOACYLCOATHIOL-RXN ; RHEA:21564 ;",1.02284,1.03069,43.18,{"v":1E-100,"d":"1.00E-100"},2,1,"2.4 : Metabolism of lipids ;","2.3.1.16","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","1a : Function from experimental evidences in the studied strain",1,392,394,1,389,391]
[null,"BRADO0538",null,"Bradyrhizobium sp. ORS278","_","putative acetyl-CoA acetyltransferase (phbA/atoB/paaJ-like)","_",1,1.0203,44.78,{"v":2E-100,"d":"2.00E-100"},2,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,392,394,1,399,402]
[null,"BN11v3_1860009",null,"Tetrasphaera australiensis Ben110","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.97995,0.99239,45.52,{"v":2E-100,"d":"2.00E-100"},1,2,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",4,391,394,7,394,399]
[null,"XDD1v4_3927",null,"Xenorhabdus doucetiae FRM16","paaJ","protein PaaJ; Beta-ketoadipyl-CoA thiolase","_",1.0099,1.03553,43.87,{"v":5e-100,"d":"5.00E-100"},1,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.174","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,394,394,1,403,404]
[null,"BN42v3_21228",null,"Mycobacterium canettii STB-K","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98477,0.99743,44.33,{"v":5e-100,"d":"5.00E-100"},1,2,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,391,394,1,386,389]
[null,"BRADO3134",null,"Bradyrhizobium sp. ORS278","atoB","acetyl-CoA acetyltransferase with thiolase domain","_",0.98734,0.98985,43.33,{"v":6e-100,"d":"6.00E-100"},3,2,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1 : Carbon compound utilization ; 1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,393,394,8,394,395]
[null,"VIBNIv4_A0031",null,"Vibrio nigripulchritudo SFn1","fadA","3-ketoacyl-CoA thiolase","_",1.0203,1.03608,45.02,{"v":8e-100,"d":"8.00E-100"},2,2,"1.1.2.6 : Aerobic fatty acid oxidation pathway ; 7.1 : Cytoplasm ;","2.3.1.16","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","1699931, 2191949, 2204034","2a : Function from experimental evidences in other organisms",1,394,394,1,387,388]
[null,"BN44v3_11488",null,"Mycobacterium canettii STB-D","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98477,0.99743,44.33,{"v":9e-100,"d":"9.00E-100"},1,2,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,391,394,1,386,389]
[null,"BN43v3_30420",null,"Mycobacterium canettii STB-L","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.98477,0.99743,44.33,{"v":9e-100,"d":"9.00E-100"},1,2,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",5,391,394,1,386,389]
[null,"RALTA_B1528",null,"Cupriavidus taiwanensis LMG19424","_","putative acetyl-CoA acetyltransferase with thiolase domain","_",1.00746,1.02792,42.47,{"v":1E-99,"d":"1.00E-99"},2,2,"1.7 : Central intermediary metabolism ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,393,394,1,401,402]
[null,"NIDE3104",null,"Candidatus Nitrospira defluvii","fadA","3-ketoacyl-CoA thiolase","_",1.00758,1.01269,42.86,{"v":3e-99,"d":"3.00E-99"},2,2,"1.1.2.4 : Anaerobic fatty acid oxidation pathway ; 7.1 : Cytoplasm ;","2.3.1.16","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","12535077, 1354266, 15229654, 2191949, 6350283","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,394,1,396,396]
[null,"MARHY2135",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","fadA","3-ketoacyl-CoA thiolase; (thiolase I, acetyl-CoA transferase), in complex with FadB catalyzes Catalyzes the final step of fatty acid oxidation","_",1.0203,1.02813,44.53,{"v":1e-98,"d":"1.00E-98"},5,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 7.1 : Cytoplasm ;","2.3.1.16","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",12115060,"2a : Function from experimental evidences in other organisms",2,394,394,6,391,391]
[null,"Spro_3039",null,"Serratia proteamaculans 568","pcaF","Beta-ketoadipyl-CoA thiolase","_",1.0225,1.03807,43.52,{"v":2e-98,"d":"2.00E-98"},2,2,"1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.-","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,394,1,400,400]
[null,"EFER_1634",null,"Escherichia fergusonii ATCC 35469T","paaJ","Beta-ketoadipyl CoA thiolase","_",1.01,1.02538,43.07,{"v":2e-97,"d":"2.00E-97"},4,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.9","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9748275,"2a : Function from experimental evidences in other organisms",1,394,394,1,400,400]
[null,"XPG1v4_0713",null,"Xenorhabdus poinarii G6","pcaF","Beta-ketoadipyl-CoA thiolase","_",1.0325,1.04822,43.34,{"v":7e-97,"d":"7.00E-97"},1,1,"_","2.3.1.174","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,394,1,400,400]
[null,"ABAYE2307",null,"Acinetobacter baumannii AYE","dcaF","beta-ketoadipyl CoA thiolase","_",1.00998,1.02792,39.26,{"v":2E-95,"d":"2.00E-95"},6,2,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",1,394,394,1,400,401]
[null,"BN381v2_70026",null,"Candidatus Microthrix parvicella RN1","_","Acetyl-CoA acetyltransferase","_",1.0199,1.04061,42.44,{"v":1e-94,"d":"1.00E-94"},2,2,"_","2.3.1.16","2 : Cytoplasmic","_","e : enzyme","1699931, 2191949, 2204034","2a : Function from experimental evidences in other organisms",1,394,394,1,401,402]
[null,"ABSDF1531",null,"Acinetobacter baumannii SDF","_","fragment of putative Beta-ketoadipyl CoA thiolase (part 2)","_",0.89673,0.90355,46.07,{"v":1e-94,"d":"1.00E-94"},4,2,"1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.9","1 : Unknown","_","e : enzyme","_","5 : Unknown function",46,394,394,45,397,397]
[null,"VCRLGP8v1_930035",null,"Vibrio crassostreae LGP8","paaE","beta-ketoadipyl CoA thiolase","RXN0-6512 ; RXN-3641 ;",1,1.0203,42.54,{"v":5e-94,"d":"5.00E-94"},4,2,"1.1.5.1 : Phenylacetic acid degradation ;","_","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","10766858, 12846838, 17259607, 9748275","2a : Function from experimental evidences in other organisms",2,392,394,4,400,402]
[null,"RALTA_A1469",null,"Cupriavidus taiwanensis LMG19424","_","putative 3-ketoacyl-CoA thiolase / acetyl-CoA acetyltransferase","_",1.03299,1.03827,43.49,{"v":7E-94,"d":"7.00E-94"},4,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16, 2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,394,394,1,392,392]
[null,"ACIAD1689",null,"Acinetobacter baylyi ADP1","dcaF","beta-ketoadipyl CoA thiolase","2.3.1.155-RXN ; KETOACYLCOATHIOL-RXN ; RXN-3641 ;",1.00499,1.02284,39.7,{"v":8e-93,"d":"8.00E-93"},6,2,"_","2.3.1.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921, 11571189","1a : Function from experimental evidences in the studied strain",1,394,394,1,400,401]
[null,"AZOLI_p30161",null,"Azospirillum lipoferum 4B","phbA4","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.99239,1.00514,41.18,{"v":3e-91,"d":"3.00E-91"},1,2,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.9","2 : Cytoplasmic","3.1 : Biosynthesis ;","e : enzyme","7582015, 1396692","2a : Function from experimental evidences in other organisms",5,392,394,6,387,389]
[null,"BN381v2_90096",null,"Candidatus Microthrix parvicella RN1","_","Thiolase","_",1.0175,1.03299,42.75,{"v":2E-90,"d":"2.00E-90"},3,1,"_","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","1699931, 2191949, 2204034","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,394,1,399,400]
[null,"BN874v1_1250003",null,"Candidatus Contendobacter odensis Run_B_J11","_","putative acetyl-CoA acetyltransferase","_",1.03015,1.04061,40.73,{"v":3e-90,"d":"3.00E-90"},3,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.16","2 : Cytoplasmic","_","e : enzyme","1699931, 2191949, 2204034","3 : Putative function from multiple computational evidences",1,394,394,5,398,398]
[null,"BN873v1_20049",null,"Candidatus Competibacter denitrificans Run_A_D11","_","putative acetyl-CoA acetyltransferase","_",1.03015,1.04061,40,{"v":1E-89,"d":"1.00E-89"},3,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.16","2 : Cytoplasmic","_","e : enzyme","1699931, 2191949, 2204034","3 : Putative function from multiple computational evidences",1,394,394,5,398,398]
[null,"PSHAa0010",null,"Pseudoalteromonas haloplanktis TAC125","fadA","3-ketoacyl-CoA thiolase; (thiolase I, acetyl-CoA transferase), in complex with FadB catalyzes EC 2.3.1.16","_",0.96875,1.02284,42.93,{"v":1E-89,"d":"1.00E-89"},3,2,"2.4.1.1 : Biosynthesis ;","2.3.1.16","cytoplasm (undefined)","16.2 : Construct biomass (Anabolism) ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",8446033,"2a : Function from experimental evidences in other organisms",1,394,394,28,414,416]
[null,"BN11v3_1350015",null,"Tetrasphaera australiensis Ben110","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",1.01232,1.04315,41.36,{"v":6e-89,"d":"6.00E-89"},2,2,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",1,394,394,1,405,406]
[null,"Pars_1071",null,"Pyrobaculum arsenaticum DSM 13514","_","putative acetyl-CoA acetyltransferase","_",1.01493,1.03553,37.25,{"v":7e-89,"d":"7.00E-89"},2,2,"1.3 : Energy metabolism (carbon) ;","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ; 15 : Cellular processes ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,394,394,8,402,402]
[null,"PSEEN3727",null,"Pseudomonas entomophila L48","fadA","3-ketoacyl-CoA thiolase (Fatty oxidation complex beta subunit) (Beta-ketothiolase) (Acetyl-CoA acyltransferase)","_",1.01777,1.02558,43.39,{"v":1e-88,"d":"1.00E-88"},6,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16","Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,394,394,6,391,391]
[null,"ACIAD0334",null,"Acinetobacter baylyi ADP1","fadA","3-ketoacyl-CoA thiolase (Fatty oxidation complex beta subunit) (Beta-ketothiolase) (Acetyl-CoA acyltransferase)","2.3.1.155-RXN ; KETOACYLCOATHIOL-RXN ; METHYLACETOACETYLCOATHIOL-RXN ;",1.01269,1.02308,41.85,{"v":2e-88,"d":"2.00E-88"},7,1,"1.1.2 : fatty acids ;","2.3.1.16","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,394,394,7,390,390]
[null,"BN13v1_250034",null,"Tetrasphaera jenkinsii Ben74","_","Putative 3-ketoacyl-CoA thiolase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",1.01238,1.03807,40.83,{"v":4e-88,"d":"4.00E-88"},2,2,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","3 : Putative function from multiple computational evidences",1,394,394,1,403,404]
[null,"Rmet_1853",null,"Cupriavidus metallidurans CH34","atoB","acetyl-CoA acetyltransferase / thiolase","_",1.03299,1.03827,42.01,{"v":5e-88,"d":"5.00E-88"},4,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","_","c : carrier","_","3 : Putative function from multiple computational evidences",1,394,394,1,392,392]
[null,"BN13v1_370004",null,"Tetrasphaera jenkinsii Ben74","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase)","_",1.00254,1.02597,40,{"v":1e-86,"d":"1.00E-86"},3,2,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",17189250,"3 : Putative function from multiple computational evidences",2,394,394,4,385,385]
[null,"BN12v2_1200011",null,"Tetrasphaera japonica T1-X7","_","Putative 3-ketoacyl-CoA thiolase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",1.01728,1.04569,40.78,{"v":2e-86,"d":"2.00E-86"},2,2,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","3 : Putative function from multiple computational evidences",1,394,394,1,404,405]
[null,"BN45v3_30114",null,"Mycobacterium canettii STB-J","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",1,1.04061,40.49,{"v":2e-86,"d":"2.00E-86"},2,2,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",1,394,394,6,409,410]
[null,"BN42v3_20922",null,"Mycobacterium canettii STB-K","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",1.01235,1.04061,40.49,{"v":4e-86,"d":"4.00E-86"},2,2,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",1,394,394,1,404,405]
[null,"BN44v3_11190",null,"Mycobacterium canettii STB-D","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",1,1.04061,40.49,{"v":5e-86,"d":"5.00E-86"},2,2,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",1,394,394,6,409,410]
[null,"BN43v3_30127",null,"Mycobacterium canettii STB-L","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",1,1.04061,40.49,{"v":5e-86,"d":"5.00E-86"},2,2,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",1,394,394,6,409,410]
[null,"CMR15v5_2683",null,"Ralstonia solanacearum CMR15","_","acetyl-CoA acetyltransferase","_",1.02792,1.03316,40.49,{"v":9e-85,"d":"9.00E-85"},4,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,394,1,390,392]
[null,"HEAR2836",null,"Herminiimonas arsenicoxydans","fadA","3-ketoacyl-CoA thiolase (Fatty acid oxidation complex beta subunit) (Beta-ketothiolase) (Acetyl-CoA acyltransferase)","_",1.03015,1.04061,39.76,{"v":3e-84,"d":"3.00E-84"},2,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.16","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","11356168, 11696182, 14630959, 15979881, 9490742","2a : Function from experimental evidences in other organisms",1,394,394,5,398,398]
[null,"RALTA_A0405",null,"Cupriavidus taiwanensis LMG19424","_","putative 3-ketoacyl-CoA thiolase","_",1.03266,1.04315,39.42,{"v":4e-84,"d":"4.00E-84"},5,2,"1 : Metabolism ;","2.3.1.16","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,394,394,4,398,398]
[null,"BN10v3_920035",null,"Tetrasphaera elongata Lp2","_","Putative 3-ketoacyl-CoA thiolase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",1.00737,1.04061,38.78,{"v":1E-83,"d":"1.00E-83"},1,2,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,394,394,3,406,407]
[null,"MARHY2410",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","paaJ","ketoadipyl CoA thiolase subunit","_",1.04975,1.07107,39.1,{"v":8e-83,"d":"8.00E-83"},6,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.16","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,394,394,4,402,402]
[null,"RALTA_B0510",null,"Cupriavidus taiwanensis LMG19424","_","putative beta-ketoadipyl CoA thiolase with thiolase-like domain, phenylacetic acid degradation","_",1.0375,1.0533,38.8,{"v":1e-82,"d":"1.00E-82"},3,2,"1.1.5.1 : Phenylacetic acid degradation ;","_","1 : Unknown","6 : Energy metabolism ;","e : enzyme","12846838, 9748275","3 : Putative function from multiple computational evidences",1,394,394,1,400,400]
[null,"AZCBGv1_p150132",null,"Azospirillum brasilense CBG497","phaA","Beta-ketothiolase (acetyl-CoA acetyltransferase with thiolase domain)(Acetyl-CoA C-acyltransferase)","_",0.98985,1.00775,40.51,{"v":5e-82,"d":"5.00E-82"},1,2,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.16","2 : Cytoplasmic","3.1 : Biosynthesis ;","e : enzyme","12039753, 7582015","1b : Function from experimental evidences in the studied species",5,392,394,14,385,387]
[null,"Rmet_0387",null,"Cupriavidus metallidurans CH34","fadA","acetyl-CoA C-acyltransferase","_",1.03266,1.04315,38.69,{"v":8e-82,"d":"8.00E-82"},5,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.16","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,394,4,398,398]
[null,"BN11v3_1360003",null,"Tetrasphaera australiensis Ben110","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase)","_",1,1.01809,37.56,{"v":3e-81,"d":"3.00E-81"},3,2,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",17189250,"3 : Putative function from multiple computational evidences",2,394,394,4,387,387]
[null,"CMR15v5_0432",null,"Ralstonia solanacearum CMR15","fadA","3-ketoacyl-CoA thiolase (Fatty acid oxidation complex beta subunit) (Beta-ketothiolase) (Acetyl-CoA acyltransferase)","_",1.03008,1.04315,37.23,{"v":3e-80,"d":"3.00E-80"},5,2,"1 : Metabolism ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.16","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","11356168, 11696182, 14630959, 15979881, 9490742","2a : Function from experimental evidences in other organisms",1,394,394,5,399,399]
[null,"AZOLI_p30357",null,"Azospirillum lipoferum 4B","phbA1","acetyl-CoA acetyltransferase with thiolase domain (Beta-ketothiolase)","_",1,1.04233,37.06,{"v":5E-80,"d":"5.00E-80"},2,2,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.-","2 : Cytoplasmic","3.1 : Biosynthesis ;","e : enzyme","12039753, 7582015","1c : Function from experimental evidences in the studied genus",1,392,394,1,376,378]
[null,"ACIAD2988",null,"Acinetobacter baylyi ADP1","_","putative thiolase; putative acyl-CoA thiolase","_",1.03731,1.05838,37.41,{"v":3E-79,"d":"3.00E-79"},8,2,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,394,394,2,402,402]
[null,"Spro_4857",null,"Serratia proteamaculans 568","atoB","3-ketoacyl-CoA thiolase / acetyl-CoA acetyltransferase","_",1.03299,1.03827,39.07,{"v":3E-79,"d":"3.00E-79"},6,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16","2 : Cytoplasmic","3.2 : Degradation ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,394,1,390,392]
[null,"BN10v3_1170012",null,"Tetrasphaera elongata Lp2","_","putative acetyl-CoA acetyltransferase (phaA)","_",0.80964,0.94379,44.83,{"v":6E-79,"d":"6.00E-79"},2,2,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,321,394,7,325,338]
[null,"BRADO2393",null,"Bradyrhizobium sp. ORS278","_","putative acetyl-CoA acyltransferase","_",1.0439,1.08629,37.15,{"v":1e-77,"d":"1.00E-77"},4,2,"_","2.3.1.16","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,394,394,1,410,410]
[null,"BRADO0983",null,"Bradyrhizobium sp. ORS278","pimB","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",1.03544,1.03807,38.39,{"v":2e-77,"d":"2.00E-77"},5,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",2883171,"2a : Function from experimental evidences in other organisms",1,394,394,1,394,395]
[null,"BBta_7072",null,"Bradyrhizobium sp. BTAi1","pimB","Acetyl-CoA acetyltransferase with thiolase domain","_",1.03797,1.04061,38.29,{"v":1e-76,"d":"1.00E-76"},4,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,394,394,1,394,395]
[null,"THI_3002",null,"Thiomonas sp. 3As","PED1","3-ketoacyl-CoA thiolase 2 (Beta- ketothiolase 2) (Acetyl-CoA acyltransferase 2)","_",1.03008,1.04315,37.47,{"v":1e-76,"d":"1.00E-76"},5,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.16","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","11356168, 11696182, 14630959, 15979881, 9490742","2a : Function from experimental evidences in other organisms",1,394,394,5,399,399]
[null,"RALTA_A1580",null,"Cupriavidus taiwanensis LMG19424","fadA","3-ketoacyl-CoA thiolase; (thiolase I, acetyl-CoA transferase)","_",1.03553,1.04082,38.24,{"v":2e-76,"d":"2.00E-76"},6,2,"1.1.2.1 : Degradation of short-chain fatty acids ; 7.1 : Cytoplasm ;","2.3.1.16","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,394,394,1,392,392]
[null,"FRAAL4934",null,"Frankia alni ACN14a","fadA","3-ketoacyl-CoA thiolase; (thiolase I, acetyl-CoA transferase)","_",1.03275,1.04061,37.07,{"v":3e-76,"d":"3.00E-76"},4,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16","1 : Unknown","3.2 : Degradation ;","e : enzyme",2191949,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,394,1,397,397]
[null,"SCFA_v1_1130010",null,"Ca. Phosphitivorax anaerolimi F81","fadA","acetyl-CoA C-acyltransferase","_",1.03242,1.05076,37.68,{"v":6e-76,"d":"6.00E-76"},5,2,"_","2.3.1.16","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,392,394,1,398,401]
[null,"BBta_5147",null,"Bradyrhizobium sp. BTAi1","pimB","Acetyl-CoA acetyltransferase with thiolase domain","_",1.03797,1.04061,36.83,{"v":9e-76,"d":"9.00E-76"},6,2,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,392,394,3,392,395]
[null,"BN42v3_20639",null,"Mycobacterium canettii STB-K","fadA","Putative acyl-CoA thiolase FadA","_",1.03722,1.06091,38.28,{"v":5e-75,"d":"5.00E-75"},3,2,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",3,394,394,4,403,403]
[null,"BN43v3_20310",null,"Mycobacterium canettii STB-L","fadA","Putative acyl-CoA thiolase FadA","_",1.022,1.06091,38.04,{"v":8e-75,"d":"8.00E-75"},3,2,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",3,394,394,10,409,409]
[null,"Rmet_5432",null,"Cupriavidus metallidurans CH34","_","acetyl-CoA acetyltransferase","_",1.01523,1.02041,36.5,{"v":8e-75,"d":"8.00E-75"},2,2,"_","2.3.1.16","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,394,1,392,392]
[null,"BRADO6724",null,"Bradyrhizobium sp. ORS278","_","putative acyl-CoA thiolase","_",1.04478,1.06599,35.95,{"v":2e-74,"d":"2.00E-74"},7,1,"_","2.3.1.16","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,394,394,1,402,402]
[null,"BN44v3_10940",null,"Mycobacterium canettii STB-D","fadA","Putative acyl-CoA thiolase FadA","_",1.022,1.06091,38.04,{"v":2e-74,"d":"2.00E-74"},3,2,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",3,394,394,10,409,409]
[null,"BN45v3_20150",null,"Mycobacterium canettii STB-J","fadA","Putative acyl-CoA thiolase FadA","_",1.01456,1.06091,37.56,{"v":1E-73,"d":"1.00E-73"},3,2,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",3,394,394,13,412,412]
[null,"BN10v3_810005",null,"Tetrasphaera elongata Lp2","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",0.99504,1.01777,36.66,{"v":1E-73,"d":"1.00E-73"},3,2,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,392,394,5,392,403]
[null,"BN44v3_110048",null,"Mycobacterium canettii STB-D","fadA","Putative Acetyl-CoA Acetyltransferase FadA6 (Acetoacetyl-CoA Thiolase)","_",1.01015,1.03109,36.18,{"v":5e-73,"d":"5.00E-73"},4,2,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","11929527, 12657046, 12775759, 15928073","3 : Putative function from multiple computational evidences",1,394,394,1,386,386]
[null,"BN43v3_90054",null,"Mycobacterium canettii STB-L","fadA","Putative Acetyl-CoA Acetyltransferase FadA6 (Acetoacetyl-CoA Thiolase)","_",1.01015,1.03109,36.18,{"v":5e-73,"d":"5.00E-73"},4,2,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","11929527, 12657046, 12775759, 15928073","3 : Putative function from multiple computational evidences",1,394,394,1,386,386]
[null,"BN42v3_90051",null,"Mycobacterium canettii STB-K","fadA","Putative Acetyl-CoA Acetyltransferase FadA6 (Acetoacetyl-CoA Thiolase)","_",1.01015,1.03109,35.93,{"v":1e-72,"d":"1.00E-72"},4,2,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","11929527, 12657046, 12775759, 15928073","3 : Putative function from multiple computational evidences",1,394,394,1,386,386]
[null,"BN45v3_100051",null,"Mycobacterium canettii STB-J","fadA","Putative Acetyl-CoA Acetyltransferase FadA6 (Acetoacetyl-CoA Thiolase)","_",1.01015,1.03109,35.93,{"v":2e-72,"d":"2.00E-72"},4,2,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","11929527, 12657046, 12775759, 15928073","3 : Putative function from multiple computational evidences",1,394,394,1,386,386]
[null,"ACIAD1569",null,"Acinetobacter baylyi ADP1","_","putative 3-ketoacyl-CoA thiolase/acetyl-CoA acetyltransferase","_",1.00508,1.02326,36.62,{"v":3e-72,"d":"3.00E-72"},9,2,"1.1.1 : carbon compounds ;","2.3.1.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,392,394,1,384,387]
[null,"Rmet_5156",null,"Cupriavidus metallidurans CH34","paaE","beta-ketoadipyl CoA thiolase","_",1.03553,1.04082,36.52,{"v":5e-72,"d":"5.00E-72"},3,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.16","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,394,1,392,392]
[null,"BN12v2_800001",null,"Tetrasphaera japonica T1-X7","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase)","_",1.03553,1.04615,36.76,{"v":1e-71,"d":"1.00E-71"},3,2,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",17189250,"3 : Putative function from multiple computational evidences",1,394,394,1,390,390]
[null,"BN11v3_4910007",null,"Tetrasphaera australiensis Ben110","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",0.99504,1.01777,36.91,{"v":1e-71,"d":"1.00E-71"},4,2,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,392,394,5,392,403]
[null,"BN13v1_130025",null,"Tetrasphaera jenkinsii Ben74","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",0.99752,1.0203,37.06,{"v":1e-71,"d":"1.00E-71"},4,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",2,394,394,6,394,403]
[null,"BN381v2_330040",null,"Candidatus Microthrix parvicella RN1","_","putative acetyl-CoA acetyltransferase","_",1.01015,1.03377,37.69,{"v":1e-71,"d":"1.00E-71"},4,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","18246303, 10416645, 1987116, 2670936","3 : Putative function from multiple computational evidences",1,394,394,1,385,385]
[null,"Rmet_5510",null,"Cupriavidus metallidurans CH34","_","beta-ketoadipyl CoA thiolase","_",1.04726,1.06853,35.63,{"v":2e-71,"d":"2.00E-71"},4,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,394,394,1,402,402]
[null,"FRAAL2097",null,"Frankia alni ACN14a","fadA","3-ketoadipyl CoA thiolase","_",1.01266,1.01523,36.25,{"v":3e-71,"d":"3.00E-71"},7,2,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.16","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,390,394,2,381,395]
[null,"METDI4034",null,"Methylobacterium extorquens DM4","_","putative acetyl-CoA acyltransferase (Fatty oxidation complex beta subunit) (3-ketoacyl-CoA thiolase) (Beta-ketothiolase) (fadA-like)","_",1.01205,1.06599,35.95,{"v":6e-71,"d":"6.00E-71"},2,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.16","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","1699931, 7961399","3 : Putative function from multiple computational evidences",1,394,394,14,415,415]
[null,"BSU10350",null,"Bacillus subtilis 168","yhfS","acetyl-CoA C-acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99746,1.07967,36.64,{"v":9e-70,"d":"9.00E-70"},3,1,"2.4 : Metabolism of lipids ;","2.3.1.9","1 : Unknown","_","e : enzyme","12368242, 23840410","1a : Function from experimental evidences in the studied strain",3,394,394,2,363,364]
[null,"BN45v3_100041",null,"Mycobacterium canettii STB-J","fadA","Putative acetyl-CoA acetyltransferase FadA5 (acetoacetyl-CoA thiolase)","_",1.03046,1.03836,36.21,{"v":9e-67,"d":"9.00E-67"},5,2,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","12657046, 17635188","3 : Putative function from multiple computational evidences",1,394,394,1,391,391]
[null,"BN43v3_90044",null,"Mycobacterium canettii STB-L","fadA","Putative acetyl-CoA acetyltransferase FadA5 (acetoacetyl-CoA thiolase)","_",1.0203,1.02813,36.57,{"v":7e-65,"d":"7.00E-65"},5,2,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","12657046, 17635188","3 : Putative function from multiple computational evidences",5,394,394,5,391,391]
[null,"BN42v3_90041",null,"Mycobacterium canettii STB-K","fadA","Putative acetyl-CoA acetyltransferase FadA5 (acetoacetyl-CoA thiolase)","_",1.03553,1.04348,35.78,{"v":8e-64,"d":"8.00E-64"},5,2,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","12657046, 17635188","3 : Putative function from multiple computational evidences",1,394,394,1,391,391]
[null,"BN44v3_110038",null,"Mycobacterium canettii STB-D","fadA","Putative acetyl-CoA acetyltransferase FadA5 (acetoacetyl-CoA thiolase)","_",1.0203,1.02813,35.82,{"v":2e-62,"d":"2.00E-62"},5,2,"1 : lipid metabolism ;","2.3.1.9","1 : Unknown","_","e : enzyme","12657046, 17635188","3 : Putative function from multiple computational evidences",5,394,394,5,391,391]
[null,"RALSYv5_mp0378",null,"Ralstonia syzygii R24","_","putative 3-ketoacyl-CoA thiolase / acetyl-CoA acetyltransferase (fragment)","_",0.45939,0.98907,38.67,{"v":2E-35,"d":"2.00E-35"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16, 2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",213,392,394,5,181,183]
[null,"RALSYv5_0673",null,"Ralstonia syzygii R24","fadI","fragment of 3-ketoacyl-CoA thiolase (Fatty acid oxidation complex subunit beta) (Beta-ketothiolase) (Acetyl-CoA acyltransferase) (Acyl- CoA ligase) (ACSs) (part 2)","_",0.13959,0.9322,41.82,9e-08,8,2,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",339,393,394,1,53,59]
[]
["AZ49_10655","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 ;",1,1.00709,60.21,{"v":3e-118,"d":"3.00E-118"},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",1,284,284,1,282,282]
[null,"BSU24160","_","Bacillus subtilis 168","mmgB","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.98258,0.99296,54.61,{"v":6e-108,"d":"6.00E-108"},1,1,"2.4 : Metabolism of lipids ;","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8759838, 18461320, 28956599","1a : Function from experimental evidences in the studied strain",1,282,284,3,282,287]
[null,"CD630_10580",null,"Clostridium difficile 630","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.99296,1.00356,58.16,{"v":4E-107,"d":"4.00E-107"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","6 : Energy metabolism ;","e : enzyme","15991056, 18060402, 7576770","1c : Function from experimental evidences in the studied genus",3,284,284,2,281,281]
[null,"CLOSTRIBL4_v1_1869",null,"Clostridiales BL-4","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.99648,1.01434,59.01,{"v":4e-105,"d":"4.00E-105"},1,1,"_","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",3,284,284,2,279,279]
[null,"MGMSRv2_3942","_","Magnetospirillum gryphiswaldense MSR-1 v2","mmgB","3-hydroxybutyryl-CoA dehydrogenase (Beta- hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.96918,0.99648,54.42,{"v":6e-104,"d":"6.00E-104"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",8759838,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,283,284,4,284,292]
[null,"CLOSTRIBL6_v1_0126","_","Clostridiales BL-6","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.99296,1.01439,54.26,{"v":6E-98,"d":"6.00E-98"},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",3,283,284,2,278,278]
[null,"AZCBGv1_p190002","_","Azospirillum brasilense CBG497","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.98288,1.01056,51.22,{"v":1E-97,"d":"1.00E-97"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.1.1.157","2 : Cytoplasmic","3.1 : Biosynthesis ;","e : enzyme","11466286, 12597275, 8655474, 8759838, 8969508","2a : Function from experimental evidences in other organisms",1,284,284,4,285,292]
[null,"AZOLI_p50063","_","Azospirillum lipoferum 4B","hbdA2","3-hydroxybutyryl-CoA dehydrogenase","_",0.96875,0.98239,52.33,{"v":1E-97,"d":"1.00E-97"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme",8655474,"2a : Function from experimental evidences in other organisms",6,284,284,12,288,288]
[null,"RALTA_A0220","_","Cupriavidus taiwanensis LMG19424","_","3-HYDROXYBUTYRYL-COA DEHYDROGENASE","_",0.98944,0.98944,50.53,{"v":1e-94,"d":"1.00E-94"},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)",4,284,284,6,284,284]
[null,"NBG4_v1_200002",null,"Candidatus Sulfobium mesophilum","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:22432 ;",0.99296,1,49.29,{"v":5e-94,"d":"5.00E-94"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",23468890,"2a : Function from experimental evidences in other organisms",1,282,284,3,281,282]
[null,"Rmet_0212","_","Cupriavidus metallidurans CH34","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.98944,0.98944,50.53,{"v":1e-93,"d":"1.00E-93"},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",4,284,284,6,284,284]
[null,"BDBv6_40067","_","Blood disease bacterium R229","_","3-HYDROXYBUTYRYL-COA DEHYDROGENASE","_",0.98944,0.98944,49.82,{"v":4e-93,"d":"4.00E-93"},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)",4,284,284,6,284,284]
[null,"BRADO3444","_","Bradyrhizobium sp. ORS278","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.98944,0.99293,50.89,{"v":4E-92,"d":"4.00E-92"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","2 : Cytoplasmic","16.7 : Manage energy ;","e : enzyme",1444364,"2a : Function from experimental evidences in other organisms",4,284,284,5,283,283]
[null,"Mchl_1824","_","Methylobacterium extorquens CM4","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.95222,0.98239,51.25,{"v":4E-92,"d":"4.00E-92"},1,1,"_","1.1.1.157","1 : Unknown","_","e : enzyme","2687255, 8655474","2a : Function from experimental evidences in other organisms",4,282,284,8,284,293]
[null,"METDI2209","_","Methylobacterium extorquens DM4","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.92079,0.98239,51.25,{"v":6e-92,"d":"6.00E-92"},1,1,"_","1.1.1.157","1 : Unknown","_","e : enzyme","2687255, 8655474","2a : Function from experimental evidences in other organisms",4,282,284,18,294,303]
[null,"CMR15v5_0701","_","Ralstonia solanacearum CMR15","_","3-HYDROXYBUTYRYL-COA DEHYDROGENASE","_",0.98944,0.98944,49.11,{"v":6e-92,"d":"6.00E-92"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","1 : Unknown","3.2 : Degradation ; 6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,284,284,6,284,284]
[null,"ADVE02_v2_10866","_","Methylosinus trichosporium OB3b","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.95563,0.98592,50,{"v":4e-91,"d":"4.00E-91"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,282,284,7,284,293]
[null,"RM41v1_680007","_","Sinorhizobium sp. Rm41","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta- hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.96207,0.98239,49.46,{"v":2e-89,"d":"2.00E-89"},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)",4,282,284,5,281,290]
[null,"BBta_4257","_","Bradyrhizobium sp. BTAi1","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.96127,1.00738,50.18,{"v":2e-88,"d":"2.00E-88"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","2 : Cytoplasmic","16.7 : Manage energy ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",12,284,284,1,271,271]
[null,"BN381v2_100132","_","Candidatus Microthrix parvicella RN1","_","putative dehydrogenase","_",0.94059,1.00352,47.72,{"v":2E-87,"d":"2.00E-87"},1,1,"_","_","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","12846838, 8001771, 1699931","3 : Putative function from multiple computational evidences",2,284,284,23,303,303]
[null,"NIDE3117","_","Candidatus Nitrospira defluvii","paaH","3-hydroxybutyryl-CoA dehydrogenase","_",0.94218,0.97535,49.1,{"v":9e-87,"d":"9.00E-87"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","1 : Unknown","6 : Energy metabolism ; 3.2 : Degradation ;","e : enzyme","10766858, 12846838, 2204034, 8001771, 9748275","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,282,284,11,285,294]
[null,"PSEEN3198","_","Pseudomonas entomophila L48","paaH","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.98592,1.01818,46.79,{"v":4e-85,"d":"4.00E-85"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,282,284,1,275,275]
[null,"PSHAa0399","_","Pseudoalteromonas haloplanktis TAC125","bhbD","3-hydroxybutyryl-CoA dehydrogenase (Beta- hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.99296,1.00356,44.68,{"v":3e-77,"d":"3.00E-77"},1,1,"_","1.1.1.157","unknown","_","e : enzyme",8001771,"2a : Function from experimental evidences in other organisms",3,282,284,2,281,281]
[null,"Npun_R3442","_","Nostoc punctiforme ATCC 29133; PCC 73102","_","3-hydroxybutyryl-CoA dehydrogenase","_",0.97222,0.98592,42.14,{"v":4E-73,"d":"4.00E-73"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,283,284,7,285,288]
[null,"BN12v2_1150036","_","Tetrasphaera japonica T1-X7","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD))","_",0.47466,0.98944,42.35,{"v":3e-72,"d":"3.00E-72"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,282,284,6,284,592]
[null,"BN10v3_1170022","_","Tetrasphaera elongata Lp2","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD))","_",0.47716,0.99296,44.33,{"v":5e-72,"d":"5.00E-72"},1,1,"_","1.1.1.157","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,282,284,312,591,591]
[null,"BN11v3_1490005","_","Tetrasphaera australiensis Ben110","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD)","_",0.47128,0.98239,47.31,{"v":1e-71,"d":"1.00E-71"},1,1,"_","1.1.1.157","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",1444364,"3 : Putative function from multiple computational evidences",4,282,284,315,591,592]
[null,"BN13v1_460001","_","Tetrasphaera jenkinsii Ben74","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD))","_",0.47466,0.98944,43.06,{"v":2e-71,"d":"2.00E-71"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,282,284,6,284,592]
[null,"BN42v3_20192","_","Mycobacterium canettii STB-K","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",1,1.00704,41.26,{"v":2e-71,"d":"2.00E-71"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",1,282,284,5,286,286]
[null,"BN44v3_10518","_","Mycobacterium canettii STB-D","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",1,1.00704,40.91,{"v":8e-71,"d":"8.00E-71"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",1,282,284,5,286,286]
[null,"BN43v3_10507","_","Mycobacterium canettii STB-L","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",1,1.00704,40.91,{"v":8e-71,"d":"8.00E-71"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",1,282,284,5,286,286]
[null,"BN45v3_10517","_","Mycobacterium canettii STB-J","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",1,1.00704,40.56,{"v":2E-70,"d":"2.00E-70"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",1,282,284,5,286,286]
[null,"SCFA_v1_130011",null,"Ca. Phosphitivorax anaerolimi F81","paaF","Enoyl-CoA hydratase/isomerase family (3-hydroxybutyryl-CoA dehydratase (Crotonase))","RXN-11667 ;",0.43009,0.99648,44.88,{"v":4E-70,"d":"4.00E-70"},3,1,"_","4.2.1.17, 5.1.2.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,283,284,4,284,658]
[null,"BN874v1_720038",null,"Candidatus Contendobacter odensis Run_B_J11","_","putative hydroxyacyl/hydroxybutyrl -CoA dehydrogenase","RXN0-2044 ;",0.94966,0.99648,42.4,{"v":7e-70,"d":"7.00E-70"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,283,284,3,283,298]
[null,"NIDE3103",null,"Candidatus Nitrospira defluvii","_","putative 3-hydroxyacyl-CoA dehydrogenase","_",0.69042,0.98944,41.99,{"v":4e-68,"d":"4.00E-68"},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",3,283,284,5,281,407]
[null,"BN873v1_210050",null,"Candidatus Competibacter denitrificans Run_A_D11","_","putative hydroxyacyl/hydroxybutyrl -CoA dehydrogenase","_",0.94966,0.99648,42.4,{"v":5e-68,"d":"5.00E-68"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,283,284,3,283,298]
[null,"AZOLI_p40260",null,"Azospirillum lipoferum 4B","paaH","3-hydroxybutyryl-CoA dehydrogenase","_",0.50722,0.98944,41.28,{"v":1e-66,"d":"1.00E-66"},1,1,"1.1.1 : carbon compounds ; 1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.-","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9748275,"2a : Function from experimental evidences in other organisms",4,283,284,10,288,554]
[null,"PSEEN2793",null,"Pseudomonas entomophila L48","paaC","3-hydroxyacyl-CoA dehydrogenase phaC","_",0.55709,0.99648,40.99,{"v":1e-65,"d":"1.00E-65"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.-","Cytoplasmic","6 : Energy metabolism ;","e : enzyme","12534466, 15474299, 9600981","2a : Function from experimental evidences in other organisms",2,283,284,11,291,508]
[null,"XDD1v4_1792",null,"Xenorhabdus doucetiae FRM16","xcnB","3-hydroxyacyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",0.99298,0.99648,38.52,{"v":1e-65,"d":"1.00E-65"},1,1,"_","1.1.1.157","1 : Unknown","15.11 : Biosynthesis of natural products ;","e : enzyme","16349198, 1955881","2a : Function from experimental evidences in other organisms",3,283,284,2,281,285]
[null,"SCFA_v1_3390003",null,"Ca. Phosphitivorax butyraticus R76","hbd","3-hydroxybutyryl-CoA dehydrogenase (modular protein)","_",0.43009,0.99648,42.05,{"v":2e-65,"d":"2.00E-65"},3,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,283,284,4,284,658]
[null,"XNC1_1710","_","Xenorhabdus nematophila ATCC19061","xcnB","3-hydroxyacyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",0.99649,1,37.68,{"v":7e-65,"d":"7.00E-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",3,283,284,2,281,285]
[null,"ABAYE2368",null,"Acinetobacter baumannii AYE","paaH","3-hydroxybutyryl-CoA dehydrogenase, phenylacetic acid degradation","_",0.55469,1,39.79,{"v":9e-65,"d":"9.00E-65"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","_","e : enzyme",9748275,"2a : Function from experimental evidences in other organisms",2,284,284,9,290,512]
[null,"PP_3282",null,"Pseudomonas putida KT2440","paaH","3-hydroxyadipyl-CoA dehydrogenase","RXN0-2044 ; RHEA:16199 ;",0.5604,0.99648,42.4,{"v":2e-64,"d":"2.00E-64"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.35","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","12846838, 15137080, 20660314, 10766858, 22961985, 22398448, 21247899, 9748275","2a : Function from experimental evidences in other organisms",3,284,284,9,289,505]
[null,"ACIAD1690",null,"Acinetobacter baylyi ADP1","dcaH","dehydrogenase","1.1.1.259-RXN ; METHELENE-THMPT-OXI-RXN ; RXN0-2044 ;",0.5604,0.99648,41.34,{"v":3e-63,"d":"3.00E-63"},1,1,"_","1.1.1.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921, 11571189","1a : Function from experimental evidences in the studied strain",1,282,284,5,285,505]
[null,"MGMSRv2_3175",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaH","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.5505,0.97887,40.65,{"v":4e-63,"d":"4.00E-63"},3,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",6,282,284,12,287,505]
[null,"SCFA_v1_100019",null,"Ca. Phosphitivorax anaerolimi F81","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.74934,1,42.25,{"v":7e-63,"d":"7.00E-63"},4,1,"_","1.1.1.157","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,283,284,3,282,379]
[null,"CLOSTRIBL3_v1_13113",null,"Clostridiaceae BL-3","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.99653,1.01056,41.46,{"v":2e-62,"d":"2.00E-62"},2,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 25112316","1c : Function from experimental evidences in the studied genus",1,282,284,3,287,288]
[null,"THI_0464","_","Thiomonas sp. 3As","_","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.56574,1,39.44,{"v":7e-61,"d":"7.00E-61"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",2,284,284,11,291,502]
[null,"ABAYE2306",null,"Acinetobacter baumannii AYE","dcaH","dehydrogenase","_",0.55819,0.99648,40.28,{"v":4e-60,"d":"4.00E-60"},2,1,"1.1.1 : carbon compounds ;","1.1.1.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",1,282,284,5,285,507]
[null,"CLOSTRIBL4_v1_1158",null,"Clostridiales BL-4","hbd","3-hydroxybutyryl-CoA dehydrogenase","RXN-12570 ; RHEA:16200 ;",0.9596,1.00352,37.89,{"v":4e-60,"d":"4.00E-60"},2,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",4,283,284,9,292,297]
[null,"NVIE_010920","_","Nitrososphaera viennensis EN76","_","hydroxyacyl-CoA dehydrogenase","_",0.73958,1,39.44,{"v":2e-58,"d":"2.00E-58"},1,1,"_","1.1.1.35","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,282,284,7,287,384]
[null,"XDD1v4_3925",null,"Xenorhabdus doucetiae FRM16","paaH","protein PaaH; 3-hydroxybutyryl-CoA dehydrogenase","_",0.51188,0.98592,40,{"v":4e-58,"d":"4.00E-58"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",4,282,284,10,287,547]
[null,"CLOSTRIBL6_v1_0555",null,"Clostridiales BL-6","hbd","3-hydroxybutyryl-CoA dehydrogenase","RXN-12705 ; RHEA:16200 ;",0.95318,1.00352,36.14,{"v":1e-55,"d":"1.00E-55"},3,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 25112316","2a : Function from experimental evidences in other organisms",4,283,284,9,292,299]
[null,"MARHY2087","_","Marinobacter hydrocarbonoclasticus ATCC 49840","fadB","bifunctional enzyme (PBE) (PBFE) [Includes: Enoyl-CoA hydratase ; 3,2-trans-enoyl-CoA isomerase ; 3-hydroxyacyl-CoA dehydrogenase ]","_",0.40486,0.99648,38.16,{"v":1E-52,"d":"1.00E-52"},1,1,"_","5.3.3.8, 4.2.1.17, 1.1.1.35","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","4019459, 8549802","2a : Function from experimental evidences in other organisms",1,282,284,291,567,699]
[null,"AZOLI_p30575","_","Azospirillum lipoferum 4B","pimF","Enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase","_",0.39604,0.98592,40.71,{"v":3E-52,"d":"3.00E-52"},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",3,282,284,307,581,707]
[null,"IBTHAUMv1_1140010","_","Ianthella basta symbiont thaum","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.83099,0.92188,39.83,{"v":3E-52,"d":"3.00E-52"},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)",6,240,284,8,242,256]
[null,"VCR9J2v1_150068","_","Vibrio crassostreae J2-9","fadB","Putative 3-hydroxybutyryl-CoA epimerase","OHBUTYRYL-COA-EPIM-RXN ; RHEA:21760 ;",0.39554,1,38.73,{"v":3E-51,"d":"3.00E-51"},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",2,284,284,318,597,718]
[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)","_",0.39213,1.01761,41.18,{"v":4E-51,"d":"4.00E-51"},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",3,282,284,328,606,737]
[null,"VS_0041","_","Vibrio tasmaniensis LGP32","_","3-hydroxybutyryl-CoA epimerase, Fatty acid oxidation complex subunit alpha","_",0.39419,1.00352,36.49,{"v":3E-49,"d":"3.00E-49"},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",3,283,284,316,594,723]
[null,"Rmet_5110","_","Cupriavidus metallidurans CH34","fadB1","short chain enoyl-CoA hydratase / 3-hydroxyacyl-CoA dehydrogenase","_",0.39441,0.99296,39.36,{"v":3E-49,"d":"3.00E-49"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","5.1.2.3, 1.1.1.35, 4.2.1.17","2 : Cytoplasmic","3.2 : Degradation ; 6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,282,284,311,587,715]
[null,"LMIv2_1447","_","Legionella micdadei","_","3-hydroxybutyryl-CoA epimerase","_",0.41456,0.98239,36.2,{"v":5e-45,"d":"5.00E-45"},1,1,"_","5.1.2.3","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,282,284,310,577,673]
[]
["AZ49_00555","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"SSV_v1_1781","_","Streptococcus sanguinis 2908","fabM","trans-2-decenoyl-[acyl-carrier-protein] isomerase","_",1,1.0038,35.23,{"v":7e-56,"d":"7.00E-56"},1,1,"_","5.3.3.14","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,264,264,1,263,263]
[null,"XDD1v4_3924","_","Xenorhabdus doucetiae FRM16","paaG","protein PaaG; acyl-CoA hydratase","_",0.95472,0.95833,36.76,{"v":5e-50,"d":"5.00E-50"},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",13,264,264,14,265,265]
[null,"NT26v4_2065","_","Rhizobium sp. NT-26","paaB","Enoyl-CoA hydratase/isomerase PhaB","_",1,1,36.74,{"v":6E-49,"d":"6.00E-49"},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",9,264,264,10,264,264]
[null,"RALTA_A3047","_","Cupriavidus taiwanensis LMG19424","_","Enoyl-CoA hydratase","_",0.98106,1,35.14,{"v":6e-48,"d":"6.00E-48"},1,1,"1 : Metabolism ;","4.2.1.17","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,264,264,7,259,259]
[null,"Rmet_3163","_","Cupriavidus metallidurans CH34","paaG","acyl-CoA hydratase","_",0.925,0.98106,36.29,{"v":2e-43,"d":"2.00E-43"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","_","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",6,263,264,27,279,280]
[null,"AZOLI_p10677","_","Azospirillum lipoferum 4B","_","putative Enoyl-CoA hydratase","_",0.97048,0.99621,37.26,{"v":5e-43,"d":"5.00E-43"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","2 : Cytoplasmic","3.2 : Degradation ; 6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",9,264,264,11,271,271]
[null,"RALTA_A2763",null,"Cupriavidus taiwanensis LMG19424","paaG1","acyl-CoA hydratase, phenylacetic acid degradation","_",0.91971,0.95455,35.32,{"v":9e-43,"d":"9.00E-43"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9748275,"2a : Function from experimental evidences in other organisms",14,264,264,27,274,274]
[null,"BRADO2571","_","Bradyrhizobium sp. ORS278","_","putative enoyl-CoA hydratase","_",0.98864,0.98864,35.25,{"v":4e-40,"d":"4.00E-40"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",9600981,"3 : Putative function from multiple computational evidences",7,264,264,5,264,264]
[]
["AZ49_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,"CLOAM0043",null,"Candidatus Cloacamonas acidaminovorans Evry","atoA","Acetoacetate:butyrate CoA-transferase beta subunit","_",0.95,0.96313,58.37,{"v":9e-85,"d":"9.00E-85"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.3.5 : Fermentation ; 1.1.3.10 : Lysine cleavage ;","2.8.3.9","1 : Unknown","_","e : enzyme",17166837,"2a : Function from experimental evidences in other organisms",7,215,220,6,214,217]
[null,"Spro_0591",null,"Serratia proteamaculans 568","atoA","Acetyl-CoA:acetoacetyl-CoA transferase, beta subunit","_",0.96364,0.97696,50.47,{"v":2E-70,"d":"2.00E-70"},1,1,"1.1.2.7 : Acetoacetate degradation ;","2.8.3.8","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,218,220,4,215,217]
[null,"CD630_26780",null,"Clostridium difficile 630","scoB","Succinyl CoA:3-oxoacid CoA-transferase subunit B","_",0.93213,0.93636,50.97,{"v":6e-69,"d":"6.00E-69"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.7 : Acetoacetate degradation ;","2.8.3.5","1 : Unknown","3.2 : Degradation ;","e : enzyme","19998280, 17363272","2a : Function from experimental evidences in other organisms",10,215,220,10,214,221]
[null,"PP_3123",null,"Pseudomonas putida KT2440","atoB","acetoacetyl CoA-transferase (subunit B)","ACETOACETYL-COA-TRANSFER-RXN ;",0.96364,0.97248,47.64,{"v":2E-66,"d":"2.00E-66"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.8.3.-","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","11741862, 11741863, 19406895","2a : Function from experimental evidences in other organisms",7,218,220,5,216,218]
[null,"ECIAI1_1490",null,"Escherichia coli IAI1","scoB","succinyl-CoA:3-ketoacid-coenzyme A transferase subunit B","_",0.96364,0.97248,47.17,{"v":2E-66,"d":"2.00E-66"},1,1,"1.3.4 : Tricarboxylic acid cycle ;","2.8.3.5","1 : Unknown","6.12 : TCA cycle ;","e : enzyme",9385134,"2a : Function from experimental evidences in other organisms",7,218,220,4,215,218]
[null,"FRAAL3149",null,"Frankia alni ACN14a","atoA","acetyl-CoA:acetoacetyl-CoA transferase, beta subunit","_",0.92273,0.95305,48.77,{"v":3e-66,"d":"3.00E-66"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.5","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,208,220,5,207,213]
[null,"VIBNIv4_B0463",null,"Vibrio nigripulchritudo SFn1","ctfB","Butyrate--acetoacetate CoA-transferase subunit B","_",0.95928,0.96364,47.17,{"v":3E-65,"d":"3.00E-65"},1,1,"1.1.2.7 : Acetoacetate degradation ;","2.8.3.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","2254264, 8226639, 8423010, 11466286, 2383002","2a : Function from experimental evidences in other organisms",7,218,220,9,219,221]
[null,"FN1856",null,"Fusobacterium nucleatum subsp. nucleatum ATCC 25586","atoA","Acetoacetate:butyrate CoA-transferase beta subunit","_",0.95,0.96313,49.76,{"v":1e-64,"d":"1.00E-64"},2,1,"1.1.3.10 : Lysine cleavage ; 1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.9","2 : Cytoplasmic","_","e : enzyme",17166837,"2a : Function from experimental evidences in other organisms",7,215,220,9,215,217]
[null,"PSEEN2465",null,"Pseudomonas entomophila L48","lpsJ","acetoacetyl-CoA transferase, beta subunit","_",0.49074,0.96364,47.64,{"v":3e-64,"d":"3.00E-64"},1,1,"1.6.3 : Lipopolysaccharide ;","2.8.3.5","Unknown","14 : Cell envelope ;","e : enzyme",9385134,"2a : Function from experimental evidences in other organisms",7,218,220,219,430,432]
[null,"PSHAa2942",null,"Pseudoalteromonas haloplanktis TAC125","_","putative succinyl-CoA transferase, beta subunit","_",0.96364,0.97248,44.34,{"v":2e-63,"d":"2.00E-63"},1,1,"2.2 : Metabolism of amino acids and related molecules ;","2.8.3.5","cytoplasm (undefined)","16.2 : Construct biomass (Anabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,218,220,5,216,218]
[null,"ABAYE1914",null,"Acinetobacter baumannii AYE","atoA","acetoacetyl-CoA transferase, beta subunit","_",0.90909,0.93897,46,{"v":5e-63,"d":"5.00E-63"},1,1,"1.1.2 : fatty acids ;","2.8.3.8","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",10,209,220,8,207,213]
[null,"AZOLI_p40133",null,"Azospirillum lipoferum 4B","scoB","Succinyl-CoA:3-ketoacid-coenzyme A transferase, subunit B","_",0.97273,0.99535,49.53,{"v":2e-62,"d":"2.00E-62"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.3.4 : Tricarboxylic acid cycle ; 1.6.3 : Lipopolysaccharide ;","2.8.3.8","2 : Cytoplasmic","3.2 : Degradation ; 6.12 : TCA cycle ; 14.3 : Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides ;","e : enzyme",9385134,"2b : Function from indirect experimental evidences (e.g. phenotypes)",7,218,220,4,213,215]
[null,"BN42v3_40460",null,"Mycobacterium canettii STB-K","scoB","Putative succinyl-CoA:3-ketoacid-coenzyme A transferase (beta subunit) ScoB (3-oxo-acid:CoA transferase) (OXCT B) (succinyl CoA:3-oxoacid CoA-transferase)","_",0.91818,0.92661,46.53,{"v":1E-61,"d":"1.00E-61"},1,1,"1 : lipid metabolism ;","2.8.3.5","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",10,211,220,11,212,218]
[null,"BN44v3_50495",null,"Mycobacterium canettii STB-D","scoB","Putative succinyl-CoA:3-ketoacid-coenzyme A transferase (beta subunit) ScoB (3-oxo-acid:CoA transferase) (OXCT B) (succinyl CoA:3-oxoacid CoA-transferase)","_",0.91818,0.92661,46.53,{"v":2e-61,"d":"2.00E-61"},1,1,"1 : lipid metabolism ;","2.8.3.5","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",10,211,220,11,212,218]
[null,"BN43v3_40170",null,"Mycobacterium canettii STB-L","scoB","Putative succinyl-CoA:3-ketoacid-coenzyme A transferase (beta subunit) ScoB (3-oxo-acid:CoA transferase) (OXCT B) (succinyl CoA:3-oxoacid CoA-transferase)","_",0.91818,0.92661,46.53,{"v":2e-61,"d":"2.00E-61"},1,1,"1 : lipid metabolism ;","2.8.3.5","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",10,211,220,11,212,218]
[null,"MGMSRv2_0177",null,"Magnetospirillum gryphiswaldense MSR-1 v2","scoB","Succinyl-CoA:3-ketoacid-coenzyme A transferase subunit B","_",0.93182,0.96244,46.83,{"v":2e-61,"d":"2.00E-61"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.3.4 : Tricarboxylic acid cycle ; 1.6.3 : Lipopolysaccharide ;","2.8.3.5","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme","9385134, 8969509, 9325289, 9923682","2a : Function from experimental evidences in other organisms",10,211,220,8,212,213]
[null,"BSU38980",null,"Bacillus subtilis 168","scoB","acetoacetyl CoA-transferase (subunit B)","ACETOACETYL-COA-TRANSFER-RXN ; RHEA:25480 ;",0.96364,0.98148,43.87,{"v":5e-61,"d":"5.00E-61"},1,1,"2.4 : Metabolism of lipids ;","2.8.3.5","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17363272, 22720735","2a : Function from experimental evidences in other organisms",4,215,220,2,213,216]
[null,"BDBv6_20236",null,"Blood disease bacterium R229","atoA","3-oxoacid CoA-transferase, beta subunit","_",0.93182,0.96698,46.83,{"v":8e-61,"d":"8.00E-61"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.-","1 : Unknown","3.2 : Degradation ;","e : enzyme",3025185,"2a : Function from experimental evidences in other organisms",10,210,220,8,212,212]
[null,"BN45v3_50888",null,"Mycobacterium canettii STB-J","scoB","Putative succinyl-CoA:3-ketoacid-coenzyme A transferase (beta subunit) ScoB (3-oxo-acid:CoA transferase) (OXCT B) (succinyl CoA:3-oxoacid CoA-transferase)","_",0.91818,0.92661,46.04,{"v":9E-61,"d":"9.00E-61"},1,1,"1 : lipid metabolism ;","2.8.3.5","2 : Cytoplasmic","_","e : enzyme","12657046, 12775759","3 : Putative function from multiple computational evidences",10,211,220,11,212,218]
[null,"Rmet_1154",null,"Cupriavidus metallidurans CH34","atoA","acetyl-CoA:acetoacetyl-CoA transferase, beta subunit","_",0.93182,0.96698,46.34,{"v":1e-60,"d":"1.00E-60"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.7 : Acetoacetate degradation ;","2.8.3.8","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",10,210,220,8,212,212]
[null,"ACIAD2514",null,"Acinetobacter baylyi ADP1","atoA","acetoacetyl-CoA transferase, beta subunit","ACECOATRANS-RXN ; ACETOACETYL-COA-TRANSFER-RXN ; R11-RXN ; R8-RXN ;",0.95455,0.98131,42.38,{"v":1e-60,"d":"1.00E-60"},1,1,"1.1.2 : fatty acids ;","2.8.3.8","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",7,216,220,5,214,214]
[null,"RALTA_A1253",null,"Cupriavidus taiwanensis LMG19424","atoA1","acetyl-CoA:acetoacetyl-CoA transferase, beta subunit","_",0.93182,0.96698,46.83,{"v":1e-60,"d":"1.00E-60"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.-","1 : Unknown","3.2 : Degradation ;","e : enzyme",3025185,"2a : Function from experimental evidences in other organisms",10,210,220,8,212,212]
[null,"CMR15v5_2481",null,"Ralstonia solanacearum CMR15","atoA","3-oxoacid CoA-transferase, beta subunit","_",0.93182,0.96698,46.34,{"v":2e-60,"d":"2.00E-60"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.-","1 : Unknown","3.2 : Degradation ;","e : enzyme",3025185,"2a : Function from experimental evidences in other organisms",10,210,220,8,212,212]
[null,"BRADO1224",null,"Bradyrhizobium sp. ORS278","scoB","Succinyl-CoA:3-ketoacid-coenzyme A transferase subunit B (Succinyl CoA:3-oxoacid CoA-transferase) (OXCT B)","_",0.94545,0.96296,47.12,{"v":7e-60,"d":"7.00E-60"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.6.3 : Lipopolysaccharide ; 1.3.4 : Tricarboxylic acid cycle ;","2.8.3.5","1 : Unknown","_","e : enzyme",9385134,"2a : Function from experimental evidences in other organisms",7,211,220,5,211,216]
[null,"CARN2_1788",null,"Carnoules 2","scoAB","Succinyl-CoA:3-ketoacid-coenzyme A transferase (OXCT AB)","_",0.45987,0.96364,45.28,{"v":8e-60,"d":"8.00E-60"},1,1,"1.3.4 : Tricarboxylic acid cycle ;","2.8.3.5","1 : Unknown","6.12 : TCA cycle ;","e : enzyme",9325289,"2a : Function from experimental evidences in other organisms",7,217,220,248,459,461]
[null,"HEAR1806",null,"Herminiimonas arsenicoxydans","scoB","Succinyl-CoA:3-ketoacid-coenzyme A transferase subunit B (Succinyl CoA:3-oxoacid CoA-transferase) (OXCT B)","_",0.92273,0.93548,47.29,{"v":5e-59,"d":"5.00E-59"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.6.3 : Lipopolysaccharide ;","2.8.3.5","1 : Unknown","3 : Fatty acid and phospholipid metabolism ; 14 : Cell envelope ;","c : carrier",9385134,"2a : Function from experimental evidences in other organisms",7,205,220,5,207,217]
[null,"METDI3688",null,"Methylobacterium extorquens DM4","atoA","acetyl-CoA:acetoacetyl-CoA transferase, beta subunit","_",0.96364,0.96804,46.7,{"v":1E-58,"d":"1.00E-58"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.-","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",7,211,220,5,216,219]
[null,"BSU19720",null,"Bacillus subtilis 168","yodR","putative acyloate-acetoacetate CoA-transferase","_",0.91818,0.93088,44.06,{"v":8e-57,"d":"8.00E-57"},2,1,"2.2 : Metabolism of amino acids and related molecules ;","2.8.3.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","15150230, 21538109, 24914178","3 : Putative function from multiple computational evidences",7,208,220,8,209,217]
[null,"HELPY_0681",null,"Helicobacter pylori B38","scoB","Succinyl-CoA-transferase subunit B","_",0.93182,0.99034,43.9,{"v":5E-56,"d":"5.00E-56"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.-","1 : Unknown","6.11 : TCA cycle ;","c : carrier","10091606, 10477311, 10477312, 10809701, 1624453, 9083111, 9325289","1a : Function from experimental evidences in the studied strain",7,211,220,2,205,207]
[null,"Rmet_3668",null,"Cupriavidus metallidurans CH34","pcaJ","3-oxoacid CoA-transferase, subunit B","_",0.93636,0.95814,43.69,{"v":2e-54,"d":"2.00E-54"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.7 : Acetoacetate degradation ;","_","1 : Unknown","_","c : carrier","_","2a : Function from experimental evidences in other organisms",2,205,220,1,205,215]
[null,"BDBv6_10149",null,"Blood disease bacterium R229","pcaJ","3-oxoadipate CoA-transferase subunit B","_",0.93182,0.93182,44.39,{"v":3e-54,"d":"3.00E-54"},2,1,"_","2.8.3.6","1 : Unknown","6 : Energy metabolism ;","e : enzyme",6780551,"2b : Function from indirect experimental evidences (e.g. phenotypes)",2,205,220,9,213,220]
[null,"CMR15v5_2037",null,"Ralstonia solanacearum CMR15","pcaJ","3-oxoadipate CoA-transferase subunit B","_",0.93182,0.93182,44.39,{"v":1E-53,"d":"1.00E-53"},2,1,"_","2.8.3.6","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,205,220,9,213,220]
[null,"RALTA_B0207",null,"Cupriavidus taiwanensis LMG19424","pcaJ","3-oxoadipate CoA-transferase subunit B (Beta- ketoadipate:succinyl-CoA transferase subunit B)","_",0.9,0.97059,44.95,{"v":1E-53,"d":"1.00E-53"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","2.8.3.6","1 : Unknown","6 : Energy metabolism ;","e : enzyme",1624453,"2a : Function from experimental evidences in other organisms",10,205,220,1,197,204]
[null,"Spro_3038",null,"Serratia proteamaculans 568","pcaJ","3-oxoadipate CoA-transferase subunit B (Beta- ketoadipate:succinyl-CoA transferase subunit B)","_",0.88496,0.90909,41.5,{"v":5E-53,"d":"5.00E-53"},2,1,"1.1.1 : Carbohydrates/Carbon compounds ;","2.8.3.6","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",10,208,220,9,208,226]
[null,"ABAYE1674",null,"Acinetobacter baumannii AYE","pcaJ","3-oxoadipate CoA-transferase subunit B (Beta- ketoadipate:succinyl-CoA transferase subunit B)","_",0.95,0.96313,41.15,{"v":5E-51,"d":"5.00E-51"},2,1,"1.1.1 : carbon compounds ;","2.8.3.6","1 : Unknown","_","e : enzyme","8063101, 8125318","2a : Function from experimental evidences in other organisms",3,210,220,4,212,217]
[null,"ABSDF1998",null,"Acinetobacter baumannii SDF","catJ","3-oxoadipate CoA-transferase subunit B (Beta- ketoadipate:succinyl-CoA transferase subunit B)","_",0.95,0.96313,41.15,{"v":6E-51,"d":"6.00E-51"},1,1,"1.1.1 : carbon compounds ;","2.8.3.6","1 : Unknown","_","e : enzyme","8063101, 8125318","2a : Function from experimental evidences in other organisms",3,210,220,4,212,217]
[null,"ABAYE1716",null,"Acinetobacter baumannii AYE","catJ","3-oxoadipate CoA-transferase subunit B (Beta- ketoadipate:succinyl-CoA transferase subunit B)","_",0.95,0.96759,41.15,{"v":7e-51,"d":"7.00E-51"},3,1,"1.1.1 : carbon compounds ;","2.8.3.6","1 : Unknown","_","e : enzyme","8063101, 8125318","2a : Function from experimental evidences in other organisms",3,210,220,4,212,216]
[null,"ACIAD1705",null,"Acinetobacter baylyi ADP1","pcaJ","3-oxoadipate CoA-transferase subunit B (Beta- ketoadipate:succinyl-CoA transferase subunit B)","3-OXOADIPATE-COA-TRANSFERASE-RXN ;",0.93182,0.9447,41.46,{"v":1E-50,"d":"1.00E-50"},2,1,"_","2.8.3.6","1 : Unknown","_","e : enzyme","8063101, 8125318, 7883173","1a : Function from experimental evidences in the studied strain",7,210,220,8,212,217]
[null,"ACIAD1449",null,"Acinetobacter baylyi ADP1","catJ","3-oxoadipate CoA-transferase subunit B (Beta-ketoadipate:succinyl-CoA transferase subunit B)","3-OXOADIPATE-COA-TRANSFERASE-RXN ;",0.93182,0.9447,41.46,{"v":1E-50,"d":"1.00E-50"},2,1,"1.1.1 : carbon compounds ;","2.8.3.6","1 : Unknown","_","e : enzyme","8063101, 8125318","1a : Function from experimental evidences in the studied strain",7,210,220,8,212,217]
[null,"EFER_1635",null,"Escherichia fergusonii ATCC 35469T","pcaJ","3-oxoadipate CoA-transferase subunit B (Beta- ketoadipate:succinyl-CoA transferase subunit B)","_",0.93182,0.94037,39.51,{"v":7e-50,"d":"7.00E-50"},2,1,"_","2.8.3.6","1 : Unknown","_","e : enzyme",8063101,"2a : Function from experimental evidences in other organisms",2,205,220,1,205,218]
[null,"PP_3952",null,"Pseudomonas putida KT2440","pcaJ","3-oxoadipate CoA-transferase subunit A","3-OXOADIPATE-COA-TRANSFERASE-RXN ; RHEA:12049 ;",0.92273,0.95305,40.39,{"v":1e-49,"d":"1.00E-49"},2,1,"1.1 : Carbon compound utilization ;","2.8.3.6","2 : Cytoplasmic","3.2 : Degradation ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","1624453, 6780551, 8905091, 8376330","1b : Function from experimental evidences in the studied species",1,202,220,3,204,213]
[null,"ABAYE2300",null,"Acinetobacter baumannii AYE","dcaJ","acyl-CoA-transferase subunit B","_",0.95455,0.96774,37.62,{"v":7e-47,"d":"7.00E-47"},4,1,"1.1.1 : carbon compounds ;","2.8.3.6","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",2,210,220,3,212,217]
[null,"VCR9J2v1_1370014","_","Vibrio crassostreae J2-9","_","Putative succinyl-CoA:3-ketoacid coenzyme A transferase","_",0.42889,0.87727,39.38,{"v":1e-44,"d":"1.00E-44"},1,1,"1.3 : Energy metabolism (carbon) ; 1.3.4 : Tricarboxylic acid cycle ;","2.8.3.5","1 : Unknown","6 : Energy metabolism ; 6.12 : TCA cycle ;","e : enzyme","_","3 : Putative function from multiple computational evidences",19,211,220,254,446,450]
[null,"VCRLGP8v1_930036","_","Vibrio crassostreae LGP8","_","putative succinyl-CoA:3-ketoacid coenzyme A transferase","_",0.42889,0.87727,38.86,{"v":2e-43,"d":"2.00E-43"},1,1,"_","2.8.3.5","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",19,211,220,254,446,450]
[null,"Rmet_5060",null,"Cupriavidus metallidurans CH34","atoA1","acetyl-CoA:acetoacetyl-CoA transferase, beta subunit","_",0.88412,0.93636,38.83,{"v":2e-42,"d":"2.00E-42"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.-","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,207,220,13,218,233]
[null,"RALTA_B0883",null,"Cupriavidus taiwanensis LMG19424","atoA2","acetyl-CoA:acetoacetyl-CoA transferase, beta subunit","_",0.86364,0.91346,39.47,{"v":3e-41,"d":"3.00E-41"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.-","1 : Unknown","3.2 : Degradation ;","e : enzyme","2883171, 3025185, 7618860","2a : Function from experimental evidences in other organisms",20,207,220,7,196,208]
[]
["AZ49_00550","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_p40132",null,"Azospirillum lipoferum 4B","scoA","Succinyl-CoA:3-ketoacid-coenzyme A transferase, subunit A","_",0.86122,0.96347,46.92,{"v":2e-64,"d":"2.00E-64"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.6.3 : Lipopolysaccharide ; 1.3.4 : Tricarboxylic acid cycle ;","2.8.3.5","1 : Unknown","3.2 : Degradation ; 6.12 : TCA cycle ; 14.3 : Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides ;","e : enzyme",8063101,"2b : Function from indirect experimental evidences (e.g. phenotypes)",3,213,245,3,213,219]
[null,"FN1857",null,"Fusobacterium nucleatum subsp. nucleatum ATCC 25586","atoD","Acetoacetate:butyrate CoA-transferase alpha subunit","_",0.85714,0.96774,44.76,{"v":4e-62,"d":"4.00E-62"},2,1,"1.1.3.10 : Lysine cleavage ; 1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.9","2 : Cytoplasmic","_","e : enzyme",17166837,"2a : Function from experimental evidences in other organisms",4,213,245,4,213,217]
[null,"CD630_26770",null,"Clostridium difficile 630","scoA","Succinyl CoA:3-oxoacid CoA-transferase subunit A","_",0.87347,0.98165,43.93,{"v":1E-61,"d":"1.00E-61"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.7 : Acetoacetate degradation ;","2.8.3.-","1 : Unknown","3.2 : Degradation ;","e : enzyme",19998280,"2a : Function from experimental evidences in other organisms",2,215,245,1,214,218]
[null,"VIBNIv4_B0464",null,"Vibrio nigripulchritudo SFn1","ctfA","Butyrate--acetoacetate CoA-transferase subunit A","_",0.88163,0.99083,43.98,{"v":5e-60,"d":"5.00E-60"},1,1,"1.1.2.7 : Acetoacetate degradation ; 7.1 : Cytoplasm ;","2.8.3.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","8226639, 8423010, 11466286, 8300540, 2383002","2a : Function from experimental evidences in other organisms",2,217,245,1,216,218]
[null,"CLOAM0042",null,"Candidatus Cloacamonas acidaminovorans Evry","atoD","Acetoacetate:butyrate CoA-transferase alpha subunit","_",0.84898,0.95413,45.19,{"v":3e-56,"d":"3.00E-56"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.3.5 : Fermentation ; 1.1.3.10 : Lysine cleavage ;","2.8.3.9","2 : Cytoplasmic","_","e : enzyme",17166837,"2a : Function from experimental evidences in other organisms",4,211,245,3,210,218]
[null,"BSU19730",null,"Bacillus subtilis 168","yodS","putative oxoacid CoA-transferase","_",0.8898,0.95197,42.2,{"v":4E-51,"d":"4.00E-51"},1,1,"2.2 : Metabolism of amino acids and related molecules ;","2.8.3.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","15150230, 21538109, 24914178","3 : Putative function from multiple computational evidences",4,220,245,6,223,229]
[null,"METDI3687",null,"Methylobacterium extorquens DM4","atoD","acetyl-CoA:acetoacetyl-CoA transferase, alpha subunit","_",0.91429,0.91429,40.18,{"v":1e-49,"d":"1.00E-49"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.-","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",15,238,245,16,239,245]
[null,"BRADO1223",null,"Bradyrhizobium sp. ORS278","scoA","Succinyl-CoA:3-ketoacid-coenzyme A transferase subunit A (Succinyl CoA:3-oxoacid CoA-transferase) (OXCT A)","_",0.82041,0.83058,43.28,{"v":2e-49,"d":"2.00E-49"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.6.3 : Lipopolysaccharide ; 1.3.4 : Tricarboxylic acid cycle ;","2.8.3.5","1 : Unknown","_","e : enzyme",9385134,"2a : Function from experimental evidences in other organisms",15,215,245,16,216,242]
[null,"HELPY_0682",null,"Helicobacter pylori B38","scoA","Succinyl-CoA-transferase subunit A","_",0.88163,0.93103,40.74,{"v":8e-49,"d":"8.00E-49"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.-","1 : Unknown","6.11 : TCA cycle ;","c : carrier","10091606, 10477311, 10477312, 10809701, 1624453, 9083111, 9325289","2a : Function from experimental evidences in other organisms",5,220,245,5,218,232]
[null,"BSU38990",null,"Bacillus subtilis 168","scoA","acetoacetyl CoA-transferase (subunit A)","ACETOACETYL-COA-TRANSFER-RXN ; RHEA:25480 ;",0.94694,0.97479,39.22,{"v":2e-48,"d":"2.00E-48"},2,1,"2.4 : Metabolism of lipids ;","2.8.3.5","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",17363272,"2a : Function from experimental evidences in other organisms",7,237,245,7,238,238]
[null,"RALTA_A1252",null,"Cupriavidus taiwanensis LMG19424","atoD1","acetyl-CoA:acetoacetyl-CoA transferase, alpha subunit","_",0.84898,0.8927,42.31,{"v":4e-48,"d":"4.00E-48"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.-","1 : Unknown","3.2 : Degradation ;","e : enzyme",3025185,"2a : Function from experimental evidences in other organisms",15,221,245,16,223,233]
[null,"HEAR1807",null,"Herminiimonas arsenicoxydans","scoA","Succinyl-CoA:3-ketoacid-coenzyme A transferase subunit A (Succinyl CoA:3-oxoacid CoA-transferase) (OXCT A)","_",0.78367,0.82759,41.15,{"v":7e-48,"d":"7.00E-48"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.6.3 : Lipopolysaccharide ;","2.8.3.5","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ; 14 : Cell envelope ;","e : enzyme","11589581, 9385134","2a : Function from experimental evidences in other organisms",15,206,245,16,207,232]
[null,"Rmet_1153",null,"Cupriavidus metallidurans CH34","atoD","acetyl-CoA:acetoacetyl-CoA transferase, alpha subunit","_",0.84898,0.89655,40.87,{"v":8e-48,"d":"8.00E-48"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.7 : Acetoacetate degradation ;","2.8.3.8","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",15,221,245,16,223,232]
[null,"CARN2_1788",null,"Carnoules 2","scoAB","Succinyl-CoA:3-ketoacid-coenzyme A transferase (OXCT AB)","_",0.43167,0.81224,44.22,{"v":1E-46,"d":"1.00E-46"},1,2,"1.3.4 : Tricarboxylic acid cycle ;","2.8.3.5","1 : Unknown","6.12 : TCA cycle ;","e : enzyme",9325289,"2a : Function from experimental evidences in other organisms",15,213,245,22,220,461]
[null,"ABAYE1913",null,"Acinetobacter baumannii AYE","atoD","acetoacetyl-CoA transferase, alpha subunit","_",0.88163,0.92308,40.74,{"v":7e-46,"d":"7.00E-46"},1,1,"1.1.2 : fatty acids ;","2.8.3.8","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",7,221,245,11,223,234]
[null,"ABAYE1717",null,"Acinetobacter baumannii AYE","catI","3-oxoadipate CoA-transferase subunit A (Beta-ketoadipate:succinyl-CoA transferase subunit A)","_",0.86939,0.95516,40.38,{"v":1e-45,"d":"1.00E-45"},2,1,"1.1.1 : carbon compounds ;","2.8.3.6","1 : Unknown","_","e : enzyme","8063101, 8125318","2a : Function from experimental evidences in other organisms",7,217,245,8,220,223]
[null,"CMR15v5_2480",null,"Ralstonia solanacearum CMR15","atoD","3-oxoacid CoA-transferase, alpha subunit","_",0.84898,0.89655,39.9,{"v":2E-45,"d":"2.00E-45"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.5","1 : Unknown","3.2 : Degradation ;","e : enzyme",3025185,"2a : Function from experimental evidences in other organisms",15,221,245,16,223,232]
[null,"ACIAD2513",null,"Acinetobacter baylyi ADP1","atoD","acetoacetyl-CoA transferase, alpha subunit","ACECOATRANS-RXN ; ACETOACETYL-COA-TRANSFER-RXN ; R11-RXN ; R8-RXN ;",0.86122,0.90171,42.18,{"v":2E-45,"d":"2.00E-45"},1,1,"1.1.2 : fatty acids ;","2.8.3.8","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,213,245,7,214,234]
[null,"ABSDF1997",null,"Acinetobacter baumannii SDF","catI","3-oxoadipate CoA-transferase subunit A (Beta- ketoadipate:succinyl-CoA transferase subunit A)","_",0.86939,0.95516,39.91,{"v":7E-45,"d":"7.00E-45"},1,1,"1.1.1 : carbon compounds ;","2.8.3.6","1 : Unknown","_","e : enzyme","8063101, 8125318","2a : Function from experimental evidences in other organisms",7,217,245,8,220,223]
[null,"ABAYE1673",null,"Acinetobacter baumannii AYE","pcaI","3-oxoadipate CoA-transferase subunit A (Beta- ketoadipate:succinyl-CoA transferase subunit A)","_",0.86939,0.95516,39.91,{"v":8e-45,"d":"8.00E-45"},3,1,"1.1.1 : carbon compounds ;","2.8.3.6","1 : Unknown","_","e : enzyme","8063101, 8125318","2a : Function from experimental evidences in other organisms",7,217,245,8,220,223]
[null,"MGMSRv2_0176",null,"Magnetospirillum gryphiswaldense MSR-1 v2","scoA","Succinyl-CoA:3-ketoacid-coenzyme A transferase subunit A (Succinyl CoA:3-oxoacid CoA-transferase) (OXCT A)","_",0.86531,0.88333,38.68,{"v":1e-44,"d":"1.00E-44"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.3.4 : Tricarboxylic acid cycle ; 1.6.3 : Lipopolysaccharide ;","2.8.3.5","1 : Unknown","16.2 : Construct biomass (Anabolism) ;","e : enzyme","9385134, 8969509, 9325289, 9923682","2a : Function from experimental evidences in other organisms",15,221,245,23,234,240]
[null,"Rmet_5059",null,"Cupriavidus metallidurans CH34","atoD","acetyl-CoA:acetoacetyl-CoA transferase, alpha subunit","_",0.85306,0.92478,40.19,{"v":2e-44,"d":"2.00E-44"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.-","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,213,245,8,216,226]
[null,"BDBv6_20237",null,"Blood disease bacterium R229","atoD","3-oxoacid CoA-transferase, alpha subunit","_",0.84898,0.89655,39.9,{"v":3e-44,"d":"3.00E-44"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.5","1 : Unknown","3.2 : Degradation ;","e : enzyme",3025185,"2a : Function from experimental evidences in other organisms",15,221,245,16,223,232]
[null,"PP_3951",null,"Pseudomonas putida KT2440","pcaI","3-oxoadipate CoA-transferase subunit A","3-OXOADIPATE-COA-TRANSFERASE-RXN ; RHEA:12049 ;",0.85306,0.90476,39.23,{"v":3e-42,"d":"3.00E-42"},1,1,"1.1 : Carbon compound utilization ;","2.8.3.6","2 : Cytoplasmic","3.2 : Degradation ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","1624453, 6780551, 8905091, 8376330","1b : Function from experimental evidences in the studied species",7,213,245,8,216,231]
[null,"PP_3122",null,"Pseudomonas putida KT2440","atoA","acetoacetyl CoA-transferase (subunit A)","ACETOACETYL-COA-TRANSFER-RXN ;",0.91429,0.96552,36.16,{"v":3e-42,"d":"3.00E-42"},2,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.8.3.-","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","11741863, 11741862, 19406895","2a : Function from experimental evidences in other organisms",4,223,245,7,230,232]
[null,"PSEEN2464",null,"Pseudomonas entomophila L48","lpsI","acetoacetyl-CoA transferase, alpha subunit","_",0.91429,0.96552,36.16,{"v":7e-42,"d":"7.00E-42"},1,1,"1.6.3 : Lipopolysaccharide ;","2.8.3.5","Unknown","14 : Cell envelope ;","e : enzyme",9385134,"2a : Function from experimental evidences in other organisms",4,223,245,7,230,232]
[null,"ACIAD1704",null,"Acinetobacter baylyi ADP1","pcaI","3-oxoadipate CoA-transferase subunit A (Beta- ketoadipate:succinyl-CoA transferase subunit A)","3-OXOADIPATE-COA-TRANSFERASE-RXN ;",0.90204,0.9693,37.56,{"v":7e-42,"d":"7.00E-42"},2,1,"_","2.8.3.6","1 : Unknown","_","e : enzyme","8063101, 8125318, 7883173","1a : Function from experimental evidences in the studied strain",7,225,245,8,228,228]
[null,"ACIAD1448",null,"Acinetobacter baylyi ADP1","catI","3-oxoadipate CoA-transferase subunit A (Beta-ketoadipate:succinyl-CoA transferase subunit A)","3-OXOADIPATE-COA-TRANSFERASE-RXN ;",0.90204,0.9693,37.56,{"v":7e-42,"d":"7.00E-42"},2,1,"1.1.1 : carbon compounds ;","2.8.3.6","1 : Unknown","_","e : enzyme","8063101, 8125318","1a : Function from experimental evidences in the studied strain",7,225,245,8,228,228]
[null,"BDBv6_10150",null,"Blood disease bacterium R229","pcaI","3-oxoadipate CoA-transferase subunit A","_",0.97551,1.04367,38.08,{"v":8e-42,"d":"8.00E-42"},2,1,"_","2.8.3.5","1 : Unknown","6 : Energy metabolism ;","e : enzyme",6780551,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,236,245,1,229,229]
[null,"PSHAa2943",null,"Pseudoalteromonas haloplanktis TAC125","_","putative succinyl-CoA transferase, alpha subunit","_",0.88571,0.9234,36.87,{"v":1E-41,"d":"1.00E-41"},1,1,"2.2 : Metabolism of amino acids and related molecules ;","2.8.3.5","cytoplasm (undefined)","16.2 : Construct biomass (Anabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,221,245,8,224,235]
[null,"CMR15v5_2036",null,"Ralstonia solanacearum CMR15","pcaI","3-oxoadipate CoA-transferase subunit A","_",0.88163,0.94323,39.35,{"v":3e-41,"d":"3.00E-41"},2,1,"_","2.8.3.5","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,213,245,1,216,229]
[null,"RALTA_B0206",null,"Cupriavidus taiwanensis LMG19424","pcaI","3-oxoadipate CoA-transferase subunit A (Beta- ketoadipate:succinyl-CoA transferase subunit A)","_",0.88163,0.98182,37.04,{"v":6e-41,"d":"6.00E-41"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","2.8.3.6","1 : Unknown","6 : Energy metabolism ;","e : enzyme",1624453,"2a : Function from experimental evidences in other organisms",1,213,245,1,216,220]
[null,"Rmet_3667",null,"Cupriavidus metallidurans CH34","pcaI","3-oxoacid CoA-transferase, subunit A","_",0.84898,0.94118,37.5,{"v":3e-40,"d":"3.00E-40"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.7 : Acetoacetate degradation ;","_","1 : Unknown","_","c : carrier","_","2a : Function from experimental evidences in other organisms",8,213,245,1,208,221]
[null,"RALTA_B0882",null,"Cupriavidus taiwanensis LMG19424","atoD2","acetyl-CoA:acetoacetyl-CoA transferase, alpha subunit","_",0.86939,0.96818,37.09,{"v":7e-40,"d":"7.00E-40"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.8.3.-","1 : Unknown","3.2 : Degradation ;","e : enzyme","2883171, 3025185, 7618860","2a : Function from experimental evidences in other organisms",5,215,245,1,213,220]
[null,"EFER_1636",null,"Escherichia fergusonii ATCC 35469T","pcaI","3-oxoadipate CoA-transferase subunit A (Beta- ketoadipate:succinyl-CoA transferase subunit A)","_",0.86939,0.8875,37.09,{"v":2e-39,"d":"2.00E-39"},2,1,"1.1.1 : Carbohydrates/Carbon compounds ;","2.8.3.6","1 : Unknown","6 : Energy metabolism ;","e : enzyme","1624453, 6780551","2a : Function from experimental evidences in other organisms",4,214,245,16,228,240]
[null,"ECIAI1_1491",null,"Escherichia coli IAI1","scoA","succinyl-CoA:3-ketoacid-coenzyme A transferase subunit A","_",0.8898,0.92766,35.78,{"v":2e-39,"d":"2.00E-39"},1,1,"1.3.4 : Tricarboxylic acid cycle ;","2.8.3.5","1 : Unknown","6.12 : TCA cycle ;","e : enzyme",9385134,"2a : Function from experimental evidences in other organisms",4,221,245,7,224,235]
[null,"FRAAL3148",null,"Frankia alni ACN14a","scoA","succinyl-CoA:3-ketoacid-coenzyme A transferase subunit A (Succinyl CoA:3-oxoacid CoA-transferase) (OXCT A)","_",0.81295,0.92245,37.17,{"v":2e-37,"d":"2.00E-37"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","2.8.3.5","1 : Unknown","6.8 : Glycolysis/gluconeogenesis ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",15,221,245,45,270,278]
[null,"NT26v4_3742",null,"Rhizobium sp. NT-26","scoA","Succinyl-CoA:3-ketoacid-coenzyme A transferase subunit A (Succinyl CoA:3-oxoacid CoA-transferase) (OXCT A)","_",0.86939,0.90638,38.5,{"v":5e-37,"d":"5.00E-37"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.6.3 : Lipopolysaccharide ; 1.3.4 : Tricarboxylic acid cycle ;","2.8.3.5","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",9385134,"2a : Function from experimental evidences in other organisms",5,215,245,5,217,235]
[null,"ABAYE2301",null,"Acinetobacter baumannii AYE","dcaI","acyl-CoA-transferase subunit A","_",0.88163,0.97297,37.5,{"v":9e-37,"d":"9.00E-37"},4,1,"1.1.1 : carbon compounds ;","2.8.3.6","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",1,213,245,1,216,222]
[null,"Spro_3037",null,"Serratia proteamaculans 568","pcaI","3-oxoadipate CoA-transferase subunit A (Beta- ketoadipate:succinyl-CoA transferase subunit A)","_",0.83265,0.89474,37.75,{"v":1E-35,"d":"1.00E-35"},2,1,"1.1.1 : Carbohydrates/Carbon compounds ;","2.8.3.6","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,206,245,6,209,228]
[]
["AZ49_02170","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"SCFA_v1_450041","_","Ca. Phosphitivorax anaerolimi F81","phaJ","crotonase","_",0.86395,0.92029,57.48,{"v":3e-48,"d":"3.00E-48"},1,1,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,135,138,8,134,147]
[null,"PSEEN3977","_","Pseudomonas entomophila L48","phaJ1","enoyl-CoA hydratase, R-specific","_",0.85256,0.96377,48.12,{"v":3e-39,"d":"3.00E-39"},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",4,136,138,6,137,156]
[null,"MGMSRv2_2229","_","Magnetospirillum gryphiswaldense MSR-1 v2","_","MaoC-like dehydratase, putative","_",0.90278,0.94203,51.54,{"v":5e-39,"d":"5.00E-39"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,136,138,11,139,144]
[null,"AZOLI_0508","_","Azospirillum lipoferum 4B","_","Putative acyl dehydratase","_",0.86577,0.93478,49.61,{"v":2e-38,"d":"2.00E-38"},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,"MARHY1690","_","Marinobacter hydrocarbonoclasticus ATCC 49840","_","conserved hypothetical protein","_",0.82609,0.96377,46.62,{"v":4e-38,"d":"4.00E-38"},1,1,"_","_","1 : Unknown","18 : Unknown function ;","u : unknown","_","4 : Unknown function but conserved in other organisms",4,136,138,10,141,161]
[null,"LEPBIa1114","_","Leptospira biflexa serovar Patoc Patoc 1","_","Putative MaoC family dehydratase","_",0.92857,0.94203,44.62,{"v":7e-37,"d":"7.00E-37"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",7,136,138,8,137,140]
[null,"THI_1475","_","Thiomonas sp. 3As","_","phosphate butyltransferase","_",0.275,0.95652,45.45,{"v":1e-33,"d":"1.00E-33"},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)",4,135,138,7,138,480]
[null,"Rmet_1672","_","Cupriavidus metallidurans CH34","_","MaoC-like dehydratase","_",0.89041,0.94203,45.38,{"v":1e-32,"d":"1.00E-32"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,136,138,9,137,146]
[null,"CLOSTRIBL3_v1_20109","_","Clostridiaceae BL-3","corR","enoyl-CoA hydratase","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; RHEA:17849 ;",0.97101,0.97101,42.54,{"v":4e-32,"d":"4.00E-32"},1,1,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme",18218779,"1c : Function from experimental evidences in the studied genus",3,136,138,2,134,138]
[null,"AZOLI_p20460","_","Azospirillum lipoferum 4B","pta2","phosphate acetyltransferase","_",0.28333,0.98551,43.38,{"v":7e-32,"d":"7.00E-32"},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",1,136,138,15,150,480]
[null,"METDI4248","_","Methylobacterium extorquens DM4","croR","crotonase","_",0.71123,0.96377,45.86,{"v":7e-31,"d":"7.00E-31"},1,1,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme",11872727,"1b : Function from experimental evidences in the studied species",3,135,138,36,167,187]
[null,"LFAv2_pA0055","_","Legionella-Like Amoebal Pathogens 10","_","Phosphate butyryltransferase","_",0.28358,0.96377,39.85,{"v":1e-30,"d":"1.00E-30"},1,1,"_","2.3.1.19","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,136,138,9,141,469]
[null,"HEAR1516","_","Herminiimonas arsenicoxydans","_","putative phosphate acetyltransferase","_",0.26862,0.86232,44.54,{"v":6e-29,"d":"6.00E-29"},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",18,136,138,1,119,443]
[null,"ADVE02_v2_12431","_","Methylosinus trichosporium OB3b","croR","Crotonase","_",0.82278,0.94203,40,{"v":3e-27,"d":"3.00E-27"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,136,138,10,138,158]
[null,"VIBNIv4_A1231","_","Vibrio nigripulchritudo SFn1","_","putative Acyl dehydratase","_",0.81879,0.88406,36.07,{"v":5e-23,"d":"5.00E-23"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",12,133,138,18,139,149]
[null,"BRADO6360","_","Bradyrhizobium sp. ORS278","_","putative phosphate acetyltransferase containing a MaoC like domain","_",0.28118,0.96377,37.59,{"v":9e-19,"d":"9.00E-19"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.19","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme",10094701,"3 : Putative function from multiple computational evidences",3,135,138,6,136,473]
[]
["AZ49_02175","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_3840003","_","Ca. Phosphitivorax butyraticus R76","_","short chain acyl-CoA transferase: fused alpha subunit ; beta subunit (Butyrate--acetoacetate CoA-transferase)","_",0.77341,0.99805,59.57,0,1,1,"_","2.8.3.9","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,512,513,23,534,662]
[null,"BN874v1_340056","_","Candidatus Contendobacter odensis Run_B_J11","_","putative coenzyme A-transferase","_",0.7574,0.99805,56.45,0,1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,512,513,20,530,676]
[null,"RALSYv5_0513","_","Ralstonia syzygii R24","_","putative CoA TRANSFERASE; exported protein","_",0.76479,1.0078,54.16,0,1,1,"_","2.8.3.1","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",2,512,513,18,534,676]
[null,"ECK1692","_","Escherichia coli K12","ydiF","short chain acyl-CoA transferase: fused alpha subunit ; beta subunit","ACECOATRANS-RXN ;",0.95857,0.9922,45.38,{"v":8e-153,"d":"8.00E-153"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","_","1 : Unknown","3.2 : Degradation ;","e : enzyme",16253988,"1b : Function from experimental evidences in the studied species",5,510,513,16,523,531]
[null,"CMR15v5_0436","_","Ralstonia solanacearum CMR15","_","putative CoA TRANSFERASE; exported protein","_",0.98553,1.06238,44.04,{"v":6e-139,"d":"6.00E-139"},1,1,"_","2.8.3.-","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,509,513,4,547,553]
[null,"EFER_4261","_","Escherichia fergusonii ATCC 35469T","_","putative CoA transferase","_",0.9883,0.9883,43.79,{"v":2e-138,"d":"2.00E-138"},1,1,"_","_","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,504,513,1,507,513]
[null,"RM41v1_720015","_","Sinorhizobium sp. Rm41","_","putative short chain acyl-CoA transferase","_",0.97398,1.02144,42.18,{"v":2e-127,"d":"2.00E-127"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.8.3.-","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,513,513,4,524,538]
[null,"AGR4A_v2_Lc60050","_","Agrobacterium genomosp. 4 B6","_","putztive acetate CoA-transferase YdiF","_",0.97952,1.02534,40.11,{"v":6e-123,"d":"6.00E-123"},1,1,"_","2.8.3.8","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,513,513,1,523,537]
[null,"RALSYv5_0596",null,"Ralstonia syzygii R24","_","fragment of putative CoA transferase; exported protein (part 1)","_",0.83626,0.89189,44.52,{"v":3e-112,"d":"3.00E-112"},2,1,"_","2.8.3.-","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,412,513,4,431,481]
[null,"RALSYv5_0597",null,"Ralstonia syzygii R24","_","fragment of putative CoA transferase; exported protein (part 2)","_",0.17934,0.92,44.57,2E-14,3,5,"_","2.8.3.-","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",424,509,513,2,93,100]
[]
["AZ49_00650","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_12012","_","Clostridiaceae BL-3","carC","Caffeyl-CoA reductase-Etf complex subunit CarC","RHEA:46956 ;",1.00259,1.01842,49.35,{"v":7e-122,"d":"7.00E-122"},1,1,"_","1.3.1.108","2 : Cytoplasmic","_","e : enzyme",23479729,"2a : Function from experimental evidences in other organisms",1,386,386,1,378,380]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.98187,1.00531,41.42,{"v":2e-94,"d":"2.00E-94"},1,5,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","1.3.99.-","2 : Cytoplasmic","3.2 : Degradation ; 6.2 : Amino acids and amines ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",5,380,386,3,372,377]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.98964,1.01596,39.27,{"v":5E-91,"d":"5.00E-91"},1,5,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,384,386,2,376,376]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.97927,1.00532,38.36,{"v":1E-87,"d":"1.00E-87"},1,5,"_","1.3.99.2","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,380,386,2,372,376]
[null,"ABAYE2315",null,"Acinetobacter baumannii AYE","dcaA","acyl-CoA dehydrogenase","_",0.98446,0.99217,40.79,{"v":7e-79,"d":"7.00E-79"},3,2,"1.1.1 : carbon compounds ;","1.3.99.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",7,380,386,3,375,383]
[null,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.98187,1.01067,37.73,{"v":9e-78,"d":"9.00E-78"},1,5,"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",4,380,386,2,372,375]
[null,"MGMSRv2_0409",null,"Magnetospirillum gryphiswaldense MSR-1 v2","_","Acyl-CoA dehydrogenase/oxidase","_",0.9509,0.95337,38.04,{"v":1e-71,"d":"1.00E-71"},2,5,"1.1.3.12 : Leucine degradation ;","1.3.8.4","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17540897, 8759838, 8655474","2a : Function from experimental evidences in other organisms",19,379,386,24,378,387]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.98718,0.99741,35.58,{"v":2e-71,"d":"2.00E-71"},3,5,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,379,386,9,381,390]
[null,"THI_3281",null,"Thiomonas sp. 3As","ivd","Isovaleryl-CoA dehydrogenase","_",0.97704,0.99223,35.51,{"v":1e-68,"d":"1.00E-68"},2,5,"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)",1,379,386,6,383,392]
[null,"Rmet_5908","_","Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase-like protein","_",0.89119,0.89351,38.95,{"v":3E-68,"d":"3.00E-68"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",43,380,386,39,379,385]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.96438,0.98187,35.62,{"v":2E-66,"d":"2.00E-66"},3,5,"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",5,379,386,11,384,393]
[null,"RALTA_A0110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL-COA DEHYDROGENASE OXIDOREDUCTASE","_",0.96438,0.98187,35.36,{"v":2E-66,"d":"2.00E-66"},2,5,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,379,386,11,384,393]
[]
["AZ49_02755","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,"BSU37170","_","Bacillus subtilis 168","acdA","acyl-CoA dehydrogenase","ACYLCOADEHYDROG-RXN ;",0.98691,0.99472,56.76,{"v":3e-145,"d":"3.00E-145"},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",1,377,382,1,374,379]
[null,"CLOSTRIBL6_v1_0135",null,"Clostridiales BL-6","bcd","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47199 ;",1,1.00792,56.54,{"v":2e-142,"d":"2.00E-142"},1,2,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","2a : Function from experimental evidences in other organisms",1,382,382,1,379,379]
[null,"CLOSTRIBL3_v1_20310",null,"Clostridiaceae BL-3","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24004 ;",1,1.00792,55.76,{"v":9e-141,"d":"9.00E-141"},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",1,382,382,1,379,379]
[null,"CD630_10540",null,"Clostridium difficile 630","bcd2","Butyryl-CoA dehydrogenase","_",0.98691,0.99735,54.91,{"v":9e-141,"d":"9.00E-141"},1,2,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",6,382,382,5,378,378]
[null,"CLOSTRIBL6_v1_3062",null,"Clostridiales BL-6","bcd","Acyl-CoA dehydrogenase, short-chain specific","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47199 ;",0.67611,1,53.66,{"v":1e-132,"d":"1.00E-132"},2,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,381,382,1,378,565]
[null,"CLOSTRIBL4_v1_1870",null,"Clostridiales BL-4","bcd","butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24007 ;",0.99481,1.00262,52.74,{"v":3e-126,"d":"3.00E-126"},1,2,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","2a : Function from experimental evidences in other organisms",1,378,382,1,380,385]
[null,"CD630_08030",null,"Clostridium difficile 630","_","Putative acyl-CoA dehydrogenase","_",1,1.00526,48.95,{"v":7e-119,"d":"7.00E-119"},2,1,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,381,382,1,379,380]
[null,"SCFA_v1_1080002","_","Ca. Phosphitivorax butyraticus R76","acdA","Acyl-CoA dehydrogenase","_",0.99739,1,46.34,{"v":3e-109,"d":"3.00E-109"},1,1,"_","1.3.8.-","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,381,382,1,379,383]
[null,"BSU18260",null,"Bacillus subtilis 168","ldeJ","isovaleryl-CoA dehydrogenase (leucine degradation)","RXN0-2301 ;",1.00262,1.00789,45.17,{"v":2e-105,"d":"2.00E-105"},3,2,"2.4 : Metabolism of lipids ;","1.3.8.4","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 17085570, 19935659","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,382,382,1,380,380]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.98953,1.00265,44.44,{"v":2e-104,"d":"2.00E-104"},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",5,382,382,3,377,377]
[null,"RSK60v3_mp750032",null,"Ralstonia solanacearum K60","_","putative Butyryl-CoA dehydrogenase","_",0.98691,1,46.15,{"v":6e-101,"d":"6.00E-101"},1,3,"1 : Metabolism ;","1.3.8.1","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,377,382,1,374,377]
[null,"RALSYv5_mp0315",null,"Ralstonia syzygii R24","_","putative Butyryl-CoA dehydrogenase","_",0.98691,1,45.89,{"v":1E-100,"d":"1.00E-100"},1,3,"1 : Metabolism ;","1.3.99.2","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,377,382,1,374,377]
[null,"BN873v1_590034",null,"Candidatus Competibacter denitrificans Run_A_D11","_","putative acyl-CoA dehydrogenase","_",0.98953,0.99736,43.92,{"v":2E-100,"d":"2.00E-100"},1,2,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.8.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,380,382,3,375,379]
[null,"CMR15v5_mp0941",null,"Ralstonia solanacearum CMR15","_","putative Butyryl-CoA dehydrogenase","_",0.98691,1,45.36,{"v":3e-100,"d":"3.00E-100"},1,3,"1 : Metabolism ;","1.3.99.2","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,377,382,1,374,377]
[null,"PP_2216",null,"Pseudomonas putida KT2440","acd","short-chain acyl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24007 ;",0.97644,0.99467,42.9,{"v":1E-97,"d":"1.00E-97"},2,3,"1.1.2.1 : Degradation of short-chain fatty acids ;","1.3.99.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","16024185, 11251808, 24317404","1a : Function from experimental evidences in the studied strain",5,377,382,3,372,375]
[null,"ACIAD1613",null,"Acinetobacter baylyi ADP1","_","putative acyl-CoA dehydrogenase protein (acdB-like)","2-METHYLACYL-COA-DEHYDROGENASE-RXN ; RXN-8568 ; RXN-12572 ;",0.98429,1.00267,42.02,{"v":1E-97,"d":"1.00E-97"},1,3,"_","1.3.8.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,380,382,3,375,375]
[null,"PSEEN2889","_","Pseudomonas entomophila L48","acdA","acyl-CoA dehydrogenase","_",0.98172,0.98429,43.09,{"v":2e-97,"d":"2.00E-97"},1,1,"_","1.3.99.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,377,382,3,375,383]
[null,"PSEEN3546",null,"Pseudomonas entomophila L48","fadFx","acyl-CoA dehydrogenase protein FadFx","_",0.97644,0.99467,42.36,{"v":3e-97,"d":"3.00E-97"},2,3,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",11251808,"2a : Function from experimental evidences in other organisms",5,377,382,3,372,375]
[null,"BN12v2_410006","_","Tetrasphaera japonica T1-X7","_","acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.99225,1.00524,44.27,{"v":2e-96,"d":"2.00E-96"},1,1,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme",17189250,"2a : Function from experimental evidences in other organisms",3,382,382,10,387,387]
[null,"ACIAD1607",null,"Acinetobacter baylyi ADP1","acads","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; RXN0-2301 ; RHEA:24007 ; RHEA:12277 ;",0.98691,1.00533,41.91,{"v":1e-95,"d":"1.00E-95"},2,2,"1.1.3.12 : Leucine degradation ; 1.1.3.14 : Valine degradation ; 1.1.5.1 : Phenylacetic acid degradation ;","1.3.8.1","1 : Unknown","3 : Fatty acid and phospholipid metabolism ; 5 : Central intermediary metabolism ;","e : enzyme","6712627, 16024185, 6261796, 11571189","2a : Function from experimental evidences in other organisms",4,380,382,2,375,375]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.98953,1.00532,40.74,{"v":9e-95,"d":"9.00E-95"},1,4,"_","1.3.99.2","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,380,382,3,375,376]
[null,"RALTA_B1110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.9555,0.99455,44.38,{"v":5e-94,"d":"5.00E-94"},1,4,"1 : Metabolism ;","1.3.99.-","2 : Cytoplasmic","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",16,380,382,6,367,367]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.98429,1,40.16,{"v":2e-93,"d":"2.00E-93"},1,4,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,380,382,3,375,376]
[null,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.98953,1.008,42.06,{"v":1e-92,"d":"1.00E-92"},1,3,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.2","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","11812788, 2777793, 8655474","2a : Function from experimental evidences in other organisms",5,380,382,3,375,375]
[null,"MARHY1099",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","_","acyl-CoA dehydrogenase","_",0.98454,1,39.53,{"v":9e-92,"d":"9.00E-92"},1,2,"_","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,381,382,1,379,388]
[null,"VIBNIv4_A0948","_","Vibrio nigripulchritudo SFn1","ACAD8","Isobutyryl-CoA dehydrogenase","_",0.9974,1.00262,40.73,{"v":4e-91,"d":"4.00E-91"},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",1,381,382,1,377,384]
[null,"MGMSRv2_0204",null,"Magnetospirillum gryphiswaldense MSR-1 v2","_","acyl-CoA dehydrogenase","_",0.99476,1.00264,39.74,{"v":9e-90,"d":"9.00E-90"},2,2,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","1.3.99.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","10524212, 8759838, 8969508, 17189250","2a : Function from experimental evidences in other organisms",1,380,382,1,376,379]
[null,"RM41v1_pld1500078","_","Sinorhizobium sp. Rm41","_","acyl-CoA dehydrogenase","_",0.99738,1.00263,40.42,{"v":2e-88,"d":"2.00E-88"},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)",1,381,382,1,377,380]
[null,"CMR15v5_0672",null,"Ralstonia solanacearum CMR15","_","putative acyl CoA dehydrogenase oxidoreductase protein","_",0.98953,1.00532,39.15,{"v":2e-88,"d":"2.00E-88"},1,3,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,380,382,3,375,376]
[null,"THI_3281",null,"Thiomonas sp. 3As","ivd","Isovaleryl-CoA dehydrogenase","_",0.96684,0.99215,37.99,{"v":3e-84,"d":"3.00E-84"},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)",1,376,382,6,383,392]
[null,"VIBNIv4_B0452","_","Vibrio nigripulchritudo SFn1","_","putative Acyl-CoA dehydrogenase","_",0.98705,0.99738,41.21,{"v":3e-84,"d":"3.00E-84"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",7,382,382,10,381,386]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.97949,1,36.91,{"v":6e-83,"d":"6.00E-83"},2,2,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,382,382,9,387,390]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.96438,0.99215,38.52,{"v":1e-82,"d":"1.00E-82"},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",1,376,382,7,384,393]
[null,"lpg1824","_","Legionella pneumophila subsp. pneumophila Philadelphia 1","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.98201,1,37.7,{"v":2e-82,"d":"2.00E-82"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,382,382,8,386,389]
[null,"RALTA_A0110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL-COA DEHYDROGENASE OXIDOREDUCTASE","_",0.96438,0.99215,38.26,{"v":2e-82,"d":"2.00E-82"},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",1,376,382,7,384,393]
[null,"lpp1787","_","Legionella pneumophila Paris","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.98201,1,37.7,{"v":2e-82,"d":"2.00E-82"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,382,382,8,386,389]
[null,"LPVv2_2096","_","Legionella pneumophila subsp. pneumophila HL06041035","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.98964,1,37.7,{"v":2e-82,"d":"2.00E-82"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,382,382,5,383,386]
[null,"LPC_1268","_","Legionella pneumophila Corby","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.98964,1,37.7,{"v":2e-82,"d":"2.00E-82"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,382,382,5,383,386]
[null,"CMR15v5_0667",null,"Ralstonia solanacearum CMR15","_","putative acyl-CoA dehydrogenase oxidoreductase","_",0.95929,0.98691,37.4,{"v":4e-82,"d":"4.00E-82"},2,1,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,376,382,9,384,393]
[null,"LPOv2_1885","_","Legionella pneumophila subsp. pneumophila Lorraine","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.98964,1,37.43,{"v":7e-82,"d":"7.00E-82"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,382,382,5,383,386]
[null,"BRADO1447","_","Bradyrhizobium sp. ORS278","ivd2","isovaleryl-CoA dehydrogenase","_",0.96154,0.98168,38.13,{"v":8e-82,"d":"8.00E-82"},1,1,"1.1.3.12 : Leucine degradation ;","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",2,376,382,10,381,390]
[null,"AZOLI_p40074","_","Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.99215,0.99475,38.79,{"v":2e-81,"d":"2.00E-81"},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)",1,377,382,1,373,381]
[null,"lpl1788","_","Legionella pneumophila Lens","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.98201,1,37.17,{"v":3e-81,"d":"3.00E-81"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,382,382,8,386,389]
[null,"ACIAD1693",null,"Acinetobacter baylyi ADP1","acads4","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; GLUTARYL-COA-DEHYDROG-RXN ; RXN0-2301 ; RHEA:24007 ; RHEA:12277 ;",0.98177,0.98691,39.79,{"v":6e-80,"d":"6.00E-80"},3,2,"1.1.3.12 : Leucine degradation ; 1.1.3.14 : Valine degradation ; 1.1.5.1 : Phenylacetic acid degradation ;","1.3.8.1","1 : Unknown","3 : Fatty acid and phospholipid metabolism ; 5 : Central intermediary metabolism ;","e : enzyme","6712627, 16024185, 6261796, 11571189","1a : Function from experimental evidences in the studied strain",8,382,382,7,380,384]
[null,"ABAYE2303",null,"Acinetobacter baumannii AYE","dcaA","acyl-CoA dehydrogenase","_",0.98177,0.98691,39.52,{"v":1E-78,"d":"1.00E-78"},4,2,"1.1.1 : carbon compounds ;","1.3.99.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",8,382,382,7,380,384]
[null,"Rmet_2599",null,"Cupriavidus metallidurans CH34","acdA","acyl-CoA dehydrogenase","_",1.00524,1.00524,35.16,{"v":2e-64,"d":"2.00E-64"},3,3,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,381,382,1,376,382]
[null,"NBG4_v1_200003",null,"Candidatus Sulfobium mesophilum","acdA","Acyl-CoA dehydrogenase","RHEA:47196 ; RHEA:24004 ;",0.94344,0.96073,35.97,{"v":2e-64,"d":"2.00E-64"},1,4,"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",18,382,382,30,387,389]
[null,"PP_0158",null,"Pseudomonas putida KT2440","gcdH","glutaryl-CoA dehydrogenase","_",0.96438,0.99215,35.88,{"v":8e-64,"d":"8.00E-64"},5,3,"_","1.3.8.6","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","18177371, 8439237","2a : Function from experimental evidences in other organisms",1,379,382,15,385,393]
[]
["AZ49_02760","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 ;",1,1.00386,61.15,{"v":4E-109,"d":"4.00E-109"},1,2,"_","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 5057466","1c : Function from experimental evidences in the studied genus",1,260,260,1,259,259]
[null,"CLOSTRIBL4_v1_1868",null,"Clostridiales BL-4","crt","Short-chain-enoyl-CoA hydratase","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; RHEA:17852 ;",0.96538,0.97287,52.59,{"v":2E-87,"d":"2.00E-87"},1,2,"_","4.2.1.55","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286, 5057466","2a : Function from experimental evidences in other organisms",6,256,260,4,252,258]
[null,"CD630_08000",null,"Clostridium difficile 630","crt1","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.98846,0.98846,50.58,{"v":2E-85,"d":"2.00E-85"},1,2,"1.6 : Macromolecules (cellular constituent) biosynthesis ;","4.2.1.55","1 : Unknown","6 : Energy metabolism ;","e : enzyme","8001771, 16346566, 11263873","2a : Function from experimental evidences in other organisms",4,260,260,5,260,260]
[null,"CD630_10570",null,"Clostridium difficile 630","crt2","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.96226,0.98077,52.16,{"v":9e-83,"d":"9.00E-83"},2,2,"_","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,"CLOSTRIBL6_v1_0134",null,"Clostridiales BL-6","ldeF","methylglutaconyl-CoA hydratase","METHYLGLUTACONYL-COA-HYDRATASE-RXN ; RHEA:21536 ;",0.96538,0.96538,50.2,{"v":2e-77,"d":"2.00E-77"},1,1,"_","4.2.1.18","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",19935659,"2b : Function from indirect experimental evidences (e.g. phenotypes)",11,260,260,11,260,260]
[null,"BN873v1_210051","_","Candidatus Competibacter denitrificans Run_A_D11","_","putative enoyl-CoA hydratase-isomerase","_",0.97692,0.9845,46.85,{"v":2e-71,"d":"2.00E-71"},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",1,254,260,1,252,258]
[null,"BN874v1_720037","_","Candidatus Contendobacter odensis Run_B_J11","_","putative enoyl-CoA hydratase-isomerase","_",0.99231,1,44.57,{"v":5E-71,"d":"5.00E-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,"LEPBIa0927","_","Leptospira biflexa serovar Patoc Patoc 1","crt","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.93077,0.95276,45.45,{"v":1e-69,"d":"1.00E-69"},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",16,257,260,14,254,254]
[null,"PSEEN3545",null,"Pseudomonas entomophila L48","fadB1x","enoyl-CoA hydratase, FadB1x","_",0.96538,1.004,44.62,{"v":2e-68,"d":"2.00E-68"},1,2,"1.5.4 : Fatty acid and phosphatidic acid ;","4.2.1.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",11251808,"2a : Function from experimental evidences in other organisms",14,260,260,7,250,250]
[null,"Rru_A3801","_","Rhodospirillum rubrum ATCC 11170","fadB","short chain enoyl-CoA hydratase","_",0.98846,0.99612,43.58,{"v":2e-68,"d":"2.00E-68"},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,"Rmet_3162",null,"Cupriavidus metallidurans CH34","paaF","enoyl-CoA hydratase-isomerase","_",1,1.00775,44.23,{"v":1e-67,"d":"1.00E-67"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","_","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",1,260,260,1,258,258]
[null,"BSU18220",null,"Bacillus subtilis 168","ldeF","methylglutaconyl-CoA hydratase (leucine degradation)","METHYLGLUTACONYL-COA-HYDRATASE-RXN ; RHEA:21536 ;",0.96538,0.96538,43.82,{"v":3e-67,"d":"3.00E-67"},1,2,"_","4.2.1.18","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",19935659,"2b : Function from indirect experimental evidences (e.g. phenotypes)",9,259,260,9,259,260]
[null,"HEAR0207",null,"Herminiimonas arsenicoxydans","ech","Enoyl-CoA hydratase","_",0.99231,1,45.35,{"v":1e-66,"d":"1.00E-66"},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,"ABAYE3764",null,"Acinetobacter baumannii AYE","_","putative Enoyl-CoA hydratase","_",1.01538,1.02724,42.42,{"v":2E-66,"d":"2.00E-66"},1,2,"_","4.2.1.17","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,260,260,1,257,257]
[null,"RALTA_A2759","_","Cupriavidus taiwanensis LMG19424","badK","cyclohex-1-ene-1-carboxyl-CoA hydratase","_",0.99231,1,43.8,{"v":3e-66,"d":"3.00E-66"},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,"ACIAD1608",null,"Acinetobacter baylyi ADP1","FadB","Enoyl-CoA hydratase (valine degradation) (valine degradation)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; ENOYL-COA-HYDRAT-RXN ; METHYLACYLYLCOA-HYDROXY-RXN ; RXN-902 ; TIGLYLCOA-HYDROXY-RXN ; RHEA:31178 ;",1.00769,1.01946,41.98,{"v":9e-65,"d":"9.00E-65"},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,"VIBNIv4_A2943","_","Vibrio nigripulchritudo SFn1","Echs1","Enoyl-CoA hydratase","_",0.95,0.97244,44.94,{"v":6e-63,"d":"6.00E-63"},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",16,259,260,13,253,254]
[null,"BN13v1_100067","_","Tetrasphaera jenkinsii Ben74","_","putative enoyl-CoA hydratase echA8","_",0.93077,0.93436,42.98,{"v":7e-63,"d":"7.00E-63"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",11,252,260,10,249,259]
[null,"CMR15v5_1457","_","Ralstonia solanacearum CMR15","paaF","enoyl-CoA hydratase-isomerase","_",0.99231,1,43.41,{"v":1E-62,"d":"1.00E-62"},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,"BDBv6_60063","_","Blood disease bacterium R229","paaF","enoyl-CoA hydratase-isomerase","_",0.97308,0.98062,43.87,{"v":2e-62,"d":"2.00E-62"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9748275,"2a : Function from experimental evidences in other organisms",1,253,260,1,251,258]
[null,"Rmet_2603",null,"Cupriavidus metallidurans CH34","paaG1","Enoyl-CoA hydratase/isomerase","_",1,1.01154,40.68,{"v":3e-61,"d":"3.00E-61"},2,2,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,260,260,1,263,263]
[null,"MGMSRv2_0209",null,"Magnetospirillum gryphiswaldense MSR-1 v2","_","probable enoyl-CoA hydratase","_",0.98462,0.98842,40.62,{"v":4e-60,"d":"4.00E-60"},2,2,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme","1743516, 2204034, 2806264, 7815937, 7751302","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,257,260,3,256,259]
[null,"ABAYE2304",null,"Acinetobacter baumannii AYE","dcaE","enoyl-CoA hydratase","_",0.91144,0.95,40.49,{"v":2e-56,"d":"2.00E-56"},2,2,"1.1.1 : carbon compounds ;","4.2.1.17","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",14,260,260,28,271,271]
[null,"ACIAD1692",null,"Acinetobacter baylyi ADP1","dcaE","Enoyl-CoA hydratase (branched-chain amino acid degradation)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; ENOYL-COA-HYDRAT-RXN ; METHYLACYLYLCOA-HYDROXY-RXN ; RXN-2425 ; RXN-902 ; TIGLYLCOA-HYDROXY-RXN ; RXN0-6513 ; RXN-7838 ; RHEA:16107 ; RHEA:17850 ; RHEA:31178 ; RHEA:31122 ;",0.94636,0.95,40.08,{"v":2E-55,"d":"2.00E-55"},2,2,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921, 11571189","1a : Function from experimental evidences in the studied strain",14,260,260,18,261,261]
[null,"ECS88_4526",null,"Escherichia coli S88","_","putative Enoyl-CoA hydratase/carnithine racemase","_",0.96154,0.96525,39.2,{"v":1e-49,"d":"1.00E-49"},1,2,"_","4.2.1.17","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",14,260,260,14,259,259]
[null,"RALTA_B1107",null,"Cupriavidus taiwanensis LMG19424","_","putative ENOYL-COA HYDRATASE ISOMERASE; similar to paaF (E.coli)","_",1,1.01562,37.31,{"v":2e-47,"d":"2.00E-47"},1,2,"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,"CMR15v5_mp0937",null,"Ralstonia solanacearum CMR15","_","putative enoyl-CoA hydratase/isomerase (paaF)","_",0.95865,0.98077,36.47,{"v":3e-46,"d":"3.00E-46"},1,1,"1 : Metabolism ;","4.2.1.-","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",6,259,260,4,257,266]
[null,"RM41v1_720016",null,"Sinorhizobium sp. Rm41","_","Enoyl-CoA hydratase","_",1.00385,1.00772,37.16,{"v":5e-46,"d":"5.00E-46"},3,2,"1 : Metabolism ; 7.1 : Cytoplasm ;","4.2.1.17","2 : Cytoplasmic","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,260,260,1,258,259]
[null,"MARHY1100",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","paaF","enoyl-CoA hydratase-isomerase","_",0.96538,0.96911,35.46,{"v":1e-43,"d":"1.00E-43"},1,2,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",14,260,260,13,259,259]
[null,"AGR4A_v2_Lc60051",null,"Agrobacterium genomosp. 4 B6","_","putative enoyl-CoA hydratase/isomerase","_",1.00385,1.00772,36.02,{"v":2E-41,"d":"2.00E-41"},1,2,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,260,260,1,258,259]
[null,"NBG4_v1_200001",null,"Candidatus Sulfobium mesophilum","echA","3-hydroxybutyryl-CoA dehydratase (fragment)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; RHEA:17849 ;",0.50769,0.93617,48.48,{"v":1e-38,"d":"1.00E-38"},1,1,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,135,260,10,139,141]
[]
["AZ49_04240","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 ;",1,1.00792,55.76,{"v":3e-140,"d":"3.00E-140"},1,3,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","2a : Function from experimental evidences in other organisms",1,382,382,1,379,379]
[null,"CLOSTRIBL3_v1_11587",null,"Clostridiaceae BL-3","bcd","Acyl-CoA dehydrogenase, short-chain specific","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24004 ; RHEA:47196 ;",1,1.00792,51.05,{"v":4e-128,"d":"4.00E-128"},2,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,382,382,1,379,379]
[null,"CLOSTRIBL4_v1_2140","_","Clostridiales BL-4","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47196 ;",0.59906,0.99738,51.97,{"v":2e-126,"d":"2.00E-126"},1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286, 8399220, 7857927","2a : Function from experimental evidences in other organisms",1,381,382,1,378,636]
[null,"CD630_03990",null,"Clostridium difficile 630","acdB","Acyl-CoA dehydrogenase, short-chain specific","_",0.97906,0.99204,47.86,{"v":1e-106,"d":"1.00E-106"},3,4,"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",9,382,382,7,377,377]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.98953,1.00265,44.97,{"v":8e-106,"d":"8.00E-106"},1,2,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","1.3.99.-","2 : Cytoplasmic","3.2 : Degradation ; 6.2 : Amino acids and amines ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",5,382,382,3,377,377]
[null,"BN873v1_590034","_","Candidatus Competibacter denitrificans Run_A_D11","_","putative acyl-CoA dehydrogenase","_",0.98953,0.99736,43.92,{"v":1E-100,"d":"1.00E-100"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.8.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,380,382,3,375,379]
[null,"ACIAD1613","_","Acinetobacter baylyi ADP1","_","putative acyl-CoA dehydrogenase protein (acdB-like)","2-METHYLACYL-COA-DEHYDROGENASE-RXN ; RXN-8568 ; RXN-12572 ;",0.98429,1.00267,42.55,{"v":2e-98,"d":"2.00E-98"},1,1,"_","1.3.8.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",5,380,382,3,375,375]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.98953,1.00532,41.01,{"v":3e-95,"d":"3.00E-95"},1,3,"_","1.3.99.2","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,380,382,3,375,376]
[null,"CLOSTRIBL3_v1_10853",null,"Clostridiaceae BL-3","carC","Caffeyl-CoA reductase-Etf complex subunit CarC","RHEA:46956 ;",0.99215,1,43.27,{"v":5e-95,"d":"5.00E-95"},4,2,"_","1.3.1.108","2 : Cytoplasmic","_","e : enzyme",23479729,"2a : Function from experimental evidences in other organisms",5,382,382,3,378,379]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.98429,1,40.43,{"v":6e-94,"d":"6.00E-94"},1,3,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,380,382,3,375,376]
[null,"MARHY1099","_","Marinobacter hydrocarbonoclasticus ATCC 49840","_","acyl-CoA dehydrogenase","_",0.98454,1,39.53,{"v":5e-92,"d":"5.00E-92"},1,1,"_","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,381,382,1,379,388]
[null,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.98953,1.008,41.8,{"v":6e-92,"d":"6.00E-92"},1,4,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.2","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","11812788, 2777793, 8655474","2a : Function from experimental evidences in other organisms",5,380,382,3,375,375]
[null,"CMR15v5_0672",null,"Ralstonia solanacearum CMR15","_","putative acyl CoA dehydrogenase oxidoreductase protein","_",0.98953,1.00532,39.15,{"v":2e-88,"d":"2.00E-88"},1,3,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,380,382,3,375,376]
[null,"THI_3281",null,"Thiomonas sp. 3As","ivd","Isovaleryl-CoA dehydrogenase","_",0.96684,0.99215,37.2,{"v":9e-82,"d":"9.00E-82"},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)",1,376,382,6,383,392]
[null,"CMR15v5_0667",null,"Ralstonia solanacearum CMR15","_","putative acyl-CoA dehydrogenase oxidoreductase","_",0.96438,0.99215,36.94,{"v":2e-81,"d":"2.00E-81"},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",1,376,382,7,384,393]
[null,"RALTA_A0110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL-COA DEHYDROGENASE OXIDOREDUCTASE","_",0.96438,0.99215,37.73,{"v":3e-81,"d":"3.00E-81"},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",1,376,382,7,384,393]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.96438,0.99215,37.99,{"v":4e-81,"d":"4.00E-81"},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",1,376,382,7,384,393]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.97949,1,36.13,{"v":4e-81,"d":"4.00E-81"},2,4,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,382,382,9,387,390]
[null,"XNC1_1707","_","Xenorhabdus nematophila ATCC19061","xcnE","Acyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",0.9765,0.97906,38.77,{"v":2e-69,"d":"2.00E-69"},1,1,"_","1.3.99.2","1 : Unknown","_","e : enzyme","16349198, 1955881","1a : Function from experimental evidences in the studied strain",12,382,382,9,373,383]
[null,"XDD1v4_1795","_","Xenorhabdus doucetiae FRM16","xcnE","Acyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",0.9765,0.97906,38.5,{"v":6e-69,"d":"6.00E-69"},1,1,"_","1.3.8.1","1 : Unknown","_","e : enzyme","16349198, 1955881","2a : Function from experimental evidences in other organisms",12,382,382,9,373,383]
[]
["AZ49_06245","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"LEPBIa0057","_","Leptospira biflexa serovar Patoc Patoc 1","acdA2","Acyl-CoA dehydrogenase","_",0.96649,0.98945,45.6,{"v":6e-107,"d":"6.00E-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,"BN45v3_60311","_","Mycobacterium canettii STB-J","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.97172,0.99736,46.03,{"v":8e-106,"d":"8.00E-106"},1,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","10510226, 12775759, 15525680","3 : Putative function from multiple computational evidences",3,378,379,13,388,389]
[null,"BN44v3_70065","_","Mycobacterium canettii STB-D","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.97172,0.99736,46.03,{"v":8e-106,"d":"8.00E-106"},1,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","10510226, 12775759, 15525680","3 : Putative function from multiple computational evidences",3,378,379,13,388,389]
[null,"BN42v3_41331","_","Mycobacterium canettii STB-K","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.97172,0.99736,46.03,{"v":8e-106,"d":"8.00E-106"},1,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","10510226, 12775759, 15525680","3 : Putative function from multiple computational evidences",3,378,379,13,388,389]
[null,"BN43v3_60289","_","Mycobacterium canettii STB-L","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.97172,0.99736,46.03,{"v":2e-105,"d":"2.00E-105"},1,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","10510226, 12775759, 15525680","3 : Putative function from multiple computational evidences",3,378,379,13,388,389]
[null,"RALSYv5_mp0315","_","Ralstonia syzygii R24","_","putative Butyryl-CoA dehydrogenase","_",0.99208,0.99735,43.88,{"v":4e-103,"d":"4.00E-103"},1,1,"1 : Metabolism ;","1.3.99.2","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,374,379,1,374,377]
[null,"RSK60v3_mp750032","_","Ralstonia solanacearum K60","_","putative Butyryl-CoA dehydrogenase","_",0.99208,0.99735,43.35,{"v":5e-102,"d":"5.00E-102"},1,1,"1 : Metabolism ;","1.3.8.1","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,374,379,1,374,377]
[null,"BN13v1_920006","_","Tetrasphaera jenkinsii Ben74","_","putative acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.98187,1,42.74,{"v":1E-97,"d":"1.00E-97"},1,1,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,378,379,8,385,386]
[null,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.97889,0.98933,41.78,{"v":3e-96,"d":"3.00E-96"},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",6,374,379,4,372,375]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.97361,0.98138,42.01,{"v":4e-96,"d":"4.00E-96"},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)",8,374,379,6,372,376]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.97625,0.98143,41.08,{"v":1e-94,"d":"1.00E-94"},1,4,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","1.3.99.-","2 : Cytoplasmic","3.2 : Degradation ; 6.2 : Amino acids and amines ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",7,374,379,5,372,377]
[null,"MGMSRv2_0204","_","Magnetospirillum gryphiswaldense MSR-1 v2","_","acyl-CoA dehydrogenase","_",0.98945,0.98945,40.27,{"v":2e-93,"d":"2.00E-93"},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",1,373,379,1,372,379]
[null,"ACIAD1693","_","Acinetobacter baylyi ADP1","acads4","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; GLUTARYL-COA-DEHYDROG-RXN ; RXN0-2301 ; RHEA:24007 ; RHEA:12277 ;",0.97135,0.98417,38.87,{"v":3e-87,"d":"3.00E-87"},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","1a : Function from experimental evidences in the studied strain",10,378,379,9,379,384]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.93077,0.95778,39.12,{"v":4e-83,"d":"4.00E-83"},3,1,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",16,376,379,24,384,390]
[null,"Npun_R3440","_","Nostoc punctiforme ATCC 29133; PCC 73102","_","putative acyl-CoA dehydrogenase","_",0.95685,0.99472,39.79,{"v":9e-81,"d":"9.00E-81"},1,1,"_","1.3.99.2","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,374,379,1,370,394]
[null,"THI_3281",null,"Thiomonas sp. 3As","ivd","Isovaleryl-CoA dehydrogenase","_",0.97704,1.01055,35.51,{"v":2E-73,"d":"2.00E-73"},2,4,"1.1.3.12 : Leucine degradation ;","1.3.99.10","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","10677295, 12477932, 12665801, 1310317, 2318964, 7640268, 8468053, 921428","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,376,379,6,386,392]
[null,"SCFA_v1_1630002","_","Ca. Propionivorax syntrophicum F70","acdB","Acyl-CoA dehydrogenase, short-chain specific","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47196 ; RHEA:24004 ;",0.96173,0.99472,35.54,{"v":2E-73,"d":"2.00E-73"},1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,378,379,17,390,392]
[null,"NBG4_v1_200003","_","Candidatus Sulfobium mesophilum","acdA","Acyl-CoA dehydrogenase","RHEA:47196 ; RHEA:24004 ;",0.96144,0.98681,35.56,{"v":9e-71,"d":"9.00E-71"},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",8,378,379,20,386,389]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.97964,1.01583,35.58,{"v":2e-69,"d":"2.00E-69"},3,4,"1.1.3.12 : Leucine degradation ;","1.3.99.10","2 : Cytoplasmic","6 : Energy metabolism ; 1 : Amino acid biosynthesis ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,376,379,7,387,393]
[]
["AZ49_06555","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",null,"Clostridiaceae BL-3","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24004 ;",1,1.01055,59.53,{"v":2e-154,"d":"2.00E-154"},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",1,383,383,1,379,379]
[null,"CD630_10540",null,"Clostridium difficile 630","bcd2","Butyryl-CoA dehydrogenase","_",1,1.01323,57.44,{"v":1e-148,"d":"1.00E-148"},1,1,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,383,383,1,378,378]
[null,"CLOSTRIBL6_v1_0135",null,"Clostridiales BL-6","bcd","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47199 ;",1,1.01055,56.92,{"v":3e-144,"d":"3.00E-144"},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,"CLOSTRIBL4_v1_1870",null,"Clostridiales BL-4","bcd","butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24007 ;",1.0026,1.00783,52.33,{"v":2E-131,"d":"2.00E-131"},1,1,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","2a : Function from experimental evidences in other organisms",1,381,383,1,382,385]
[null,"CLOSTRIBL6_v1_3216",null,"Clostridiales BL-6","bud","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; RHEA:47199 ;",0.98956,0.99737,53.03,{"v":3E-131,"d":"3.00E-131"},3,1,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","2a : Function from experimental evidences in other organisms",1,379,383,1,375,380]
[null,"CD630_08030",null,"Clostridium difficile 630","_","Putative acyl-CoA dehydrogenase","_",1,1.00789,48.83,{"v":1e-116,"d":"1.00E-116"},2,2,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,382,383,1,379,380]
[null,"CD630_03990",null,"Clostridium difficile 630","acdB","Acyl-CoA dehydrogenase, short-chain specific","_",0.97911,0.99469,49.07,{"v":2e-112,"d":"2.00E-112"},3,1,"7.1 : Cytoplasm ;","1.3.99.-","2 : Cytoplasmic","6.2 : Amino acids and amines ;","e : enzyme","16802151, 16233311","2a : Function from experimental evidences in other organisms",9,383,383,7,377,377]
[null,"SCFA_v1_2690009","_","Ca. Phosphitivorax butyraticus R76","acdA","Acyl-CoA dehydrogenase (Butyryl-CoA dehydrogenase)","_",0.98433,0.98691,47.48,{"v":1e-111,"d":"1.00E-111"},1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,376,383,1,373,382]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.99217,1.00796,44.21,{"v":3e-110,"d":"3.00E-110"},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",4,383,383,2,377,377]
[null,"SCFA_v1_500014",null,"Ca. Phosphitivorax anaerolimi F81","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.96606,0.96606,45.68,{"v":4E-109,"d":"4.00E-109"},3,2,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",14,382,383,14,379,383]
[null,"PSEEN3546","_","Pseudomonas entomophila L48","fadFx","acyl-CoA dehydrogenase protein FadFx","_",0.97128,0.992,45.7,{"v":1E-107,"d":"1.00E-107"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",11251808,"2a : Function from experimental evidences in other organisms",5,376,383,3,370,375]
[null,"SCFA_v1_1080002",null,"Ca. Phosphitivorax butyraticus R76","acdA","Acyl-CoA dehydrogenase","_",1,1,45.43,{"v":2E-107,"d":"2.00E-107"},3,4,"_","1.3.8.-","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,382,383,1,379,383]
[null,"ACIAD1607","_","Acinetobacter baylyi ADP1","acads","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; RXN0-2301 ; RHEA:24007 ; RHEA:12277 ;",0.95822,0.97867,44.41,{"v":4e-105,"d":"4.00E-105"},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",15,381,383,13,375,375]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.98433,1.00266,43.5,{"v":6e-105,"d":"6.00E-105"},1,1,"_","1.3.99.2","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,381,383,3,375,376]
[null,"PP_2216","_","Pseudomonas putida KT2440","acd","short-chain acyl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24007 ;",0.97128,0.992,45.16,{"v":9e-105,"d":"9.00E-105"},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",5,376,383,3,370,375]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.98433,1.00266,42.71,{"v":4e-104,"d":"4.00E-104"},1,1,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,381,383,3,375,376]
[null,"CMR15v5_mp0941","_","Ralstonia solanacearum CMR15","_","putative Butyryl-CoA dehydrogenase","_",0.98172,0.99735,45.74,{"v":1e-101,"d":"1.00E-101"},1,1,"1 : Metabolism ;","1.3.99.2","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,376,383,1,372,377]
[null,"MGMSRv2_0193","_","Magnetospirillum gryphiswaldense MSR-1 v2","_","Acyl-CoA dehydrogenase","_",0.98433,0.99211,42.44,{"v":4e-101,"d":"4.00E-101"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","1.3.99.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","10524212, 8759838, 8969508, 17189250","2a : Function from experimental evidences in other organisms",5,381,383,3,375,380]
[null,"RALTA_B1110","_","Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.95561,0.99728,44.26,{"v":6e-99,"d":"6.00E-99"},1,1,"1 : Metabolism ;","1.3.99.-","2 : Cytoplasmic","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",16,381,383,6,367,367]
[null,"CMR15v5_0672",null,"Ralstonia solanacearum CMR15","_","putative acyl CoA dehydrogenase oxidoreductase protein","_",0.98433,1.00266,41.38,{"v":4e-98,"d":"4.00E-98"},1,1,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,381,383,3,375,376]
[null,"BN42v3_40456","_","Mycobacterium canettii STB-K","fadE","Putative acyl-CoA dehydrogenase FadE19 (MMGC)","_",0.95939,0.98695,43.39,{"v":2e-94,"d":"2.00E-94"},1,1,"1 : lipid metabolism ;","1.3.99.-","1 : Unknown","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",10,381,383,18,391,394]
[null,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.98433,1.00533,41.38,{"v":2e-94,"d":"2.00E-94"},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",5,381,383,3,375,375]
[null,"CLOSTRIBL3_v1_12012",null,"Clostridiaceae BL-3","carC","Caffeyl-CoA reductase-Etf complex subunit CarC","RHEA:46956 ;",1.00783,1.01579,42.75,{"v":8e-94,"d":"8.00E-94"},4,3,"_","1.3.1.108","2 : Cytoplasmic","_","e : enzyme",23479729,"2a : Function from experimental evidences in other organisms",1,383,383,1,377,380]
[null,"BN10v3_30013","_","Tetrasphaera elongata Lp2","_","putative Butyryl-CoA dehydrogenase","_",0.98232,1.01567,43.44,{"v":3e-92,"d":"3.00E-92"},1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,378,383,2,388,396]
[null,"CLOSTRIBL3_v1_10853",null,"Clostridiaceae BL-3","carC","Caffeyl-CoA reductase-Etf complex subunit CarC","RHEA:46956 ;",0.99217,1.00264,40.53,{"v":2E-91,"d":"2.00E-91"},5,4,"_","1.3.1.108","2 : Cytoplasmic","_","e : enzyme",23479729,"2a : Function from experimental evidences in other organisms",5,383,383,3,378,379]
[null,"MARHY1166",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","ivdA","Isovaleryl-coenzyme A dehydrogenase","_",0.98196,0.99478,38.32,{"v":3e-83,"d":"3.00E-83"},2,1,"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",1,381,383,8,384,388]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.98462,1.00261,38.02,{"v":4e-81,"d":"4.00E-81"},2,3,"_","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,"VIBNIv4_B0452",null,"Vibrio nigripulchritudo SFn1","_","putative Acyl-CoA dehydrogenase","_",0.97668,0.98433,37.67,{"v":5e-78,"d":"5.00E-78"},1,4,"_","_","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","_",0.98469,1.00783,37.56,{"v":7e-78,"d":"7.00E-78"},2,3,"1.1.3.12 : Leucine degradation ;","1.3.99.10","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","10677295, 12477932, 12665801, 1310317, 2318964, 7640268, 8468053, 921428","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,381,383,6,387,392]
[null,"RALTA_A0110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL-COA DEHYDROGENASE OXIDOREDUCTASE","_",0.93893,0.96345,37.4,{"v":3e-73,"d":"3.00E-73"},3,3,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",18,381,383,24,388,393]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.98219,1.00783,36.27,{"v":4E-73,"d":"4.00E-73"},2,3,"1.1.3.12 : Leucine degradation ;","1.3.99.10","2 : Cytoplasmic","6 : Energy metabolism ; 1 : Amino acid biosynthesis ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,381,383,7,388,393]
[null,"CMR15v5_0667",null,"Ralstonia solanacearum CMR15","_","putative acyl-CoA dehydrogenase oxidoreductase","_",0.9771,1.00261,35.68,{"v":5e-73,"d":"5.00E-73"},2,3,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,381,383,9,388,393]
[null,"SCFA_v1_1630002",null,"Ca. Propionivorax syntrophicum F70","acdB","Acyl-CoA dehydrogenase, short-chain specific","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47196 ; RHEA:24004 ;",0.96939,0.99217,36.32,{"v":1e-71,"d":"1.00E-71"},1,2,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,383,383,21,391,392]
[null,"LEPBIa1138",null,"Leptospira biflexa serovar Patoc Patoc 1","_","Putative acyl-CoA dehydrogenase, short-chain specific (SCAD) (Butyryl-CoA dehydrogenase)","_",0.94162,0.96867,36.39,{"v":1e-67,"d":"1.00E-67"},4,3,"_","1.3.8.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,371,383,14,378,394]
[null,"MARHY1169",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","fadE","long chain acyl coenzyme A dehydrogenase","_",0.95039,0.95288,35.44,{"v":6e-67,"d":"6.00E-67"},5,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.13","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",21,382,383,22,380,382]
[null,"Rmet_4427","_","Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase(Butyryl-CoA dehydrogenase)","_",0.99485,1.00783,35.23,{"v":2E-66,"d":"2.00E-66"},1,1,"_","_","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,382,383,4,383,388]
[null,"BN874v1_280009","_","Candidatus Contendobacter odensis Run_B_J11","_","putative acyl-CoA dehydrogenase","_",0.60908,0.91123,35.82,{"v":7e-59,"d":"7.00E-59"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme",19703103,"3 : Putative function from multiple computational evidences",41,371,383,204,550,573]
[null,"METDI3005","_","Methylobacterium extorquens DM4","msd","methylsuccinyl-CoA dehydrogenase","_",0.66726,0.97911,35.73,{"v":5e-58,"d":"5.00E-58"},1,1,"_","1.3.8.4","2 : Cytoplasmic","_","e : enzyme","16856937, 17548827","1c : Function from experimental evidences in the studied genus",19,382,383,191,560,562]
[null,"META1_2223","_","Methylobacterium extorquens AM1","mcd","methylsuccinyl-CoA dehydrogenase, putative isobutyryl-CoA dehydrogenase","_",0.66726,0.97911,35.73,{"v":6e-58,"d":"6.00E-58"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","16856937, 17548827","2a : Function from experimental evidences in other organisms",19,382,383,191,560,562]
[]
["AZ49_06560","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_3218",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein subunit beta","_",0.92593,0.93284,52.8,{"v":4e-84,"d":"4.00E-84"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme",9694853,"2a : Function from experimental evidences in other organisms",1,249,270,1,249,268]
[null,"CLOSTRIBL3_v1_12011",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1.0037,1.03435,50.18,{"v":2e-83,"d":"2.00E-83"},1,1,"1.3 : Energy metabolism (carbon) ;","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,270,270,1,262,262]
[null,"CD630_08040",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein beta-subunit, core","_",1.01111,1.03409,49.08,{"v":1e-80,"d":"1.00E-80"},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",1,270,270,1,255,264]
[null,"CD630_04000",null,"Clostridium difficile 630","etfB1","Beta-subunit of electron transfer flavoprotein","_",0.92963,0.96169,50.6,{"v":4E-78,"d":"4.00E-78"},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",1,251,270,1,245,261]
[null,"CLOSTRIBL3_v1_20311",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.91111,0.94981,48.78,{"v":7e-75,"d":"7.00E-75"},3,1,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286, 9694853","2a : Function from experimental evidences in other organisms",1,246,270,1,238,259]
[null,"CLOSTRIBL6_v1_0136",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein subunit beta","_",0.98889,1.03089,47.19,{"v":2e-74,"d":"2.00E-74"},2,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,265,270,1,258,259]
[null,"SBF1_v1_470015",null,"Desulfosporosinus sp. SbF1","fixA","electron-transferring flavoprotein, subunit FixA","_",0.97834,1.0037,45.39,{"v":8e-72,"d":"8.00E-72"},1,1,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,270,270,1,266,277]
[null,"AZOLI_0535",null,"Azospirillum lipoferum 4B","fixA","electron transfer flavoprotein beta subunit","_",0.89399,0.93704,45.85,{"v":1e-69,"d":"1.00E-69"},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",1,250,270,1,249,283]
[null,"CLOSTRIBL4_v1_1871",null,"Clostridiales BL-4","etfB","Electron transfer flavoprotein subunit beta","_",0.94074,0.95489,46.06,{"v":2e-67,"d":"2.00E-67"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,250,270,1,249,266]
[null,"MGMSRv2_0362",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","Electron transfer flavoprotein, beta-subunit","_",0.95423,1.0037,42.8,{"v":5e-67,"d":"5.00E-67"},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",1,266,270,1,268,284]
[null,"CD630_10550",null,"Clostridium difficile 630","etfB","Electron transfer flavoproteins subunit beta","_",0.99259,1.01132,44.78,{"v":4e-66,"d":"4.00E-66"},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",1,265,270,6,264,265]
[null,"MGMSRv2_1063",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.97842,1.00741,41.54,{"v":2e-63,"d":"2.00E-63"},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)",1,267,270,1,268,278]
[null,"pRALTA_0381",null,"Cupriavidus taiwanensis LMG19424","fixA","Electron transfer flavoprotein beta-subunit","_",0.97163,1.01481,43.07,{"v":1E-62,"d":"1.00E-62"},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",1,267,270,1,268,282]
[null,"BURPHP2_0599",null,"Burkholderia phymatum STM815","fixA","protein fixA, electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.86879,0.90741,43.67,{"v":6e-62,"d":"6.00E-62"},1,1,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ; 6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",1,241,270,1,241,282]
[null,"CLOSTRIBL3_v1_20124",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1.00741,1.02642,38.97,{"v":2e-61,"d":"2.00E-61"},4,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,270,270,1,265,265]
[null,"CLOSTRIBL3_v1_11115",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1.00741,1.03817,40.07,{"v":3e-60,"d":"3.00E-60"},5,1,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,270,270,1,262,262]
[null,"CD630_11710",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein subunit alpha","_",1,1.01887,42.59,{"v":4e-60,"d":"4.00E-60"},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",1,265,270,4,265,265]
[null,"BRADO5386",null,"Bradyrhizobium sp. ORS278","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.96085,1,42.59,{"v":1E-59,"d":"1.00E-59"},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)",1,263,270,1,266,281]
[null,"SBF1_v1_6700003",null,"Desulfosporosinus sp. SbF1","etfB_2","electron-transferring flavoprotein, beta subunit EtfB (lutD-associated)","_",0.94815,1.01186,40.62,{"v":3e-59,"d":"3.00E-59"},2,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,254,270,1,249,253]
[null,"CLOSTRIBL6_v1_2821",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein, beta subunit","_",1.01111,1.02632,39.56,{"v":4e-58,"d":"4.00E-58"},3,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,270,270,1,266,266]
[null,"RM41v1_psym670028",null,"Sinorhizobium sp. Rm41","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.83562,0.9037,42.21,{"v":3e-55,"d":"3.00E-55"},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)",1,240,270,1,241,292]
[null,"FRAAL5878",null,"Frankia alni ACN14a","fixA","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",1.01111,1.04598,38.46,{"v":1E-53,"d":"1.00E-53"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","16.1 : Circulate ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,270,270,1,261,261]
[null,"CLOSTRIBL3_v1_11488",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1.00741,1.02642,41.54,{"v":5E-52,"d":"5.00E-52"},6,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,265,270,1,255,265]
[null,"SCFA_v1_500013",null,"Ca. Phosphitivorax anaerolimi F81","etfB","Electron transfer flavoprotein, beta subunit","_",0.96703,0.97778,35.98,{"v":1E-51,"d":"1.00E-51"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,263,270,2,256,273]
[null,"SCFA_v1_1630003",null,"Ca. Propionivorax syntrophicum F70","FixA","Electron transfer flavoproteins subunit beta","_",0.94074,0.96212,36.22,{"v":2e-48,"d":"2.00E-48"},1,2,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,251,270,1,247,264]
[null,"SCFA_v1_3390002","_","Ca. Phosphitivorax butyraticus R76","etfB","Electron transfer flavoprotein subunit beta","_",0.92593,0.96899,38.8,{"v":4e-45,"d":"4.00E-45"},1,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,250,270,4,239,258]
[null,"SCFA_v1_130010",null,"Ca. Phosphitivorax anaerolimi F81","etfB","Electron transfer flavoprotein subunit beta","_",0.92963,0.97287,39.04,{"v":3e-44,"d":"3.00E-44"},2,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,250,270,4,239,258]
[null,"SCFA_v1_1080001",null,"Ca. Phosphitivorax butyraticus R76","etfB","Electron transfer flavoprotein subunit beta (fragment)","_",0.67778,1.01105,38.8,{"v":6e-39,"d":"6.00E-39"},2,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,183,270,2,178,181]
[null,"HEAR0619",null,"Herminiimonas arsenicoxydans","etfB","electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.91852,0.99598,36.69,{"v":1e-38,"d":"1.00E-38"},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",1,246,270,1,232,249]
[null,"PSEEN3658",null,"Pseudomonas entomophila L48","etfB","electron transfer flavoprotein beta-subunit","_",0.91852,0.99598,35.08,{"v":1e-34,"d":"1.00E-34"},1,1,"1.4.3 : Electron carrier ;","_","Unknown","6 : Energy metabolism ;","c : carrier","_","2a : Function from experimental evidences in other organisms",1,247,270,1,233,249]
[null,"BRADO6492",null,"Bradyrhizobium sp. ORS278","etfB","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.81111,0.87952,36.99,{"v":6e-33,"d":"6.00E-33"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8599534,"2a : Function from experimental evidences in other organisms",1,218,270,1,210,249]
[null,"BN77v1_0452","_","Rhizobium mesoamericanum STM3625","etfB","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.63333,0.855,37.43,{"v":2e-24,"d":"2.00E-24"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier",10026281,"2a : Function from experimental evidences in other organisms",1,170,270,34,195,200]
[null,"NMCC_2114",null,"Neisseria meningitidis 053442","etfB","electron transfer flavoprotein beta-subunit (beta-ETF; electron transfer flavoprotein small subunit; ETFSS) (pseudogene part 2)","_",0.55185,0.81868,37.58,{"v":1e-17,"d":"1.00E-17"},1,1,"_","_","2 : Cytoplasmic","_","f : factor","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",71,218,270,5,143,182]
[]
["AZ49_06565","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","_",0.99112,1.00601,57.31,{"v":5e-129,"d":"5.00E-129"},1,1,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","c : carrier","17189250, 20059546, 21398533, 8655474, 11466286","2a : Function from experimental evidences in other organisms",1,335,338,1,333,333]
[null,"CD630_04010",null,"Clostridium difficile 630","etfA1","Alpha-subunit of electron transfer flavoprotein","_",0.95652,0.97633,56.67,{"v":2e-122,"d":"2.00E-122"},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",2,331,338,6,333,345]
[null,"CLOSTRIBL3_v1_12010",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",1,1.00595,50.59,{"v":3e-118,"d":"3.00E-118"},3,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,337,338,1,336,336]
[null,"CLOSTRIBL6_v1_0137",null,"Clostridiales BL-6","etfA","electron transfer flavoprotein (alpha subunit)","_",0.97399,0.99704,51.93,{"v":3e-115,"d":"3.00E-115"},1,1,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 20059546, 21398533","2a : Function from experimental evidences in other organisms",1,335,338,8,340,346]
[null,"CD630_08050",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein alpha-subunit","_",0.97941,0.98521,48.95,{"v":1e-112,"d":"1.00E-112"},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",1,333,338,10,340,340]
[null,"CLOSTRIBL6_v1_3217",null,"Clostridiales BL-6","etfA","Electron transfer flavoprotein subunit alpha","_",0.97929,0.99102,50.76,{"v":1E-107,"d":"1.00E-107"},2,1,"_","_","2 : Cytoplasmic","_","e : enzyme",9694853,"2a : Function from experimental evidences in other organisms",7,335,338,6,333,334]
[null,"CLOSTRIBL4_v1_1872",null,"Clostridiales BL-4","etfA","Electron transfer flavoprotein subunit alpha","_",0.96467,1.0503,49.3,{"v":2e-106,"d":"2.00E-106"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",2,332,338,8,362,368]
[null,"CD630_10560",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.97633,0.98214,50,{"v":6E-102,"d":"6.00E-102"},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",9,336,338,4,331,336]
[null,"SBF1_v1_470014",null,"Desulfosporosinus sp. SbF1","fixB","electron-transferring flavoprotein, subunit FixB","_",0.75621,0.99112,46.87,{"v":8e-99,"d":"8.00E-99"},1,1,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,338,338,110,442,443]
[null,"CLOSTRIBL3_v1_20125",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.97633,0.99099,48.18,{"v":6E-98,"d":"6.00E-98"},4,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",7,335,338,2,329,333]
[null,"pRALTA_0380",null,"Cupriavidus taiwanensis LMG19424","fixB","Electron transfer flavoprotein, alpha subunit","_",0.88533,0.98225,45.78,{"v":4E-95,"d":"4.00E-95"},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",3,330,338,29,358,375]
[null,"BURPHP2_0598",null,"Burkholderia phymatum STM815","fixB","Protein fixB, Electron transfer flavoprotein, alpha subunit","_",0.8877,0.98225,45.18,{"v":1e-92,"d":"1.00E-92"},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",3,330,338,29,358,374]
[null,"MGMSRv2_1064",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.9235,1,43.49,{"v":8e-91,"d":"8.00E-91"},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)",2,334,338,24,358,366]
[null,"AZOLI_0536",null,"Azospirillum lipoferum 4B","fixB","electron transfer flavoprotein alpha chain","_",0.94429,1.00296,44.54,{"v":9e-90,"d":"9.00E-90"},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",3,337,338,18,354,359]
[null,"CLOSTRIBL3_v1_11114",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.84158,1.00592,43.53,{"v":9e-88,"d":"9.00E-88"},5,1,"_","_","2 : Cytoplasmic","_","c : carrier",17189250,"2a : Function from experimental evidences in other organisms",1,337,338,66,400,404]
[null,"MGMSRv2_0361",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","Electron transfer flavoprotein, alpha subunit","_",0.91576,0.99704,41.84,{"v":5e-86,"d":"5.00E-86"},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",5,337,338,30,363,368]
[null,"CLOSTRIBL3_v1_11487",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.98225,1.0122,46.99,{"v":9e-84,"d":"9.00E-84"},6,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",5,334,338,4,325,328]
[null,"BSU28520",null,"Bacillus subtilis 168","etfA","electron transfer flavoprotein (alpha subunit)","_",0.97337,1.01231,44.38,{"v":9e-84,"d":"9.00E-84"},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",7,333,338,3,320,325]
[null,"SBF1_v1_6700004",null,"Desulfosporosinus sp. SbF1","etfA_2","electron-transferring flavoprotein, alpha subunit EtfA (lutD-associated)","_",0.83831,0.99704,41.84,{"v":1e-81,"d":"1.00E-81"},3,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,335,338,66,396,402]
[null,"CD630_11720",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.81527,0.97929,39.58,{"v":1e-81,"d":"1.00E-81"},4,1,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",5,335,338,68,394,406]
[null,"BRADO5385",null,"Bradyrhizobium sp. ORS278","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.89946,0.97929,43.2,{"v":1e-81,"d":"1.00E-81"},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)",6,332,338,28,355,368]
[null,"RM41v1_psym670029",null,"Sinorhizobium sp. Rm41","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.94901,0.99112,39.7,{"v":5e-77,"d":"5.00E-77"},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",5,334,338,11,342,353]
[null,"SCFA_v1_130009",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",0.98225,1.03106,43.37,{"v":7E-72,"d":"7.00E-72"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,336,338,3,322,322]
[null,"CLOSTRIBL6_v1_2820",null,"Clostridiales BL-6","etfA","Electron transfer flavoprotein subunit alpha","_",0.97633,1.0061,43.33,{"v":1E-70,"d":"1.00E-70"},3,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",7,335,338,6,326,328]
[null,"SCFA_v1_2400007","_","Ca. Phosphitivorax butyraticus R76","etfA","Electron transfer flavoprotein subunit alpha","_",0.92308,0.93694,41.35,{"v":6e-70,"d":"6.00E-70"},1,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",23,334,338,22,330,333]
[null,"SCFA_v1_500012",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",0.92308,0.93694,40.71,{"v":3e-69,"d":"3.00E-69"},2,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",23,334,338,22,330,333]
[null,"LEPBIa1132",null,"Leptospira biflexa serovar Patoc Patoc 1","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.97041,1.02821,42.38,{"v":3E-68,"d":"3.00E-68"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","16.10 : Respire ;","c : carrier","_","2a : Function from experimental evidences in other organisms",9,336,338,4,319,319]
[null,"BN45v3_60005",null,"Mycobacterium canettii STB-J","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97337,1.03459,39.51,{"v":2e-61,"d":"2.00E-61"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",9,336,338,4,318,318]
[null,"BN44v3_60522",null,"Mycobacterium canettii STB-D","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97337,1.03459,39.51,{"v":2e-61,"d":"2.00E-61"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",9,336,338,4,318,318]
[null,"BN43v3_60007",null,"Mycobacterium canettii STB-L","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97337,1.03459,39.51,{"v":2e-61,"d":"2.00E-61"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",9,336,338,4,318,318]
[null,"BN42v3_41031",null,"Mycobacterium canettii STB-K","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.97337,1.03459,39.51,{"v":2e-61,"d":"2.00E-61"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",9,336,338,4,318,318]
[null,"FRAAL5877",null,"Frankia alni ACN14a","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.97337,1.02812,40.43,{"v":1e-60,"d":"1.00E-60"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","16.1 : Circulate ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,335,338,4,318,320]
[null,"MARHY1802",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","etfA","electron transfer flavoprotein alpha-subunit","_",0.9645,1.04153,36.5,{"v":5E-56,"d":"5.00E-56"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6 : Energy metabolism ;","c : carrier",3415685,"2a : Function from experimental evidences in other organisms",9,333,338,3,311,313]
[null,"AZOLI_p50300",null,"Azospirillum lipoferum 4B","etfA2","Electron transfer flavoprotein alpha-subunit","_",0.95858,1.03846,38.89,{"v":7e-54,"d":"7.00E-54"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier","10984043, 16159782, 8599534","2b : Function from indirect experimental evidences (e.g. phenotypes)",9,331,338,4,311,312]
[null,"BURPHK2_1883",null,"Burkholderia phymatum STM815","etfA","electron transfer flavoprotein, alpha subunit","_",0.97929,1.0609,37.16,{"v":1E-51,"d":"1.00E-51"},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",9,332,338,3,311,312]
[null,"AZCBGv1_p190001","_","Azospirillum brasilense CBG497","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.80769,0.88065,42.49,{"v":2e-49,"d":"2.00E-49"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ;","c : carrier","10984043, 16159782, 8599534","2b : Function from indirect experimental evidences (e.g. phenotypes)",62,333,338,51,309,310]
[null,"PSHAa1617",null,"Pseudoalteromonas haloplanktis TAC125","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.95266,1.04545,36.65,{"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",11,331,338,5,308,308]
[null,"HEAR0620",null,"Herminiimonas arsenicoxydans","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.96154,1.05178,37.85,{"v":4e-48,"d":"4.00E-48"},1,2,"1.4.3 : electron carrier ;","_","1 : Unknown","6 : Energy metabolism ;","c : carrier","10026281, 1576992, 8376381, 8599534","2a : Function from experimental evidences in other organisms",11,331,338,5,308,309]
[null,"METDI2208",null,"Methylobacterium extorquens DM4","etfA","electron transfer flavoprotein, NAD/FAD-binding domain and ETFP adenine nucleotide-binding domain-like","_",0.96154,1.02524,37.54,{"v":4e-47,"d":"4.00E-47"},1,2,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","15188393, 16926146, 8599534","2a : Function from experimental evidences in other organisms",14,335,338,8,315,317]
[null,"Mchl_1823",null,"Methylobacterium extorquens CM4","etfA","electron transfer flavoprotein alpha subunit","_",0.96154,1.02524,37.23,{"v":2E-46,"d":"2.00E-46"},1,2,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","15188393, 16926146, 8599534","2a : Function from experimental evidences in other organisms",14,335,338,8,315,317]
[null,"CMR15v5_3436",null,"Ralstonia solanacearum CMR15","etfA","Electron transfer flavoprotein, alpha-subunit","_",0.88166,0.9582,38.93,{"v":9E-46,"d":"9.00E-46"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",39,331,338,29,310,311]
[null,"NT26v4_3414",null,"Rhizobium sp. NT-26","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.95858,1.04854,35.49,{"v":1e-45,"d":"1.00E-45"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",9,331,338,3,309,309]
[null,"Rmet_0738",null,"Cupriavidus metallidurans CH34","etfA","Electron transfer flavoprotein subunit alpha (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.88462,0.96141,38.46,{"v":7E-45,"d":"7.00E-45"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",39,331,338,29,310,311]
[null,"Rmet_5518",null,"Cupriavidus metallidurans CH34","etfA","electron transfer flavoprotein, alpha subunit","_",0.88166,0.96129,36.91,{"v":9e-44,"d":"9.00E-44"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier","10026281, 1576992, 8376381, 8599534","2a : Function from experimental evidences in other organisms",39,331,338,29,310,310]
[null,"BRADO6491",null,"Bradyrhizobium sp. ORS278","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.95858,1.0418,35.49,{"v":1e-43,"d":"1.00E-43"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",11,333,338,5,311,311]
[null,"RALTA_A0796",null,"Cupriavidus taiwanensis LMG19424","etfA","ELECTRON TRANSFER FLAVOPROTEIN, ALPHA-SUBUNIT","_",0.88166,0.9582,37.25,{"v":1e-43,"d":"1.00E-43"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",39,331,338,29,310,311]
[null,"PSEEN3657",null,"Pseudomonas entomophila L48","etfA","electron transfer flavoprotein alpha-subunit","_",0.80178,0.98188,38.75,{"v":1e-40,"d":"1.00E-40"},1,2,"1.4.3 : Electron carrier ;","_","Unknown","6 : Energy metabolism ;","c : carrier","_","2a : Function from experimental evidences in other organisms",62,331,338,20,276,276]
[]
["AZ49_07320","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","_",1,1.00769,40.84,{"v":3e-62,"d":"3.00E-62"},1,2,"1.3 : Energy metabolism (carbon) ;","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,260,260,1,262,262]
[null,"SBF1_v1_470015",null,"Desulfosporosinus sp. SbF1","fixA","electron-transferring flavoprotein, subunit FixA","_",0.96029,1.02308,39.1,{"v":2e-57,"d":"2.00E-57"},1,2,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,260,260,1,266,277]
[null,"BN11v3_3200005",null,"Tetrasphaera australiensis Ben110","etfB","Electron transfer flavoprotein subunit beta","_",0.99242,1.00769,38.55,{"v":4e-57,"d":"4.00E-57"},1,1,"_","_","2 : Cytoplasmic","6.5 : Electron transport ;","e : enzyme","10026281, 9694853","2a : Function from experimental evidences in other organisms",1,260,260,5,264,264]
[null,"CD630_08040",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein beta-subunit, core","_",0.97727,0.99231,35.27,{"v":6e-55,"d":"6.00E-55"},1,2,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","c : carrier","17941859, 2326318","2a : Function from experimental evidences in other organisms",1,254,260,1,258,264]
[null,"SCFA_v1_1630003","_","Ca. Propionivorax syntrophicum F70","FixA","Electron transfer flavoproteins subunit beta","_",1,1.01538,36.36,{"v":2E-50,"d":"2.00E-50"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,260,260,1,263,264]
[null,"BRADO5386",null,"Bradyrhizobium sp. ORS278","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.91815,0.99231,37.98,{"v":3e-50,"d":"3.00E-50"},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)",1,246,260,1,258,281]
[null,"CLOSTRIBL3_v1_20311",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.91923,0.92278,36.4,{"v":1e-49,"d":"1.00E-49"},4,2,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286, 9694853","2a : Function from experimental evidences in other organisms",1,238,260,1,238,259]
[null,"CLOSTRIBL6_v1_3218",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein subunit beta","_",0.97761,1.00769,38.93,{"v":5e-49,"d":"5.00E-49"},1,2,"_","_","2 : Cytoplasmic","_","e : enzyme",9694853,"2a : Function from experimental evidences in other organisms",1,254,260,1,261,268]
[null,"CD630_10550",null,"Clostridium difficile 630","etfB","Electron transfer flavoproteins subunit beta","_",0.90189,0.91923,35.15,{"v":1e-48,"d":"1.00E-48"},3,2,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","c : carrier","18060402, 17873051, 15991056","2a : Function from experimental evidences in other organisms",1,237,260,6,243,265]
[null,"BURPHP2_0599",null,"Burkholderia phymatum STM815","fixA","protein fixA, electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.93972,1.01923,35.85,{"v":1e-48,"d":"1.00E-48"},1,2,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ; 6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",1,257,260,1,260,282]
[null,"AZOLI_0535",null,"Azospirillum lipoferum 4B","fixA","electron transfer flavoprotein beta subunit","_",0.90813,0.98846,35.41,{"v":2e-48,"d":"2.00E-48"},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",1,248,260,1,257,283]
[null,"BN42v3_41032",null,"Mycobacterium canettii STB-K","fixA","Putative electron transfer flavoprotein (beta-subunit) FixA (beta-ETF) (electron transfer flavoprotein small subunit) (ETFSS)","_",1.0038,1.01538,37.5,{"v":3e-48,"d":"3.00E-48"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,260,260,3,263,263]
[null,"CLOSTRIBL3_v1_11488",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.88302,0.9,38.89,{"v":1e-47,"d":"1.00E-47"},5,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,230,260,1,234,265]
[null,"CLOSTRIBL6_v1_0136",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein subunit beta","_",0.91923,0.92278,35.98,{"v":1e-47,"d":"1.00E-47"},2,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,238,260,1,238,259]
[null,"BN45v3_60006",null,"Mycobacterium canettii STB-J","fixA","Putative electron transfer flavoprotein (beta-subunit) FixA (beta-ETF) (electron transfer flavoprotein small subunit) (ETFSS)","_",1.00376,1.02692,36.7,{"v":2e-47,"d":"2.00E-47"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,260,260,3,266,266]
[null,"BN44v3_60523",null,"Mycobacterium canettii STB-D","fixA","Putative electron transfer flavoprotein (beta-subunit) FixA (beta-ETF) (electron transfer flavoprotein small subunit) (ETFSS)","_",1.00376,1.02692,36.7,{"v":2e-47,"d":"2.00E-47"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,260,260,3,266,266]
[null,"BN43v3_60008",null,"Mycobacterium canettii STB-L","fixA","Putative electron transfer flavoprotein (beta-subunit) FixA (beta-ETF) (electron transfer flavoprotein small subunit) (ETFSS)","_",1.00376,1.02692,36.7,{"v":2e-47,"d":"2.00E-47"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,260,260,3,266,266]
[null,"MGMSRv2_0362",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","Electron transfer flavoprotein, beta-subunit","_",0.84507,0.92308,37.5,{"v":1E-46,"d":"1.00E-46"},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",1,231,260,1,240,284]
[null,"MGMSRv2_1063",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.96763,1.03462,35.69,{"v":1E-46,"d":"1.00E-46"},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)",1,258,260,1,269,278]
[null,"CLOSTRIBL6_v1_2821",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein, beta subunit","_",0.8985,0.91923,39.33,{"v":1e-44,"d":"1.00E-44"},3,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,229,260,1,234,266]
[null,"pRALTA_0381",null,"Cupriavidus taiwanensis LMG19424","fixA","Electron transfer flavoprotein beta-subunit","_",0.84043,0.91154,35.44,{"v":1e-44,"d":"1.00E-44"},1,2,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ;  6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",1,229,260,1,237,282]
[null,"RM41v1_psym670028",null,"Sinorhizobium sp. Rm41","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.81507,0.91538,35.29,{"v":1E-41,"d":"1.00E-41"},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)",1,229,260,1,238,292]
[null,"SBF1_v1_550001",null,"Desulfosporosinus sp. SbF1","etfB","electron-transferring flavoprotein, beta subunit EtfB","_",0.98462,0.99611,35.55,{"v":6e-41,"d":"6.00E-41"},2,1,"_","_","2 : Cytoplasmic","_","c : carrier",23468890,"2a : Function from experimental evidences in other organisms",1,253,260,1,252,257]
[]
["AZ49_07325","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","_",1.00599,1.00901,41.96,{"v":4e-83,"d":"4.00E-83"},1,2,"_","_","2 : Cytoplasmic","_","e : enzyme",9694853,"2a : Function from experimental evidences in other organisms",1,332,333,1,333,334]
[null,"AZOLI_0536",null,"Azospirillum lipoferum 4B","fixB","electron transfer flavoprotein alpha chain","_",0.91365,0.98498,39.33,{"v":2e-75,"d":"2.00E-75"},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",1,324,333,18,344,359]
[null,"SBF1_v1_550002",null,"Desulfosporosinus sp. SbF1","etfA","electron-transferring flavoprotein, alpha subunit EtfA","_",0.98799,1.00305,39.21,{"v":1E-73,"d":"1.00E-73"},1,2,"_","_","2 : Cytoplasmic","_","c : carrier",23468890,"2a : Function from experimental evidences in other organisms",3,331,333,1,326,328]
[null,"MGMSRv2_0361",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","Electron transfer flavoprotein, alpha subunit","_",0.89674,0.99099,39.09,{"v":4e-72,"d":"4.00E-72"},1,2,"1.4.3 : Electron carrier ;","_","1 : Unknown","5.6 : Nitrogen fixation ;","c : carrier","15028689, 3029021, 7875566, 8796346, 9163424, 8599534, 2503674","2a : Function from experimental evidences in other organisms",5,330,333,32,359,368]
[null,"MGMSRv2_1064",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.91257,1.003,37.13,{"v":2e-71,"d":"2.00E-71"},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)",1,330,333,25,357,366]
[null,"CLOSTRIBL3_v1_20312",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.98799,0.98799,37.99,{"v":2e-71,"d":"2.00E-71"},1,2,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","c : carrier","17189250, 20059546, 21398533, 8655474, 11466286","2a : Function from experimental evidences in other organisms",5,332,333,7,333,333]
[null,"BURPHP2_0598",null,"Burkholderia phymatum STM815","fixB","Protein fixB, Electron transfer flavoprotein, alpha subunit","_",0.87166,0.97898,36.5,{"v":6e-70,"d":"6.00E-70"},1,2,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ; 6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",5,324,333,33,355,374]
[null,"CLOSTRIBL3_v1_12010",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.97917,0.98799,36.47,{"v":9e-70,"d":"9.00E-70"},3,2,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",5,332,333,7,334,336]
[null,"RM41v1_psym670029",null,"Sinorhizobium sp. Rm41","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.94051,0.997,38.25,{"v":3e-69,"d":"3.00E-69"},1,2,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ; 7.1 : Cytoplasm ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ; 16.15 : Symbiosis ;","c : carrier","15028689, 3029021","1c : Function from experimental evidences in the studied genus",5,330,333,13,341,353]
[null,"CD630_08050",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein alpha-subunit","_",0.92941,0.94895,35.76,{"v":3e-69,"d":"3.00E-69"},2,2,"1.3 : Energy metabolism (carbon) ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","c : carrier","17941859, 2326318","2a : Function from experimental evidences in other organisms",16,330,333,27,340,340]
[null,"pRALTA_0380",null,"Cupriavidus taiwanensis LMG19424","fixB","Electron transfer flavoprotein, alpha subunit","_",0.86933,0.97898,35.58,{"v":5e-68,"d":"5.00E-68"},1,2,"1.4.3 : Electron carrier ; 1.8.4 : Nitrogen fixation ;","_","1 : Unknown","5.6 : Nitrogen fixation ;  6.5 : Electron transport ;","c : carrier",3029021,"2a : Function from experimental evidences in other organisms",5,324,333,33,355,375]
[null,"CLOSTRIBL6_v1_0137",null,"Clostridiales BL-6","etfA","electron transfer flavoprotein (alpha subunit)","_",0.94509,0.98198,35.78,{"v":1e-66,"d":"1.00E-66"},2,2,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 20059546, 21398533","2a : Function from experimental evidences in other organisms",5,330,333,14,338,346]
[null,"SBF1_v1_470014",null,"Desulfosporosinus sp. SbF1","fixB","electron-transferring flavoprotein, subunit FixB","_",0.73363,0.97598,35.69,{"v":1e-65,"d":"1.00E-65"},2,2,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,330,333,113,435,443]
[null,"CD630_10560",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.96429,0.97297,37.04,{"v":1e-64,"d":"1.00E-64"},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",6,328,333,3,324,336]
[null,"BRADO5385",null,"Bradyrhizobium sp. ORS278","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.89402,0.98799,36.78,{"v":5e-64,"d":"5.00E-64"},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)",5,329,333,29,355,368]
[null,"CLOSTRIBL3_v1_11487",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.97598,0.99085,36.31,{"v":1E-62,"d":"1.00E-62"},4,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",5,329,333,6,323,328]
[null,"CLOSTRIBL6_v1_2820",null,"Clostridiales BL-6","etfA","Electron transfer flavoprotein subunit alpha","_",0.98198,0.99695,35.47,{"v":3e-59,"d":"3.00E-59"},3,2,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",2,328,333,3,322,328]
[null,"BN43v3_60007",null,"Mycobacterium canettii STB-L","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.99399,1.04088,37.16,{"v":1e-55,"d":"1.00E-55"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",7,333,333,4,318,318]
[null,"BN45v3_60005",null,"Mycobacterium canettii STB-J","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.98799,1.03459,36.47,{"v":2E-55,"d":"2.00E-55"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",7,333,333,4,318,318]
[null,"BN44v3_60522",null,"Mycobacterium canettii STB-D","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.99399,1.04088,37.16,{"v":6e-55,"d":"6.00E-55"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",7,333,333,4,318,318]
[null,"BN42v3_41031",null,"Mycobacterium canettii STB-K","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.99399,1.04088,36.86,{"v":3e-54,"d":"3.00E-54"},1,2,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",7,333,333,4,318,318]
[null,"HEAR0620","_","Herminiimonas arsenicoxydans","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.87688,0.94498,38.7,{"v":8e-52,"d":"8.00E-52"},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",37,328,333,29,308,309]
[null,"THI_1679",null,"Thiomonas sp. 3As","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF)(Electron transfer flavoprotein large subunit) (ETFLS)","_",0.87688,0.94194,36.64,{"v":8e-47,"d":"8.00E-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",39,328,333,31,310,310]
[null,"PSEEN3657","_","Pseudomonas entomophila L48","etfA","electron transfer flavoprotein alpha-subunit","_",0.86486,1.04348,35.07,{"v":9e-44,"d":"9.00E-44"},1,1,"1.4.3 : Electron carrier ;","_","Unknown","6 : Energy metabolism ;","c : carrier","_","2a : Function from experimental evidences in other organisms",44,328,333,3,276,276]
[]
["AZ49_01090","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","_",0.96864,0.97887,55.04,{"v":5e-111,"d":"5.00E-111"},1,1,"_","7.1.1.-","5 : Inner membrane protein","_","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",7,282,284,5,279,287]
[null,"NBG4_v1_240023",null,"Candidatus Sulfobium mesophilum","_","Putative electron transport complex protein RnfB","_",0.66414,0.92606,46.01,{"v":6e-83,"d":"6.00E-83"},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",11,273,284,58,315,396]
[null,"CD630_11420",null,"Clostridium difficile 630","rnfB","Electron transport complex protein","_",0.85538,0.97887,39.57,{"v":3E-68,"d":"3.00E-68"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","9492268, 9154934, 8264535, 12773378, 11160111","2a : Function from experimental evidences in other organisms",6,283,284,4,270,325]
[null,"SCFA_v1_420041",null,"Ca. Phosphitivorax anaerolimi F81","RnfB","electron transport complex protein RnfB","_",0.8179,0.9331,38.11,{"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)",8,272,284,2,261,324]
[null,"SCFA_v1_1220011",null,"Ca. Phosphitivorax butyraticus R76","rnfB","Electron transport complex protein RnfB","_",0.80864,0.92254,36.64,{"v":9e-58,"d":"9.00E-58"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,269,284,2,258,324]
[null,"CLOSTRIBL4_v1_2204",null,"Clostridiales BL-4","rnfB","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit B","_",0.92254,0.99242,37.02,{"v":1E-56,"d":"1.00E-56"},1,1,"_","7.1.1.1","2 : Cytoplasmic","_","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",11,272,284,8,262,264]
[null,"MALCv4_3932",null,"Methylomicrobium alcaliphilum 20Z","rnfB","electron transport complex protein RnfB","_",0.97213,0.98239,35.13,{"v":2E-55,"d":"2.00E-55"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,280,284,4,275,287]
[null,"SCFA_v1_1550009",null,"Ca. Phosphitivorax anaerolimi F81","_","putative ferredoxin","_",0.18662,0.92982,39.62,1e-07,3,5,"_","_","9 : Periplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",217,269,284,7,54,57]
[]
["AZ49_01095","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","_",0.97409,0.98429,70.74,{"v":4e-97,"d":"4.00E-97"},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",4,191,191,4,191,193]
[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,"ECK1623",null,"Escherichia coli K12","rsxA","putative inner membrane subunit of an electron transport system","_",0.97927,0.98953,51.85,{"v":9e-71,"d":"9.00E-71"},1,1,"6.1 : Membrane ;","_","11 : Membrane","14 : Cell envelope ;","m : membrane component","10411911, 10637328, 12773378","3 : Putative function from multiple computational evidences",3,191,191,3,191,193]
[null,"ECUMN_1918",null,"Escherichia coli UMN026","rsxA","putative inner membrane subunit of an electron transport system","_",0.97927,0.98953,51.85,{"v":1E-70,"d":"1.00E-70"},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",3,191,191,3,191,193]
[null,"ECS88_1675",null,"Escherichia coli S88","rsxA","putative inner membrane subunit of an electron transport system","_",0.97927,0.98953,51.85,{"v":1E-70,"d":"1.00E-70"},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",3,191,191,3,191,193]
[null,"EFER_1416",null,"Escherichia fergusonii ATCC 35469T","rsxA","putative inner membrane subunit of an electron transport system","_",0.97927,0.98953,51.32,{"v":5e-70,"d":"5.00E-70"},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",3,191,191,3,191,193]
[null,"SCFA_v1_1220010",null,"Ca. Phosphitivorax butyraticus R76","rnfA","Electron transport complex protein rnfA","_",0.99476,0.99476,50.53,{"v":4e-68,"d":"4.00E-68"},1,1,"6.1 : Membrane ;","_","11 : Membrane","14 : Cell envelope ;","m : membrane component","10411911, 10637328, 12773378","3 : Putative function from multiple computational evidences",2,191,191,1,190,191]
[null,"SCFA_v1_420040",null,"Ca. Phosphitivorax anaerolimi F81","rnfA","Electron transport complex protein rnfA","_",0.91388,1,48.69,{"v":5e-67,"d":"5.00E-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)",1,191,191,18,208,209]
[null,"VIBNIv4_A0909",null,"Vibrio nigripulchritudo SFn1","rnfA","Electron transport complex protein rnfA","_",0.97927,0.98953,50.79,{"v":5e-67,"d":"5.00E-67"},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",3,191,191,3,191,193]
[null,"PSHAa1105",null,"Pseudoalteromonas haloplanktis TAC125","rsxA","Electron transport complex protein rnfA, inner membrane protein","_",0.97927,0.98953,49.21,{"v":6e-66,"d":"6.00E-66"},1,1,"1.4.2 : Electron transport ;","_","integral inner membrane","_","t : transporter",10411911,"2a : Function from experimental evidences in other organisms",3,191,191,3,191,193]
[null,"MAGMOv5_3973",null,"Magnetotactic ovoidal bacterium MO-1","rnfA","Electron transport complex protein rnfA","_",0.95431,0.98429,47.87,{"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","_",0.97927,0.98953,47.09,{"v":8e-63,"d":"8.00E-63"},1,1,"6.1 : Membrane ;","_","11 : Membrane","_","t : transporter","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,191,191,3,191,193]
[null,"CD630_11410",null,"Clostridium difficile 630","rnfA","Electron transport complex protein","_",0.99476,0.99476,48.95,{"v":6e-62,"d":"6.00E-62"},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",2,191,191,1,189,191]
[null,"CLOSTRIBL4_v1_2203",null,"Clostridiales BL-4","rnfA","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit A","_",0.93434,0.96859,43.78,{"v":9e-59,"d":"9.00E-59"},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,"MALCv4_3934",null,"Methylomicrobium alcaliphilum 20Z","rnfA","electron transport complex protein RnfA","_",0.96891,0.97906,47.59,{"v":1E-58,"d":"1.00E-58"},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",4,190,191,6,191,193]
[null,"MARHY1378",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","nqrE","Na(+)-translocating NADH-quinone reductase subunit E","_",0.97525,1.03141,39.59,{"v":3e-48,"d":"3.00E-48"},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",4,190,191,4,200,202]
[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)","_",0.97462,1.00524,41.67,{"v":5e-48,"d":"5.00E-48"},1,1,"_","1.6.5.8","11 : Membrane","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,190,191,4,195,197]
[null,"VIBNIv4_A0570",null,"Vibrio nigripulchritudo SFn1","nqrE","Na(+)-translocating NADH-quinone reductase subunit E","_",0.97475,1.01047,39.9,{"v":7e-47,"d":"7.00E-47"},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",4,190,191,4,196,198]
[]
["AZ49_01100","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-90,"d":"2.00E-90"},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","_",0.91304,0.95939,55.03,{"v":3e-70,"d":"3.00E-70"},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_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,"SCFA_v1_190015",null,"Ca. Phosphitivorax butyraticus R76","rnfE","Ion-translocating oxidoreductase complex subunit E (Predicted NADH:ubiquinone oxidoreductase, subunit RnfE)","_",0.93578,0.98551,45.59,{"v":2e-60,"d":"2.00E-60"},1,1,"6.1 : Membrane ;","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","c : carrier","10411911, 10637328, 12773378","3 : Putative function from multiple computational evidences",1,196,207,1,204,218]
[null,"CLOSTRIBL4_v1_2202",null,"Clostridiales BL-4","rnfE","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit E","_",0.8087,0.89855,44.62,{"v":1E-54,"d":"1.00E-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":9e-51,"d":"9.00E-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","_",0.89286,0.96618,41.5,{"v":1e-49,"d":"1.00E-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)",5,203,207,8,206,224]
[null,"MALCv4_3935",null,"Methylomicrobium alcaliphilum 20Z","rnfE","electron transport complex protein RnfE","_",0.85915,0.88406,43.17,{"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","_",0.93074,1.03865,36.28,{"v":5e-44,"d":"5.00E-44"},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",6,206,207,7,220,231]
[null,"ECUMN_1923",null,"Escherichia coli UMN026","rsxE","putative inner membrane NADH-quinone reductase","_",0.93074,1.03865,36.28,{"v":6e-44,"d":"6.00E-44"},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",6,206,207,7,220,231]
[null,"ECS88_1680",null,"Escherichia coli S88","rsxE","putative inner membrane NADH-quinone reductase","_",0.90476,1.00966,36.84,{"v":1e-43,"d":"1.00E-43"},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,"EFER_1411",null,"Escherichia fergusonii ATCC 35469T","rsxE","putative inner membrane NADH-quinone reductase","_",0.9087,1.00966,36.36,{"v":2e-43,"d":"2.00E-43"},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,"MARHY2355",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","rsxE","Electron transport complex protein rnfE. Required for the reduction of SoxR","_",0.88235,1.01449,35.71,{"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,"PSHAa1100",null,"Pseudoalteromonas haloplanktis TAC125","rsxE","Electron transport complex protein rnfE","_",0.90086,1.00966,36.36,{"v":2e-40,"d":"2.00E-40"},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,"VC2292",null,"Vibrio cholerae N16961","nqrD","Na(+)-translocating NADH-quinone reductase subunit D","_",0.95714,0.97101,36.82,{"v":2e-38,"d":"2.00E-38"},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,"MARHY1377",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","nqrD","Na(+)-translocating NADH-quinone reductase subunit D","_",0.90045,0.96135,36.18,{"v":2e-37,"d":"2.00E-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",5,197,207,8,206,221]
[null,"VIBNIv4_A0569",null,"Vibrio nigripulchritudo SFn1","nqrD","Na(+)-translocating NADH-quinone reductase subunit D","_",0.95714,0.97101,35.82,{"v":4e-36,"d":"4.00E-36"},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]
[]
["AZ49_01105","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","_",0.98378,0.99454,49.45,{"v":7e-59,"d":"7.00E-59"},1,1,"_","7.1.1.-","5 : Inner membrane protein","_","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",3,183,183,4,185,185]
[null,"NBG4_v1_240020",null,"Candidatus Sulfobium mesophilum","_","Putative electron transport complex protein RnfG","_",0.83673,0.89617,37.8,{"v":7e-26,"d":"7.00E-26"},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",9,167,183,6,168,196]
[]
["AZ49_01110","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","_",0.93023,0.96677,60.31,{"v":8e-135,"d":"8.00E-135"},1,1,"_","7.1.1.-","5 : Inner membrane protein","_","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",23,338,344,12,329,331]
[null,"SCFA_v1_420043",null,"Ca. Phosphitivorax anaerolimi F81","rnfD","Electron transport complex subunit D","_",1.0029,1.00581,48.55,{"v":2e-103,"d":"2.00E-103"},1,1,"_","_","5 : Inner membrane protein","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",12,340,344,11,345,345]
[null,"CD630_11380",null,"Clostridium difficile 630","rnfD","Electron transport complex protein","_",0.95349,1.00923,49.39,{"v":4e-98,"d":"4.00E-98"},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",19,341,344,2,325,325]
[null,"NBG4_v1_240019",null,"Candidatus Sulfobium mesophilum","_","Putative electron transport complex protein RnfD","_",0.98841,0.99128,45.16,{"v":1e-95,"d":"1.00E-95"},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",18,344,344,6,342,345]
[null,"SCFA_v1_190017",null,"Ca. Phosphitivorax butyraticus R76","rnfD","putative Ion-translocating oxidoreductase complex subunit D","_",0.87791,1.03425,50,{"v":3e-94,"d":"3.00E-94"},1,1,"6.1 : Membrane ;","_","11 : Membrane","18.1 : Enzymes of unknown specificity ;","e : enzyme","10637328, 12773378","3 : Putative function from multiple computational evidences",54,340,344,2,292,292]
[null,"MALCv4_3937",null,"Methylomicrobium alcaliphilum 20Z","rnfD","electron transport complex protein RnfD","_",0.98547,1.02108,44.25,{"v":2e-86,"d":"2.00E-86"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier",8264535,"2a : Function from experimental evidences in other organisms",22,337,344,6,331,332]
[null,"MAGMOv5_3970",null,"Magnetotactic ovoidal bacterium MO-1","rnfD","Electron transport complex protein rnfD","_",0.99721,1.0407,39.94,{"v":5e-85,"d":"5.00E-85"},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)",21,344,344,2,354,359]
[null,"CLOSTRIBL4_v1_2200",null,"Clostridiales BL-4","rnfD","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit D","RHEA:47995 ;",0.92151,1.01603,44.79,{"v":1E-84,"d":"1.00E-84"},1,1,"_","7.1.1.1","2 : Cytoplasmic","_","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",21,337,344,4,306,312]
[]
["AZ49_01115","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","_",0.97374,0.9867,58.2,0,1,1,"_","7.1.1.-","2 : Cytoplasmic","_","e : enzyme","20616070, 23269825","2a : Function from experimental evidences in other organisms",7,448,451,6,447,457]
[null,"NBG4_v1_240018",null,"Candidatus Sulfobium mesophilum","rnfC","Electron transport complex protein RnfC","_",0.96674,1.0023,51.38,{"v":2E-150,"d":"2.00E-150"},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","_",0.99557,1.02278,48.33,{"v":9e-147,"d":"9.00E-147"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,445,451,1,437,439]
[null,"SCFA_v1_420042",null,"Ca. Phosphitivorax anaerolimi F81","rnfC","Electron transport complex subunit RnfC","_",0.99113,1.02523,50.11,{"v":5e-146,"d":"5.00E-146"},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","_",0.99113,1.00449,46.31,{"v":9e-134,"d":"9.00E-134"},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","_",0.70323,0.96674,41.74,{"v":2E-121,"d":"2.00E-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)",8,439,451,13,446,620]
[null,"CLOSTRIBL4_v1_2199",null,"Clostridiales BL-4","rnfC","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit C","_",0.98261,1.00222,42.7,{"v":6e-112,"d":"6.00E-112"},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","_",0.73563,0.99335,39.29,{"v":1e-109,"d":"1.00E-109"},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","_",0.52837,0.99113,38.03,{"v":6e-95,"d":"6.00E-95"},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","_",0.43854,0.98891,37.89,{"v":1e-94,"d":"1.00E-94"},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","_",0.96452,0.97534,39.54,{"v":3e-94,"d":"3.00E-94"},2,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8264535,"2b : Function from indirect experimental evidences (e.g. phenotypes)",3,431,451,7,434,446]
[null,"ECK1625",null,"Escherichia coli K12","rsxC","putative 4Fe-4S ferredoxin-type protein fused with unknown protein","_",0.61216,1.00443,37.97,{"v":1E-91,"d":"1.00E-91"},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","_",0.54545,0.8913,37.4,{"v":5e-45,"d":"5.00E-45"},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]

{"sheet":"SwissProt","index":6,"n_rows":635,"n_cols":22,"rows_kept":635}
["AZ49_00320","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?",1.00234,1.00469,57.94,{"v":3e-173,"d":"3.00E-173"},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?",1.00234,1.00943,56.54,{"v":2E-159,"d":"2.00E-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]
[]
["AZ49_00330","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?",0.8714,0.95781,44.05,{"v":1E-127,"d":"1.00E-127"},1,2,"lctP","L-lactate permease","_","Cell membrane, Membrane, Transmembrane, Transmembrane helix, Transport",10508058,"Streptococcus iniae","_",9,462,521,5,451,474]
[null,"Q46839","IPMed?",0.97143,1.04415,32.35,{"v":8e-84,"d":"8.00E-84"},2,1,"glcA","Glycolate permease GlcA","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport","9278503, 16738553, 11283302, 11785976, 15919996","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / MG1655 / ATCC 47076",1,511,521,11,549,560]
[null,"P71067","IPMed?",0.99112,1.07102,32.8,{"v":6e-77,"d":"6.00E-77"},3,2,"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",9,520,521,19,562,563]
[null,"Q8ZL63","_",0.98367,1.04031,32.84,{"v":3e-76,"d":"3.00E-76"},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",9,520,521,19,550,551]
[null,"P33231","IPMed?",0.97641,1.03263,32.9,{"v":6e-76,"d":"6.00E-76"},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",9,520,521,19,550,551]
[null,"P65253","_",0.97641,1.03263,32.71,{"v":2e-75,"d":"2.00E-75"},6,2,"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",9,520,521,19,550,551]
[null,"P65254","_",0.97641,1.03263,32.71,{"v":2e-75,"d":"2.00E-75"},6,2,"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",9,520,521,19,550,551]
[null,"Q8Z2E3","_",0.98367,1.04031,32.66,{"v":3e-75,"d":"3.00E-75"},7,2,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Transmembrane, Transmembrane helix, Transport","11677608, 12644504","Salmonella typhi","CT18 / ATCC 700931 / Ty2",9,520,521,19,550,551]
[null,"P55910","IPMed?",0.97782,1.01536,32.14,{"v":2e-71,"d":"2.00E-71"},8,1,"lctP","L-lactate permease","_","Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport","8969502, 9384377, 19383706, 10809684","Bacillus subtilis (strain 168)","168 / 168",5,511,521,13,535,541]
[null,"Q9K5Z9","_",0.98282,0.98848,29.13,{"v":4e-68,"d":"4.00E-68"},9,2,"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",6,511,521,14,519,524]
[null,"Q57251","_",1.03008,1.05182,25.55,{"v":2e-37,"d":"2.00E-37"},10,1,"_","Putative L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",9,521,521,5,531,532]
[null,"P39344","IPMed?",0.83877,0.99544,18.99,0.005,11,3,"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",7,434,521,3,365,439]
[null,"P52071","IPMed?",0.49904,0.94203,20,0.058,12,1,"_","Uncharacterized protein in phaC 3'region","_","Cell membrane, Membrane, Transmembrane, Transmembrane helix, Transport",7763712,"Methylorubrum extorquens","IBT 6",35,244,521,13,268,276]
[null,"Q8TSY1","IPMed?",0.28215,0.69014,25.17,0.25,13,3,"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",124,262,521,69,209,213]
[null,"Q9HU16","IPMed?",0.46449,0.56674,22.31,0.31,14,1,"dctM","C4-dicarboxylate TRAP transporter large permease protein DctM","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport","10984043, 21725012","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",1,228,521,206,421,427]
[null,"Q9KQS1","IPMed?",0.37236,0.42826,21.13,0.32,15,1,"dctM","C4-dicarboxylate TRAP transporter large permease protein DctM","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport","10952301, 22556361","Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","ATCC 39315 / El Tor Inaba N16961",35,204,521,1,190,453]
[]
["AZ49_04210","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?",0.89328,0.95359,44.91,{"v":2e-138,"d":"2.00E-138"},1,1,"lctP","L-lactate permease","_","Cell membrane, Membrane, Transmembrane, Transmembrane helix, Transport",10508058,"Streptococcus iniae","_",4,453,506,5,451,474]
[null,"P71067","IPMed?",0.96092,1.06917,32.53,{"v":4e-82,"d":"4.00E-82"},2,1,"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",4,502,506,19,554,563]
[null,"Q46839","IPMed?",0.95,1.05138,32.33,{"v":2e-81,"d":"2.00E-81"},3,2,"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",4,497,506,19,546,560]
[null,"P65253","_",0.94918,1.0336,32.5,{"v":1E-78,"d":"1.00E-78"},4,1,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Transmembrane, Transmembrane helix, Transport",12471157,"Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","CFT073 / ATCC 700928 / UPEC",4,497,506,19,538,551]
[null,"P33231","IPMed?",0.94918,1.0336,32.5,{"v":1E-78,"d":"1.00E-78"},4,1,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport","8407843, 8041620, 9278503, 16738553, 11283302, 11785976, 15919996","Escherichia coli (strain K12)","K12 / K12 / MG1655 / ATCC 47076 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / MC4100 / ATCC 35695 / DSM 6574 / K12 / MG1655 / ATCC 47076",4,497,506,19,538,551]
[null,"P65254","_",0.94918,1.0336,32.5,{"v":1E-78,"d":"1.00E-78"},4,1,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",4,497,506,19,538,551]
[null,"Q8ZL63","_",0.94918,1.0336,32.5,{"v":2e-77,"d":"2.00E-77"},5,1,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport",11677609,"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720",4,497,506,19,538,551]
[null,"Q8Z2E3","_",0.94918,1.0336,32.31,{"v":2e-76,"d":"2.00E-76"},6,1,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Transmembrane, Transmembrane helix, Transport","11677608, 12644504","Salmonella typhi","CT18 / ATCC 700931 / Ty2",4,497,506,19,538,551]
[null,"Q9K5Z9","_",0.97901,1.01383,30.8,{"v":2e-72,"d":"2.00E-72"},7,1,"lctP","L-lactate permease","_","Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport",11058132,"Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)","ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125",5,504,506,18,523,524]
[null,"P55910","IPMed?",0.97043,1.03755,32.76,{"v":2E-70,"d":"2.00E-70"},8,2,"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",4,498,506,17,529,541]
[null,"Q57251","_",1.01128,1.06324,22.86,{"v":4e-31,"d":"4.00E-31"},9,2,"_","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",3,505,506,4,525,532]
[null,"Q55BU0","IPMed?",0.09684,0.77778,30.61,0.44,10,1,"_","UPF0512 protein X","_","Complete proteome, Reference proteome","15875012, 18173832","Dictyostelium discoideum","AX4",407,455,506,3,51,63]
[]
["AZ49_00515","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P0C0J3","IPMed?",0.60121,0.63175,22.61,8e-06,1,2,"ldh","L-lactate dehydrogenase","1.1.1.27","Complete proteome, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","7679720, 16077101","Mycoplasma hyopneumoniae (strain J / ATCC 25934 / NCTC 10110)","J / ATCC 25934 / NCTC 10110",33,227,331,5,185,315]
[null,"P13714","IPMed?",0.84894,0.87813,22.78,3e-05,2,2,"ldh","L-lactate dehydrogenase","1.1.1.27","3D-structure, Allosteric enzyme, Complete proteome, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","8969502, 9384377, 19383706, 3098260, 10809684, 17218307","Bacillus subtilis (strain 168)","168 / 168 / 168",33,286,331,7,273,320]
[null,"P20619","IPMed?",0.4713,0.48903,26.28,0.0003,3,2,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",2334516,"Bacillus psychrosaccharolyticus","_",33,187,331,8,148,319]
[null,"P14561","IPMed?",0.4713,0.49057,27.56,0.0005,4,2,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Allosteric enzyme, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","2334516, 3435642","Bacillus psychrosaccharolyticus","_",33,187,331,8,148,318]
[null,"P00344","IPMed?",0.56798,0.59306,23.94,0.0005,5,2,"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",32,219,331,7,180,317]
[null,"Q5HCV0","IPMed?",0.55589,0.5768,23.37,2E-3,6,2,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Stress response","15774886, 18356528","Staphylococcus aureus (strain COL)","COL",36,219,331,8,179,319]
[null,"A6QK89","IPMed?",0.55589,0.5768,23.37,2E-3,6,2,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Stress response","17951380, 18356528","Staphylococcus aureus (strain Newman)","Newman",36,219,331,8,179,319]
[null,"Q59244","IPMed?",0.56495,0.58991,22.99,0.008,7,2,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",3675869,"Bacillus caldolyticus","_",33,219,331,8,180,317]
[null,"P10655","IPMed?",0.47734,0.49842,24.05,0.011,8,2,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","3675869, 3297694","Bacillus caldotenax","_",30,187,331,5,148,317]
[null,"A6QDL6","IPMed?",0.67372,0.70347,22.87,0.059,9,2,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Stress response","17951380, 18356528","Staphylococcus aureus (strain Newman)","Newman",33,253,331,8,197,317]
[null,"Q5HJD7","IPMed?",0.67372,0.70347,22.87,0.059,9,2,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","3D-structure, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Stress response","15774886, 18356528","Staphylococcus aureus (strain COL)","COL",33,253,331,8,197,317]
[null,"Q9CGG8","_",0.4713,0.48297,23.72,0.06,10,2,"ldh3","L-lactate dehydrogenase 3","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Reference proteome",11337471,"Lactococcus lactis subsp. lactis (strain IL1403)","IL1403",33,187,331,7,151,323]
[null,"P14295","IPMed?",0.48338,0.51613,24.38,0.077,11,2,"_","L-2-hydroxyisocaproate dehydrogenase","1.1.1.-","3D-structure, Direct protein sequencing, NADP, Oxidoreductase","2684788, 7643402","Weissella confusa","ATCC 10881 / DSM 20196 / JCM 1093 / NBRC 106469 / NCIMB 9311 / NRRL B-1064 / 548-D",28,187,331,1,148,310]
[]
["AZ49_11470","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","_",0.98428,0.98428,36.74,{"v":4E-73,"d":"4.00E-73"},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",6,315,318,5,315,318]
[null,"Q815X8","_",0.93082,0.93671,38.85,{"v":6E-65,"d":"6.00E-65"},2,1,"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",6,298,318,6,300,316]
[null,"E8MJ15","_",0.97799,0.98418,37.3,{"v":3e-64,"d":"3.00E-64"},4,1,"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",1,308,318,2,311,316]
[null,"P59050","_",0.97799,0.98418,37.3,{"v":3e-64,"d":"3.00E-64"},4,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Reference proteome",12381787,"Bifidobacterium longum (strain NCC 2705)","NCC 2705",1,308,318,2,311,316]
[null,"Q631X2","_",0.93082,0.93671,38.18,{"v":3e-64,"d":"3.00E-64"},3,1,"ldh3","L-lactate dehydrogenase 3","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase",16621833,"Bacillus cereus (strain ZK / E33L)","ZK / E33L",6,298,318,6,300,316]
[null,"Q6HBQ8","_",0.93082,0.93671,38.18,{"v":3e-64,"d":"3.00E-64"},3,1,"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",6,298,318,6,300,316]
[null,"Q81XJ7","_",0.93082,0.93671,38.18,{"v":4e-64,"d":"4.00E-64"},5,1,"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",6,298,318,6,300,316]
[null,"P62049","_",0.94654,0.95253,37.54,{"v":9e-64,"d":"9.00E-64"},6,1,"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",1,298,318,1,300,316]
[null,"Q71ZD6","_",0.96541,0.98714,35.5,{"v":2e-58,"d":"2.00E-58"},7,1,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Cytoplasm, NAD, Oxidoreductase",15115801,"Listeria monocytogenes serotype 4b (strain F2365)","F2365",4,309,318,2,308,311]
[null,"Q8Y6Z6","_",0.9717,0.99357,35.28,{"v":2e-58,"d":"2.00E-58"},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",4,311,318,2,310,311]
[null,"Q92BI0","_",0.96541,0.98714,35.5,{"v":6e-58,"d":"6.00E-58"},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",4,309,318,2,308,311]
[null,"P00344","IPMed?",0.98428,0.98738,35.78,{"v":4e-54,"d":"4.00E-54"},10,1,"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,"Q59244","IPMed?",0.97799,0.98107,35.69,{"v":5e-54,"d":"5.00E-54"},11,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",3675869,"Bacillus caldolyticus","_",8,310,318,9,312,317]
[null,"D8KFT1","IPMed?",0.97799,0.99045,32.15,{"v":5E-53,"d":"5.00E-53"},12,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","12867459, 20639323","Lactococcus lactis subsp. cremoris (strain NZ9000)","NZ9000 / NZ9000",1,309,318,1,310,314]
[null,"P14295","IPMed?",0.92767,0.95161,34.92,{"v":1E-52,"d":"1.00E-52"},13,1,"_","L-2-hydroxyisocaproate dehydrogenase","1.1.1.-","3D-structure, Direct protein sequencing, NADP, Oxidoreductase","2684788, 7643402","Weissella confusa","ATCC 10881 / DSM 20196 / JCM 1093 / NBRC 106469 / NCIMB 9311 / NRRL B-1064 / 548-D",6,297,318,3,291,310]
[null,"P10655","IPMed?",0.97799,0.98107,34.41,{"v":3e-50,"d":"3.00E-50"},14,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","3675869, 3297694","Bacillus caldotenax","_",8,310,318,9,312,317]
[null,"P13714","IPMed?",0.93437,0.94025,33.78,{"v":1e-48,"d":"1.00E-48"},15,1,"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",8,298,318,8,299,320]
[null,"Q5HJD7","IPMed?",0.98113,0.98423,33.65,{"v":2e-48,"d":"2.00E-48"},16,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","3D-structure, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Stress response","15774886, 18356528","Staphylococcus aureus (strain COL)","COL",3,313,318,4,314,317]
[null,"P20619","IPMed?",0.96552,0.96855,32.79,{"v":2e-48,"d":"2.00E-48"},17,1,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",2334516,"Bacillus psychrosaccharolyticus","_",8,307,318,9,309,319]
[null,"A6QDL6","IPMed?",0.98113,0.98423,33.65,{"v":2e-48,"d":"2.00E-48"},16,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Stress response","17951380, 18356528","Staphylococcus aureus (strain Newman)","Newman",3,313,318,4,314,317]
[null,"P00345","IPMed?",0.97484,0.97484,33.87,{"v":1e-47,"d":"1.00E-47"},18,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","3122782, 3118900","Bacillus megaterium","DSM 090",4,307,318,8,311,318]
[null,"P14561","IPMed?",0.97799,0.97799,31.19,{"v":8e-47,"d":"8.00E-47"},19,1,"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]
[]
["AZ49_01710","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?",0.99915,1.00171,59.73,0,1,2,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Plasmid, Repeat, Transport","2504647, 1708766","Enterobacter agglomerans","333 / 333",7,1166,1170,6,1173,1173]
[null,"P03833","IPMed?",0.99317,0.99402,58.21,0,2,2,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","3062178, 3060860, 8483412, 6306580","Klebsiella pneumoniae","_",7,1163,1170,6,1167,1171]
[null,"Q2RMD6","IPMed?",1,1.00085,57.56,0,3,3,"_","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",7,1165,1170,4,1170,1171]
[null,"P94692","IPMed?",0.94724,0.99744,52.61,0,4,2,"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",1,1158,1170,1,1161,1232]
[null,"Q94IN5","IPMed?",0.6528,1.00598,46.9,0,5,2,"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",4,1170,1170,67,1239,1803]
[null,"Q968X7","IPMed?",0.63857,1.05556,45.34,0,6,2,"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",9,1158,1170,7,1235,1934]
[null,"Q06879","IPMed?",1.0025,1.02735,45.17,0,7,3,"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",6,1160,1170,5,1193,1199]
[null,"P52965","_",0.98666,1.01111,46.49,0,8,3,"nifJ","Putative pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8590279, 8905231","Synechocystis sp. (strain PCC 6803 / Kazusa)","ATCC 27184 / PCC 6803 / N-1 / PCC 6803 / Kazusa",1,1165,1170,1,1174,1199]
[null,"Q3M8N0","IPMed?",0.99916,1.01624,45.5,0,9,3,"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",1,1160,1170,1,1179,1190]
[null,"Q53046","IPMed?",1.0084,1.0265,44.88,0,10,3,"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",1,1170,1170,1,1184,1191]
[null,"P52647","IPMed?",0.99744,1.00085,43.89,0,11,3,"ydbK","Probable pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","9097039, 9278503, 16738553, 9025293","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",8,1158,1170,3,1159,1174]
[]
["AZ49_05490","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?",1.00425,1.00854,56.56,0,1,2,"_","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",7,1175,1176,4,1170,1171]
[null,"P19543","IPMed?",1.0017,1.00426,53.65,0,2,3,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Plasmid, Repeat, Transport","2504647, 1708766","Enterobacter agglomerans","333 / 333",6,1174,1176,5,1171,1173]
[null,"P03833","IPMed?",1.00085,1.00512,53.61,0,3,3,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","3062178, 3060860, 8483412, 6306580","Klebsiella pneumoniae","_",6,1176,1176,5,1170,1171]
[null,"P94692","IPMed?",0.95373,0.99915,51.4,0,4,3,"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",8,1174,1176,7,1167,1232]
[null,"Q06879","IPMed?",1.00834,1.02806,45.74,0,5,1,"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",2,1176,1176,1,1199,1199]
[null,"Q3M8N0","IPMed?",0.99664,1.0085,46.96,0,6,1,"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",8,1174,1176,8,1183,1190]
[null,"Q94IN5","IPMed?",0.65724,1.00765,46.33,0,7,3,"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",4,1175,1176,67,1234,1803]
[null,"P52965","_",0.98499,1.00425,46.74,0,8,1,"nifJ","Putative pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8590279, 8905231","Synechocystis sp. (strain PCC 6803 / Kazusa)","ATCC 27184 / PCC 6803 / N-1 / PCC 6803 / Kazusa",8,1174,1176,8,1173,1199]
[null,"Q968X7","IPMed?",0.64271,1.05697,45.62,0,10,1,"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",9,1175,1176,7,1242,1934]
[null,"P52647","IPMed?",1.0068,1.00852,46.28,0,9,1,"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",8,1174,1176,3,1165,1174]
[null,"Q53046","IPMed?",0.99496,1.00765,45.4,0,11,1,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8736535, 21886856","Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)","ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1",9,1174,1176,9,1178,1191]
[]
["AZ49_06970","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P03833","IPMed?",0.99658,0.99658,61.35,0,1,1,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","3062178, 3060860, 8483412, 6306580","Klebsiella pneumoniae","_",3,1165,1171,4,1167,1171]
[null,"P19543","IPMed?",1.00171,1.00342,60.85,0,2,1,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Plasmid, Repeat, Transport","2504647, 1708766","Enterobacter agglomerans","333 / 333",3,1165,1171,4,1170,1173]
[null,"Q2RMD6","IPMed?",1.00256,1.00256,60.05,0,3,1,"_","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Reference proteome, Transport","18631365, 9214293, 10878009, 29581263","Moorella thermoacetica (strain ATCC 39073 / JCM 9320)","ATCC 39073 / JCM 9320 / ATCC 39073 / JCM 9320",5,1168,1171,4,1171,1171]
[null,"P94692","IPMed?",0.96104,1.0111,55.32,0,4,1,"por","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Calcium, Cytoplasm, Direct protein sequencing, Disulfide bond, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Thiamine pyrophosphate, Transport","9294422, 7612653, 10048931, 11752578, 16472741","Desulfocurvibacter africanus","ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi / ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi",3,1170,1171,4,1173,1232]
[null,"Q94IN5","IPMed?",0.65225,1.00427,49.66,0,5,1,"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",4,1168,1171,69,1235,1803]
[null,"P52965","_",0.98249,1.00598,47.28,0,6,2,"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",4,1167,1171,6,1174,1199]
[null,"Q968X7","IPMed?",0.64064,1.05807,46.57,0,7,3,"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",1,1158,1171,1,1233,1934]
[null,"Q3M8N0","IPMed?",1.00084,1.01708,47.52,0,8,2,"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",4,1162,1171,6,1179,1190]
[null,"Q06879","IPMed?",0.99666,1.0205,47.11,0,9,2,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8415612, 11759840","Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)","PCC 7120 / SAG 25.82 / UTEX 2576",4,1162,1171,5,1193,1199]
[null,"Q53046","IPMed?",0.98908,1.00598,46.52,0,10,2,"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",3,1158,1171,5,1170,1191]
[null,"P52647","IPMed?",0.9983,1.00085,45.82,0,11,2,"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",6,1158,1171,3,1157,1174]
[]
["AZ49_06950","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q8XJN2","_",1,1,62.56,{"v":2E-180,"d":"2.00E-180"},1,1,"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",1,397,398,1,398,398]
[null,"C1FSN0","_",0.99749,1,63.48,{"v":6e-180,"d":"6.00E-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)","_",1,397,398,1,397,397]
[null,"A7FW24","_",0.99749,1,63.48,{"v":1E-179,"d":"1.00E-179"},3,1,"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",1,397,398,1,397,397]
[null,"A5I4N7","_",0.99749,1,63.48,{"v":1E-179,"d":"1.00E-179"},3,1,"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",1,397,398,1,397,397]
[null,"B1KWP9","_",0.99749,1,63.48,{"v":2E-179,"d":"2.00E-179"},4,1,"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",1,397,398,1,397,397]
[null,"C3L0F7","_",0.99749,1,63.22,{"v":3e-179,"d":"3.00E-179"},5,1,"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)","_",1,397,398,1,397,397]
[null,"A7GG48","_",0.99749,1,62.97,{"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)","_",1,397,398,1,397,397]
[null,"B1II90","_",0.99749,1,62.97,{"v":1e-177,"d":"1.00E-177"},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",1,397,398,1,397,397]
[null,"Q895N2","_",0.9925,0.99749,62.72,{"v":2e-177,"d":"2.00E-177"},8,1,"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",1,396,398,1,397,400]
[null,"Q59331","_",0.99,0.99497,61.87,{"v":2E-175,"d":"2.00E-175"},9,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",1,395,398,1,396,400]
[null,"A0Q0Z5","_",0.99002,0.99749,62.72,{"v":4E-175,"d":"4.00E-175"},10,1,"ackA","Acetate kinase","2.7.2.1","ATP-binding, Complete proteome, Cytoplasm, Kinase, Magnesium, Metal-binding, Nucleotide-binding, Reference proteome, Transferase",17115055,"Clostridium novyi (strain NT)","NT",1,397,398,1,397,401]
[null,"Q9WYB1","IPMed?",0.99256,1.00503,57.25,{"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",1,397,398,1,400,403]
[null,"P38502","IPMed?",0.97794,1.00251,57.14,{"v":2e-162,"d":"2.00E-162"},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",1,398,398,1,399,408]
[null,"P71104","IPMed?",0.99751,1.00503,54.5,{"v":4e-156,"d":"4.00E-156"},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",4,397,398,4,399,401]
[null,"P37877","IPMed?",0.97487,0.98228,55.67,{"v":7e-154,"d":"7.00E-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",3,390,398,4,389,395]
[null,"P74879","IPMed?",0.9703,0.98492,47.45,{"v":5e-129,"d":"5.00E-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",3,394,398,5,392,404]
[null,"Q9X4M1","IPMed?",0.98744,0.99746,45.55,{"v":1e-114,"d":"1.00E-114"},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",3,394,398,4,393,394]
[null,"P77845","IPMed?",0.98492,0.98741,46.68,{"v":4e-114,"d":"4.00E-114"},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",2,389,398,3,391,397]
[null,"P0A6A3","IPMed?",1.0025,1.00754,42.89,{"v":1e-101,"d":"1.00E-101"},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",2,396,398,5,400,400]
[null,"P63411","IPMed?",1.0025,1.00754,41.9,{"v":2E-100,"d":"2.00E-100"},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",2,396,398,5,400,400]
[null,"Q49113","IPMed?",0.99497,1.00763,40.15,{"v":1e-96,"d":"1.00E-96"},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)","_",2,395,398,1,392,393]
[]
["AZ49AM_0981","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O83132","_",0.72917,0.9761,44.49,{"v":1E-54,"d":"1.00E-54"},1,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",9665876,"Treponema pallidum (strain Nichols)","Nichols",2,241,251,83,323,336]
[null,"P71103","IPMed?",0.76276,1.01195,41.34,{"v":3e-54,"d":"3.00E-54"},2,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","8702268, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",2,251,251,78,329,333]
[null,"O52593","_",0.75,0.99203,40.56,{"v":3e-53,"d":"3.00E-53"},3,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","_","Hungateiclostridium thermocellum (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)","_",3,251,251,81,327,332]
[null,"P9WHP0","_",0.35942,0.98805,44.76,{"v":1e-49,"d":"1.00E-49"},4,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",4,251,251,447,685,690]
[null,"P9WHP1","_",0.35942,0.98805,44.76,{"v":1e-49,"d":"1.00E-49"},4,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","9634230, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",4,251,251,447,685,690]
[null,"Q59330","_",0.7561,0.98805,40.32,{"v":2e-49,"d":"2.00E-49"},5,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",4,251,251,82,327,328]
[null,"Q726S7","_",0.35653,1,41.43,{"v":8e-48,"d":"8.00E-48"},6,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",15077118,"Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)","Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303",1,251,251,456,697,704]
[null,"P38503","IPMed?",0.75375,1,36.25,{"v":6e-47,"d":"6.00E-47"},7,2,"pta","Phosphate acetyltransferase","2.3.1.8","3D-structure, Acyltransferase, Cell membrane, Direct protein sequencing, Membrane, Transferase","8226623, 9401029, 15062079","Methanosarcina thermophila","ATCC 43570 / DSM 1825 / OCM 12 / TM-1",1,251,251,80,328,333]
[null,"Q9ZKU4","_",0.47013,0.97211,40.57,{"v":1e-45,"d":"1.00E-45"},8,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",9923682,"Helicobacter pylori (strain J99 / ATCC 700824)","J99 / ATCC 700824",8,251,251,282,516,519]
[null,"P73662","_",0.35151,0.9761,42.45,{"v":2E-45,"d":"2.00E-45"},9,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",8905231,"Synechocystis sp. (strain PCC 6803 / Kazusa)","PCC 6803 / Kazusa",2,246,251,456,691,697]
[null,"Q8CJR5","_",0.35868,0.99602,41.6,{"v":1e-44,"d":"1.00E-44"},10,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",12000953,"Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)","ATCC BAA-471 / A3(2) / M145",2,251,251,446,686,697]
[null,"P41790","IPMed?",0.66272,0.89243,39.73,{"v":3E-43,"d":"3.00E-43"},11,2,"eutD","Ethanolamine utilization protein EutD","_","Acyltransferase, Complete proteome, Reference proteome, Transferase","10464203, 11677609, 7868611","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / LT2 / SGSC1412 / ATCC 700720 / ATCC 14028s / SGSG 2262",23,246,251,100,318,338]
[null,"Q8ZND6","IPMed?",0.35154,1,38.65,{"v":5e-41,"d":"5.00E-41"},12,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","11677609, 16272400, 17339319","Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720 / LT2",1,251,251,468,709,714]
[null,"P39197","IPMed?",0.75157,0.95219,39.75,{"v":6e-41,"d":"6.00E-41"},13,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Cytoplasm, Transferase",7480167,"Paracoccus denitrificans","_",8,246,251,76,312,318]
[null,"P0A9M8","IPMed?",0.33473,0.95219,39.75,{"v":2e-40,"d":"2.00E-40"},14,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","7883769, 7918659, 9205837, 9278503, 16738553, 2536666, 10542166, 15687190, 19852855, 20236319","Escherichia coli (strain K12)","K12 / KH131 / K12 / 1100 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / K12 / W3110 / ATCC 27325 / DSM 5911",8,246,251,476,705,714]
[null,"Q9I5A5","IPMed?",0.35795,1.00398,38.1,{"v":8e-39,"d":"8.00E-39"},15,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","10984043, 15231792","Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1",1,251,251,457,698,704]
[null,"P77844","IPMed?",0.75988,0.99602,36,{"v":8e-38,"d":"8.00E-38"},16,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase","10075432, 12743753, 12948626, 15090522, 16179344, 16547043","Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)","ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 / ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025",2,251,251,85,325,329]
[null,"Q49112","IPMed?",0.74845,0.96016,33.2,{"v":7e-33,"d":"7.00E-33"},17,2,"pta","Phosphate acetyltransferase","2.3.1.8","Acyltransferase, Complete proteome, Cytoplasm, Transferase",8844861,"Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)","_",7,246,251,84,316,322]
[null,"P76558","IPMed?",0.32806,0.99203,31.73,{"v":2e-29,"d":"2.00E-29"},18,3,"maeB","NADP-dependent malic enzyme","1.1.1.40","Acetylation, Complete proteome, Metal-binding, Multifunctional enzyme, NADP, Oxidoreductase, Reference proteome","9205837, 9278503, 16738553, 36376, 17557829, 18723842","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / W / ATCC 11105 / DSM 1900 / K12 / K12 / JW1106",4,251,251,514,754,759]
[]
["AZ49_00050","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?",0.93299,0.99178,31.22,{"v":2e-42,"d":"2.00E-42"},1,1,"adh1","NADPH-dependent butanol dehydrogenase","1.1.1.-","NADP, Oxidoreductase",2673928,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",1,355,365,1,352,388]
[null,"Q9F282","IPMed?",0.94486,1.03288,31.3,{"v":4e-42,"d":"4.00E-42"},2,1,"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",11,360,365,21,397,399]
[null,"Q59477","_",0.94832,1.00548,31.61,{"v":4E-41,"d":"4.00E-41"},3,2,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","3D-structure, Iron, NAD, Oxidoreductase","_","Klebsiella pneumoniae","_",1,353,365,5,360,387]
[null,"P76553","_",0.79494,0.86027,32.48,{"v":1e-40,"d":"1.00E-40"},4,1,"eutG","Ethanolamine utilization protein EutG","1.1.-.-","Complete proteome, NAD, Oxidoreductase, Reference proteome","9205837, 9278503, 16738553","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",3,313,365,23,336,395]
[null,"P0A9S1","IPMed?",0.78534,0.82192,30.67,{"v":5e-40,"d":"5.00E-40"},5,1,"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",11,304,365,12,308,382]
[null,"P0A9S2","_",0.78534,0.82192,30.67,{"v":5e-40,"d":"5.00E-40"},5,1,"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",11,304,365,12,308,382]
[null,"F8DVL8","IPMed?",0.79634,0.83562,31.48,{"v":7e-40,"d":"7.00E-40"},6,2,"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",3,304,365,5,309,383]
[null,"P0DJA2","IPMed?",0.79634,0.83562,31.48,{"v":7e-40,"d":"7.00E-40"},6,2,"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",3,304,365,5,309,383]
[null,"A6ZTT5","_",0.73822,0.7726,31.56,{"v":1e-39,"d":"1.00E-39"},7,1,"ADH4","Alcohol dehydrogenase 4","1.1.1.1","Complete proteome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Zinc",17652520,"Saccharomyces cerevisiae (strain YJM789)","YJM789",4,281,365,7,287,382]
[null,"P45513","IPMed?",0.7416,0.7863,35.89,{"v":4e-39,"d":"4.00E-39"},8,2,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","Iron, NAD, Oxidoreductase",7721705,"Citrobacter freundii","ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK",1,281,365,5,290,387]
[null,"O05239","_",0.93798,0.99452,29.2,{"v":5e-39,"d":"5.00E-39"},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",2,340,365,4,366,387]
[null,"P31005","IPMed?",0.74541,0.77808,29.58,{"v":5e-39,"d":"5.00E-39"},9,2,"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",1,281,365,1,284,381]
[null,"P10127","IPMed?",0.73822,0.7726,31.21,{"v":1e-38,"d":"1.00E-38"},11,2,"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",4,281,365,7,287,382]
[null,"A4IP64","IPMed?",0.71646,0.77534,35.69,{"v":2e-38,"d":"2.00E-38"},12,1,"adh1","Long-chain-alcohol dehydrogenase 1","1.1.1.192","Complete proteome, NAD, Oxidoreductase","17372208, 19383697, 24826896","Geobacillus thermodenitrificans (strain NG80-2)","NG80-2 / NG80-2",27,303,365,29,309,395]
[null,"P41795","IPMed?",0.79494,0.86027,31.21,{"v":1e-37,"d":"1.00E-37"},13,1,"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",3,313,365,23,336,395]
[null,"P37686","IPMed?",0.79896,0.83836,30.07,{"v":4e-37,"d":"4.00E-37"},14,2,"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",3,304,365,5,309,383]
[]
["AZ49_02525","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","_",1.03599,1.04134,33.25,{"v":3E-49,"d":"3.00E-49"},1,1,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","3D-structure, Iron, NAD, Oxidoreductase","_","Klebsiella pneumoniae","_",1,388,389,1,387,387]
[null,"P37686","IPMed?",0.99486,1.01044,31.27,{"v":7e-49,"d":"7.00E-49"},2,1,"yiaY","Probable alcohol dehydrogenase","1.1.1.1","Complete proteome, Iron, NAD, Oxidoreductase, Reference proteome","8041620, 9278503, 16397293, 16738553, 7768815","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",6,387,389,7,382,383]
[null,"P45513","IPMed?",0.96401,0.96899,34.13,{"v":5e-48,"d":"5.00E-48"},3,1,"dhaT","1,3-propanediol dehydrogenase","1.1.1.202","Iron, NAD, Oxidoreductase",7721705,"Citrobacter freundii","ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK",1,360,389,1,361,387]
[null,"A4ISB9","IPMed?",1.00771,1.01292,32.91,{"v":1e-47,"d":"1.00E-47"},4,2,"adh2","Long-chain-alcohol dehydrogenase 2","1.1.1.192","Complete proteome, NAD, Oxidoreductase","17372208, 19383697","Geobacillus thermodenitrificans (strain NG80-2)","NG80-2 / NG80-2",8,387,389,9,386,387]
[null,"Q09669","IPMed?",0.91943,0.99743,30.67,{"v":5e-47,"d":"5.00E-47"},5,1,"adh4","Alcohol dehydrogenase 4","1.1.1.1","Complete proteome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide, Zinc","11859360, 15040954, 16823372, 16999687, 18203864","Schizosaccharomyces pombe (strain 972 / ATCC 24843)","972 / ATCC 24843",6,387,389,50,421,422]
[null,"P31005","IPMed?",0.9383,0.95801,31.51,{"v":3e-46,"d":"3.00E-46"},6,1,"mdh","NAD-dependent methanol dehydrogenase","1.1.1.244","Cytoplasm, Direct protein sequencing, Magnesium, Methanol utilization, NAD, Oxidoreductase, Zinc","1644761, 1995642, 2673121, 1995643, 12089158, 12351635","Bacillus methanolicus","C1 / C1 / C1 / C1 / C1 / C1",6,360,389,5,355,381]
[null,"O05239","_",1.01285,1.01809,29.44,{"v":1e-44,"d":"1.00E-44"},7,2,"yugJ","Probable NADH-dependent butanol dehydrogenase 1","1.1.1.-","Complete proteome, NAD, Oxidoreductase, Reference proteome","9274030, 9384377","Bacillus subtilis (strain 168)","168 / 168",2,387,389,3,386,387]
[null,"O05240","_",1.01538,1.01799,30.05,{"v":8e-44,"d":"8.00E-44"},8,2,"yugK","Probable NADH-dependent butanol dehydrogenase 2","1.1.1.-","Complete proteome, NAD, Oxidoreductase, Reference proteome","9274030, 9384377","Bacillus subtilis (strain 168)","168 / 168",2,387,389,3,389,390]
[null,"P10127","IPMed?",0.98972,1.00785,29.61,{"v":2e-43,"d":"2.00E-43"},9,1,"ADH4","Alcohol dehydrogenase 4","1.1.1.1","Complete proteome, Metal-binding, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Zinc","2823079, 8972578, 9169869, 24374639, 3282541, 10978274, 10884426, 14562095, 14562106, 17139254, 16503288, 17933919, 17938904","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 96604 / S288c / FY1679 / ATCC 204508 / S288c / ATCC 204508 / S288c",6,388,389,8,380,382]
[null,"P0DJA2","IPMed?",0.93573,0.95039,32.14,{"v":3E-43,"d":"3.00E-43"},10,1,"adhB","Alcohol dehydrogenase 2","1.1.1.1","3D-structure, Complete proteome, Direct protein sequencing, Iron, NAD, Oxidoreductase, Reference proteome","3584063, 15592456, 2935393","Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)","ATCC 31821 / ZM4 / CP4 / ATCC 31821 / ZM4 / CP4 / ATCC 31821 / ZM4 / CP4",2,360,389,3,357,383]
[null,"F8DVL8","IPMed?",0.93573,0.95039,31.87,{"v":1E-42,"d":"1.00E-42"},11,1,"adhB","Alcohol dehydrogenase 2","1.1.1.1","Complete proteome, Iron, NAD, Oxidoreductase","2308827, 21725006","Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1)","ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1 / ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1",2,360,389,3,357,383]
[null,"P71017","IPMed?",0.89801,0.92802,33.8,{"v":6e-42,"d":"6.00E-42"},12,1,"gbsB","Choline dehydrogenase","1.1.1.-","Alternative initiation, Complete proteome, Direct protein sequencing, NAD, Oxidoreductase, Reference proteome","8752328, 9384377, 19383706, 22408163","Bacillus subtilis (strain 168)","168 / JH642 / 168 / 168 / JH642",7,360,389,18,369,402]
[null,"Q04944","IPMed?",1.02828,1.02828,30,{"v":7e-42,"d":"7.00E-42"},13,2,"bdhA","NADH-dependent butanol dehydrogenase A","1.1.1.-","Complete proteome, Direct protein sequencing, NAD, Oxidoreductase, Reference proteome","1385386, 11466286, 1809209","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,388,389,2,389,389]
[]
["AZ49_03535","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O32144","IPMed?",0.82031,0.98658,32.38,{"v":4e-94,"d":"4.00E-94"},1,1,"pucD","Probable xanthine dehydrogenase subunit D","1.17.1.4","Complete proteome, Metal-binding, Molybdenum, NAD, Oxidoreductase, Purine metabolism, Reference proteome","9384377, 11344136","Bacillus subtilis (strain 168)","168 / 168",176,886,896,14,727,745]
[null,"Q46509","IPMed?",0.98897,1.00112,29.54,{"v":3e-93,"d":"3.00E-93"},2,1,"mop","Aldehyde oxidoreductase","1.2.99.7","2Fe-2S, 3D-structure, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD, Oxidoreductase","8143744, 7502041, 8799115, 11713686","Desulfovibrio gigas","_",17,872,896,18,882,907]
[null,"Q46799","IPMed?",0.82924,0.98803,30.69,{"v":4e-82,"d":"4.00E-82"},3,2,"xdhA","Putative xanthine dehydrogenase molybdenum-binding subunit XdhA","1.17.1.4","Complete proteome, Metal-binding, Molybdenum, NAD, Oxidoreductase, Purine metabolism, Purine salvage, Reference proteome","9278503, 16738553, 10986234","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / W3110 / ATCC 27325 / DSM 5911",172,886,896,2,737,752]
[null,"Q8X6C7","_",0.82924,0.98803,30.69,{"v":4e-82,"d":"4.00E-82"},3,2,"xdhA","Xanthine dehydrogenase molybdenum-binding subunit","1.17.1.4","Complete proteome, Metal-binding, Molybdenum, NAD, Oxidoreductase, Purine metabolism, Purine salvage, Reference proteome","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",172,886,896,2,737,752]
[null,"Q0QLF2","IPMed?",0.46429,0.97882,37.26,{"v":3e-74,"d":"3.00E-74"},4,1,"ndhL","Nicotinate dehydrogenase large molybdopterin subunit","1.17.1.5","3D-structure, Direct protein sequencing, Metal-binding, Molybdenum, NADP, Oxidoreductase, Selenium","16894175, 8555176, 19549881","Eubacterium barkeri","ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 10623 / ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 10623 / ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 10623",163,577,896,5,413,425]
[null,"O33819","IPMed?",0.82701,0.96359,27.53,{"v":3E-52,"d":"3.00E-52"},5,2,"hcrA","4-hydroxybenzoyl-CoA reductase subunit alpha","1.3.7.9","3D-structure, Direct protein sequencing, Molybdenum, Oxidoreductase","9490068, 11602591, 15576037","Thauera aromatica","DSM 6984 / K172 / DSM 6984 / K172",178,886,896,23,753,769]
[null,"Q46814","IPMed?",0.94874,1.01228,24.37,{"v":2E-51,"d":"2.00E-51"},6,2,"xdhD","Probable hypoxanthine oxidase XdhD","1.-.-.-","2Fe-2S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Molybdenum, Oxidoreductase, Purine metabolism, Purine salvage, Reference proteome","9278503, 16738553, 10986234","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / W3110 / ATCC 27325 / DSM 5911",42,874,896,42,932,956]
[null,"Q8XD64","_",0.94874,1.01228,24.15,{"v":6e-50,"d":"6.00E-50"},7,2,"xdhD","Probable hypoxanthine oxidase XdhD","1.-.-.-","2Fe-2S, Complete proteome, Iron, Iron-sulfur, Metal-binding, Molybdenum, Oxidoreductase, Purine metabolism, Purine salvage, Reference proteome","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",42,874,896,42,932,956]
[null,"Q6AUV1","_",0.52155,0.79688,25.21,{"v":2E-45,"d":"2.00E-45"},8,1,"XDH","Xanthine dehydrogenase","1.17.1.4","2Fe-2S, Complete proteome, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD, Oxidoreductase, Reference proteome","16109971, 16100779, 18089549, 24280374, 15685292, 12869764","Oryza sativa subsp. japonica","cv. Nipponbare / cv. Nipponbare / cv. Nipponbare / cv. Nipponbare / cv. Nipponbare / cv. Nipponbare",130,812,896,579,1247,1369]
[null,"P47989","IPMed?",0.52813,0.78571,25.43,{"v":8e-45,"d":"8.00E-45"},9,2,"XDH","Xanthine dehydrogenase / Xanthine oxidase","1.17.1.4, 1.17.3.2","2Fe-2S, 3D-structure, Complete proteome, Cytoplasm, Disease mutation, Disulfide bond, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD, Oxidoreductase, Peroxisome, Polymorphism, Reference proteome, Secreted","8224915, 8135849, 7575623, 8670112, 9153281, 10844591, 18780401, 24275569, 17301077, 11379872, 14551354, 16959974","Homo sapiens","_",166,844,896,574,1239,1333]
[null,"P19913","IPMed?",0.78571,0.87671,26.85,{"v":2e-44,"d":"2.00E-44"},10,2,"cutL","Carbon monoxide dehydrogenase large chain","1.2.5.3","3D-structure, Copper, Direct protein sequencing, Hydroxylation, Metal-binding, Molybdenum, Oxidoreductase","10482497, 2818128, 10966817, 11076018","Hydrogenophaga pseudoflava","_",179,816,896,31,712,803]
[null,"Q00519","IPMed?",0.53708,0.80022,25.8,{"v":3e-44,"d":"3.00E-44"},11,2,"Xdh","Xanthine dehydrogenase / Xanthine oxidase","1.17.1.4, 1.17.3.2","2Fe-2S, Complete proteome, Cytoplasm, Direct protein sequencing, Disulfide bond, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD, Oxidoreductase, Peroxisome, Reference proteome, Secreted","7835888, 1590774, 19468303, 8541302, 21183079","Mus musculus","129/Sv / C57BL/6J / C57BL/6J",166,844,896,576,1241,1335]
[null,"Q933N0","IPMed?",0.84152,0.94962,26.39,{"v":9e-44,"d":"9.00E-44"},12,2,"kdhC","6-hydroxypseudooxynicotine dehydrogenase complex subunit gamma","1.5.99.14","Direct protein sequencing, Metal-binding, Molybdenum, Oxidoreductase, Plasmid","9878353, 11514508, 12618462, 16820521","Paenarthrobacter nicotinovorans","_",166,872,896,26,761,794]
[]
["AZ49_05685","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P45359","IPMed?",0.99237,0.9949,68.46,0,1,1,"thlA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","7867955, 11075929, 11466286, 1685080","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,390,393,1,390,392]
[null,"Q0AVM3","IPMed?",0.99242,1,65.65,{"v":8e-179,"d":"8.00E-179"},2,1,"_","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",2,390,393,3,394,396]
[null,"Q18AR0","_",0.99237,0.99744,62.05,{"v":3e-169,"d":"3.00E-169"},3,1,"thlA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",16804543,"Peptoclostridium difficile (strain 630)",630,1,390,393,1,390,391]
[null,"P44873","_",1,1,62.85,{"v":4e-169,"d":"4.00E-169"},4,1,"atoB","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",1,392,393,1,393,393]
[null,"Q9I2A8","_",0.98473,0.98473,62.79,{"v":1E-168,"d":"1.00E-168"},5,1,"atoB","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase",10984043,"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1",1,386,393,1,387,393]
[null,"P14611","IPMed?",0.99491,0.99491,63.43,{"v":2e-168,"d":"2.00E-168"},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",1,390,393,1,391,393]
[null,"Q9ZHI1","IPMed?",0.98982,0.99235,62.47,{"v":1E-166,"d":"1.00E-166"},7,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, PHA biosynthesis, Reference proteome, Transferase","14500782, 10427049","Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)","ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757 / ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757",3,390,393,2,390,392]
[null,"P45369","IPMed?",0.99492,0.99746,59.18,{"v":4e-163,"d":"4.00E-163"},8,1,"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",2,392,393,3,394,394]
[null,"P45363","IPMed?",0.98985,0.99237,59.49,{"v":2E-160,"d":"2.00E-160"},9,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase","7763384, 1476773","Thiocystis violacea","2311 / DSM 208",4,392,393,5,394,394]
[null,"P76461","_",1,1.00254,60.66,{"v":9e-160,"d":"9.00E-160"},10,1,"atoB","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","9097040, 9278503, 16738553","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",1,393,393,1,394,394]
[null,"P54810","IPMed?",0.99237,0.99744,59.74,{"v":2e-157,"d":"2.00E-157"},11,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase",8566717,"Paracoccus denitrificans","_",1,390,393,1,389,391]
[null,"P50174","IPMed?",0.98982,0.98982,59.38,{"v":1E-153,"d":"1.00E-153"},12,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, PHB biosynthesis, Reference proteome, Transferase","7582015, 11481430, 11474104","Rhizobium meliloti (strain 1021)","41 / 1021 / 1021",4,392,393,6,393,393]
[null,"P07097","IPMed?",0.98728,0.9898,57.22,{"v":8e-153,"d":"8.00E-153"},13,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase","2878929, 2670935, 1673680, 1476773, 10764581, 10545327, 12501183","Zoogloea ramigera","ATCC 19623 / I-16-M / NCIB 10340 / NCTC 10482",5,392,393,6,392,392]
[null,"Q8CAY6","IPMed?",0.97985,0.98982,54.24,{"v":2E-136,"d":"2.00E-136"},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",4,390,393,8,395,397]
[]
["AZ49_05690","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","_",0.99746,1.00512,61.07,{"v":5e-167,"d":"5.00E-167"},1,2,"thlA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",16804543,"Peptoclostridium difficile (strain 630)",630,1,393,394,1,391,391]
[null,"P44873","_",1.00254,1.00509,58.23,{"v":1e-158,"d":"1.00E-158"},2,2,"atoB","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",1,394,394,1,393,393]
[null,"P45359","IPMed?",0.99746,1.00255,58.27,{"v":6E-158,"d":"6.00E-158"},3,2,"thlA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","7867955, 11075929, 11466286, 1685080","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,393,394,1,391,392]
[null,"Q0AVM3","IPMed?",1.00253,1.00761,57.68,{"v":8e-152,"d":"8.00E-152"},4,2,"_","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",2,394,394,3,396,396]
[null,"P76461","_",1.00254,1.00254,55.95,{"v":6e-146,"d":"6.00E-146"},5,2,"atoB","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","9097040, 9278503, 16738553","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",1,394,394,1,393,394]
[null,"P45369","IPMed?",0.99239,0.99239,54.48,{"v":8e-146,"d":"8.00E-146"},6,2,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, PHB biosynthesis, Reference proteome, Transferase","1396692, 22675582, 1476773","Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)","ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D / ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D",5,394,394,6,394,394]
[null,"P14611","IPMed?",1,1.00254,54.57,{"v":4e-145,"d":"4.00E-145"},7,2,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, PHB biosynthesis, Reference proteome, Transferase","2670935, 16964242, 2670936, 4198758, 1476773, 25152395","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337",1,393,394,1,392,393]
[null,"P45363","IPMed?",0.99239,0.99239,54.73,{"v":3e-144,"d":"3.00E-144"},8,2,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase","7763384, 1476773","Thiocystis violacea","2311 / DSM 208",5,394,394,6,394,394]
[null,"Q9I2A8","_",1,1.00254,54.06,{"v":2e-142,"d":"2.00E-142"},9,2,"atoB","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase",10984043,"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1",1,393,394,1,392,393]
[null,"P50174","IPMed?",0.98985,0.99237,54.36,{"v":2e-142,"d":"2.00E-142"},10,2,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, PHB biosynthesis, Reference proteome, Transferase","7582015, 11481430, 11474104","Rhizobium meliloti (strain 1021)","41 / 1021 / 1021",5,394,394,7,393,393]
[null,"Q9ZHI1","IPMed?",0.99492,1,54.08,{"v":4e-141,"d":"4.00E-141"},11,2,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, PHA biosynthesis, Reference proteome, Transferase","14500782, 10427049","Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)","ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757 / ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757",3,393,394,2,391,392]
[null,"P07097","IPMed?",0.99239,0.99745,50.9,{"v":2E-137,"d":"2.00E-137"},12,2,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase","2878929, 2670935, 1673680, 1476773, 10764581, 10545327, 12501183","Zoogloea ramigera","ATCC 19623 / I-16-M / NCIB 10340 / NCTC 10482",4,394,394,5,392,392]
[null,"P54810","IPMed?",0.99746,1.00512,52.16,{"v":2E-136,"d":"2.00E-136"},13,2,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase",8566717,"Paracoccus denitrificans","_",1,393,394,1,390,391]
[null,"Q8CAY6","IPMed?",0.98489,0.99239,52.17,{"v":1E-135,"d":"1.00E-135"},14,2,"Acat2","Acetyl-CoA acetyltransferase, cytosolic","2.3.1.9","Acetylation, Acyltransferase, Complete proteome, Cytoplasm, Direct protein sequencing, Reference proteome, Transferase","16141072, 15489334, 2055458, 21183079","Mus musculus","C57BL/6J / C57BL/6J / C57BL/6J",5,393,394,9,396,397]
[]
["AZ49_10655","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P52041","IPMed?",1,1.00709,61.62,{"v":2e-115,"d":"2.00E-115"},1,1,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,284,284,1,282,282]
[null,"P77851","_",0.99296,1.00356,59.93,{"v":2e-115,"d":"2.00E-115"},2,1,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",1,282,284,1,280,281]
[null,"Q0AVM2","IPMed?",0.98592,1.00358,60,{"v":9e-112,"d":"9.00E-112"},3,1,"_","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.35","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, NAD, Oxidoreductase, Reference proteome","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",3,282,284,2,279,279]
[null,"P45856","IPMed?",0.98258,0.99296,54.61,{"v":9e-106,"d":"9.00E-106"},4,1,"mmgB","Probable 3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",1,282,284,3,282,287]
[null,"P45364","IPMed?",0.99296,1.00356,57.09,{"v":9E-102,"d":"9.00E-102"},5,1,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase",8001771,"Clostridioides difficile","E",3,284,284,2,281,281]
[null,"Q9RVG1","_",0.98592,1.00719,55.36,{"v":1e-95,"d":"1.00E-95"},6,1,"hbd","Probable 3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome",10567266,"Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)","ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422",3,282,284,2,278,278]
[null,"Q45223","_",0.96246,0.99296,49.65,{"v":6e-89,"d":"6.00E-89"},7,1,"hbdA","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome",12597275,"Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110",1,282,284,5,284,293]
[null,"Q16836","IPMed?",0.90764,1.00352,45.26,{"v":1e-69,"d":"1.00E-69"},8,1,"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","_",4,282,284,30,313,314]
[null,"P00348","IPMed?",0.91083,1.00704,44.41,{"v":2e-69,"d":"2.00E-69"},9,1,"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","_",4,282,284,30,313,314]
[null,"P9WNP7","IPMed?",1,1.00704,40.91,{"v":1e-68,"d":"1.00E-68"},10,1,"fadB2","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","9634230, 11489128, 12081975, 20378648, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",1,282,284,5,286,286]
[null,"P9WNP6","_",1,1.00704,40.91,{"v":1e-68,"d":"1.00E-68"},10,1,"fadB2","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",1,282,284,5,286,286]
[null,"Q9WVK7","IPMed?",0.91083,1.00704,44.76,{"v":5e-68,"d":"5.00E-68"},11,1,"Hadh","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","Acetylation, Complete proteome, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide",10064895,"Rattus norvegicus","Sprague-Dawley",4,282,284,30,313,314]
[null,"Q61425","IPMed?",0.91083,1.00704,44.06,{"v":2e-67,"d":"2.00E-67"},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",4,282,284,30,313,314]
[null,"P76083","IPMed?",0.58947,0.98592,43.57,{"v":2E-66,"d":"2.00E-66"},13,1,"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",4,282,284,8,285,475]
[]
["AZ49_00555","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q8DSN0","IPMed?",1,1.0038,35.98,{"v":4e-56,"d":"4.00E-56"},1,1,"fabM","Trans-2-decenoyl-[acyl-carrier-protein] isomerase","5.3.3.14","Complete proteome, Fatty acid metabolism, Isomerase, Lipid metabolism, Reference proteome","21741617, 12397186, 15205416","Streptococcus mutans serotype c (strain ATCC 700610 / UA159)","ATCC 700610 / UA159 / ATCC 700610 / UA159 / ATCC 700610 / UA159",1,264,264,1,263,263]
[null,"Q8DR19","IPMed?",0.97348,0.98467,33.07,{"v":7e-46,"d":"7.00E-46"},2,1,"fabM","Trans-2-decenoyl-[acyl-carrier-protein] isomerase","5.3.3.14","Complete proteome, Fatty acid metabolism, Isomerase, Lipid metabolism, Reference proteome","11544234, 12237320","Streptococcus pneumoniae (strain ATCC BAA-255 / R6)","ATCC BAA-255 / R6 / ATCC BAA-255 / R6",8,264,264,6,261,261]
[null,"P77467","IPMed?",1.00379,1.01145,34.72,{"v":1E-42,"d":"1.00E-42"},3,1,"paaG","1,2-epoxyphenylacetyl-CoA isomerase","5.3.3.18","3D-structure, Complete proteome, Isomerase, Lyase, Reference proteome","9748275, 9097039, 9278503, 16738553, 10766858, 12846838, 20660314","Escherichia coli (strain K12)","W / ATCC 11105 / DSM 1900 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",10,264,264,9,262,262]
[null,"P24162","IPMed?",1.00379,1.03113,33.58,{"v":1E-42,"d":"1.00E-42"},4,1,"fadB1","Probable enoyl-CoA hydratase","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","1743516, 20418398","Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)","ATCC BAA-309 / NBRC 16581 / SB1003 / ATCC BAA-309 / NBRC 16581 / SB1003",1,264,264,1,257,257]
[null,"O07533","_",0.97348,1.00784,34.63,{"v":5e-38,"d":"5.00E-38"},5,1,"yhaR","Putative enoyl-CoA hydratase/isomerase YhaR","_","Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix","9384377, 19383706, 9579061","Bacillus subtilis (strain 168)","168 / 168",6,261,264,4,253,255]
[null,"A4YI89","IPMed?",1.00379,1.02317,32.83,{"v":4E-35,"d":"4.00E-35"},6,3,"_","3-hydroxypropionyl-coenzyme A dehydratase","4.2.1.116","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","18083856, 19429610","Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)","ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2",1,264,264,1,259,259]
[null,"P30084","IPMed?",0.86552,0.95076,33.86,{"v":6e-33,"d":"6.00E-33"},7,3,"ECHS1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Disease mutation, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Neurodegeneration, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","8012501, 9073515, 15164054, 15489334, 1286669, 11271497, 19608861, 21269460, 25125611, 24275569, 25393721, 25944712, 26000322, 26251176, 27221955, 26741492","Homo sapiens","_",14,264,264,47,290,290]
[null,"Q5R646","_",0.86552,0.95076,33.86,{"v":1e-32,"d":"1.00E-32"},8,3,"ECHS1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","Acetylation, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Phosphoprotein, Reference proteome, Transit peptide","_","Pongo abelii","_",14,264,264,47,290,290]
[null,"G4V4T7","IPMed?",1.03396,1.03788,34.67,{"v":3E-32,"d":"3.00E-32"},9,3,"dpgD","Enoyl-CoA-hydratase","4.2.1.17","Antibiotic biosynthesis, Lyase",11752437,"Amycolatopsis orientalis","NRRL18098",1,264,264,1,265,265]
[null,"P34559","_",0.88194,0.96212,32.28,{"v":3e-31,"d":"3.00E-31"},10,3,"ech-6","Probable enoyl-CoA hydratase, mitochondrial","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome","7906398, 9851916","Caenorhabditis elegans","Bristol N2 / Bristol N2",11,261,264,42,285,288]
[null,"Q52995","IPMed?",0.98864,1.01556,32.18,{"v":3e-31,"d":"3.00E-31"},11,3,"fadB1","Probable enoyl-CoA hydratase","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","7751302, 11481430, 11474104","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",1,261,264,1,254,257]
[null,"P14604","IPMed?",0.85517,0.93939,33.06,{"v":6e-31,"d":"6.00E-31"},12,3,"Echs1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide","2806264, 15489334, 7883013, 8895557, 9480773, 11851409, 12445775","Rattus norvegicus","_",14,261,264,47,287,290]
[null,"P94549","IPMed?",0.99621,1.01938,28.9,{"v":2e-29,"d":"2.00E-29"},13,3,"fadB","Probable enoyl-CoA hydratase","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid degradation, Lipid metabolism, Lyase, Reference proteome","8969504, 9384377, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",3,264,264,1,258,258]
[]
["AZ49_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,"P44874","_",0.95067,0.96364,53.3,{"v":2e-69,"d":"2.00E-69"},1,1,"atoA","Acetate CoA-transferase subunit beta","2.8.3.8","Complete proteome, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",7,218,220,4,214,223]
[null,"P76459","_",0.91818,0.93519,51.98,{"v":2e-65,"d":"2.00E-65"},2,1,"atoA","Acetate CoA-transferase subunit beta","2.8.3.8","3D-structure, Complete proteome, 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",10,211,220,7,205,216]
[null,"P23673","IPMed?",0.95928,0.96364,48.58,{"v":5e-64,"d":"5.00E-64"},3,1,"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",7,218,220,9,219,221]
[null,"P0C7I8","_",0.93182,0.96244,48.78,{"v":3e-63,"d":"3.00E-63"},4,1,"lpsJ","Succinyl-CoA:3-ketoacid coenzyme A transferase subunit B","2.8.3.5","Complete proteome, Lipopolysaccharide biosynthesis, Reference proteome, Transferase",12024217,"Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)","ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25",7,211,220,5,209,213]
[null,"B0RVK3","IPMed?",0.93182,0.96244,48.78,{"v":5e-63,"d":"5.00E-63"},5,1,"lpsJ","Succinyl-CoA:3-ketoacid coenzyme A transferase subunit B","2.8.3.5","Complete proteome, Lipopolysaccharide biosynthesis, Transferase","9385134, 18304669","Xanthomonas campestris pv. campestris (strain B100)","B100",7,211,220,5,209,213]
[null,"P9WPW3","_",0.91818,0.92661,46.53,{"v":2e-59,"d":"2.00E-59"},6,1,"scoB","Probable succinyl-CoA:3-ketoacid coenzyme A transferase subunit B","2.8.3.5","Complete proteome, Reference proteome, Transferase","9634230, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",10,211,220,11,212,218]
[null,"P9WPW2","_",0.91818,0.92661,46.53,{"v":2e-59,"d":"2.00E-59"},6,1,"scoB","Probable succinyl-CoA:3-ketoacid coenzyme A transferase subunit B","2.8.3.5","Complete proteome, Transferase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",10,211,220,11,212,218]
[null,"P63651","_",0.91818,0.92661,46.53,{"v":2e-59,"d":"2.00E-59"},6,1,"scoB","Probable succinyl-CoA:3-ketoacid coenzyme A transferase subunit B","2.8.3.5","Complete proteome, Transferase","12788972, 28385856","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97",10,211,220,11,212,218]
[null,"P42316","_",0.96364,0.98148,43.87,{"v":8e-59,"d":"8.00E-59"},7,1,"scoB","Probable succinyl-CoA:3-ketoacid coenzyme A transferase subunit B","2.8.3.5","3D-structure, Complete proteome, Reference proteome, Transferase","8969509, 9384377","Bacillus subtilis (strain 168)","168 / BGSC1A1 / 168",4,215,220,2,213,216]
[null,"Q9ESL0","IPMed?",0.41154,0.97273,47.66,{"v":4e-58,"d":"4.00E-58"},8,1,"Oxct2b","Succinyl-CoA:3-ketoacid coenzyme A transferase 2B, mitochondrial","2.8.3.5","Complete proteome, Mitochondrion, Reference proteome, Transferase, Transit peptide","11090426, 15028287, 15489334","Mus musculus","129/Sv",7,218,220,300,513,520]
[null,"Q9JJN4","IPMed?",0.41154,0.97273,47.66,{"v":4e-58,"d":"4.00E-58"},8,1,"Oxct2a","Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial","2.8.3.5","Complete proteome, Mitochondrion, Reference proteome, Transferase, Transit peptide","15028287, 16141072, 19468303, 15489334","Mus musculus","129/Sv / C57BL/6J / C57BL/6J",7,218,220,300,513,520]
[null,"Q54JD9","_",0.41061,0.95,44.98,{"v":2e-56,"d":"2.00E-56"},9,1,"oxct1","Probable succinyl-CoA:3-ketoacid coenzyme A transferase, mitochondrial","2.8.3.5","Complete proteome, Mitochondrion, Reference proteome, Transferase, Transit peptide",15875012,"Dictyostelium discoideum","AX4",7,215,220,293,501,509]
[null,"Q29551","IPMed?",0.41154,0.97273,45.79,{"v":4e-56,"d":"4.00E-56"},10,1,"OXCT1","Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial","2.8.3.5","3D-structure, Complete proteome, Direct protein sequencing, Mitochondrion, Phosphoprotein, Reference proteome, Transferase, Transit peptide","1730685, 7915164, 12463743, 15388917, 17718512, 20606260, 20977214","Sus scrofa","_",7,218,220,302,515,520]
[null,"P55809","IPMed?",0.41154,0.97273,44.39,{"v":2E-55,"d":"2.00E-55"},11,1,"OXCT1","Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial","2.8.3.5","3D-structure, Alternative splicing, Complete proteome, Direct protein sequencing, Disease mutation, Mitochondrion, Phosphoprotein, Polymorphism, Reference proteome, Transferase, Transit peptide","8751852, 10964512, 15372022, 14702039, 15489334, 19608861, 20068231, 21269460, 25944712, 9671268, 21296660","Homo sapiens","_",7,218,220,302,515,520]
[null,"Q9BYC2","IPMed?",0.42166,0.99091,45.41,{"v":3e-55,"d":"3.00E-55"},12,1,"OXCT2","Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial","2.8.3.5","Complete proteome, Mitochondrion, Polymorphism, Reference proteome, Transferase, Transit peptide","11756565, 14702039, 16710414","Homo sapiens","_",3,218,220,295,512,517]
[null,"Q9W058","IPMed?",0.4186,0.98182,45.83,{"v":4E-55,"d":"4.00E-55"},13,1,"SCOT","Succinyl-CoA:3-ketoacid-coenzyme A transferase, mitochondrial","2.8.3.5","3D-structure, Alternative splicing, Complete proteome, Mitochondrion, Reference proteome, Transferase, Transit peptide","10731132, 12537572, 12537569, 24100554","Drosophila melanogaster","Berkeley / Berkeley / Berkeley",7,220,220,298,513,516]
[null,"Q9D0K2","IPMed?",0.41154,0.97273,44.86,{"v":6e-54,"d":"6.00E-54"},14,1,"Oxct1","Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial","2.8.3.5","Complete proteome, Direct protein sequencing, Mitochondrion, Phosphoprotein, Reference proteome, Transferase, Transit peptide","12534938, 16141072, 15489334, 21183079, 23806337","Mus musculus","C57BL/6J",7,218,220,302,515,520]
[null,"P56007","IPMed?",0.93182,0.99034,43.9,{"v":2e-53,"d":"2.00E-53"},15,1,"scoB","Succinyl-CoA:3-ketoacid coenzyme A transferase subunit B","2.8.3.5","3D-structure, Complete proteome, Reference proteome, Transferase","9252185, 9325289","Helicobacter pylori (strain ATCC 700392 / 26695)","ATCC 700392 / 26695 / 69A",7,211,220,2,205,207]
[null,"Q59091","IPMed?",0.93182,0.9447,41.46,{"v":2e-48,"d":"2.00E-48"},16,1,"pcaJ","3-oxoadipate CoA-transferase subunit B","2.8.3.6","Aromatic hydrocarbons catabolism, Complete proteome, Direct protein sequencing, Transferase","8063101, 8125318, 15514110","Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)","ATCC 33305 / BD413 / ADP1",7,210,220,8,212,217]
[]
["AZ49_00550","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P44875","_",0.85714,0.96774,51.43,{"v":1e-69,"d":"1.00E-69"},1,1,"atoD","Acetate CoA-transferase subunit alpha","2.8.3.8","Complete proteome, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",4,213,245,4,213,217]
[null,"P76458","_",0.8898,0.99091,46.79,{"v":2e-64,"d":"2.00E-64"},2,1,"atoD","Acetate CoA-transferase subunit alpha","2.8.3.8","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","9097040, 9278503, 16738553","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",3,220,245,3,220,220]
[null,"O34317","_",0.8898,0.95197,42.2,{"v":7e-49,"d":"7.00E-49"},3,1,"yodS","Probable coenzyme A transferase subunit alpha","2.8.3.-","Complete proteome, Reference proteome, Transferase","9734814, 9384377","Bacillus subtilis (strain 168)","168 / 168",4,220,245,6,223,229]
[null,"P33752","IPMed?",0.86122,0.96789,39.34,{"v":1e-48,"d":"1.00E-48"},4,1,"ctfA","Butyrate--acetoacetate CoA-transferase subunit A","2.8.3.9","Complete proteome, Direct protein sequencing, Plasmid, Reference proteome, Transferase","8226639, 8423010, 11466286, 8300540, 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",3,213,245,3,213,218]
[null,"P42315","_",0.94694,0.97479,39.22,{"v":3e-46,"d":"3.00E-46"},6,1,"scoA","Probable succinyl-CoA:3-ketoacid coenzyme A transferase subunit A","2.8.3.5","3D-structure, Complete proteome, Reference proteome, Transferase","8969509, 9384377","Bacillus subtilis (strain 168)","168 / BGSC1A1 / 168",7,237,245,7,238,238]
[null,"B0RVK4","IPMed?",0.84898,0.8595,41.83,{"v":3e-46,"d":"3.00E-46"},5,1,"lpsI","Succinyl-CoA:3-ketoacid coenzyme A transferase subunit A","2.8.3.5","Complete proteome, Lipopolysaccharide biosynthesis, Transferase","9385134, 11589581, 18304669","Xanthomonas campestris pv. campestris (strain B100)","B100",15,221,245,24,231,242]
[null,"Q9ZLE3","_",0.88163,0.93103,40.74,{"v":5e-46,"d":"5.00E-46"},7,1,"scoA","Succinyl-CoA:3-ketoacid coenzyme A transferase subunit A","2.8.3.5","Complete proteome, Transferase",9923682,"Helicobacter pylori (strain J99 / ATCC 700824)","J99 / ATCC 700824",5,220,245,5,218,232]
[null,"P0C7I7","_",0.84898,0.8595,41.35,{"v":3e-45,"d":"3.00E-45"},8,1,"lpsI","Succinyl-CoA:3-ketoacid coenzyme A transferase subunit A","2.8.3.5","Complete proteome, Lipopolysaccharide biosynthesis, Reference proteome, Transferase",12024217,"Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)","ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25",15,221,245,24,231,242]
[null,"P56006","IPMed?",0.88163,0.93103,40.28,{"v":3e-45,"d":"3.00E-45"},9,1,"scoA","Succinyl-CoA:3-ketoacid coenzyme A transferase subunit A","2.8.3.5","3D-structure, Complete proteome, Reference proteome, Transferase","9252185, 9325289","Helicobacter pylori (strain ATCC 700392 / 26695)","ATCC 700392 / 26695 / 69A",5,220,245,5,218,232]
[null,"Q9W058","IPMed?",0.43411,0.91429,37.95,{"v":5E-42,"d":"5.00E-42"},10,2,"SCOT","Succinyl-CoA:3-ketoacid-coenzyme A transferase, mitochondrial","2.8.3.5","3D-structure, Alternative splicing, Complete proteome, Mitochondrion, Reference proteome, Transferase, Transit peptide","10731132, 12537572, 12537569, 24100554","Drosophila melanogaster","Berkeley / Berkeley / Berkeley",10,215,245,42,265,516]
[null,"Q9BYC2","IPMed?",0.44681,0.94286,39.83,{"v":1e-40,"d":"1.00E-40"},11,2,"OXCT2","Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial","2.8.3.5","Complete proteome, Mitochondrion, Polymorphism, Reference proteome, Transferase, Transit peptide","11756565, 14702039, 16710414","Homo sapiens","_",10,221,245,48,278,517]
[null,"Q01103","IPMed?",0.87347,0.92641,38.32,{"v":1e-39,"d":"1.00E-39"},12,1,"pcaI","3-oxoadipate CoA-transferase subunit A","2.8.3.6","Aromatic hydrocarbons catabolism, Direct protein sequencing, Transferase","1624453, 6780551","Pseudomonas putida","PRS2000",7,218,245,8,221,231]
[null,"Q43973","IPMed?",0.90204,0.9693,37.56,{"v":1e-39,"d":"1.00E-39"},13,1,"pcaI","3-oxoadipate CoA-transferase subunit A","2.8.3.6","Aromatic hydrocarbons catabolism, Complete proteome, Direct protein sequencing, Transferase","8063101, 8125318, 15514110","Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)","ATCC 33305 / BD413 / ADP1",7,225,245,8,228,228]
[null,"P55809","IPMed?",0.475,1.00816,35.22,{"v":3e-39,"d":"3.00E-39"},14,2,"OXCT1","Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial","2.8.3.5","3D-structure, Alternative splicing, Complete proteome, Direct protein sequencing, Disease mutation, Mitochondrion, Phosphoprotein, Polymorphism, Reference proteome, Transferase, Transit peptide","8751852, 10964512, 15372022, 14702039, 15489334, 19608861, 20068231, 21269460, 25944712, 9671268, 21296660","Homo sapiens","_",10,238,245,48,294,520]
[null,"Q9JJN4","IPMed?",0.42308,0.89796,38.64,{"v":7E-39,"d":"7.00E-39"},15,2,"Oxct2a","Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial","2.8.3.5","Complete proteome, Mitochondrion, Reference proteome, Transferase, Transit peptide","15028287, 16141072, 19468303, 15489334","Mus musculus","129/Sv / C57BL/6J / C57BL/6J",12,213,245,50,269,520]
[null,"Q9ESL0","IPMed?",0.42308,0.89796,38.64,{"v":9e-38,"d":"9.00E-38"},16,2,"Oxct2b","Succinyl-CoA:3-ketoacid coenzyme A transferase 2B, mitochondrial","2.8.3.5","Complete proteome, Mitochondrion, Reference proteome, Transferase, Transit peptide","11090426, 15028287, 15489334","Mus musculus","129/Sv",12,213,245,50,269,520]
[]
["AZ49_02170","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?",0.90278,0.94203,56.15,{"v":3e-40,"d":"3.00E-40"},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?",0.84713,0.96377,45.86,{"v":4e-29,"d":"4.00E-29"},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",3,135,138,6,137,157]
[null,"P86397","IPMed?",0.79762,0.97101,37.31,{"v":4e-24,"d":"4.00E-24"},3,1,"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","_",3,136,138,29,161,168]
[null,"O32472","IPMed?",0.92754,0.95522,39.84,{"v":7e-24,"d":"7.00E-24"},4,1,"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",8,135,138,4,131,134]
[null,"P49251","IPMed?",0.33433,0.81159,32.14,2e-07,5,1,"maoC","Protein MaoC","_","_",1556068,"Klebsiella aerogenes","W70",7,113,138,198,306,335]
[null,"P77455","IPMed?",0.16446,0.81159,30.36,6e-07,6,3,"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",7,113,138,531,639,681]
[null,"P22414","IPMed?",0.12472,0.81884,30.09,8e-05,7,4,"_","2-enoyl-CoA hydratase / (3R)-3-hydroxyacyl-CoA dehydrogenase","4.2.1.119","3D-structure, Fatty acid metabolism, Isomerase, Lipid metabolism, Lyase, Multifunctional enzyme, NAD, Oxidoreductase, Peroxisome, Repeat","3267241, 1937002, 2394320, 15051722, 16574148","Candida tropicalis","ATCC 20336 / pK233 / NCYC 997 / ATCC 20336 / pK233 / NCYC 997",26,136,138,798,900,906]
[null,"Q9VXJ0","IPMed?",0.19231,0.83333,28.7,1E-4,8,4,"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",16,129,138,477,585,598]
[null,"Q8VYI3","IPMed?",0.30097,0.67391,32.26,1E-4,9,1,"ECH2","Enoyl-CoA hydratase 2, peroxisomal","4.2.1.119","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Oxidoreductase, Peroxisome, Reference proteome","11130712, 27862469, 14593172, 16982622, 17951448","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia",33,124,138,205,292,309]
[null,"P07149","IPMed?",0.05217,0.77536,26.17,0.0002,10,2,"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","3D-structure, Acetylation, Complete proteome, Fatty acid biosynthesis, Fatty acid metabolism, Hydrolase, Isopeptide bond, Lipid biosynthesis, Lipid metabolism, Lyase, Multifunctional enzyme, NAD, NADP, Oxidoreductase, Phosphoprotein, Reference proteome, Transferase, Ubl conjugation","2034224, 8154185, 8196765, 24374639, 3528750, 3031066, 7992503, 14562106, 18407956, 19779198, 22814378, 22106047","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 26787 / X2180-1B / ATCC 26786 / X2180-1A",30,135,138,1553,1657,2051]
[]
["AZ49_02175","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"F1CYZ5","IPMed?",0.99427,1.01559,50.48,{"v":3e-161,"d":"3.00E-161"},1,1,"carA","Caffeate CoA-transferase","2.8.3.23","Transferase","17873051, 21131487, 23315745","Acetobacterium woodii","DSM1030 / DSM1030",1,511,513,1,518,524]
[null,"P37766","IPMed?",0.95857,0.9922,45.38,{"v":1E-150,"d":"1.00E-150"},2,1,"ydiF","Acetate CoA-transferase YdiF","2.8.3.8","Complete proteome, Reference proteome, Transferase","9097039, 9278503, 16738553, 3541912, 7984428","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",5,510,513,16,523,531]
[null,"Q8X5X6","IPMed?",0.95857,0.9922,45.38,{"v":2E-150,"d":"2.00E-150"},3,1,"ydiF","Acetate CoA-transferase YdiF","2.8.3.8","3D-structure, Complete proteome, Reference proteome, Transferase","11206551, 11258796, 16253988","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC / O157:H7 / EDL933 / ATCC 700927 / EHEC",5,510,513,16,523,531]
[null,"Q9W058","IPMed?",0.98837,0.99415,23.73,2e-13,4,6,"SCOT","Succinyl-CoA:3-ketoacid-coenzyme A transferase, mitochondrial","2.8.3.5","3D-structure, Alternative splicing, Complete proteome, Mitochondrion, Reference proteome, Transferase, Transit peptide","10731132, 12537572, 12537569, 24100554","Drosophila melanogaster","Berkeley / Berkeley / Berkeley",4,485,513,37,496,516]
[null,"Q9D0K2","IPMed?",0.97885,0.9922,23.77,3E-11,5,6,"Oxct1","Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial","2.8.3.5","Complete proteome, Direct protein sequencing, Mitochondrion, Phosphoprotein, Reference proteome, Transferase, Transit peptide","12534938, 16141072, 15489334, 21183079, 23806337","Mus musculus","C57BL/6J",3,477,513,41,493,520]
[null,"Q9ESL0","IPMed?",0.95192,0.96491,22.42,5e-11,6,6,"Oxct2b","Succinyl-CoA:3-ketoacid coenzyme A transferase 2B, mitochondrial","2.8.3.5","Complete proteome, Mitochondrion, Reference proteome, Transferase, Transit peptide","11090426, 15028287, 15489334","Mus musculus","129/Sv",4,476,513,43,490,520]
[null,"Q29551","IPMed?",0.95962,0.97271,22.85,7e-11,7,6,"OXCT1","Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial","2.8.3.5","3D-structure, Complete proteome, Direct protein sequencing, Mitochondrion, Phosphoprotein, Reference proteome, Transferase, Transit peptide","1730685, 7915164, 12463743, 15388917, 17718512, 20606260, 20977214","Sus scrofa","_",3,477,513,41,493,520]
[null,"P55809","IPMed?",0.96154,0.97466,23.2,2e-10,8,6,"OXCT1","Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial","2.8.3.5","3D-structure, Alternative splicing, Complete proteome, Direct protein sequencing, Disease mutation, Mitochondrion, Phosphoprotein, Polymorphism, Reference proteome, Transferase, Transit peptide","8751852, 10964512, 15372022, 14702039, 15489334, 19608861, 20068231, 21269460, 25944712, 9671268, 21296660","Homo sapiens","_",3,477,513,41,493,520]
[null,"Q9JJN4","IPMed?",0.95192,0.96491,22.22,2e-10,9,6,"Oxct2a","Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial","2.8.3.5","Complete proteome, Mitochondrion, Reference proteome, Transferase, Transit peptide","15028287, 16141072, 19468303, 15489334","Mus musculus","129/Sv / C57BL/6J / C57BL/6J",4,476,513,43,490,520]
[null,"P44874","_",0.42105,0.96861,30.09,5e-10,10,3,"atoA","Acetate CoA-transferase subunit beta","2.8.3.8","Complete proteome, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",277,480,513,4,195,223]
[null,"P23673","IPMed?",0.40546,0.94118,27.4,5e-09,11,3,"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",277,473,513,9,193,221]
[]
["AZ49_00650","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?",1.01036,1.01828,50.26,{"v":3e-110,"d":"3.00E-110"},1,5,"_","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","_",1,381,386,1,379,383]
[null,"P45867","IPMed?",1.00259,1.02111,45.48,{"v":1e-103,"d":"1.00E-103"},2,5,"acdA","Acyl-CoA dehydrogenase","1.3.99.-","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid degradation, Lipid metabolism, Oxidoreductase, Reference proteome","9353933, 9384377, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",1,385,386,1,379,379]
[null,"P52042","IPMed?",0.99223,1.01055,43.34,{"v":1e-98,"d":"1.00E-98"},3,5,"bcd","Acyl-CoA dehydrogenase, short-chain specific","1.3.8.1","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,381,386,1,375,379]
[null,"P45857","IPMed?",0.97927,0.99736,42.33,{"v":8e-98,"d":"8.00E-98"},4,5,"mmgC","Acyl-CoA dehydrogenase","1.3.99.-","3D-structure, Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",7,383,386,5,375,379]
[null,"P45952","IPMed?",0.90261,0.98446,45,{"v":3e-97,"d":"3.00E-97"},5,1,"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",5,380,386,41,412,421]
[null,"A5A6I0","_",0.89786,0.97927,44.18,{"v":8e-97,"d":"8.00E-97"},6,2,"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","_",7,380,386,43,412,421]
[null,"P11310","IPMed?",0.89786,0.97927,44.18,{"v":8e-97,"d":"8.00E-97"},6,2,"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","_",7,380,386,43,412,421]
[null,"P08503","IPMed?",0.90261,0.98446,44.47,{"v":2e-96,"d":"2.00E-96"},7,1,"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","_",5,380,386,41,412,421]
[null,"O34421","IPMed?",0.98964,1.00526,43.72,{"v":4e-96,"d":"4.00E-96"},8,5,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,380,386,1,375,380]
[null,"Q3SZB4","_",0.89786,0.97927,44.97,{"v":2E-95,"d":"2.00E-95"},9,2,"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","_",7,380,386,43,412,421]
[null,"Q8HXY8","_",0.89786,0.97927,43.92,{"v":7E-94,"d":"7.00E-94"},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","_",7,380,386,43,412,421]
[null,"P41367","IPMed?",0.90261,0.98446,43.95,{"v":1e-93,"d":"1.00E-93"},11,2,"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","_",5,380,386,41,412,421]
[null,"G3KIM8","IPMed?",0.97208,0.99223,43.34,{"v":2E-91,"d":"2.00E-91"},12,5,"acrC","Acryloyl-CoA reductase (NADH)","1.3.1.95","Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",1,380,386,14,388,394]
[]
["AZ49_02755","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?",1.00522,1.00785,64.16,{"v":4e-170,"d":"4.00E-170"},1,3,"_","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","_",1,382,382,1,383,383]
[null,"P45867","IPMed?",0.98691,0.99472,56.76,{"v":5e-143,"d":"5.00E-143"},2,1,"acdA","Acyl-CoA dehydrogenase","1.3.99.-","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid degradation, Lipid metabolism, Oxidoreductase, Reference proteome","9353933, 9384377, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",1,377,382,1,374,379]
[null,"P52042","IPMed?",1,1.00792,56.02,{"v":9e-141,"d":"9.00E-141"},3,2,"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",1,382,382,1,379,379]
[null,"P45857","IPMed?",0.99738,1.00528,48.56,{"v":4e-118,"d":"4.00E-118"},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",5,381,382,3,376,379]
[null,"Q07417","IPMed?",0.9199,0.99215,45.91,{"v":5E-110,"d":"5.00E-110"},5,1,"Acads","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","8276399, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / FVB/N",4,382,382,33,408,412]
[null,"P15651","IPMed?",0.9199,0.99215,45.38,{"v":1E-108,"d":"1.00E-108"},6,1,"Acads","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","2777793, 3968063, 11812788","Rattus norvegicus","_",4,382,382,33,408,412]
[null,"G3KIM8","IPMed?",0.97208,1.00262,47.78,{"v":3e-108,"d":"3.00E-108"},7,3,"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",1,382,382,14,393,394]
[null,"Q5RAS0","_",0.9199,0.99215,45.38,{"v":7E-106,"d":"7.00E-106"},8,2,"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","_",4,382,382,33,408,412]
[null,"Q3ZBF6","IPMed?",0.92233,0.99476,45,{"v":2e-105,"d":"2.00E-105"},9,1,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide",6712627,"Bos taurus","_",4,382,382,33,408,412]
[null,"P16219","IPMed?",0.9199,0.99215,45.12,{"v":6e-105,"d":"6.00E-105"},10,2,"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","_",4,382,382,33,408,412]
[null,"O34421","IPMed?",1.00262,1.00789,45.43,{"v":7e-104,"d":"7.00E-104"},11,2,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,382,382,1,380,380]
[]
["AZ49_02760","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P52046","IPMed?",0.96935,0.97308,59.68,{"v":2e-103,"d":"2.00E-103"},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",1,253,260,1,253,261]
[null,"Q0AVM1","IPMed?",1,1,55.38,{"v":3e-96,"d":"3.00E-96"},2,2,"_","Crotonyl-CoA hydratase","4.2.1.150","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",1,260,260,1,260,260]
[null,"A4YI89","IPMed?",1,1.00386,45,{"v":2E-73,"d":"2.00E-73"},3,2,"_","3-hydroxypropionyl-coenzyme A dehydratase","4.2.1.116","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","18083856, 19429610","Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)","ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2",1,260,260,1,259,259]
[null,"O34893","IPMed?",0.96538,0.96538,43.82,{"v":5e-65,"d":"5.00E-65"},4,2,"yngF","Putative enoyl-CoA hydratase/isomerase YngF","_","Complete proteome, Lyase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",9,259,260,9,259,260]
[null,"P9WNN8","_",0.98846,1,42.41,{"v":1e-63,"d":"1.00E-63"},5,2,"echA8","Probable enoyl-CoA hydratase echA8","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",1,257,260,1,254,257]
[null,"P9WNN9","_",0.98846,1,42.41,{"v":1e-63,"d":"1.00E-63"},5,2,"echA8","Probable enoyl-CoA hydratase echA8","4.2.1.17","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","9634230, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",1,257,260,1,254,257]
[null,"P64017","_",0.98846,1,42.41,{"v":1e-63,"d":"1.00E-63"},5,2,"echA8","Probable enoyl-CoA hydratase echA8","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase","12788972, 28385856","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97",1,257,260,1,254,257]
[null,"Q52995","IPMed?",0.99231,1.00389,41.86,{"v":9e-63,"d":"9.00E-63"},6,2,"fadB1","Probable enoyl-CoA hydratase","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","7751302, 11481430, 11474104","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",1,258,260,1,255,257]
[null,"Q58DM8","_",0.84828,0.94615,44.31,{"v":6e-62,"d":"6.00E-62"},7,2,"ECHS1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","Acetylation, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide",16305752,"Bos taurus","_",14,258,260,47,288,290]
[null,"Q8BH95","_",0.84828,0.94615,44.31,{"v":2e-61,"d":"2.00E-61"},9,2,"Echs1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Phosphoprotein, Reference proteome, Transit peptide","16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / C57BL/6J",14,258,260,47,288,290]
[null,"P14604","IPMed?",0.84828,0.94615,44.72,{"v":2e-61,"d":"2.00E-61"},8,2,"Echs1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide","2806264, 15489334, 7883013, 8895557, 9480773, 11851409, 12445775","Rattus norvegicus","_",14,258,260,47,288,290]
[null,"Q1ZXF1","_",0.8917,0.95,43.72,{"v":3e-61,"d":"3.00E-61"},10,2,"echs1","Probable enoyl-CoA hydratase, mitochondrial","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide",15875012,"Dictyostelium discoideum","AX4",14,260,260,34,277,277]
[null,"P30084","IPMed?",0.85172,0.95,43.72,{"v":4e-59,"d":"4.00E-59"},11,2,"ECHS1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Disease mutation, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Neurodegeneration, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","8012501, 9073515, 15164054, 15489334, 1286669, 11271497, 19608861, 21269460, 25125611, 24275569, 25393721, 25944712, 26000322, 26251176, 27221955, 26741492","Homo sapiens","_",14,258,260,47,288,290]
[null,"Q9JLZ3","IPMed?",0.80255,0.96923,41.27,{"v":3e-56,"d":"3.00E-56"},12,2,"Auh","Methylglutaconyl-CoA hydratase, mitochondrial","4.2.1.18","Acetylation, Alternative splicing, Branched-chain amino acid catabolism, Complete proteome, Lyase, Mitochondrion, Reference proteome, RNA-binding, Transit peptide","10072761, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","BALB/cJ / C57BL/6J",13,260,260,63,314,314]
[null,"F1LU71","IPMed?",0.8,0.96923,40.87,{"v":2E-55,"d":"2.00E-55"},13,2,"Auh","Methylglutaconyl-CoA hydratase, mitochondrial","4.2.1.18","Acetylation, Branched-chain amino acid catabolism, Complete proteome, Lyase, Mitochondrion, Reference proteome, RNA-binding, Transit peptide","15057822, 13783048","Rattus norvegicus","Brown Norway",13,260,260,64,315,315]
[null,"Q13825","IPMed?",0.74336,0.96923,40.08,{"v":3e-54,"d":"3.00E-54"},14,2,"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]
[]
["AZ49_04240","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?",1.00522,1.00785,64.68,{"v":4e-171,"d":"4.00E-171"},1,2,"_","Acyl-CoA dehydrogenase, short-chain specific","1.3.8.1","3D-structure, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Oxidoreductase","8399220, 7857927","Megasphaera elsdenii","_",1,382,382,1,383,383]
[null,"P45867","IPMed?",0.98691,0.99472,55.97,{"v":9e-141,"d":"9.00E-141"},2,2,"acdA","Acyl-CoA dehydrogenase","1.3.99.-","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid degradation, Lipid metabolism, Oxidoreductase, Reference proteome","9353933, 9384377, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",1,377,382,1,374,379]
[null,"P52042","IPMed?",1,1.00792,55.24,{"v":1e-138,"d":"1.00E-138"},3,3,"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",1,382,382,1,379,379]
[null,"P45857","IPMed?",0.99738,1.00528,47.51,{"v":3e-115,"d":"3.00E-115"},4,3,"mmgC","Acyl-CoA dehydrogenase","1.3.99.-","3D-structure, Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",5,381,382,3,376,379]
[null,"Q07417","IPMed?",0.9199,0.99215,45.38,{"v":1E-108,"d":"1.00E-108"},5,2,"Acads","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","8276399, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / FVB/N",4,382,382,33,408,412]
[null,"P15651","IPMed?",0.9199,0.99215,44.85,{"v":3e-107,"d":"3.00E-107"},6,2,"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","_",4,382,382,33,408,412]
[null,"G3KIM8","IPMed?",0.97208,1.00262,46.48,{"v":7E-105,"d":"7.00E-105"},7,4,"acrC","Acryloyl-CoA reductase (NADH)","1.3.1.95","Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",1,382,382,14,393,394]
[null,"Q5RAS0","_",0.9199,0.99215,44.85,{"v":2e-104,"d":"2.00E-104"},8,3,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","_","Pongo abelii","_",4,382,382,33,408,412]
[null,"Q3ZBF6","IPMed?",0.92233,0.99476,44.47,{"v":5e-104,"d":"5.00E-104"},9,3,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide",6712627,"Bos taurus","_",4,382,382,33,408,412]
[null,"P16219","IPMed?",0.9199,0.99215,44.59,{"v":1e-103,"d":"1.00E-103"},10,3,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Disease mutation, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","2565344, 9383286, 15489334, 1286669, 21269460, 21237683, 24275569, 25944712, 1692038, 9499414, 11134486","Homo sapiens","_",4,382,382,33,408,412]
[null,"O34421","IPMed?",1.00262,1.00789,45.17,{"v":2e-102,"d":"2.00E-102"},11,3,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,382,382,1,380,380]
[]
["AZ49_06245","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?",0.99208,0.99208,47.87,{"v":1e-116,"d":"1.00E-116"},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",1,374,379,1,374,379]
[null,"Q06319","IPMed?",1,1.01055,48.56,{"v":8e-114,"d":"8.00E-114"},2,4,"_","Acyl-CoA dehydrogenase, short-chain specific","1.3.8.1","3D-structure, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Oxidoreductase","8399220, 7857927","Megasphaera elsdenii","_",1,378,379,1,382,383]
[null,"P45857","IPMed?",0.98417,0.98417,47.18,{"v":9e-112,"d":"9.00E-112"},3,4,"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",8,378,379,6,376,379]
[null,"G3KIM8","IPMed?",0.96193,1,46.17,{"v":5E-110,"d":"5.00E-110"},4,1,"acrC","Acryloyl-CoA reductase (NADH)","1.3.1.95","Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",1,378,379,14,392,394]
[null,"P52042","IPMed?",0.99736,0.99736,44.71,{"v":9e-110,"d":"9.00E-110"},5,4,"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",1,376,379,1,376,379]
[null,"P9WQG1","_",0.97172,0.99736,46.03,{"v":2e-103,"d":"2.00E-103"},6,1,"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,"P9WQG0","_",0.97172,0.99736,46.03,{"v":2e-103,"d":"2.00E-103"},6,1,"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,"P63428","_",0.97172,0.99736,46.03,{"v":2e-103,"d":"2.00E-103"},6,1,"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,"P46703","_",0.97172,0.99736,44.44,{"v":1e-101,"d":"1.00E-101"},7,1,"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,"P15651","IPMed?",0.8835,0.96042,44.78,{"v":2e-101,"d":"2.00E-101"},8,4,"Acads","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","2777793, 3968063, 11812788","Rattus norvegicus","_",17,378,379,46,407,412]
[null,"Q07417","IPMed?",0.8835,0.96042,44.51,{"v":5e-100,"d":"5.00E-100"},9,4,"Acads","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","8276399, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / FVB/N",17,378,379,46,407,412]
[null,"P41367","IPMed?",0.89786,0.99736,46.03,{"v":1e-98,"d":"1.00E-98"},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,"P11310","IPMed?",0.89786,0.99736,44.18,{"v":1e-98,"d":"1.00E-98"},11,1,"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,"O34421","IPMed?",1.00263,1.00528,42.78,{"v":2e-98,"d":"2.00E-98"},12,4,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,378,379,1,379,380]
[]
["AZ49_06555","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?",1,1,100,0,1,1,"_","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?",1,1.01055,56.92,{"v":2e-143,"d":"2.00E-143"},2,1,"bcd","Acyl-CoA dehydrogenase, short-chain specific","1.3.8.1","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,383,383,1,379,379]
[null,"P45867","IPMed?",0.98172,0.99208,54.52,{"v":7e-135,"d":"7.00E-135"},3,3,"acdA","Acyl-CoA dehydrogenase","1.3.99.-","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid degradation, Lipid metabolism, Oxidoreductase, Reference proteome","9353933, 9384377, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",1,376,383,1,372,379]
[null,"P45857","IPMed?",0.98956,1,51.98,{"v":4E-125,"d":"4.00E-125"},4,1,"mmgC","Acyl-CoA dehydrogenase","1.3.99.-","3D-structure, Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",4,382,383,2,376,379]
[null,"O34421","IPMed?",1.00261,1.01053,48.44,{"v":4e-113,"d":"4.00E-113"},5,1,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,383,383,1,380,380]
[null,"G3KIM8","IPMed?",0.97462,1.00261,46.61,{"v":2e-108,"d":"2.00E-108"},6,2,"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",1,383,383,14,393,394]
[null,"P15651","IPMed?",0.9199,0.98956,44.85,{"v":7e-107,"d":"7.00E-107"},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","_",5,383,383,34,408,412]
[null,"Q07417","IPMed?",0.9199,0.98956,44.85,{"v":7e-107,"d":"7.00E-107"},7,3,"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",5,383,383,34,408,412]
[null,"Q5RAS0","_",0.9199,0.98956,45.12,{"v":4e-106,"d":"4.00E-106"},8,1,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","_","Pongo abelii","_",5,383,383,34,408,412]
[null,"P16219","IPMed?",0.9199,0.98956,44.85,{"v":3e-105,"d":"3.00E-105"},10,1,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Disease mutation, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","2565344, 9383286, 15489334, 1286669, 21269460, 21237683, 24275569, 25944712, 1692038, 9499414, 11134486","Homo sapiens","_",5,383,383,34,408,412]
[null,"Q3ZBF6","IPMed?",0.9199,0.98956,45.12,{"v":3e-105,"d":"3.00E-105"},9,2,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide",6712627,"Bos taurus","_",5,383,383,34,408,412]
[null,"H6LGM6","IPMed?",0.96867,0.97889,44.74,{"v":3e-100,"d":"3.00E-100"},11,3,"carC","Caffeyl-CoA reductase-Etf complex subunit CarC","1.3.1.108","3D-structure, Complete proteome, Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",14,383,383,12,378,379]
[]
["AZ49_06560","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?",1,1,99.63,0,1,1,"etfB","Electron transfer flavoprotein subunit beta","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,270,270,1,270,270]
[null,"P97089","_",1.0037,1.04231,49.45,{"v":1e-80,"d":"1.00E-80"},2,1,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",1,270,270,1,260,260]
[null,"P52040","IPMed?",0.91111,0.94981,52.44,{"v":6E-79,"d":"6.00E-79"},3,1,"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",1,246,270,1,238,259]
[null,"H6LGM7","IPMed?",0.98148,1.01145,49.06,{"v":2e-77,"d":"2.00E-77"},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",1,263,270,1,259,262]
[null,"G3KIM7","IPMed?",1.00741,1.01873,46.32,{"v":3E-65,"d":"3.00E-65"},5,1,"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",1,265,270,1,266,267]
[null,"P26482","IPMed?",0.87189,0.90741,45.31,{"v":7e-61,"d":"7.00E-61"},6,1,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Reference proteome, Transport","1850088, 3216855","Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)","_",1,241,270,1,242,281]
[null,"P53577","IPMed?",0.92014,0.98148,42.26,{"v":4e-60,"d":"4.00E-60"},7,1,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Reference proteome, Transport","8599534, 11157954, 12597275","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","USDA 3I1b110 / USDA 110spc4 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110",1,260,270,1,262,288]
[null,"P53576","_",0.96797,1.00741,41.18,{"v":6e-59,"d":"6.00E-59"},8,1,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",1,267,270,1,268,281]
[null,"Q53210","_",0.95789,1.01111,39.93,{"v":2e-56,"d":"2.00E-56"},9,1,"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",1,268,270,1,270,285]
[null,"Q05559","IPMed?",0.87814,0.90741,42.04,{"v":4E-55,"d":"4.00E-55"},10,1,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport",8369342,"Rhizobium leguminosarum bv. phaseoli","_",1,241,270,1,240,279]
[null,"P09818","IPMed?",0.83562,0.9037,42.21,{"v":3e-53,"d":"3.00E-53"},11,1,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104, 6317191","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",1,240,270,1,241,292]
[null,"P64098","IPMed?",1.01111,1.02632,34.43,{"v":2E-46,"d":"2.00E-46"},12,1,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Transport","12788972, 28385856, 16006064","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97 / BCG / Pasteur",3,270,270,4,266,266]
[null,"Q0AZ34","IPMed?",0.93704,1.00397,35.97,{"v":1e-37,"d":"1.00E-37"},13,1,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Cytoplasm, Electron transport, Fatty acid metabolism, Lipid metabolism, Nucleotide-binding, Reference proteome, Transport","21966920, 19648244, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",1,253,270,3,233,252]
[]
["AZ49_06565","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O85692","IPMed?",1,1,99.7,0,1,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,338,338,1,338,338]
[null,"P71153","_",0.97929,1.00303,57.4,{"v":1e-123,"d":"1.00E-123"},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)","_",5,335,338,3,330,330]
[null,"H6LGM8","IPMed?",0.83838,0.98225,55.42,{"v":8e-120,"d":"8.00E-120"},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",2,333,338,64,393,396]
[null,"P53578","IPMed?",0.98521,0.99701,55.86,{"v":3e-117,"d":"3.00E-117"},4,1,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Transport",7875566,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",1,333,338,1,329,334]
[null,"P52039","IPMed?",0.98817,0.99405,52.4,{"v":4e-113,"d":"4.00E-113"},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",1,332,338,1,332,336]
[null,"G3KIM6","IPMed?",0.9782,1.06213,48.19,{"v":6e-106,"d":"6.00E-106"},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",2,335,338,7,365,367]
[null,"P26483","IPMed?",0.89702,0.97929,43.2,{"v":5e-82,"d":"5.00E-82"},7,1,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Reference proteome, Transport",1850088,"Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)","_",6,332,338,29,356,369]
[null,"P94551","_",0.97337,1.01231,44.38,{"v":1e-81,"d":"1.00E-81"},8,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","8969504, 9384377","Bacillus subtilis (strain 168)","168 / 168",7,333,338,3,320,325]
[null,"P53574","_",0.93611,0.99704,42.73,{"v":4e-80,"d":"4.00E-80"},9,1,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",5,336,338,21,354,360]
[null,"Q53209","_",0.90515,0.98817,41.62,{"v":3e-78,"d":"3.00E-78"},10,1,"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",5,334,338,28,358,369]
[null,"P09819","IPMed?",0.94901,0.99112,39.7,{"v":4e-75,"d":"4.00E-75"},11,1,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",5,334,338,11,342,353]
[null,"P10449","IPMed?",0.89702,0.97929,39.58,{"v":4E-73,"d":"4.00E-73"},12,1,"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",6,332,338,29,356,369]
[null,"Q0AZ33","IPMed?",0.9645,1.02839,40.18,{"v":1e-71,"d":"1.00E-71"},13,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Cytoplasm, Electron transport, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Reference proteome, Transport","21966920, 19648244, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",8,333,338,3,317,317]
[null,"P13803","IPMed?",0.98521,1,35.74,{"v":6E-49,"d":"6.00E-49"},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","_",3,334,338,16,333,333]
[]
["AZ49_07320","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"H6LGM7","IPMed?",1,1.00769,37.4,{"v":9e-54,"d":"9.00E-54"},1,2,"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",1,260,260,1,262,262]
[null,"O85691","IPMed?",0.91481,0.95,39.68,{"v":1E-53,"d":"1.00E-53"},2,2,"etfB","Electron transfer flavoprotein subunit beta","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,239,260,1,247,270]
[null,"P97089","_",1.00769,1.00769,37.02,{"v":9e-53,"d":"9.00E-53"},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)","_",1,260,260,1,260,260]
[null,"P26482","IPMed?",0.91815,0.99231,37.6,{"v":6E-49,"d":"6.00E-49"},4,2,"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)","_",1,246,260,1,258,281]
[null,"P53577","IPMed?",0.82639,0.91538,38.66,{"v":4e-48,"d":"4.00E-48"},5,2,"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",1,229,260,1,238,288]
[null,"P52040","IPMed?",1.00385,1.00772,35.25,{"v":9e-48,"d":"9.00E-48"},6,2,"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",1,260,260,1,259,259]
[null,"Q53210","_",0.94035,1.03077,36.19,{"v":5e-47,"d":"5.00E-47"},7,2,"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",1,256,260,1,268,285]
[null,"O33095","_",1.00376,1.02692,37.45,{"v":2E-46,"d":"2.00E-46"},8,1,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport",11234002,"Mycobacterium leprae (strain TN)","TN",2,260,260,3,266,266]
[null,"P64098","IPMed?",1.00376,1.02692,36.7,{"v":3e-45,"d":"3.00E-45"},9,2,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Transport","12788972, 28385856, 16006064","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97 / BCG / Pasteur",2,260,260,3,266,266]
[null,"P9WNG7","_",1.00376,1.02692,36.7,{"v":3e-45,"d":"3.00E-45"},9,2,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","9634230, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",2,260,260,3,266,266]
[null,"P9WNG6","_",1.00376,1.02692,36.7,{"v":3e-45,"d":"3.00E-45"},9,2,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Transport",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",2,260,260,3,266,266]
[null,"G3KIM7","IPMed?",1.00375,1.03077,34.33,{"v":3e-42,"d":"3.00E-42"},10,2,"acrB","Acryloyl-CoA reductase electron transfer subunit gamma","_","Cytoplasm, Electron transport, Transport","22810300, 12603323","Anaerotignum propionicum","ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2 / ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2",1,260,260,1,267,267]
[null,"Q05559","IPMed?",0.94265,1.01154,36.12,{"v":1E-41,"d":"1.00E-41"},11,2,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport",8369342,"Rhizobium leguminosarum bv. phaseoli","_",1,251,260,1,261,279]
[null,"P09818","IPMed?",0.81507,0.91538,35.29,{"v":1e-39,"d":"1.00E-39"},12,2,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104, 6317191","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",1,229,260,1,238,292]
[null,"Q0AZ34","IPMed?",0.92692,0.95635,29.46,{"v":4e-25,"d":"4.00E-25"},13,2,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Cytoplasm, Electron transport, Fatty acid metabolism, Lipid metabolism, Nucleotide-binding, Reference proteome, Transport","21966920, 19648244, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",1,239,260,3,229,252]
[]
["AZ49_07325","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","_",0.99099,1,41.21,{"v":8e-77,"d":"8.00E-77"},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)","_",5,332,333,5,330,330]
[null,"O85692","IPMed?",0.98521,1,40.24,{"v":1E-70,"d":"1.00E-70"},2,2,"etfA","Electron transfer flavoprotein subunit alpha","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",5,333,333,7,336,338]
[null,"P09819","IPMed?",0.94051,0.997,38.25,{"v":3e-67,"d":"3.00E-67"},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",5,330,333,13,341,353]
[null,"P10449","IPMed?",0.87805,0.97297,38.89,{"v":8e-67,"d":"8.00E-67"},4,2,"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",5,324,333,30,351,369]
[null,"H6LGM8","IPMed?",0.83838,0.997,34.94,{"v":2E-66,"d":"2.00E-66"},5,2,"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",1,331,333,65,394,396]
[null,"P26483","IPMed?",0.8916,0.98799,37.39,{"v":3e-66,"d":"3.00E-66"},6,2,"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)","_",5,329,333,30,356,369]
[null,"P52039","IPMed?",0.97024,0.97898,36.2,{"v":5e-66,"d":"5.00E-66"},7,2,"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",5,329,333,7,332,336]
[null,"Q53209","_",0.89431,0.99099,36.67,{"v":1e-65,"d":"1.00E-65"},8,2,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Plasmid, Transport","8796346, 9163424, 19376903","Sinorhizobium fredii (strain NBRC 101917 / NGR234)","NBRC 101917 / NGR234 / NBRC 101917 / NGR234",5,330,333,30,357,369]
[null,"P53574","_",0.91944,0.99399,36.56,{"v":7e-65,"d":"7.00E-65"},9,2,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",5,329,333,23,350,360]
[null,"P53578","IPMed?",0.98204,0.98498,37.5,{"v":1e-63,"d":"1.00E-63"},10,2,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Transport",7875566,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",5,331,333,7,330,334]
[null,"Q0AZ33","IPMed?",0.96697,1.01577,34.78,{"v":1e-57,"d":"1.00E-57"},11,2,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Cytoplasm, Electron transport, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Reference proteome, Transport","21966920, 19648244, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",9,330,333,6,317,317]
[null,"G3KIM6","IPMed?",0.97003,1.06907,33.99,{"v":2e-54,"d":"2.00E-54"},12,2,"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",5,330,333,12,363,367]
[null,"P38974","IPMed?",0.94595,1.02273,33.97,{"v":8e-42,"d":"8.00E-42"},13,2,"etfA","Electron transfer flavoprotein subunit alpha","_","3D-structure, Direct protein sequencing, Electron transport, FAD, Flavoprotein, Transport","8376381, 1576992, 10026281","Paracoccus denitrificans","ATCC 13543 / NRRL B-3784 / NRC 449 / ATCC 13543 / NRRL B-3784 / NRC 449",12,324,333,8,304,308]
[]
["AZ49_01090","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?",0.96831,0.96831,54.91,{"v":6e-114,"d":"6.00E-114"},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",8,282,284,5,276,284]
[null,"Q8TSX9","IPMed?",0.93662,1.00758,40.23,{"v":2e-68,"d":"2.00E-68"},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",4,269,284,2,261,264]
[null,"H6LC27","IPMed?",0.78979,0.92606,36.5,{"v":5e-54,"d":"5.00E-54"},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",8,270,284,6,262,333]
[null,"A8GE01","_",0.66197,0.98947,32.45,{"v":4e-26,"d":"4.00E-26"},4,1,"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)","_",9,196,284,6,166,190]
[null,"A7MMM3","_",0.66549,0.98438,32.28,{"v":5e-26,"d":"5.00E-26"},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",8,196,284,5,168,192]
[null,"B4T595","_",0.66197,0.97917,34.04,{"v":5e-26,"d":"5.00E-26"},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 newport (strain SL254)","SL254",9,196,284,6,168,192]
[null,"A9N024","_",0.66197,0.97917,33.51,{"v":2e-25,"d":"2.00E-25"},7,1,"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)","_",9,196,284,6,168,192]
[null,"A8A0H1","_",0.66197,0.97917,31.91,{"v":2e-25,"d":"2.00E-25"},8,1,"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",9,196,284,6,168,192]
[null,"B4THD5","_",0.66197,0.97917,33.51,{"v":2e-25,"d":"2.00E-25"},7,1,"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",9,196,284,6,168,192]
[null,"B5FIE6","_",0.66197,0.97917,33.51,{"v":2e-25,"d":"2.00E-25"},7,1,"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",9,196,284,6,168,192]
[null,"P77223","IPMed?",0.66197,0.97917,31.91,{"v":2e-25,"d":"2.00E-25"},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, 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",9,196,284,6,168,192]
[null,"B1IQC6","_",0.66197,0.97917,31.91,{"v":2e-25,"d":"2.00E-25"},8,1,"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)","_",9,196,284,6,168,192]
[null,"B1XF93","_",0.66197,0.97917,31.91,{"v":2e-25,"d":"2.00E-25"},8,1,"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",9,196,284,6,168,192]
[null,"C4ZY91","_",0.66197,0.97917,31.91,{"v":2e-25,"d":"2.00E-25"},8,1,"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",9,196,284,6,168,192]
[null,"Q8ZPM1","_",0.66197,0.97917,33.51,{"v":2e-25,"d":"2.00E-25"},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",11677609,"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","LT2 / SGSC1412 / ATCC 700720",9,196,284,6,168,192]
[null,"B6EGH6","_",0.66549,0.97423,31.75,{"v":3e-25,"d":"3.00E-25"},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",19099551,"Aliivibrio salmonicida (strain LFI1238)","LFI1238",8,196,284,5,165,194]
[null,"B4TV18","_",0.66197,0.97917,33.51,{"v":4e-25,"d":"4.00E-25"},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, Repeat, Translocase, Transport",21602358,"Salmonella schwarzengrund (strain CVM19633)","CVM19633",9,196,284,6,168,192]
[null,"Q8Z6R0","_",0.66197,0.97917,33.51,{"v":4e-25,"d":"4.00E-25"},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, Repeat, Translocase, Transport","11677608, 12644504","Salmonella typhi","CT18 / ATCC 700931 / Ty2",9,196,284,6,168,192]
[null,"C0Q507","_",0.66197,0.97917,33.51,{"v":4e-25,"d":"4.00E-25"},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, Repeat, Translocase, Transport",19229335,"Salmonella paratyphi C (strain RKS4594)","RKS4594",9,196,284,6,168,192]
[null,"B5F6I9","_",0.66197,0.97917,33.51,{"v":4e-25,"d":"4.00E-25"},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, Repeat, Translocase, Transport",21602358,"Salmonella agona (strain SL483)","SL483",9,196,284,6,168,192]
[null,"B5BKB1","_",0.66197,0.97917,33.51,{"v":4e-25,"d":"4.00E-25"},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",19159446,"Salmonella paratyphi A (strain AKU_12601)","AKU_12601",9,196,284,6,168,192]
[null,"A5F2R3","IPMed?",0.66197,0.9641,30.85,{"v":5e-23,"d":"5.00E-23"},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",8,195,284,5,164,195]
[null,"P0CZ14","IPMed?",0.64437,0.97861,29.51,{"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",8,190,284,2,157,187]
[null,"D5ARZ0","IPMed?",0.64437,0.97861,29.51,{"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",8,190,284,2,157,187]
[null,"Q00388","IPMed?",0.39698,0.55634,27.85,7e-09,13,1,"vhuB","Polyferredoxin protein VhuB","_","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",1603063,"Methanococcus voltae","ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS",128,283,284,44,190,398]
[null,"Q01700","IPMed?",0.16901,0.82759,37.5,2e-07,14,3,"_","Probable ferredoxin","_","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Repeat, Transport",1379583,"Methanosarcina thermophila","ATCC 43570 / DSM 1825 / OCM 12 / TM-1",145,192,284,10,57,58]
[null,"Q49180","IPMed?",0.51214,0.74296,27.49,4e-07,15,2,"mvhB","Polyferredoxin protein MvhB","_","4Fe-4S, Iron, Iron-sulfur, Metal-binding, Repeat",2115877,"Methanothermus fervidus","_",77,269,284,151,339,412]
[null,"P84626","IPMed?",0.07275,0.17958,43.14,1e-05,16,1,"hdlA","Heterodisulfide reductase subunit A-like protein","1.8.-.-","4Fe-4S, Complete proteome, Cytoplasm, Direct protein sequencing, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat","21304717, 15009189","Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18)","DSM 5631 / JCM 9629 / NBRC 100127 / Av18",145,192,284,627,677,701]
[]
["AZ49_01095","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?",0.97409,0.98429,70.74,{"v":7e-95,"d":"7.00E-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",4,191,191,4,191,193]
[null,"B5XWQ1","_",0.97927,0.98953,52.38,{"v":1e-68,"d":"1.00E-68"},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",18654632,"Klebsiella pneumoniae (strain 342)",342,3,191,191,3,191,193]
[null,"B7NB81","_",0.97927,0.98953,51.85,{"v":1e-68,"d":"1.00E-68"},4,1,"rsxA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",19165319,"Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC)","UMN026 / ExPEC",3,191,191,3,191,193]
[null,"B6IB62","_",0.97927,0.98953,51.85,{"v":1e-68,"d":"1.00E-68"},4,1,"rsxA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",18931093,"Escherichia coli (strain SE11)","SE11",3,191,191,3,191,193]
[null,"B1IQC7","_",0.97927,0.98953,51.85,{"v":1e-68,"d":"1.00E-68"},4,1,"rsxA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport","_","Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)","_",3,191,191,3,191,193]
[null,"B1LEQ9","_",0.97927,0.98953,51.85,{"v":1e-68,"d":"1.00E-68"},4,1,"rsxA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",18708504,"Escherichia coli (strain SMS-3-5 / SECEC)","SMS-3-5 / SECEC",3,191,191,3,191,193]
[null,"A8GE02","_",0.97927,0.98953,52.91,{"v":1e-68,"d":"1.00E-68"},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","_","Serratia proteamaculans (strain 568)","_",3,191,191,3,191,193]
[null,"P0A766","IPMed?",0.97927,0.98953,51.85,{"v":1e-68,"d":"1.00E-68"},4,1,"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",3,191,191,3,191,193]
[null,"Q1RBG9","_",0.97927,0.98953,51.85,{"v":2e-68,"d":"2.00E-68"},5,1,"rsxA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",16585510,"Escherichia coli (strain UTI89 / UPEC)","UTI89 / UPEC",3,191,191,3,191,193]
[null,"A1ABH2","_",0.97927,0.98953,51.85,{"v":2e-68,"d":"2.00E-68"},5,1,"rsxA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",17293413,"Escherichia coli O1:K1 / APEC","_",3,191,191,3,191,193]
[null,"Q7N4G1","_",0.97927,0.98953,51.32,{"v":2e-68,"d":"2.00E-68"},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",14528314,"Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)","DSM 15139 / CIP 105565 / TT01",3,191,191,3,191,193]
[null,"B7M9Y1","_",0.97927,0.98953,51.85,{"v":2e-68,"d":"2.00E-68"},5,1,"rsxA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",19165319,"Escherichia coli O45:K1 (strain S88 / ExPEC)","S88 / ExPEC",3,191,191,3,191,193]
[null,"Q3Z1Y2","_",0.97927,0.98953,51.32,{"v":4e-68,"d":"4.00E-68"},7,1,"rsxA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",16275786,"Shigella sonnei (strain Ss046)","Ss046",3,191,191,3,191,193]
[null,"Q320Y4","_",0.97927,0.98953,50.79,{"v":8e-68,"d":"8.00E-68"},9,1,"rsxA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",16275786,"Shigella boydii serotype 4 (strain Sb227)","Sb227",3,191,191,3,191,193]
[null,"A8AH08","_",0.97927,0.98953,51.32,{"v":8e-68,"d":"8.00E-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","_","Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)","_",3,191,191,3,191,193]
[null,"B7LQP3","_",0.97927,0.98953,51.32,{"v":8e-68,"d":"8.00E-68"},8,1,"rsxA","Ion-translocating oxidoreductase complex subunit A","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",19165319,"Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73)","ATCC 35469 / DSM 13698 / CDC 0568-73",3,191,191,3,191,193]
[null,"A9MRW5","_",0.97927,0.98953,51.32,{"v":1e-67,"d":"1.00E-67"},10,1,"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","_","Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980)","_",3,191,191,3,191,193]
[null,"A0A0H3AKU6","IPMed?",0.88732,0.98953,52.38,{"v":3e-66,"d":"3.00E-66"},11,1,"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",3,191,191,23,211,213]
[null,"H6LC28","IPMed?",0.98438,0.98953,50.26,{"v":2e-62,"d":"2.00E-62"},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",2,190,191,1,189,192]
[null,"Q8TSY0","IPMed?",0.94472,0.98429,45.74,{"v":1e-55,"d":"1.00E-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?",0.98964,1,42.41,{"v":3E-52,"d":"3.00E-52"},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?",0.98964,1,42.41,{"v":3E-52,"d":"3.00E-52"},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?",0.97475,1.01047,41.97,{"v":3e-46,"d":"3.00E-46"},15,1,"nqrE","Na(+)-translocating NADH-quinone reductase subunit E","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, 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",4,190,191,4,196,198]
[null,"Q9X4Q7","IPMed?",0.97475,1.01047,40.41,{"v":3e-46,"d":"3.00E-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",4,190,191,4,196,198]
[null,"A5F5Y5","IPMed?",0.97475,1.01047,40.41,{"v":3e-46,"d":"3.00E-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",4,190,191,4,196,198]
[null,"Q9RFV7","IPMed?",0.97475,1.01047,40.41,{"v":4e-45,"d":"4.00E-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, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",10587447,"Vibrio campbellii (strain ATCC BAA-1116 / BB120)","_",4,190,191,4,196,198]
[null,"Q56589","IPMed?",0.97475,1.01047,40.41,{"v":6e-45,"d":"6.00E-45"},18,1,"nqrE","Na(+)-translocating NADH-quinone reductase subunit E","7.2.1.1","Cell inner membrane, Cell membrane, Direct protein sequencing, Ion transport, Membrane, NAD, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7729558, 7805867, 9490015, 10549856, 11248187, 11248188","Vibrio alginolyticus","NCIMB 11038 / LMG 3418",4,190,191,4,196,198]
[]
["AZ49_01100","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?",0.94836,0.97585,64.36,{"v":1E-89,"d":"1.00E-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?",0.89855,0.94898,49.46,{"v":1e-60,"d":"1.00E-60"},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?",0.99061,1.01932,44.08,{"v":8e-48,"d":"8.00E-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,{"v":3e-46,"d":"3.00E-46"},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":2e-44,"d":"2.00E-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,"Q89AW5","_",0.85477,0.99517,37.86,{"v":3e-44,"d":"3.00E-44"},6,1,"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",2,194,207,3,208,241]
[null,"Q57020","_",0.85106,0.96618,40.5,{"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,"Q4QJQ3","_",0.85106,0.96618,40.5,{"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,"A5UFC5","_",0.8547,0.96618,40.5,{"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,"Q9F5Y1","_",0.90336,1.03865,39.07,{"v":6e-43,"d":"6.00E-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",19429624,"Azotobacter vinelandii (strain DJ / ATCC BAA-1303)","DJ / ATCC BAA-1303",4,204,207,18,232,238]
[null,"A5F2S7","IPMed?",0.87826,0.97585,40.1,{"v":7e-43,"d":"7.00E-43"},9,1,"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,"A5UBI7","_",0.85106,0.96618,40,{"v":8e-43,"d":"8.00E-43"},10,1,"rnfE","Ion-translocating oxidoreductase complex subunit E","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Membrane, Translocase, Transmembrane, Transmembrane helix, Transport",17550610,"Haemophilus influenzae (strain PittEE)","PittEE",2,187,207,26,225,235]
[null,"P97055","IPMed?",0.8107,0.95169,41.62,{"v":5E-42,"d":"5.00E-42"},11,1,"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?",0.93074,1.03865,36.28,{"v":8e-42,"d":"8.00E-42"},12,1,"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",6,206,207,7,220,231]
[null,"A5F5Y6","IPMed?",0.95714,0.97101,36.82,{"v":5E-36,"d":"5.00E-36"},13,1,"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?",0.95714,0.97101,36.82,{"v":5E-36,"d":"5.00E-36"},13,1,"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?",1,1.01449,36.19,{"v":5E-36,"d":"5.00E-36"},14,1,"nqrD","Na(+)-translocating NADH-quinone reductase subunit D","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Ion transport, Membrane, NAD, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone",10587447,"Vibrio campbellii (strain ATCC BAA-1116 / BB120)","_",2,206,207,6,210,210]
[null,"Q57095","IPMed?",1,1.01449,35.71,{"v":2E-35,"d":"2.00E-35"},15,1,"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]
[null,"P43958","IPMed?",0.89904,0.90338,36.9,{"v":8e-35,"d":"8.00E-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, 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]
[]
["AZ49_01105","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?",0.98378,0.99454,49.45,{"v":5e-57,"d":"5.00E-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",3,183,183,4,185,185]
[null,"H6LC30","IPMed?",0.90821,1.02732,29.79,{"v":4e-20,"d":"4.00E-20"},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",9,175,183,14,200,207]
[null,"A3QEN8","_",0.53302,0.61749,41.59,7e-14,3,1,"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)","_",70,174,183,81,190,212]
[null,"Q8TSY2","IPMed?",0.98936,1.01639,26.88,2e-13,4,1,"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",1,175,183,1,181,188]
[null,"B8E552","_",0.53302,0.61749,43.36,3e-13,5,1,"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)","_",70,174,183,81,190,212]
[null,"P77285","IPMed?",0.57282,0.64481,40.68,5e-13,6,1,"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",64,173,183,73,187,206]
[null,"P58345","_",0.57282,0.64481,40.68,5e-13,6,1,"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","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",64,173,183,73,187,206]
[null,"C3LTR1","_",0.94258,1.0765,31.47,7e-13,7,1,"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",17,179,183,1,194,209]
[null,"Q9KT90","_",0.94258,1.0765,31.47,7e-13,7,1,"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",17,179,183,1,194,209]
[null,"A5F2S8","IPMed?",0.94258,1.0765,31.47,7e-13,7,1,"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",17,179,183,1,194,209]
[null,"C6DH13","_",0.8756,1,32.24,2E-12,8,1,"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","_","Pectobacterium carotovorum subsp. carotovorum (strain PC1)","_",13,173,183,9,188,209]
[null,"Q8EE77","_",0.53302,0.61749,40.71,3e-12,9,1,"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",12368813,"Shewanella oneidensis (strain MR-1)","MR-1",70,174,183,81,190,212]
[null,"Q9HYB6","_",0.62617,0.73224,35.82,9e-12,10,1,"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",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",50,174,183,64,194,214]
[null,"B7UVW9","_",0.62617,0.73224,35.82,9e-12,10,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",19047519,"Pseudomonas aeruginosa (strain LESB58)","LESB58",50,174,183,64,194,214]
[null,"Q02QY2","_",0.62617,0.73224,35.82,9e-12,10,1,"rnfG","Ion-translocating oxidoreductase complex subunit G","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",17038190,"Pseudomonas aeruginosa (strain UCBPP-PA14)","UCBPP-PA14",50,174,183,64,194,214]
[null,"P97054","IPMed?",0.77419,0.91803,28.57,2E-8,11,1,"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",16,165,183,26,190,217]
[null,"Q56582","IPMed?",0.57031,0.79781,26.71,4e-05,12,1,"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",32,163,183,82,227,256]
[null,"P43957","IPMed?",0.56148,0.74863,26.28,0.0008,13,1,"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",38,162,183,79,215,244]
[null,"A5F5Y7","IPMed?",0.56809,0.79781,25.34,2E-3,14,1,"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",32,163,183,83,228,257]
[null,"Q9RFV9","IPMed?",0.39464,0.56284,29.13,0.024,15,1,"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)","_",70,162,183,129,231,261]
[]
["AZ49_01110","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?",0.92733,0.96375,61.13,{"v":4e-138,"d":"4.00E-138"},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",23,337,344,12,328,331]
[null,"H6LC31","IPMed?",0.96512,1.04403,44.58,{"v":6e-90,"d":"6.00E-90"},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",17,344,344,1,317,318]
[null,"Q9EVN4","_",0.9661,0.99419,37.43,{"v":1E-70,"d":"1.00E-70"},3,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","_","Pseudomonas stutzeri","_",35,342,344,5,336,354]
[null,"A1WTR8","_",0.98319,1.02035,35.61,{"v":3e-67,"d":"3.00E-67"},4,1,"rnfD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport","_","Halorhodospira halophila (strain DSM 244 / SL1)","_",24,343,344,4,348,357]
[null,"A6VQ43","_",1.00282,1.03488,36.24,{"v":4e-64,"d":"4.00E-64"},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",20,337,344,2,348,355]
[null,"A8A0H3","_",0.99432,1.01744,34,{"v":8e-61,"d":"8.00E-61"},8,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",18676672,"Escherichia coli O9:H4 (strain HS)","HS",24,337,344,5,348,352]
[null,"B6IB68","_",0.99432,1.01744,34.29,{"v":8e-61,"d":"8.00E-61"},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",24,337,344,5,348,352]
[null,"B7M0I7","_",0.99432,1.01744,34.29,{"v":8e-61,"d":"8.00E-61"},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",24,337,344,5,348,352]
[null,"A7MML0","_",1.00286,1.02035,35.04,{"v":8e-61,"d":"8.00E-61"},6,1,"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",20221447,"Cronobacter sakazakii (strain ATCC BAA-894)","ATCC BAA-894",24,337,344,5,348,350]
[null,"B7L5I3","_",0.99432,1.01744,34.29,{"v":8e-61,"d":"8.00E-61"},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",24,337,344,5,348,352]
[null,"P76182","IPMed?",0.99432,1.01744,34,{"v":8e-61,"d":"8.00E-61"},8,1,"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",24,337,344,5,348,352]
[null,"B1XFU2","_",0.99432,1.01744,34,{"v":8e-61,"d":"8.00E-61"},8,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",18245285,"Escherichia coli (strain K12 / DH10B)","K12 / DH10B",24,337,344,5,348,352]
[null,"C4ZY93","_",0.99432,1.01744,34,{"v":8e-61,"d":"8.00E-61"},8,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport",19376874,"Escherichia coli (strain K12 / MC4100 / BW2952)","K12 / MC4100 / BW2952",24,337,344,5,348,352]
[null,"Q32FE3","_",0.99432,1.01744,34,{"v":2e-60,"d":"2.00E-60"},9,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Reference proteome, Translocase, Transmembrane, Transmembrane helix, Transport",16275786,"Shigella dysenteriae serotype 1 (strain Sd197)","Sd197",24,337,344,5,348,352]
[null,"P58325","_",0.99432,1.01744,34,{"v":2e-60,"d":"2.00E-60"},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",24,337,344,5,348,352]
[null,"B5Z464","_",0.99432,1.01744,34,{"v":2e-60,"d":"2.00E-60"},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",24,337,344,5,348,352]
[null,"B1IQC4","_",0.99432,1.01744,34.29,{"v":3e-60,"d":"3.00E-60"},10,1,"rsxD","Ion-translocating oxidoreductase complex subunit D","7.-.-.-","Cell inner membrane, Cell membrane, Electron transport, Flavoprotein, FMN, Membrane, Phosphoprotein, Translocase, Transmembrane, Transmembrane helix, Transport","_","Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)","_",24,337,344,5,348,352]
[null,"A5F2R1","IPMed?",1.01437,1.02616,33.71,{"v":9e-53,"d":"9.00E-53"},11,1,"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",24,337,344,5,347,348]
[null,"Q8TSY3","IPMed?",0.92442,1.10417,32.08,{"v":4E-51,"d":"4.00E-51"},12,1,"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",23,339,344,5,285,288]
[null,"Q52715","IPMed?",0.86313,0.89826,36.89,{"v":9e-51,"d":"9.00E-51"},13,1,"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",26,303,344,6,306,358]
[null,"Q9KPS2","IPMed?",0.88916,1.07267,31.17,{"v":1e-37,"d":"1.00E-37"},14,1,"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",22,331,344,39,400,415]
[null,"A5F5X0","IPMed?",0.88916,1.07267,31.17,{"v":1e-37,"d":"1.00E-37"},14,1,"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",22,331,344,39,400,415]
[null,"Q9RFW0","IPMed?",0.64649,0.77616,34.46,{"v":4e-36,"d":"4.00E-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",10587447,"Vibrio campbellii (strain ATCC BAA-1116 / BB120)","_",80,331,344,142,399,413]
[null,"Q56587","IPMed?",0.64493,0.77616,34.46,{"v":1E-35,"d":"1.00E-35"},16,1,"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",80,331,344,143,400,414]
[null,"O05011","IPMed?",0.70073,0.83721,33.33,{"v":2e-32,"d":"2.00E-32"},17,1,"nqrB","Na(+)-translocating NADH-quinone reductase subunit B","7.2.1.1","Cell inner membrane, Cell membrane, Complete proteome, Flavoprotein, FMN, Ion transport, Membrane, NAD, Phosphoprotein, Reference proteome, Sodium, Sodium transport, Translocase, Transmembrane, Transmembrane helix, Transport, Ubiquinone","7542800, 8601449","Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd / ATCC 51907 / DSM 11121 / KW20 / Rd",62,331,344,120,397,411]
[]
["AZ49_01115","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?",0.99125,1.00443,59.16,0,1,1,"rnfC","Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit C","7.1.1.-","4Fe-4S, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, NAD, Repeat, Translocase, Transport","20616070, 23269825","Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC)","ATCC 55383 / DSM 13528 / PETC / ATCC 55383 / DSM 13528 / PETC",1,450,451,1,449,457]
[null,"H6LC32","IPMed?",0.97783,0.99549,47.39,{"v":7e-138,"d":"7.00E-138"},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?",0.86127,0.99113,40.94,{"v":2e-108,"d":"2.00E-108"},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",7,448,451,19,462,519]
[null,"D5ARZ1","IPMed?",0.86127,0.99113,40.94,{"v":2e-108,"d":"2.00E-108"},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",7,448,451,19,462,519]
[null,"Q9KT88","_",0.57881,0.99335,39.51,{"v":1E-97,"d":"1.00E-97"},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",8,450,451,18,460,774]
[null,"A0A0H3AJC2","IPMed?",0.57956,0.99335,39.51,{"v":1E-97,"d":"1.00E-97"},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",8,450,451,18,460,773]
[null,"A8GE00","_",0.63158,0.98448,39.41,{"v":5e-96,"d":"5.00E-96"},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","_","Serratia proteamaculans (strain 568)","_",8,447,451,18,457,703]
[null,"Q1C7K3","_",0.73065,1.00443,39.07,{"v":1e-95,"d":"1.00E-95"},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",16740952,"Yersinia pestis bv. Antiqua (strain Antiqua)","Antiqua",8,450,451,18,466,620]
[null,"Q1CIY9","_",0.68741,1.00443,39.07,{"v":3e-95,"d":"3.00E-95"},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",16740952,"Yersinia pestis bv. Antiqua (strain Nepal516)","Nepal516",8,450,451,18,466,659]
[null,"A9R8U6","_",0.68741,1.00443,39.07,{"v":3e-95,"d":"3.00E-95"},7,1,"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","_",0.68741,1.00443,39.07,{"v":3e-95,"d":"3.00E-95"},7,1,"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","_",0.649,1.00443,39.07,{"v":7e-95,"d":"7.00E-95"},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",17784789,"Yersinia pseudotuberculosis serotype O:1b (strain IP 31758)","IP 31758",8,450,451,18,466,698]
[null,"B1JKN4","_",0.649,1.00443,39.07,{"v":3e-94,"d":"3.00E-94"},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","_","Yersinia pseudotuberculosis serotype O:3 (strain YPIII)","_",8,450,451,18,466,698]
[null,"A1JM81","_",0.6528,1.00887,39.12,{"v":7E-94,"d":"7.00E-94"},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",17173484,"Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)","NCTC 13174 / 8081",8,450,451,18,466,697]
[null,"P77611","IPMed?",0.61216,1.00443,37.97,{"v":1E-89,"d":"1.00E-89"},11,1,"rsxC","Ion-translocating oxidoreductase complex subunit C","7.-.-.-","4Fe-4S, Cell inner membrane, Cell membrane, Complete proteome, Electron transport, Iron, Iron-sulfur, Membrane, Metal-binding, Reference proteome, Repeat, Translocase, Transport","9097039, 9278503, 16738553, 12773378","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",8,450,451,18,466,740]
[null,"Q8TSY4","IPMed?",0.95787,0.96644,29.17,{"v":5e-60,"d":"5.00E-60"},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,"P25708","IPMed?",0.46336,0.47672,28.84,5e-06,13,1,"NDUFV1","NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial","1.6.99.3, 7.1.1.2","3D-structure, 4Fe-4S, Acetylation, Complete proteome, Direct protein sequencing, Electron transport, Flavoprotein, FMN, Iron, Iron-sulfur, Membrane, Metal-binding, Methylation, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","2034666, 1900194, 10852722, 18721790","Bos taurus","_",103,279,451,47,256,464]
[null,"Q91YT0","IPMed?",0.46336,0.47672,28.84,2e-05,14,1,"Ndufv1","NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial","1.6.99.3, 7.1.1.2","3D-structure, 4Fe-4S, Acetylation, Complete proteome, Direct protein sequencing, Electron transport, Flavoprotein, FMN, Iron, Iron-sulfur, Membrane, Metal-binding, Methylation, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","16141072, 15489334, 10870971, 21183079, 23806337, 23576753, 24129315","Mus musculus","C57BL/6J / FVB/N / C57BL/6J",103,279,451,47,256,464]
[null,"P49821","IPMed?",0.46336,0.47672,28.84,3e-05,15,1,"NDUFV1","NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial","1.6.99.3, 7.1.1.2","3D-structure, 4Fe-4S, Acetylation, Alternative splicing, Complete proteome, Disease mutation, Electron transport, Flavoprotein, FMN, Iron, Iron-sulfur, Leigh syndrome, Membrane, Metal-binding, Methylation, Mitochondrion, Mitochondrion inner membrane, NAD, Oxidoreductase, Polymorphism, Primary mitochondrial disease, Reference proteome, Respiratory chain, Transit peptide, Translocase, Transport, Ubiquinone","9892733, 9571201, 10931946, 15489334, 1478657, 8288251, 12611891, 21269460, 24275569, 25944712, 10080174, 11349233","Homo sapiens","_",103,279,451,47,256,464]
[null,"Q46507","IPMed?",0.64082,0.69623,24.2,6e-05,16,1,"hndC","NADP-reducing hydrogenase subunit HndC","1.12.1.3","4Fe-4S, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat","7751270, 9703971","Desulfovibrio fructosivorans","_",124,380,451,48,357,490]

{"sheet":"UniFIRE ","index":7,"n_rows":321,"n_cols":8,"rows_kept":321}
["AZ49_11470","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"]
[]
["AZ49_01710","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"]
[]
["AZ49_05490","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"]
[]
["AZ49_06970","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000001527","catalytic activity","Pyruvate + CoA + oxidized flavodoxin = acetyl-CoA + CO(2) + reduced flavodoxin","_","_","PIRNR000159","PIR"]
[null,"UR000001527","function","Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Electron transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Transport","_","_","PIRNR000159","PIR"]
[null,"UR000001527","keyword","Oxidoreductase","_","_","PIRNR000159","PIR"]
[null,"UR000001527","product - EC number","1.2.7.-","_","_","PIRNR000159","PIR"]
[null,"UR000001527","product name","Pyruvate-flavodoxin oxidoreductase","_","_","PIRNR000159","PIR"]
[null,"UR000001527","similarity","Belongs to the nifJ family","_","_","PIRNR000159","PIR"]
[]
["AZ49_06950","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"SAAS00672006","cofactor","Name=Mg(2+); Xref=ChEBI:CHEBI:18420"]
[null,"SAAS00483886","keyword","ATP-binding"]
[null,"SAAS00483909","keyword","Kinase"]
[null,"SAAS00011608, SAAS00091199","keyword","Magnesium"]
[null,"SAAS00011656, SAAS00091203","keyword","Metal-binding"]
[null,"SAAS00483892","keyword","Nucleotide-binding"]
[null,"SAAS00483925","keyword","Transferase"]
[null,"SAAS00688878","similarity","Belongs to the acetokinase family"]
[null,"SAAS00011637, SAAS00011667, SAAS00130554, SAAS00130644","subcellular location,keyword","Cytoplasm"]
[null,"UR000037499","catalytic activity","ATP + acetate = ADP + acetyl phosphate","_","_","MF_00020","HAMAP"]
[null,"UR000037499","cofactor","Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Mg(2+). Can also accept Mn(2+)","_","_","MF_00020","HAMAP"]
[null,"UR000037499","function","Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction","_","_","MF_00020","HAMAP"]
[null,"UR000037499","gene name","ackA","_","_","MF_00020","HAMAP"]
[null,"UR000037499","GO","GO:0016310","_","_","MF_00020","HAMAP"]
[null,"UR000037499","GO","GO:0005737","_","_","MF_00020","HAMAP"]
[null,"UR000037499","GO","GO:0000287","_","_","MF_00020","HAMAP"]
[null,"UR000037499","GO","GO:0008776","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Nucleotide-binding","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Cytoplasm","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","ATP-binding","_","_","MF_00020","HAMAP"]
[null,"UR000000717","keyword","Kinase","_","_","RU003835","RuleBase"]
[null,"UR000037499","keyword","Metal-binding","_","_","MF_00020","HAMAP"]
[null,"UR000000717","keyword","Transferase","_","_","RU003835","RuleBase"]
[null,"UR000037499","keyword","Transferase","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Kinase","_","_","MF_00020","HAMAP"]
[null,"UR000037499","keyword","Magnesium","_","_","MF_00020","HAMAP"]
[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"]
[]
["AZ49_05685","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000000536","keyword","Transferase","_","_","RU003557","RuleBase"]
[null,"UR000000536","keyword","Acyltransferase","_","_","RU003557","RuleBase"]
[null,"UR000000536","similarity","Belongs to the thiolase family","_","_","RU003557","RuleBase"]
[]
["AZ49_05690","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000000536","keyword","Transferase","_","_","RU003557","RuleBase"]
[null,"UR000000536","keyword","Acyltransferase","_","_","RU003557","RuleBase"]
[null,"UR000000536","similarity","Belongs to the thiolase family","_","_","RU003557","RuleBase"]
[]
["AZ49_10655","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"SAAS00649305","keyword","Oxidoreductase"]
[]
["AZ49_00555","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000000628","similarity","Belongs to the enoyl-CoA hydratase/isomerase family","_","_","RU003707","RuleBase"]
[]
["AZ49_02175","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000038423","keyword","Transferase","_","_","PIRNR000858","PIR"]
[null,"UR000038423","similarity","Belongs to the 3-oxoacid CoA-transferase family","_","_","PIRNR000858","PIR"]
[]
["AZ49_00650","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000170765","cofactor","Name=FAD; Xref=ChEBI:CHEBI:57692","_","_","RU362125","RuleBase"]
[null,"UR000170765","GO","GO:0050660","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Flavoprotein","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Oxidoreductase","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","FAD","_","_","RU362125","RuleBase"]
[null,"UR000170765","similarity","Belongs to the acyl-CoA dehydrogenase family","_","_","RU362125","RuleBase"]
[]
["AZ49_02755","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000170765","cofactor","Name=FAD; Xref=ChEBI:CHEBI:57692","_","_","RU362125","RuleBase"]
[null,"UR000170765","GO","GO:0050660","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Flavoprotein","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Oxidoreductase","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","FAD","_","_","RU362125","RuleBase"]
[null,"UR000170765","similarity","Belongs to the acyl-CoA dehydrogenase family","_","_","RU362125","RuleBase"]
[]
["AZ49_04240","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000170765","cofactor","Name=FAD; Xref=ChEBI:CHEBI:57692","_","_","RU362125","RuleBase"]
[null,"UR000170765","GO","GO:0050660","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Oxidoreductase","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","FAD","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Flavoprotein","_","_","RU362125","RuleBase"]
[null,"UR000170765","similarity","Belongs to the acyl-CoA dehydrogenase family","_","_","RU362125","RuleBase"]
[]
["AZ49_06245","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"]
[]
["AZ49_06555","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000170765","cofactor","Name=FAD; Xref=ChEBI:CHEBI:57692","_","_","RU362125","RuleBase"]
[null,"UR000170765","GO","GO:0050660","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","FAD","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Flavoprotein","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Oxidoreductase","_","_","RU362125","RuleBase"]
[null,"UR000170765","similarity","Belongs to the acyl-CoA dehydrogenase family","_","_","RU362125","RuleBase"]
[]
["AZ49_01090","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[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"]
[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:0022900","_","_","MF_00463","HAMAP"]
[null,"UR000090116","GO","GO:0051539","_","_","MF_00463","HAMAP"]
[null,"UR000090116","GO","GO:0005886","_","_","MF_00463","HAMAP"]
[null,"UR000090116","GO","GO:0055114","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Electron transport","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Cell membrane","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Repeat","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Iron-sulfur","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Membrane","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Oxidoreductase","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","4Fe-4S","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Transport","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Iron","_","_","MF_00463","HAMAP"]
[null,"UR000090116","keyword","Metal-binding","_","_","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"]
[]
["AZ49_01095","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:0055114","_","_","MF_00459","HAMAP"]
[null,"UR000062678","GO","GO:0005886","_","_","MF_00459","HAMAP"]
[null,"UR000062678","GO","GO:0022900","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Transport","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Transmembrane","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Cell membrane","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Oxidoreductase","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Transmembrane helix","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Membrane","_","_","MF_00459","HAMAP"]
[null,"UR000062678","keyword","Electron transport","_","_","MF_00459","HAMAP"]
[null,"UR000062678","product  name (synonym)","Rnf electron transport complex subunit A","_","_","MF_00459","HAMAP"]
[null,"UR000062678","product - EC number","1.18.1.-","_","_","MF_00459","HAMAP"]
[null,"UR000062678","product name","Ion-translocating oxidoreductase complex subunit A","_","_","MF_00459","HAMAP"]
[null,"UR000062678","similarity","Belongs to the NqrDE/RnfAE family","_","_","MF_00459","HAMAP"]
[null,"UR000062678","subunit","The complex is composed of six subunits: RnfA, RnfB, RnfC, RnfD, RnfE and RnfG","_","_","MF_00459","HAMAP"]
[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"]
[]
["AZ49_01100","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[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"]
[]
["AZ49_01105","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:0022900","_","_","MF_00479","HAMAP"]
[null,"UR000064652","GO","GO:0055114","_","_","MF_00479","HAMAP"]
[null,"UR000064652","GO","GO:0005886","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Transmembrane helix","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Oxidoreductase","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Electron transport","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Phosphoprotein","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Membrane","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Cell membrane","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","FMN","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Transmembrane","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Transport","_","_","MF_00479","HAMAP"]
[null,"UR000064652","keyword","Flavoprotein","_","_","MF_00479","HAMAP"]
[null,"UR000064652","modified residue","FMN phosphoryl threonine",160,160,"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"]
[]
["AZ49_01110","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:0022900","_","_","MF_00462","HAMAP"]
[null,"UR000062690","GO","GO:0055114","_","_","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","Electron transport","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Flavoprotein","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Transmembrane helix","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","FMN","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Transport","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Phosphoprotein","_","_","MF_00462","HAMAP"]
[null,"UR000062690","keyword","Membrane","_","_","MF_00462","HAMAP"]
[null,"UR000062690","modified residue","FMN phosphoryl threonine",174,174,"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"]
[]
["AZ49_01115","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000090104","cofactor","Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 2 [4Fe-4S] clusters per subunit","_","_","MF_00461","HAMAP"]
[null,"UR000090104","function","Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane","_","_","MF_00461","HAMAP"]
[null,"UR000090104","gene name","rnfC","_","_","MF_00461","HAMAP"]
[null,"UR000090104","GO","GO:0022900","_","_","MF_00461","HAMAP"]
[null,"UR000090104","GO","GO:0005886","_","_","MF_00461","HAMAP"]
[null,"UR000090104","GO","GO:0055114","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Oxidoreductase","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Iron","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","4Fe-4S","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Iron-sulfur","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Transport","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Membrane","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Repeat","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Cell membrane","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Electron transport","_","_","MF_00461","HAMAP"]
[null,"UR000090104","keyword","Metal-binding","_","_","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"]

{"sheet":"PRIAM EC number","index":8,"n_rows":170,"n_cols":15,"rows_kept":170}
["AZ49_11470","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":2e-71,"d":"2.00E-71"},35,1,307,307,"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":7e-27,"d":"7.00E-27"},28,102,310,209,"Malate dehydrogenase","Malic dehydrogenase","(S)-malate + NAD(+) = oxaloacetate + NADH","_","-!- Also oxidizes some other 2-hydroxydicarboxylic acids"]
[null,"1.1.1.82","no",1,322,7e-11,19,8,297,290,"Malate dehydrogenase (NADP(+))","NADP-linked malate dehydrogenase","(S)-malate + NADP(+) = oxaloacetate + NADPH","_","-!- Activated by light"]
[]
["AZ49_01710","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",1,1928,0,44,9,1165,1157,"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",1,1803,0,46,4,1170,1167,"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":5e-38,"d":"5.00E-38"},28,5,389,385,"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":2e-27,"d":"2.00E-27"},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,"1.2.7.1","no",1,184,7e-13,23,421,612,192,"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"]
[null,"1.2.7.3","no",3,344,9E-13,24,9,311,303,"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"]
[]
["AZ49_05490","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",1,1928,0,44,9,1173,1165,"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",1,1803,0,46,4,1173,1170,"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":8E-55,"d":"8.00E-55"},29,5,379,375,"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-32,"d":"3.00E-32"},23,7,330,324,"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-16,"d":"3.00E-16"},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",2,265,5e-11,25,967,1135,169,"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"]
[]
["AZ49_06970","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":3e-45,"d":"3.00E-45"},30,5,392,388,"Pyruvate synthase","2-oxobutyrate synthase. 2-oxobutyrate-ferredoxin oxidoreductase. Alpha-ketobutyrate synthase. Alpha-ketobutyrate-ferredoxin oxidoreductase. Pyruvate oxidoreductase. Pyruvate synthetase. Pyruvic-ferredoxin oxidoreductase","Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Thiamine diphosphate","-!- The enzyme also decarboxylates 2-oxobutanoate with lower efficiency, but shows no activity with 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to fo"]
[null,"1.2.7.7","no",4,328,{"v":7e-26,"d":"7.00E-26"},23,5,328,324,"3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)","2-ketoisovalerate ferredoxin reductase. 2-oxoisovalerate ferredoxin reductase. 3-methyl-2-oxobutanoate synthase (ferredoxin). Branched-chain ketoacid ferredoxin reductase. Branched-chain oxo acid ferredoxin reductase. Keto-valine-ferredoxin oxidoreductase. Ketoisovalerate ferredoxin reductase. Ketoisovalerate oxidoreductase. VOR","3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO(2) + 2 reduced ferredoxin + H(+)","Iron-sulfur; Tungstopterin","-!- The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. -!- Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo- pentanoate, and 2-oxobutanoate. -!"]
[null,"1.6.99.5","no",2,145,2e-11,26,681,775,95,"Transferred entry: 1.6.5.11","_","_","_","_"]
[null,"1.2.7.3","no",3,344,3E-11,24,3,327,325,"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"]
[]
["AZ49_06950","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",1,410,0,61,3,395,393,"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-112,"d":"1.00E-112"},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":7e-18,"d":"7.00E-18"},30,174,331,158,"Butyrate kinase","_","ATP + butanoate = ADP + butanoyl phosphate","_","-!- The enzyme from Clostridium sp. also acts, more slowly on pentanoate and propanoate, and on some branched-chain fatty acids (cf. EC 2.7.1.14)"]
[]
["AZ49AM_0981","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":3e-59,"d":"3.00E-59"},41,1,251,251,"Phosphate acetyltransferase","Phosphoacylase. Phosphotransacetylase","Acetyl-CoA + phosphate = CoA + acetyl phosphate","_","-!- Also acts with other short-chain acyl-CoAs"]
[]
["AZ49_00050","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.1.1","high",9,419,{"v":2E-52,"d":"2.00E-52"},33,3,285,283,"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-41,"d":"1.00E-41"},30,1,285,285,"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":2e-38,"d":"2.00E-38"},31,1,353,353,"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":1e-37,"d":"1.00E-37"},30,11,304,294,"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-36,"d":"1.00E-36"},31,1,281,281,"Methanol dehydrogenase","_","Methanol + NAD(+) = formaldehyde + NADH","_","_"]
[null,"1.1.99.24","no",1,479,{"v":7e-34,"d":"7.00E-34"},26,12,360,349,"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-29,"d":"3.00E-29"},27,5,321,317,"Maleylacetate reductase","Maleolylacetate reductase","3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H","_","_"]
[null,"1.1.1.61","no",1,371,{"v":4e-27,"d":"4.00E-27"},31,47,289,243,"4-hydroxybutyrate dehydrogenase","_","4-hydroxybutanoate + NAD(+) = succinate semialdehyde + NADH","_","_"]
[]
["AZ49_02525","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-60,"d":"9.00E-60"},32,6,389,384,"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":2E-45,"d":"2.00E-45"},33,1,360,360,"1,3-propanediol dehydrogenase","1,3-propanediol oxidoreductase. 3-hydroxypropionaldehyde reductase","Propane-1,3-diol + NAD(+) = 3-hydroxypropanal + NADH","_","_"]
[null,"1.1.1.244","no",1,381,{"v":1E-42,"d":"1.00E-42"},31,6,360,355,"Methanol dehydrogenase","_","Methanol + NAD(+) = formaldehyde + NADH","_","_"]
[null,"1.2.1.10","no",2,875,{"v":3e-41,"d":"3.00E-41"},28,7,378,372,"Acetaldehyde dehydrogenase (acetylating)","Acylating acetaldehyde dehydrogenase. Aldehyde dehydrogenase (acylating)","Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH","_","-!- Also acts, more slowly, on glycolaldehyde, propanal and butanal. -!- In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39. -!- The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perfor"]
[null,"1.1.99.24","no",1,479,{"v":6E-34,"d":"6.00E-34"},24,24,387,364,"Hydroxyacid-oxoacid transhydrogenase","_","(1) (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2- hydroxyglutarate. (2) 4-hydroxybutanoate + 2-oxoglutarate = succinic semialdehyde + (R)-2- hydroxyglutarate","_","_"]
[null,"1.1.1.77","no",1,383,{"v":2e-28,"d":"2.00E-28"},30,4,283,280,"Lactaldehyde reductase","Propanediol oxidoreductase","(1) (R)-propane-1,2-diol + NAD(+) = (R)-lactaldehyde + NADH. (2) (S)-propane-1,2-diol + NAD(+) = (S)-lactaldehyde + NADH","_","_"]
[null,"1.3.1.32","no",1,356,{"v":4e-20,"d":"4.00E-20"},25,6,389,384,"Maleylacetate reductase","Maleolylacetate reductase","3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H","_","_"]
[null,"1.1.1.61","no",1,371,{"v":2e-17,"d":"2.00E-17"},24,85,388,304,"4-hydroxybutyrate dehydrogenase","_","4-hydroxybutanoate + NAD(+) = succinate semialdehyde + NADH","_","_"]
[]
["AZ49_03535","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.17.1.4","high",2,775,{"v":1e-106,"d":"1.00E-106"},26,164,888,725,"Xanthine dehydrogenase","NAD-xanthine dehydrogenase. Xanthine oxidoreductase. Xanthine-NAD oxidoreductase. Xanthine/NAD(+) oxidoreductase","Xanthine + NAD(+) + H(2)O = urate + NADH","FAD; Iron-sulfur; Mo cation","-!- Acts on a variety of purines and aldehydes, including hypoxanthine. -!- The mammalian enzyme can also convert all-trans retinol to all-trans- retinoate, while the substrate is bound to a retinoid-binding protein. -!- The enzyme from eukaryotes contain"]
[null,"1.17.1.4","high",3,178,{"v":2e-28,"d":"2.00E-28"},36,13,143,131,"Xanthine dehydrogenase","NAD-xanthine dehydrogenase. Xanthine oxidoreductase. Xanthine-NAD oxidoreductase. Xanthine/NAD(+) oxidoreductase","Xanthine + NAD(+) + H(2)O = urate + NADH","FAD; Iron-sulfur; Mo cation","-!- Acts on a variety of purines and aldehydes, including hypoxanthine. -!- The mammalian enzyme can also convert all-trans retinol to all-trans- retinoate, while the substrate is bound to a retinoid-binding protein. -!- The enzyme from eukaryotes contain"]
[null,"1.2.99.7","no",1,907,{"v":1E-89,"d":"1.00E-89"},29,17,885,869,"Aldehyde dehydrogenase (FAD-independent)","Aldehyde oxidase. Aldehyde oxidoreductase. AORDd","An aldehyde + H(2)O + acceptor = a carboxylate + reduced acceptor","Iron-sulfur; Molybdopterin cytosine dinucleotide","_"]
[null,"1.3.99.20","no",3,769,{"v":1e-49,"d":"1.00E-49"},27,178,886,709,"Transferred entry: 1.3.7.9","_","_","_","_"]
[null,"1.2.99.2","no",17,783,{"v":6E-49,"d":"6.00E-49"},25,181,860,680,"Transferred entry: 1.2.7.4","_","_","_","_"]
[null,"1.17.3.2","no",1,1358,{"v":5e-47,"d":"5.00E-47"},24,166,844,679,"Xanthine oxidase","Hypoxanthine oxidase. Hypoxanthine-xanthine oxidase. Schardinger enzyme. Xanthine oxidoreductase","Xanthine + H(2)O + O(2) = urate + H(2)O(2)","FAD; Iron-sulfur; Mo-molybdopterin","-!- Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1. -!- Under some conditions the product is mainly superoxide rather than peroxide: R-H + H(2)O + 2 O(2) = ROH + 2 O(2)(.-) + 2 H(+). -!- The mamm"]
[null,"1.2.3.14","no",1,1332,{"v":4e-27,"d":"4.00E-27"},22,151,842,692,"Abscisic-aldehyde oxidase","AO-delta","Abscisic aldehyde + H(2)O + O(2) = abscisate + H(2)O(2)","_","-!- Acts on both (+)- and (-)-abscisic aldehyde. -!- Involved in the abscisic-acid biosynthesis pathway in plants, along with EC 1.1.1.288, EC 1.13.11.51 and EC 1.14.13.93. -!- While abscisic aldehyde is the best substrate, the enzyme also acts with indol"]
[null,"1.3.99.20","no",1,161,{"v":5e-26,"d":"5.00E-26"},40,1,148,148,"Transferred entry: 1.3.7.9","_","_","_","_"]
[null,"1.2.99.2","no",14,156,{"v":4e-23,"d":"4.00E-23"},35,22,148,127,"Transferred entry: 1.2.7.4","_","_","_","_"]
[null,"1.2.3.1","no",1,875,{"v":1e-21,"d":"1.00E-21"},30,150,406,257,"Aldehyde oxidase","Quinoline oxidase. Retinal oxidase","An aldehyde + H(2)O + O(2) = a carboxylate + H(2)O(2)","FAD; Iron-sulfur; Mo cation","-!- The enzyme from liver exhibits a broad substrate specificity, and is involved in the metabolism of xenobiotics, including the oxidation of N-heterocycles and aldehydes and the reduction of N-oxides, nitrosamines, hydroxamic acids, azo dyes, nitropolyc"]
[null,"1.3.99.16","no",1,152,{"v":2e-20,"d":"2.00E-20"},37,12,148,137,"Isoquinoline 1-oxidoreductase","_","Isoquinoline + acceptor + H(2)O = isoquinolin-1(2H)-one + reduced acceptor","_","-!- The enzyme from Pseudomonas diminuta is specific toward N-containing N-heterocyclic substrates, including isoquinoline, isoquinolin-5-ol, phthalazine and quinazoline. -!- Electron acceptors include 1,2-benzoquinone, cytochrome c, ferricyanide, iodonit"]
[]
["AZ49_05685","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-165,"d":"1.00E-165"},67,5,390,386,"Acetyl-CoA C-acetyltransferase","Acetoacetyl-CoA thiolase","2 acetyl-CoA = CoA + acetoacetyl-CoA","_","-!- The enzyme, found in both eukaryotes and prokaryotes, catalyzes the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. -!- The reaction starts w"]
[null,"2.3.1.16","no",1,420,{"v":1e-113,"d":"1.00E-113"},45,1,392,392,"Acetyl-CoA C-acyltransferase","3-ketoacyl-CoA thiolase. Beta-ketothiolase","Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA","_","-!- The enzyme, found in both eukaryotes and in prokaryotes, is involved in degradation pathways such as fatty acid beta-oxidation. -!- The enzyme acts on 3-oxoacyl-CoAs to produce acetyl-CoA and an acyl- CoA shortened by two carbon atoms. -!- The reactio"]
[null,"2.3.1.174","no",1,401,{"v":4e-93,"d":"4.00E-93"},45,1,392,392,"3-oxoadipyl-CoA thiolase","Beta-ketoadipyl-CoA thiolase","Succinyl-CoA + acetyl-CoA = CoA + 3-oxoadipyl-CoA","_","-!- The enzyme from the bacterium Escherichia coli also has the activity of EC 2.3.1.223"]
[]
["AZ49_05690","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-156,"d":"1.00E-156"},61,5,393,389,"Acetyl-CoA C-acetyltransferase","Acetoacetyl-CoA thiolase","2 acetyl-CoA = CoA + acetoacetyl-CoA","_","-!- The enzyme, found in both eukaryotes and prokaryotes, catalyzes the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. -!- The reaction starts w"]
[null,"2.3.1.16","no",1,420,{"v":1e-115,"d":"1.00E-115"},45,1,394,394,"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-102,"d":"1.00E-102"},48,1,394,394,"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"]
[null,"2.3.1.176","no",1,547,3e-14,24,28,354,327,"Propanoyl-CoA C-acyltransferase","3-oxopristanoyl-CoA hydrolase. 3-oxopristanoyl-CoA thiolase. Peroxisomal thiolase 2. Propionyl-CoA C(2)-trimethyltridecanoyltransferase. PTE-2. SCP(chi). SCP-X. Sterol carrier protein-chi. Sterol carrier protein-X","3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3-alpha,7-alpha,12-alpha-trihydroxy-24-oxo-5-beta-cholestanoyl- CoA","_","-!- Also acts on dihydroxy-5-beta-cholestanoyl-CoA and other branched chain acyl-CoA derivatives. -!- Catalyzes the penultimate step in the formation of bile acids. -!- The bile acid moiety is transferred from the acyl-CoA thioester (RCO- SCoA) to either "]
[]
["AZ49_10655","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-109,"d":"1.00E-109"},58,3,282,280,"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":2e-82,"d":"2.00E-82"},42,2,284,283,"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":1e-71,"d":"1.00E-71"},39,3,282,280,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"1.1.1.211","no",1,763,{"v":3e-50,"d":"3.00E-50"},38,1,282,282,"Long-chain-3-hydroxyacyl-CoA dehydrogenase","Beta-hydroxyacyl-CoA dehydrogenase","A long-chain (S)-3-hydroxyacyl-CoA + NAD(+) = a long-chain 3-oxoacyl-CoA + NADH","_","-!- This enzyme was purified from the mitochondrial inner membrane. -!- The enzyme has a preference for long-chain substrates, and activity with C(16) substrates was 6- to 15-fold higher than with C(4) substrates (cf. EC 1.1.1.35)"]
[]
["AZ49_00555","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"4.2.1.17","high",1,264,{"v":2e-44,"d":"2.00E-44"},30,11,263,253,"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,"5.3.3.8","no",1,265,{"v":3e-30,"d":"3.00E-30"},28,10,205,196,"Delta(3)-Delta(2)-enoyl-CoA isomerase","3,2-trans-enoyl-CoA isomerase. Acetylene-allene isomerase. Delta(3),Delta(2)-enoyl-CoA isomerase. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase. Dodecenoyl-CoA Delta-isomerase. Dodecenoyl-CoA isomerase","(1) A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA. (2) A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA","_","-!- The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position. -!- Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C(3), which canno"]
[null,"4.2.1.55","no",1,261,{"v":1E-25,"d":"1.00E-25"},30,1,258,258,"3-hydroxybutyryl-CoA dehydratase","Crotonase","(3R)-3-hydroxybutanoyl-CoA = crotonoyl-CoA + H(2)O","_","-!- Also acts on crotonoyl thioesters of pantetheine and acyl-carrier protein"]
[null,"5.1.2.3","no",1,707,{"v":2e-25,"d":"2.00E-25"},29,11,205,195,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"4.1.3.36","no",1,263,{"v":3e-20,"d":"3.00E-20"},29,12,261,250,"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,"4.1.1.41","no",1,261,{"v":6e-20,"d":"6.00E-20"},25,14,263,250,"Transferred entry: 7.2.4.3","_","_","_","_"]
[null,"3.1.2.4","no",1,408,{"v":6e-18,"d":"6.00E-18"},23,8,210,203,"3-hydroxyisobutyryl-CoA hydrolase","_","3-hydroxy-2-methylpropanoyl-CoA + H(2)O = CoA + 3-hydroxy-2- methylpropanoate","_","-!- Also hydrolyzes 3-hydroxypropanoyl-CoA"]
[null,"4.2.1.18","no",1,276,{"v":4e-17,"d":"4.00E-17"},24,13,264,252,"Methylglutaconyl-CoA hydratase","_","(S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA + H(2)O","_","_"]
[null,"1.1.1.211","no",1,763,2e-15,26,6,203,198,"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,"2.3.1.48","no",43,544,3e-12,26,26,204,179,"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"]
[]
["AZ49_00545","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.8.3.5","high",1,210,{"v":9e-63,"d":"9.00E-63"},50,7,211,205,"3-oxoacid CoA-transferase","Succinyl-CoA:3-ketoacid-CoA transferase","Succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA","_","-!- Acetoacetate or, more slowly, 3-oxopropanoate, 3-oxopentanoate, 3-oxo-4-methylpentanoate or 3-oxohexanoate can act as acceptor. -!- Malonyl-CoA can act instead of succinyl-CoA"]
[null,"2.8.3.9","no",2,221,{"v":4E-55,"d":"4.00E-55"},48,7,218,212,"Butyrate--acetoacetate CoA-transferase","_","Butanoyl-CoA + acetoacetate = butanoate + acetoacetyl-CoA","_","-!- Butanoate, acetoacetate and their CoA thioesters are the preferred substrates, but the enzyme also acts, more slowly, on the derivatives of a number of C(2) to C(6) monocarboxylic acids"]
[null,"2.8.3.8","no",1,210,{"v":4e-53,"d":"4.00E-53"},37,7,211,205,"Acetate CoA-transferase","_","Acyl-CoA + acetate = a fatty acid anion + acetyl-CoA","_","-!- The enzyme belongs to family I of CoA-transferases, which operate with a ping-pong kinetic mechanism. -!- The reaction takes place in two half-reactions and involves the formation of a CoA thioester intermediate with a glutamate residue. -!- Unlike EC"]
[null,"2.8.3.6","no",1,220,{"v":2e-44,"d":"2.00E-44"},38,7,210,204,"3-oxoadipate CoA-transferase","Beta-ketoadipate:succinyl-CoA transferase","Succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA","_","-!- The enzyme, often found in soil bacteria and fungi, is involved in the catabolism of a variety of aromatic compounds, including catechol and protocatechuate, which are degraded via 3-oxoadipate"]
[]
["AZ49_00550","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.8.3.5","high",2,252,{"v":2e-43,"d":"2.00E-43"},35,2,221,220,"3-oxoacid CoA-transferase","Succinyl-CoA:3-ketoacid-CoA transferase","Succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA","_","-!- Acetoacetate or, more slowly, 3-oxopropanoate, 3-oxopentanoate, 3-oxo-4-methylpentanoate or 3-oxohexanoate can act as acceptor. -!- Malonyl-CoA can act instead of succinyl-CoA"]
[null,"2.8.3.9","no",1,218,{"v":8e-43,"d":"8.00E-43"},39,3,213,211,"Butyrate--acetoacetate CoA-transferase","_","Butanoyl-CoA + acetoacetate = butanoate + acetoacetyl-CoA","_","-!- Butanoate, acetoacetate and their CoA thioesters are the preferred substrates, but the enzyme also acts, more slowly, on the derivatives of a number of C(2) to C(6) monocarboxylic acids"]
[null,"2.8.3.8","no",1,210,{"v":2e-31,"d":"2.00E-31"},41,11,160,150,"Acetate CoA-transferase","_","Acyl-CoA + acetate = a fatty acid anion + acetyl-CoA","_","-!- The enzyme belongs to family I of CoA-transferases, which operate with a ping-pong kinetic mechanism. -!- The reaction takes place in two half-reactions and involves the formation of a CoA thioester intermediate with a glutamate residue. -!- Unlike EC"]
[]
["AZ49_02175","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"2.8.3.6","high",1,220,3e-12,22,277,481,205,"3-oxoadipate CoA-transferase","Beta-ketoadipate:succinyl-CoA transferase","Succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA","_","-!- The enzyme, often found in soil bacteria and fungi, is involved in the catabolism of a variety of aromatic compounds, including catechol and protocatechuate, which are degraded via 3-oxoadipate"]
[]
["AZ49_00650","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-104,"d":"1.00E-104"},43,1,381,381,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":1e-94,"d":"1.00E-94"},44,5,380,376,"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-73,"d":"3.00E-73"},34,4,379,376,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":2E-55,"d":"2.00E-55"},34,17,380,364,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":1E-35,"d":"1.00E-35"},29,1,380,380,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":4e-33,"d":"4.00E-33"},27,5,379,375,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":6e-16,"d":"6.00E-16"},22,68,382,315,"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)"]
[]
["AZ49_02755","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-138,"d":"1.00E-138"},55,1,382,382,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":3e-85,"d":"3.00E-85"},40,3,377,375,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":8e-76,"d":"8.00E-76"},34,7,376,370,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":1E-59,"d":"1.00E-59"},33,4,380,377,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":5e-54,"d":"5.00E-54"},34,17,381,365,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":4e-36,"d":"4.00E-36"},29,1,381,381,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":8e-23,"d":"8.00E-23"},20,21,382,362,"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)"]
[]
["AZ49_02760","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":5e-86,"d":"5.00E-86"},59,1,253,253,"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":2e-65,"d":"2.00E-65"},41,9,259,251,"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-53,"d":"2.00E-53"},40,13,260,248,"Methylglutaconyl-CoA hydratase","_","(S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA + H(2)O","_","_"]
[null,"5.1.2.3","no",1,707,{"v":2E-45,"d":"2.00E-45"},42,9,199,191,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"5.3.3.8","no",1,265,{"v":3e-45,"d":"3.00E-45"},42,11,188,178,"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":1E-42,"d":"1.00E-42"},35,3,257,255,"1,4-dihydroxy-2-naphthoyl-CoA synthase","DHNA synthetase. Dihydroxynaphthoic acid synthetase. Naphthoate synthase. o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing)","4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H(2)O","_","-!- This enzyme is involved in the synthesis of 1,4-dihydroxy-2- naphthoate, a branch point metabolite leading to the biosynthesis of menaquinone (vitamin K(2), in bacteria), phylloquinone (vitamin K(1) in plants), and many plant pigments. -!- The coenzym"]
[null,"1.1.1.211","no",1,763,{"v":7e-29,"d":"7.00E-29"},32,5,196,192,"Long-chain-3-hydroxyacyl-CoA dehydrogenase","Beta-hydroxyacyl-CoA dehydrogenase","A long-chain (S)-3-hydroxyacyl-CoA + NAD(+) = a long-chain 3-oxoacyl-CoA + NADH","_","-!- This enzyme was purified from the mitochondrial inner membrane. -!- The enzyme has a preference for long-chain substrates, and activity with C(16) substrates was 6- to 15-fold higher than with C(4) substrates (cf. EC 1.1.1.35)"]
[null,"3.1.2.4","no",1,408,{"v":4e-25,"d":"4.00E-25"},31,8,188,181,"3-hydroxyisobutyryl-CoA hydrolase","_","3-hydroxy-2-methylpropanoyl-CoA + H(2)O = CoA + 3-hydroxy-2- methylpropanoate","_","-!- Also hydrolyzes 3-hydroxypropanoyl-CoA"]
[null,"4.1.1.41","no",1,261,{"v":5e-25,"d":"5.00E-25"},29,1,259,259,"Transferred entry: 7.2.4.3","_","_","_","_"]
[null,"4.2.1.100","no",1,258,{"v":5e-19,"d":"5.00E-19"},28,17,260,244,"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",43,544,1E-13,24,3,257,255,"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"]
[]
["AZ49_04240","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-137,"d":"1.00E-137"},55,1,382,382,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":6e-84,"d":"6.00E-84"},39,3,377,375,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":1e-75,"d":"1.00E-75"},34,5,376,372,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":1E-59,"d":"1.00E-59"},33,1,380,380,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":2e-53,"d":"2.00E-53"},34,17,381,365,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":5e-34,"d":"5.00E-34"},28,1,381,381,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":3e-22,"d":"3.00E-22"},20,21,382,362,"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)"]
[]
["AZ49_06245","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":4e-96,"d":"4.00E-96"},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":5E-79,"d":"5.00E-79"},34,5,373,369,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":2e-54,"d":"2.00E-54"},33,5,379,375,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":1e-48,"d":"1.00E-48"},30,8,373,366,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":1e-34,"d":"1.00E-34"},29,1,378,378,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":7e-17,"d":"7.00E-17"},22,71,375,305,"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)"]
[]
["AZ49_06555","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",1,383,0,64,1,383,383,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":4e-82,"d":"4.00E-82"},41,3,376,374,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":5e-82,"d":"5.00E-82"},36,5,383,379,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":4e-61,"d":"4.00E-61"},33,16,381,366,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":2e-54,"d":"2.00E-54"},34,12,372,361,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":5e-33,"d":"5.00E-33"},29,1,382,382,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":1E-26,"d":"1.00E-26"},22,21,383,363,"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)"]

{"sheet":"COG","index":9,"n_rows":46,"n_cols":7,"rows_kept":46}
["CDS","COG id","Score","Begin","End","Classes","Function"]
["AZ49_00320","COG3875",317,8,324,"S","Uncharacterized conserved protein"]
["AZ49_00330","COG1620",517,5,521,"C","L-lactate permease"]
["AZ49_04210","COG1620",504,1,504,"C","L-lactate permease"]
["AZ49_00515","COG0039",271,28,298,"C","Malate/lactate dehydrogenases"]
["AZ49_11470","COG0039",318,1,318,"C","Malate/lactate dehydrogenases"]
["AZ49_01710","COG0674",410,1,410,"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"]
["AZ49_05490","COG0674",404,2,405,"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",381,796,1176,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
["AZ49_06970","COG0674",408,1,408,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
[null,"COG1014",381,414,794,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
[null,"COG1013",375,795,1169,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
["AZ49_06950","COG0282",398,1,398,"C","Acetate kinase"]
["AZ49AM_0981","COG0280",251,1,251,"C","Phosphotransacetylase"]
["AZ49_00050","COG1454",364,1,364,"C","Alcohol dehydrogenase, class IV"]
["AZ49_02525","COG1454",385,4,388,"C","Alcohol dehydrogenase, class IV"]
["AZ49_03535","COG1529",731,166,896,"C","Aerobic-type carbon monoxide dehydrogenase, large subunit CoxL/CutL homologs"]
[null,"COG2080",154,3,156,"C","Aerobic-type carbon monoxide dehydrogenase, small subunit CoxS/CutS homologs"]
["AZ49_05685","COG0183",393,1,393,"I","Acetyl-CoA acetyltransferase"]
["AZ49_05690","COG0183",394,1,394,"I","Acetyl-CoA acetyltransferase"]
["AZ49_10655","COG1250",284,1,284,"I","3-hydroxyacyl-CoA dehydrogenase"]
["AZ49_00555","COG1024",264,1,264,"I","Enoyl-CoA hydratase/carnithine racemase"]
["AZ49_00545","COG2057",217,4,220,"I","Acyl CoA:acetate/3-ketoacid CoA transferase, beta subunit"]
["AZ49_00550","COG1788",220,2,221,"I","Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit"]
["AZ49_02170","COG2030",138,1,138,"I","Acyl dehydratase"]
["AZ49_02175","COG4670",513,1,513,"I","Acyl CoA:acetate/3-ketoacid CoA transferase"]
["AZ49_00650","COG1960",386,1,386,"I","Acyl-CoA dehydrogenases"]
["AZ49_02755","COG1960",382,1,382,"I","Acyl-CoA dehydrogenases"]
["AZ49_02760","COG1024",260,1,260,"I","Enoyl-CoA hydratase/carnithine racemase"]
["AZ49_04240","COG1960",382,1,382,"I","Acyl-CoA dehydrogenases"]
["AZ49_06245","COG1960",379,1,379,"I","Acyl-CoA dehydrogenases"]
["AZ49_06555","COG1960",383,1,383,"I","Acyl-CoA dehydrogenases"]
["AZ49_06560","COG2086",270,1,270,"C","Electron transfer flavoprotein, beta subunit"]
["AZ49_06565","COG2025",335,3,337,"C","Electron transfer flavoprotein, alpha subunit"]
["AZ49_07320","COG2086",260,1,260,"C","Electron transfer flavoprotein, beta subunit"]
["AZ49_07325","COG2025",331,3,333,"C","Electron transfer flavoprotein, alpha subunit"]
["AZ49_01090","COG2878",196,4,199,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfB"]
[null,"COG2878",65,206,270,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfB"]
["AZ49_01095","COG4657",189,3,191,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfA"]
["AZ49_01100","COG4660",202,1,202,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfE"]
["AZ49_01105","COG4659",159,16,174,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfG"]
["AZ49_01110","COG4658",320,22,341,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfD"]
["AZ49_01115","COG4656",444,7,450,"C","Predicted NADH:ubiquinone oxidoreductase, subunit RnfC"]

{"sheet":"EGGNOG","index":10,"n_rows":38,"n_cols":7,"rows_kept":38}
["CDS","OG ID","Score","Eval","Class ID","OG function","KEGG map"]
["AZ49_00320","05QUH","840.5",{"v":1.3E-241,"d":"1.30E-241"},"S","Domain of unknown function (DUF2088)","-"]
["AZ49_00330","05DAA","936.4",{"v":2.1E-270,"d":"2.10E-270"},"C","L-lactate","-"]
["AZ49_04210","05DAA","921.8",{"v":5.3e-266,"d":"5.30E-266"},"C","L-lactate","-"]
["AZ49_00515","07WFN","674.1",{"v":1.3e-191,"d":"1.30E-191"},"S","Malate lactate","-"]
["AZ49_11470","05C80","656.4",{"v":2.6e-186,"d":"2.60E-186"},"C","Catalyzes the reversible oxidation of malate to oxaloacetate (By similarity)","00010, 00020, 00270, 00620, 00630, 00640, 00680, 00710, 00720, 01100, 01110, 01120"]
["AZ49_01710","05D95","2383.2",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"]
["AZ49_05490","05D95","2395.9",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"]
["AZ49_06970","05D95","2367.4",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"]
["AZ49_06950","05C6H","789.6",{"v":2.5e-226,"d":"2.50E-226"},"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"]
["AZ49AM_0981","08IJ2","493",{"v":3e-137,"d":"3.00E-137"},"C","phosphate acetyltransferase","00430, 00620, 00640, 00680, 00720, 01100, 01120"]
["AZ49_00050","05C0A","707.2",{"v":1.5E-201,"d":"1.50E-201"},"C","alcohol dehydrogenase","00010, 00071, 00350, 00362, 00620, 00621, 00622, 00625, 00626, 00650, 01100, 01110, 01120"]
["AZ49_02525","05C0A","770.4",{"v":1.5e-220,"d":"1.50E-220"},"C","alcohol dehydrogenase","00010, 00071, 00350, 00362, 00620, 00621, 00622, 00625, 00626, 00650, 01100, 01110, 01120"]
["AZ49_03535","05C7W","1812.3",0,"C","Xanthine dehydrogenase","00230, 00633, 00680, 00720, 01100, 01120"]
["AZ49_05685","05CHU","766.9",{"v":1.7e-219,"d":"1.70E-219"},"I","acetyl-coa acetyltransferase","00071, 00072, 00280, 00281, 00310, 00362, 00380, 00592, 00620, 00630, 00640, 00642, 00650, 00720, 00900, 01100, 01110, 01120, 02020"]
["AZ49_05690","05CHU","775",{"v":6.2e-222,"d":"6.20E-222"},"I","acetyl-coa acetyltransferase","00071, 00072, 00280, 00281, 00310, 00362, 00380, 00592, 00620, 00630, 00640, 00642, 00650, 00720, 00900, 01100, 01110, 01120, 02020"]
["AZ49_10655","05DYT","564.3",{"v":1.2E-158,"d":"1.20E-158"},"I","3-hydroxyacyl-CoA dehydrogenase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00640, 00650, 00720, 00903, 00930, 01040, 01100, 01110, 01120"]
["AZ49_00555","05CGU","515.4",{"v":5.9e-144,"d":"5.90E-144"},"I","Enoyl-CoA hydratase","00360, 01120"]
["AZ49_00545","08IIH","447.2",{"v":1.7E-123,"d":"1.70E-123"},"I","CoA-transferase subunit B","00072, 00280, 00627, 00640, 00650, 01100, 01120, 02020"]
["AZ49_00550","05D6N","477.2",{"v":1.7e-132,"d":"1.70E-132"},"I","CoA-transferase, subunit a","00072, 00280, 00627, 00640, 00650, 01100, 01120, 02020"]
["AZ49_02170","08Z7G","193.4",{"v":2.7e-47,"d":"2.70E-47"},"I","MaoC domain protein dehydratase","-"]
["AZ49_02175","08IIG","679.5",{"v":4.6e-193,"d":"4.60E-193"},"I","CoA transferase having broad substrate specificity for short-chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons (By similarity)","00620, 00640, 00643, 01100, 01120"]
["AZ49_00650","05C1G","754.2",{"v":1.1E-215,"d":"1.10E-215"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["AZ49_02755","05C1G","740.3",{"v":1.6e-211,"d":"1.60E-211"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["AZ49_02760","05E39","521.2",{"v":1.1E-145,"d":"1.10E-145"},"I","Enoyl-CoA hydratase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00627, 00630, 00640, 00650, 00720, 00903, 00930, 01100, 01110, 01120"]
["AZ49_04240","05C1G","740",{"v":2.1e-211,"d":"2.10E-211"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["AZ49_06245","05C1G","743.4",{"v":1.9e-212,"d":"1.90E-212"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["AZ49_06555","05C1G","756.1",{"v":2.9e-216,"d":"2.90E-216"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["AZ49_06560","05BZJ","520.4",{"v":1.9e-145,"d":"1.90E-145"},"C","Electron transfer flavoprotein","00910"]
["AZ49_06565","05C10","683.3",{"v":2.1e-194,"d":"2.10E-194"},"C","Electron transfer flavoprotein","00910"]
["AZ49_07320","05BZJ","484.2",{"v":1.4e-134,"d":"1.40E-134"},"C","Electron transfer flavoprotein","00910"]
["AZ49_07325","05C10","647.1",{"v":1.6e-183,"d":"1.60E-183"},"C","Electron transfer flavoprotein","00910"]
["AZ49_01090","07SVV","468.4",{"v":9E-130,"d":"9.00E-130"},"C","electron transport complex, RnfABCDGE type, B subunit","-"]
["AZ49_01095","05DGN","355.1",{"v":7.4e-96,"d":"7.40E-96"},"C","Electron transport complex","-"]
["AZ49_01100","05DZB","402.1",{"v":5.7e-110,"d":"5.70E-110"},"C","Electron transport complex","-"]
["AZ49_01105","080WF","357.1",{"v":1.9E-96,"d":"1.90E-96"},"C","Electron transport complex, RnfABCDGE type, G subunit","-"]
["AZ49_01110","05D6A","683.3",{"v":2.1e-194,"d":"2.10E-194"},"C","Electron transport complex","-"]
["AZ49_01115","07QTR","928.3",{"v":5e-268,"d":"5.00E-268"},"C","Required for nitrogen fixation. May be part of a membrane complex functioning as an intermediate in the electron transport to nitrogenase (By similarity)","-"]

{"sheet":"FigFam","index":11,"n_rows":26,"n_cols":4,"rows_kept":26}
["CDS","FIGFAM id","FIGFAM Description","EC number"]
["AZ49_11470","FIG000812","L-lactate dehydrogenase","1.1.1.27"]
["AZ49_01710","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["AZ49_05490","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["AZ49_06970","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["AZ49_06950","FIG134300","Acetate kinase","2.7.2.1"]
["AZ49AM_0981","FIG000522","Phosphate acetyltransferase","2.3.1.8"]
["AZ49_03535","FIG000962","Xanthine dehydrogenase, molybdenum binding subunit","1.17.1.4"]
["AZ49_05685","FIG002604","Acetyl-CoA acetyltransferase","2.3.1.9"]
["AZ49_05690","FIG002604","Acetyl-CoA acetyltransferase","2.3.1.9"]
["AZ49_10655","FIG133011","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157"]
["AZ49_00650","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["AZ49_02755","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["AZ49_02760","FIG002255","3-hydroxybutyryl-CoA dehydratase","4.2.1.55"]
["AZ49_04240","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["AZ49_06245","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["AZ49_06555","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["AZ49_06560","FIG136866","Electron transfer flavoprotein, beta subunit","_"]
["AZ49_06565","FIG000366","Electron transfer flavoprotein, alpha subunit","_"]
["AZ49_07325","FIG000366","Electron transfer flavoprotein, alpha subunit","_"]
["AZ49_01090","FIG133292","Electron transport complex protein RnfB","_"]
["AZ49_01095","FIG001505","Electron transport complex protein RnfA","_"]
["AZ49_01100","FIG134060","Electron transport complex protein RnfE","_"]
["AZ49_01105","FIG002689","Electron transport complex protein RnfG","_"]
["AZ49_01110","FIG022976","Electron transport complex protein RnfD","_"]
["AZ49_01115","FIG018536","Electron transport complex protein RnfC","_"]

{"sheet":"InterProScan","index":12,"n_rows":481,"n_cols":13,"rows_kept":481}
["AZ49_00320","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":5.5e-73,"d":"5.50E-73"},"LarA-like_N","Domain","LarA-like, N-terminal","Molecular Function: lactate racemase activity (GO:0050043)"]
[null,"_","_","PTHR33171","_",1,426,0.995316,{"v":1.9e-116,"d":"1.90E-116"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.11440","_",34,269,0.550351,{"v":2.4e-155,"d":"2.40E-155"},"_","_","_","-"]
[null,"_","_","G3DSA:3.90.226.30","_",6,421,0.971897,{"v":2.4e-155,"d":"2.40E-155"},"_","_","_","-"]
[]
["AZ49_00330","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",7,515,0.975048,{"v":4.8E-123,"d":"4.80E-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",8,511,0.965451,{"v":2.5E-119,"d":"2.50E-119"},"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",8,511,0.965451,{"v":3.5e-112,"d":"3.50E-112"},"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)"]
[]
["AZ49_04210","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",1,500,0.986166,{"v":3.6e-122,"d":"3.60E-122"},"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",2,500,0.98419,{"v":1.9e-119,"d":"1.90E-119"},"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",2,500,0.98419,{"v":2.7E-113,"d":"2.70E-113"},"Lactate_perm","Family","L-lactate permease","Cellular Component: integral component of plasma membrane (GO:0005887); Molecular Function: lactate transmembrane transporter activity (GO:0015129); Biological Process: lactate transport (GO:0015727)"]
[null,"_","_","PTHR30003:SF0","_",1,500,0.986166,{"v":3.6e-122,"d":"3.60E-122"},"_","_","_","-"]
[]
["AZ49_00515","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",30,185,0.468278,5.05E-11,"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR001236","PFAM","PF00056","Ldh_1_N",33,183,0.453172,5.5e-05,"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","_",11,187,0.531722,{"v":2.7e-25,"d":"2.70E-25"},"_","_","_","-"]
[]
["AZ49_11470","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,{"v":8.51e-34,"d":"8.51E-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":2.1e-21,"d":"2.10E-21"},"Lactate/malate_DH_C","Domain","Lactate/malate dehydrogenase, C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR018177","PROSITE","PS00064","L_LDH",176,182,0.0188679,"_","L-lactate_DH_AS","Active_site","L-lactate dehydrogenase, active site","Molecular Function: L-lactate dehydrogenase activity (GO:0004459); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR015955","CATHGENE3D","G3DSA:3.90.110.10","G3DSA:3.90.110.10",148,312,0.515723,{"v":4.7e-49,"d":"4.70E-49"},"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",147,310,0.512579,{"v":2.88e-42,"d":"2.88E-42"},"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",2,316,0.987421,{"v":5.2e-77,"d":"5.20E-77"},"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":3.5e-25,"d":"3.50E-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":3.5e-25,"d":"3.50E-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":3.5e-25,"d":"3.50E-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":3.5e-25,"d":"3.50E-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":3.5e-25,"d":"3.50E-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":8.5e-18,"d":"8.50E-18"},"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":5.6e-37,"d":"5.60E-37"},"_","_","_","-"]
[null,"_","_","PTHR43128","_",4,311,0.965409,{"v":5.8e-75,"d":"5.80E-75"},"_","_","_","-"]
[null,"_","_","PTHR43128:SF4","_",4,311,0.965409,{"v":5.8e-75,"d":"5.80E-75"},"_","_","_","-"]
[null,"_","_","cd05291","_",6,310,0.955975,{"v":6.08768e-132,"d":"6.09E-132"},"_","_","_","-"]
[]
["AZ49_01710","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",270,369,0.0846154,2.1e-12,"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",7,259,0.215385,5.59E-68,"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",783,1166,0.32735,{"v":2.36e-121,"d":"2.36E-121"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",426,609,0.15641,{"v":4.2e-30,"d":"4.20E-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",629,679,0.042735,4.4e-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",622,680,0.0495727,{"v":1.7E-16,"d":"1.70E-16"},"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",689,758,0.0589744,3.6E-9,"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",735,764,0.0247863,9.978,"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",952,1062,0.0940171,8.2e-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",260,412,0.129915,{"v":3.4E-53,"d":"3.40E-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,{"v":7e-41,"d":"7.00E-41"},"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",21,248,0.194017,{"v":4.7E-67,"d":"4.70E-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",416,625,0.178632,{"v":8.4e-90,"d":"8.40E-90"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","SSF","SSF53323","SSF53323",418,669,0.21453,{"v":5.62e-84,"d":"5.62E-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,{"v":4.74e-21,"d":"4.74E-21"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",670,781,0.0948718,{"v":2.9e-35,"d":"2.90E-35"},"_","_","_","-"]
[null,"_","_","cd07034","_",11,174,0.139316,{"v":1.46061E-40,"d":"1.46E-40"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",3,259,0.218803,{"v":4.9e-92,"d":"4.90E-92"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",782,1167,0.32906,{"v":2.4e-164,"d":"2.40E-164"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",5,1163,0.989744,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",5,1163,0.989744,0,"_","_","_","-"]
[null,"_","_","cd03377","_",800,1163,0.310256,0,"_","_","_","-"]
[]
["AZ49_05490","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",270,370,0.085034,6.5e-14,"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",7,259,0.214286,{"v":9.71e-73,"d":"9.71E-73"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",788,1174,0.328231,{"v":4.08e-123,"d":"4.08E-123"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",425,609,0.156463,{"v":2.4e-34,"d":"2.40E-34"},"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",632,681,0.0416667,{"v":4.7E-19,"d":"4.70E-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",622,682,0.0510204,{"v":2.5e-18,"d":"2.50E-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",748,759,0.00935374,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",692,703,0.00935374,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",683,712,0.0246599,9.777,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",739,768,0.0246599,9.348,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011895","PIRSF","PIRSF000159","NifJ",1,1176,0.99915,0,"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",7,1175,0.993197,0,"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",961,1073,0.0952381,1.8E-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",260,413,0.130102,{"v":1.5e-55,"d":"1.50E-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",260,405,0.123299,{"v":5.85e-43,"d":"5.85E-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",18,248,0.195578,{"v":6.7e-76,"d":"6.70E-76"},"Pyrv_Fd/Flavodoxin_OxRdtase_N","Domain","Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","CATHGENE3D","G3DSA:3.40.920.10","G3DSA:3.40.920.10",415,626,0.179422,{"v":2.9e-86,"d":"2.90E-86"},"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",415,669,0.215986,{"v":4.05e-78,"d":"4.05E-78"},"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","_",691,760,0.0586735,1.3e-08,"_","_","_","-"]
[null,"_","_","SSF54862","_",668,829,0.136905,{"v":1.27e-21,"d":"1.27E-21"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",672,785,0.0960884,{"v":2.3E-42,"d":"2.30E-42"},"_","_","_","-"]
[null,"_","_","cd07034","_",11,174,0.138605,{"v":5.25994e-48,"d":"5.26E-48"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",4,259,0.216837,{"v":1.2e-100,"d":"1.20E-100"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",787,1176,0.330782,{"v":1e-154,"d":"1.00E-154"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",5,1174,0.994048,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",5,1174,0.994048,0,"_","_","_","-"]
[null,"_","_","cd03377","_",804,1174,0.314626,0,"_","_","_","-"]
[]
["AZ49_06970","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",629,667,0.0324509,2.8e-06,"Pyrv-flavodox_OxR_EKR_sf","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, EKR domain superfamily","-"]
[null,"IPR033412","PFAM","PF17147","PFOR_II",268,372,0.088813,2.4e-15,"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",3,257,0.216909,2.16E-75,"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",784,1166,0.326217,{"v":4.24e-127,"d":"4.24E-127"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",424,607,0.156277,{"v":5.7e-28,"d":"5.70E-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",625,673,0.0409906,{"v":9.5e-16,"d":"9.50E-16"},"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",620,678,0.0495303,2.3e-12,"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","PFAM","PF12838","Fer4_7",687,757,0.059778,3.1E-8,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",734,763,0.0247652,10.449,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",679,708,0.0247652,10.003,"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",953,1064,0.0947908,1E-8,"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":1.6E-52,"d":"1.60E-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",258,410,0.129804,{"v":3.85e-43,"d":"3.85E-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",17,246,0.195559,{"v":5.8e-77,"d":"5.80E-77"},"Pyrv_Fd/Flavodoxin_OxRdtase_N","Domain","Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","CATHGENE3D","G3DSA:3.40.920.10","G3DSA:3.40.920.10",414,624,0.179334,{"v":1.6E-89,"d":"1.60E-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",415,667,0.215201,{"v":9.81e-83,"d":"9.81E-83"},"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","_",665,829,0.140051,{"v":8.37e-23,"d":"8.37E-23"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",668,780,0.0956447,{"v":5.5e-31,"d":"5.50E-31"},"_","_","_","-"]
[null,"_","_","cd07034","_",9,172,0.139197,{"v":1.13012e-49,"d":"1.13E-49"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",2,257,0.217763,{"v":5.4e-105,"d":"5.40E-105"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",784,1168,0.327925,{"v":6.5e-168,"d":"6.50E-168"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",1,1166,0.994876,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",1,1166,0.994876,0,"_","_","_","-"]
[null,"_","_","cd03377","_",801,1166,0.311699,0,"_","_","_","-"]
["AZ49_06950","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",3,14,0.0276382,"_","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",203,220,0.0427136,"_","Aliphatic_acid_kinase_CS","Conserved_site","Aliphatic acid kinase, short-chain, conserved site","Molecular Function: kinase activity (GO:0016301); Biological Process: phosphorylation (GO:0016310); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR004372","HAMAP","MF_00020","Acetate_kinase",1,398,0.997487,191.31,"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",1,398,0.997487,{"v":1.2e-153,"d":"1.20E-153"},"Ac/propionate_kinase","Family","Acetate/propionate kinase","Biological Process: organic acid metabolic process (GO:0006082); Molecular Function: kinase activity (GO:0016301); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR004372","TIGRFAMs","TIGR00016","ackA",2,394,0.984925,{"v":1.7E-155,"d":"1.70E-155"},"Ac/propionate_kinase","Family","Acetate/propionate kinase","Biological Process: organic acid metabolic process (GO:0006082); Molecular Function: kinase activity (GO:0016301); Molecular Function: phosphotransferase activity, carboxyl group as acceptor (GO:0016774)"]
[null,"IPR000890","PANTHER","PTHR21060","PTHR21060",1,397,0.994975,{"v":4.2e-164,"d":"4.20E-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",3,389,0.969849,{"v":9.1E-159,"d":"9.10E-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",322,338,0.040201,{"v":8.6e-43,"d":"8.60E-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",3,14,0.0276382,{"v":8.6e-43,"d":"8.60E-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",300,313,0.0326633,{"v":8.6e-43,"d":"8.60E-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",376,388,0.0301508,{"v":8.6e-43,"d":"8.60E-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",173,186,0.0326633,{"v":8.6e-43,"d":"8.60E-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",203,224,0.0527638,{"v":8.6e-43,"d":"8.60E-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","_",1,195,0.487437,{"v":9.5e-72,"d":"9.50E-72"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",1,195,0.487437,{"v":1.7e-78,"d":"1.70E-78"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.420.40","_",196,398,0.507538,{"v":6.5e-82,"d":"6.50E-82"},"_","_","_","-"]
[null,"_","_","SSF53067","_",158,394,0.592965,{"v":5.74e-90,"d":"5.74E-90"},"_","_","_","-"]
[null,"_","_","PTHR21060:SF15","_",1,397,0.994975,{"v":4.2e-164,"d":"4.20E-164"},"_","_","_","-"]
[]
["AZ49AM_0981","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",1,251,0.996016,{"v":1.1e-87,"d":"1.10E-87"},"P_AcTrfase_dom1","Homologous_superfamily","Phosphate acetyltransferase, domain 1","-"]
[null,"IPR042112","CATHGENE3D","G3DSA:3.40.50.10750","G3DSA:3.40.50.10750",63,224,0.641434,{"v":1.1e-87,"d":"1.10E-87"},"P_AcTrfase_dom2","Homologous_superfamily","Phosphate acetyltransferase, domain 2","-"]
[null,"IPR002505","PFAM","PF01515","PTA_PTB",2,247,0.976096,{"v":1.4E-77,"d":"1.40E-77"},"PTA_PTB","Domain","Phosphate acetyl/butaryl transferase","Molecular Function: transferase activity, transferring acyl groups (GO:0016746)"]
[null,"_","_","SSF53659","_",2,251,0.992032,1.23E-67,"_","_","_","-"]
[null,"_","_","PTHR43356","_",1,249,0.988048,{"v":6.6e-77,"d":"6.60E-77"},"_","_","_","-"]
[null,"_","_","PTHR43356:SF3","_",1,249,0.988048,{"v":6.6e-77,"d":"6.60E-77"},"_","_","_","-"]
[]
["AZ49_00050","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR039697","PANTHER","PTHR11496","PTHR11496",4,361,0.978082,{"v":6.8e-88,"d":"6.80E-88"},"Alcohol_dehydrogenase_Fe","Family","Iron-type alcohol dehydrogenase-like","-"]
[null,"IPR018211","PROSITE","PS00913","ADH_IRON_1",169,197,0.0767123,"_","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,"IPR001670","PFAM","PF00465","Fe-ADH",7,352,0.945205,{"v":1.4e-94,"d":"1.40E-94"},"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","_",182,362,0.493151,{"v":1.2e-41,"d":"1.20E-41"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1970","_",1,180,0.490411,{"v":7.2e-58,"d":"7.20E-58"},"_","_","_","-"]
[null,"_","_","SSF56796","_",1,360,0.983562,{"v":4.84e-96,"d":"4.84E-96"},"_","_","_","-"]
[]
["AZ49_02525","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",7,388,0.979434,{"v":3.9e-86,"d":"3.90E-86"},"Alcohol_dehydrogenase_Fe","Family","Iron-type alcohol dehydrogenase-like","-"]
[null,"IPR001670","PFAM","PF00465","Fe-ADH",8,376,0.946015,{"v":4.7e-96,"d":"4.70E-96"},"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","_",189,387,0.508997,{"v":3.1e-36,"d":"3.10E-36"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1970","_",1,188,0.48072,{"v":7.4E-57,"d":"7.40E-57"},"_","_","_","-"]
[null,"_","_","SSF56796","_",3,388,0.989717,{"v":5.5e-98,"d":"5.50E-98"},"_","_","_","-"]
[null,"_","_","cd08185","_",5,385,0.976864,0,"_","_","_","-"]
[]
["AZ49_03535","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037165","SSF","SSF56003","SSF56003",297,886,0.657366,2.09E-140,"AldOxase/xan_DH_Mopterin-bd_sf","Homologous_superfamily","Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain superfamily","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR036884","SSF","SSF47741","SSF47741",73,155,0.0915179,2.09E-24,"2Fe-2S-bd_dom_sf","Homologous_superfamily","[2Fe-2S]-binding domain superfamily","-"]
[null,"IPR036856","SSF","SSF54665","SSF54665",161,311,0.167411,{"v":2.62e-33,"d":"2.62E-33"},"Ald_Oxase/Xan_DH_a/b_sf","Homologous_superfamily","Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead superfamily","-"]
[null,"IPR036010","SSF","SSF54292","SSF54292",7,78,0.0792411,{"v":1.14e-17,"d":"1.14E-17"},"2Fe-2S_ferredoxin-like_sf","Homologous_superfamily","2Fe-2S ferredoxin-like superfamily","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"IPR017697","TIGRFAMs","TIGR03311","Se_dep_XDH",7,698,0.771205,0,"Xdh","Family","Selenium-dependent xanthine dehydrogenase","-"]
[null,"IPR013087","PROSITE","PS00028","ZINC_FINGER_C2H2_1",422,443,0.0234375,"_","Znf_C2H2_type","Domain","Zinc finger C2H2-type","Molecular Function: nucleic acid binding (GO:0003676)"]
[null,"IPR008274","PFAM","PF02738","Ald_Xan_dh_C2",307,816,0.56808,{"v":1.2e-115,"d":"1.20E-115"},"AldOxase/xan_DH_Mopterin-bd","Domain","Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006058","PROSITE","PS00197","2FE2S_FER_1",39,47,0.00892857,"_","2Fe2S_fd_BS","Binding_site","2Fe-2S ferredoxin, iron-sulphur binding site","Molecular Function: 2 iron, 2 sulfur cluster binding (GO:0051537)"]
[null,"IPR002888","PFAM","PF01799","Fer2_2",73,144,0.0792411,{"v":1.6e-22,"d":"1.60E-22"},"2Fe-2S-bd","Domain","[2Fe-2S]-binding","Molecular Function: oxidoreductase activity (GO:0016491); Molecular Function: metal ion binding (GO:0046872); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001041","CDD","cd00207","fer2",10,52,0.046875,0.0005769,"2Fe-2S_ferredoxin-type","Domain","2Fe-2S ferredoxin-type iron-sulfur binding domain","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"IPR001041","PFAM","PF00111","Fer2",11,55,0.0491071,1e-05,"2Fe-2S_ferredoxin-type","Domain","2Fe-2S ferredoxin-type iron-sulfur binding domain","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"IPR001041","PROFILE","PS51085","2FE2S_FER_2",1,77,0.0848214,10.081,"2Fe-2S_ferredoxin-type","Domain","2Fe-2S ferredoxin-type iron-sulfur binding domain","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"IPR000674","PFAM","PF01315","Ald_Xan_dh_C",183,291,0.120536,{"v":8.7e-23,"d":"8.70E-23"},"Ald_Oxase/Xan_DH_a/b","Domain","Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead","-"]
[null,"IPR000674","SMART","SM01008","Ald_Xan_dh_C",180,291,0.123884,{"v":1.1E-35,"d":"1.10E-35"},"Ald_Oxase/Xan_DH_a/b","Domain","Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead","-"]
[null,"_","_","G3DSA:3.30.365.10","_",2,156,0.171875,{"v":1.3e-45,"d":"1.30E-45"},"_","_","_","-"]
[null,"_","_","G3DSA:3.30.365.10","_",157,887,0.814732,{"v":1.3e-164,"d":"1.30E-164"},"_","_","_","-"]
[null,"_","_","PTHR11908","_",39,891,0.950893,{"v":8.4e-221,"d":"8.40E-221"},"_","_","_","-"]
[null,"_","_","PTHR11908:SF136","_",39,891,0.950893,{"v":8.4e-221,"d":"8.40E-221"},"_","_","_","-"]
[]
["AZ49_05685","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",269,390,0.307888,{"v":3.5e-51,"d":"3.50E-51"},"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",4,261,0.653944,{"v":1.3E-106,"d":"1.30E-106"},"Thiolase_N","Domain","Thiolase, N-terminal","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020613","PROSITE","PS00737","THIOLASE_2",338,354,0.0407125,"_","Thiolase_CS","Conserved_site","Thiolase, conserved site","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020610","PROSITE","PS00099","THIOLASE_3",373,386,0.0330789,"_","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",126,389,0.669211,{"v":2e-166,"d":"2.00E-166"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","CATHGENE3D","G3DSA:3.40.47.10","G3DSA:3.40.47.10",6,275,0.684478,{"v":2e-166,"d":"2.00E-166"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",270,391,0.307888,1.29E-45,"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",3,269,0.676845,{"v":1.18e-95,"d":"1.18E-95"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002155","CDD","cd00751","thiolase",5,391,0.982188,0,"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",1,393,0.997455,{"v":2.3e-139,"d":"2.30E-139"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR002155","TIGRFAMs","TIGR01930","AcCoA-C-Actrans",6,390,0.977099,{"v":5.2e-153,"d":"5.20E-153"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"_","_","PTHR18919","_",1,391,0.992366,{"v":1.6E-178,"d":"1.60E-178"},"_","_","_","-"]
[null,"_","_","PTHR18919:SF132","_",1,391,0.992366,{"v":1.6E-178,"d":"1.60E-178"},"_","_","_","-"]
[]
["AZ49_05690","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR020617","PFAM","PF02803","Thiolase_C",270,393,0.312183,{"v":3.7e-49,"d":"3.70E-49"},"Thiolase_C","Domain","Thiolase, C-terminal","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020616","PFAM","PF00108","Thiolase_N",5,261,0.649746,{"v":8.1e-104,"d":"8.10E-104"},"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",84,102,0.0456853,"_","Thiolase_acyl_enz_int_AS","Active_site","Thiolase, acyl-enzyme intermediate active site","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020613","PROSITE","PS00737","THIOLASE_2",338,354,0.0406091,"_","Thiolase_CS","Conserved_site","Thiolase, conserved site","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020610","PROSITE","PS00099","THIOLASE_3",375,388,0.0329949,"_","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",6,275,0.682741,{"v":7.8e-163,"d":"7.80E-163"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","CATHGENE3D","G3DSA:3.40.47.10","G3DSA:3.40.47.10",126,391,0.672589,{"v":7.8e-163,"d":"7.80E-163"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",270,393,0.312183,{"v":6.67e-44,"d":"6.67E-44"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",3,269,0.675127,{"v":8.4e-93,"d":"8.40E-93"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002155","CDD","cd00751","thiolase",5,393,0.984772,0,"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",1,394,0.997462,{"v":6.4e-141,"d":"6.40E-141"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR002155","TIGRFAMs","TIGR01930","AcCoA-C-Actrans",6,392,0.979695,{"v":4.2E-152,"d":"4.20E-152"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"_","_","PTHR18919","_",1,394,0.997462,{"v":2e-166,"d":"2.00E-166"},"_","_","_","-"]
[null,"_","_","PTHR18919:SF132","_",1,394,0.997462,{"v":2e-166,"d":"2.00E-166"},"_","_","_","-"]
[]
["AZ49_10655","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",1,185,0.647887,{"v":3.63e-58,"d":"3.63E-58"},"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR022694","PIRSF","PIRSF000105","HCDH",1,284,0.996479,{"v":8.7e-90,"d":"8.70E-90"},"3-OHacyl-CoA_DH","Family","3-hydroxyacyl-CoA dehydrogenase","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Biological Process: oxidation-reduction process (GO:0055114); Molecular Function: NAD+ binding (GO:0070403)"]
[null,"IPR013328","CATHGENE3D","G3DSA:1.10.1040.10","G3DSA:1.10.1040.10",193,278,0.299296,{"v":2E-35,"d":"2.00E-35"},"6PGD_dom2","Homologous_superfamily","6-phosphogluconate dehydrogenase, domain 2","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR008927","SSF","SSF48179","SSF48179",185,283,0.34507,{"v":3.4e-34,"d":"3.40E-34"},"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",183,208,0.0880282,"_","3-OHacyl-CoA_DH_CS","Conserved_site","3-hydroxyacyl-CoA dehydrogenase, conserved site","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006176","PFAM","PF02737","3HCDH_N",3,183,0.633803,{"v":3.6e-66,"d":"3.60E-66"},"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",186,282,0.338028,{"v":4.7e-36,"d":"4.70E-36"},"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","_",1,188,0.658451,{"v":2.4e-70,"d":"2.40E-70"},"_","_","_","-"]
[null,"_","_","PTHR43145","_",2,283,0.989437,{"v":1.3E-123,"d":"1.30E-123"},"_","_","_","-"]
[null,"_","_","PTHR43145:SF8","_",2,283,0.989437,{"v":1.3E-123,"d":"1.30E-123"},"_","_","_","-"]
[]
["AZ49_00555","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR029045","SSF","SSF52096","SSF52096",3,263,0.984848,2.77E-74,"ClpP/crotonase-like_dom_sf","Homologous_superfamily","ClpP/crotonase-like domain superfamily","-"]
[null,"IPR018376","PROSITE","PS00166","ENOYL_COA_HYDRATASE",104,124,0.0757576,"_","Enoyl-CoA_hyd/isom_CS","Conserved_site","Enoyl-CoA hydratase/isomerase, conserved site","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR014748","CATHGENE3D","G3DSA:1.10.12.10","G3DSA:1.10.12.10",206,264,0.219697,1.2e-14,"Enoyl-CoA_hydra_C","Homologous_superfamily","Enoyl-CoA hydratase, C-terminal","-"]
[null,"IPR001753","PFAM","PF00378","ECH_1",11,264,0.958333,{"v":2.1e-61,"d":"2.10E-61"},"Enoyl-CoA_hydra/iso","Family","Enoyl-CoA hydratase/isomerase","Molecular Function: catalytic activity (GO:0003824)"]
[null,"_","_","cd06558","_",6,202,0.742424,{"v":4.2539e-54,"d":"4.25E-54"},"_","_","_","-"]
[null,"_","_","G3DSA:3.90.226.10","_",1,204,0.768939,{"v":1.2E-61,"d":"1.20E-61"},"_","_","_","-"]
[null,"_","_","PTHR11941","_",1,264,0.996212,{"v":4.4e-115,"d":"4.40E-115"},"_","_","_","-"]
[null,"_","_","PTHR11941:SF139","_",1,264,0.996212,{"v":4.4e-115,"d":"4.40E-115"},"_","_","_","-"]
[]
["AZ49_00545","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037171","SSF","SSF100950","SSF100950",7,218,0.959091,{"v":2.74e-67,"d":"2.74E-67"},"NagB/RpiA_transferase-like","Homologous_superfamily","NagB/RpiA transferase-like","-"]
[null,"IPR012791","TIGRFAMs","TIGR02428","pcaJ_scoB_fam",7,211,0.927273,{"v":2.5e-92,"d":"2.50E-92"},"3-oxoacid_CoA-transf_B","Domain","3-oxoacid CoA-transferase, subunit B","Molecular Function: CoA-transferase activity (GO:0008410)"]
[null,"IPR004165","PANTHER","PTHR13707","PTHR13707",6,215,0.95,{"v":4.2e-88,"d":"4.20E-88"},"CoA_trans_fam_I","Family","Coenzyme A transferase family I","Molecular Function: CoA-transferase activity (GO:0008410)"]
[null,"IPR004165","PFAM","PF01144","CoA_trans",13,201,0.854545,{"v":8.2e-26,"d":"8.20E-26"},"CoA_trans_fam_I","Family","Coenzyme A transferase family I","Molecular Function: CoA-transferase activity (GO:0008410)"]
[null,"IPR004165","SMART","SM00882","CoA_trans",8,204,0.890909,{"v":1.4e-54,"d":"1.40E-54"},"CoA_trans_fam_I","Family","Coenzyme A transferase family I","Molecular Function: CoA-transferase activity (GO:0008410)"]
[null,"_","_","G3DSA:3.40.1080.10","_",3,215,0.963636,{"v":1.3e-85,"d":"1.30E-85"},"_","_","_","-"]
[null,"_","_","PTHR13707:SF23","_",6,215,0.95,{"v":4.2e-88,"d":"4.20E-88"},"_","_","_","-"]
[]
["AZ49_00550","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037171","SSF","SSF100950","SSF100950",3,224,0.902041,{"v":5.16e-63,"d":"5.16E-63"},"NagB/RpiA_transferase-like","Homologous_superfamily","NagB/RpiA transferase-like","-"]
[null,"IPR012792","TIGRFAMs","TIGR02429","pcaI_scoA_fam",6,217,0.861224,{"v":1.1E-51,"d":"1.10E-51"},"3-oxoacid_CoA-transf_A","Domain","3-oxoacid CoA-transferase, subunit A","Molecular Function: CoA-transferase activity (GO:0008410)"]
[null,"IPR004165","PANTHER","PTHR13707","PTHR13707",3,215,0.865306,{"v":2.8E-93,"d":"2.80E-93"},"CoA_trans_fam_I","Family","Coenzyme A transferase family I","Molecular Function: CoA-transferase activity (GO:0008410)"]
[null,"IPR004165","PFAM","PF01144","CoA_trans",8,215,0.844898,{"v":3E-49,"d":"3.00E-49"},"CoA_trans_fam_I","Family","Coenzyme A transferase family I","Molecular Function: CoA-transferase activity (GO:0008410)"]
[null,"IPR004165","SMART","SM00882","CoA_trans",5,216,0.861224,{"v":9.6e-51,"d":"9.60E-51"},"CoA_trans_fam_I","Family","Coenzyme A transferase family I","Molecular Function: CoA-transferase activity (GO:0008410)"]
[null,"_","_","G3DSA:3.40.1080.10","_",2,220,0.889796,{"v":6.1e-67,"d":"6.10E-67"},"_","_","_","-"]
[null,"_","_","PTHR13707:SF49","_",3,215,0.865306,{"v":2.8E-93,"d":"2.80E-93"},"_","_","_","-"]
[]
["AZ49_02170","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",4,138,0.971014,{"v":8.73e-41,"d":"8.73E-41"},"HotDog_dom_sf","Homologous_superfamily","HotDog domain superfamily","-"]
[null,"IPR002539","PFAM","PF01575","MaoC_dehydratas",18,121,0.746377,{"v":3e-26,"d":"3.00E-26"},"MaoC-like_dom","Domain","MaoC-like dehydratase domain","-"]
[null,"_","_","PTHR43437","_",4,136,0.956522,{"v":3.7E-40,"d":"3.70E-40"},"_","_","_","-"]
[null,"_","_","PTHR43437:SF5","_",4,136,0.956522,{"v":3.7E-40,"d":"3.70E-40"},"_","_","_","-"]
[null,"_","_","G3DSA:3.10.129.10","_",2,138,0.985507,{"v":1.8E-45,"d":"1.80E-45"},"_","_","_","-"]
[null,"_","_","cd03449","_",10,136,0.913043,{"v":2.77262e-66,"d":"2.77E-66"},"_","_","_","-"]
[]
["AZ49_02175","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR037171","SSF","SSF100950","SSF100950",272,512,0.467836,2.09E-74,"NagB/RpiA_transferase-like","Homologous_superfamily","NagB/RpiA transferase-like","-"]
[null,"IPR037171","SSF","SSF100950","SSF100950",3,257,0.495127,{"v":9.77e-81,"d":"9.77E-81"},"NagB/RpiA_transferase-like","Homologous_superfamily","NagB/RpiA transferase-like","-"]
[null,"IPR014388","PIRSF","PIRSF000858","SCOT-t",1,513,0.998051,{"v":3.5e-221,"d":"3.50E-221"},"3-oxoacid_CoA-transferase","Family","3-oxoacid CoA-transferase","Molecular Function: CoA-transferase activity (GO:0008410); Biological Process: ketone body catabolic process (GO:0046952)"]
[null,"IPR004165","PFAM","PF01144","CoA_trans",5,240,0.45809,{"v":1.4e-28,"d":"1.40E-28"},"CoA_trans_fam_I","Family","Coenzyme A transferase family I","Molecular Function: CoA-transferase activity (GO:0008410)"]
[null,"IPR004165","SMART","SM00882","CoA_trans",278,485,0.403509,0.0012,"CoA_trans_fam_I","Family","Coenzyme A transferase family I","Molecular Function: CoA-transferase activity (GO:0008410)"]
[null,"IPR004165","SMART","SM00882","CoA_trans",4,241,0.461988,{"v":6.9E-55,"d":"6.90E-55"},"CoA_trans_fam_I","Family","Coenzyme A transferase family I","Molecular Function: CoA-transferase activity (GO:0008410)"]
[null,"_","_","G3DSA:3.40.1080.10","_",1,265,0.51462,{"v":5.4E-102,"d":"5.40E-102"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.1080.10","_",272,513,0.469786,{"v":5.3e-108,"d":"5.30E-108"},"_","_","_","-"]
[null,"_","_","PTHR43293","_",1,512,0.996101,{"v":1.6e-221,"d":"1.60E-221"},"_","_","_","-"]
[null,"_","_","PTHR43293:SF1","_",1,512,0.996101,{"v":1.6e-221,"d":"1.60E-221"},"_","_","_","-"]
[]
["AZ49_00650","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",1,121,0.310881,{"v":2e-30,"d":"2.00E-30"},"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",231,385,0.398964,{"v":5.96e-52,"d":"5.96E-52"},"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",7,112,0.272021,{"v":1.1E-23,"d":"1.10E-23"},"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",3,244,0.624352,1.31E-71,"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",233,380,0.380829,{"v":2.2e-45,"d":"2.20E-45"},"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",126,221,0.246114,{"v":6.4e-27,"d":"6.40E-27"},"Acyl-CoA_Oxase/DH_cen-dom","Domain","Acyl-CoA oxidase/dehydrogenase, central domain","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00072","ACYL_COA_DH_1",128,140,0.0310881,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00073","ACYL_COA_DH_2",342,361,0.0492228,"_","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","_",4,386,0.989637,{"v":4.8e-18,"d":"4.80E-18"},"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",125,238,0.292746,{"v":3.9e-44,"d":"3.90E-44"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",239,385,0.378238,{"v":6.6e-51,"d":"6.60E-51"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",3,384,0.987047,{"v":4e-130,"d":"4.00E-130"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",3,384,0.987047,{"v":4e-130,"d":"4.00E-130"},"_","_","_","-"]
[]
["AZ49_02755","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",1,120,0.311518,{"v":9.4e-39,"d":"9.40E-39"},"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",228,382,0.403141,{"v":1.53e-59,"d":"1.53E-59"},"AcylCo_DH-like_C","Homologous_superfamily","Acyl-CoA dehydrogenase-like, C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR013786","PFAM","PF02771","Acyl-CoA_dh_N",6,117,0.290576,{"v":8.2E-33,"d":"8.20E-33"},"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",1,243,0.633508,{"v":2.75e-78,"d":"2.75E-78"},"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",230,380,0.39267,{"v":4.2e-49,"d":"4.20E-49"},"AcylCo_DH/oxidase_C","Domain","Acyl-CoA dehydrogenase/oxidase C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006091","PFAM","PF02770","Acyl-CoA_dh_M",122,218,0.251309,{"v":8.3e-22,"d":"8.30E-22"},"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",339,358,0.0497382,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PIRSF016578","_",3,97,0.246073,0.55,"_","_","_","-"]
[null,"_","_","PIRSF016578","_",130,381,0.657068,7.5e-14,"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",121,235,0.298429,{"v":1.2e-39,"d":"1.20E-39"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",236,382,0.382199,{"v":8e-58,"d":"8.00E-58"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",2,381,0.992147,{"v":4.5e-146,"d":"4.50E-146"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",2,381,0.992147,{"v":4.5e-146,"d":"4.50E-146"},"_","_","_","-"]
[null,"_","_","cd01158","_",7,382,0.981675,0,"_","_","_","-"]
[null,"_","_","Coil","_",5,25,0.052356,"_","_","_","_","-"]
[]
["AZ49_02760","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR029045","SSF","SSF52096","SSF52096",2,260,0.992308,{"v":3.52e-91,"d":"3.52E-91"},"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":1.7E-21,"d":"1.70E-21"},"Enoyl-CoA_hydra_C","Homologous_superfamily","Enoyl-CoA hydratase, C-terminal","-"]
[null,"IPR001753","PFAM","PF00378","ECH_1",11,259,0.953846,{"v":5.3e-74,"d":"5.30E-74"},"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":7.2e-77,"d":"7.20E-77"},"_","_","_","-"]
[null,"_","_","cd06558","_",6,199,0.742308,{"v":1.13209E-83,"d":"1.13E-83"},"_","_","_","-"]
[null,"_","_","PTHR11941","_",5,258,0.973077,{"v":6.2e-88,"d":"6.20E-88"},"_","_","_","-"]
[null,"_","_","PTHR11941:SF140","_",5,258,0.973077,{"v":6.2e-88,"d":"6.20E-88"},"_","_","_","-"]
[]
["AZ49_04240","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",1,120,0.311518,{"v":7.7e-37,"d":"7.70E-37"},"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",228,382,0.403141,{"v":1.01e-59,"d":"1.01E-59"},"AcylCo_DH-like_C","Homologous_superfamily","Acyl-CoA dehydrogenase-like, C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR013786","PFAM","PF02771","Acyl-CoA_dh_N",7,117,0.287958,{"v":3.9e-31,"d":"3.90E-31"},"AcylCoA_DH/ox_N","Domain","Acyl-CoA dehydrogenase/oxidase, N-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR009100","SSF","SSF56645","SSF56645",2,243,0.63089,{"v":7.33e-77,"d":"7.33E-77"},"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",230,380,0.39267,{"v":3.6e-49,"d":"3.60E-49"},"AcylCo_DH/oxidase_C","Domain","Acyl-CoA dehydrogenase/oxidase C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006091","PFAM","PF02770","Acyl-CoA_dh_M",122,218,0.251309,{"v":8.3e-22,"d":"8.30E-22"},"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",339,358,0.0497382,"_","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","_",4,97,0.243455,0.5,"_","_","_","-"]
[null,"_","_","PIRSF016578","_",130,381,0.657068,6.9e-14,"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",121,235,0.298429,{"v":1.2e-39,"d":"1.20E-39"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",236,382,0.382199,{"v":6.9e-58,"d":"6.90E-58"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",2,381,0.992147,{"v":8.9E-146,"d":"8.90E-146"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",2,381,0.992147,{"v":8.9E-146,"d":"8.90E-146"},"_","_","_","-"]
[null,"_","_","cd01158","_",7,382,0.981675,0,"_","_","_","-"]
[null,"_","_","Coil","_",5,25,0.052356,"_","_","_","_","-"]
[]
["AZ49_06245","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",1,115,0.300792,{"v":6.6e-35,"d":"6.60E-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":1.1E-58,"d":"1.10E-58"},"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":4.3E-27,"d":"4.30E-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":4.45e-75,"d":"4.45E-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":2e-47,"d":"2.00E-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":3.6e-28,"d":"3.60E-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","_",3,372,0.973615,{"v":2.3e-22,"d":"2.30E-22"},"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",119,234,0.30343,{"v":5.6E-42,"d":"5.60E-42"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",235,379,0.379947,{"v":2.4e-57,"d":"2.40E-57"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",2,378,0.992084,{"v":6.8e-141,"d":"6.80E-141"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",2,378,0.992084,{"v":6.8e-141,"d":"6.80E-141"},"_","_","_","-"]
[]
["AZ49_06555","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",1,123,0.318538,{"v":1.4e-31,"d":"1.40E-31"},"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,{"v":1.4e-60,"d":"1.40E-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",6,120,0.29765,{"v":3.2e-26,"d":"3.20E-26"},"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":1.7e-78,"d":"1.70E-78"},"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",233,377,0.375979,{"v":2.5e-50,"d":"2.50E-50"},"AcylCo_DH/oxidase_C","Domain","Acyl-CoA dehydrogenase/oxidase C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006091","PFAM","PF02770","Acyl-CoA_dh_M",125,221,0.250653,{"v":2.3e-27,"d":"2.30E-27"},"Acyl-CoA_Oxase/DH_cen-dom","Domain","Acyl-CoA oxidase/dehydrogenase, central domain","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00072","ACYL_COA_DH_1",127,139,0.0313316,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00073","ACYL_COA_DH_2",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","_",6,383,0.984334,{"v":2.3e-17,"d":"2.30E-17"},"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",124,238,0.29765,{"v":3.5E-43,"d":"3.50E-43"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",239,383,0.375979,{"v":1.7e-55,"d":"1.70E-55"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",2,382,0.992167,{"v":2.1e-145,"d":"2.10E-145"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",2,382,0.992167,{"v":2.1e-145,"d":"2.10E-145"},"_","_","_","-"]
[null,"_","_","cd01158","_",7,383,0.981723,0,"_","_","_","-"]
[]
["AZ49_06560","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",2,210,0.77037,{"v":8.33911e-95,"d":"8.34E-95"},"ETF_beta_N","Domain","Electron transfer flavoprotein, beta subunit, N-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",24,214,0.703704,{"v":2.4e-53,"d":"2.40E-53"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",22,219,0.72963,{"v":1.6e-56,"d":"1.60E-56"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014729","CATHGENE3D","G3DSA:3.40.50.620","G3DSA:3.40.50.620",1,270,0.996296,{"v":2.5e-95,"d":"2.50E-95"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR012255","PANTHER","PTHR21294","PTHR21294",1,269,0.992593,{"v":7.4E-93,"d":"7.40E-93"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"IPR012255","PIRSF","PIRSF000090","Beta-ETF",1,270,0.996296,{"v":3.2e-98,"d":"3.20E-98"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"_","_","SSF52402","_",1,254,0.937037,2.51E-77,"_","_","_","-"]
[null,"_","_","PTHR21294:SF17","_",1,269,0.992593,{"v":7.4E-93,"d":"7.40E-93"},"_","_","_","-"]
[]
["AZ49_06565","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",8,186,0.526627,{"v":1.63321E-58,"d":"1.63E-58"},"ETF_alpha_N","Domain","Electron transfer flavoprotein, alpha subunit, N-terminal","-"]
[null,"IPR029035","SSF","SSF52467","SSF52467",209,331,0.360947,{"v":4.25e-45,"d":"4.25E-45"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR018206","PROSITE","PS00696","ETF_ALPHA",275,301,0.0769231,"_","ETF_asu_C_CS","Conserved_site","Electron transfer flavoprotein subunit alpha, conserved site","-"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",209,294,0.251479,{"v":5e-33,"d":"5.00E-33"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",11,187,0.52071,{"v":1.7e-47,"d":"1.70E-47"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",9,198,0.559172,{"v":1.4E-49,"d":"1.40E-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",5,204,0.588757,{"v":4.8e-77,"d":"4.80E-77"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR001308","PIRSF","PIRSF000089","Electra_flavoP_a",5,336,0.97929,{"v":8e-123,"d":"8.00E-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","_",205,337,0.390533,{"v":1.2E-55,"d":"1.20E-55"},"_","_","_","-"]
[null,"_","_","SSF52402","_",7,202,0.576923,1.26E-57,"_","_","_","-"]
[null,"_","_","PTHR43153","_",1,336,0.991124,{"v":3.8E-137,"d":"3.80E-137"},"_","_","_","-"]
[null,"_","_","PTHR43153:SF9","_",1,336,0.991124,{"v":3.8E-137,"d":"3.80E-137"},"_","_","_","-"]
[]
["AZ49_07320","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",2,203,0.773077,{"v":1.96789e-71,"d":"1.97E-71"},"ETF_beta_N","Domain","Electron transfer flavoprotein, beta subunit, N-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",24,206,0.7,{"v":7.8e-45,"d":"7.80E-45"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",21,211,0.730769,{"v":9.6e-49,"d":"9.60E-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",1,260,0.996154,{"v":2.8e-84,"d":"2.80E-84"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR012255","PANTHER","PTHR21294","PTHR21294",1,258,0.988462,{"v":1.4e-79,"d":"1.40E-79"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"IPR012255","PIRSF","PIRSF000090","Beta-ETF",1,260,0.996154,{"v":5.7e-75,"d":"5.70E-75"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"_","_","SSF52402","_",1,254,0.973077,2.58E-65,"_","_","_","-"]
[null,"_","_","PTHR21294:SF17","_",1,258,0.988462,{"v":1.4e-79,"d":"1.40E-79"},"_","_","_","-"]
[]
["AZ49_07325","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",6,182,0.528529,{"v":5.67455e-43,"d":"5.67E-43"},"ETF_alpha_N","Domain","Electron transfer flavoprotein, alpha subunit, N-terminal","-"]
[null,"IPR029035","SSF","SSF52467","SSF52467",209,327,0.354354,{"v":9.81e-43,"d":"9.81E-43"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR018206","PROSITE","PS00696","ETF_ALPHA",272,298,0.0780781,"_","ETF_asu_C_CS","Conserved_site","Electron transfer flavoprotein subunit alpha, conserved site","-"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",210,291,0.243243,{"v":2.8e-30,"d":"2.80E-30"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",9,185,0.528529,{"v":5.7e-42,"d":"5.70E-42"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",7,191,0.552553,{"v":1.2E-37,"d":"1.20E-37"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014729","CATHGENE3D","G3DSA:3.40.50.620","G3DSA:3.40.50.620",6,187,0.543544,{"v":1.8e-52,"d":"1.80E-52"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR001308","PIRSF","PIRSF000089","Electra_flavoP_a",4,333,0.987988,{"v":8.4e-97,"d":"8.40E-97"},"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","_",6,199,0.57958,{"v":1.26e-48,"d":"1.26E-48"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1220","_",203,333,0.39039,{"v":9.6e-50,"d":"9.60E-50"},"_","_","_","-"]
[null,"_","_","PTHR43153","_",4,332,0.984985,{"v":1e-103,"d":"1.00E-103"},"_","_","_","-"]
[null,"_","_","PTHR43153:SF9","_",4,332,0.984985,{"v":1e-103,"d":"1.00E-103"},"_","_","_","-"]
[]
["AZ49_01090","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",175,186,0.0387324,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PFAM","PF13187","Fer4_9",145,190,0.158451,6e-08,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",166,195,0.102113,10.801,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",243,275,0.112676,8.332,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",132,165,0.116197,8.147,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",209,242,0.116197,6.744,"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",40,135,0.334507,9.4e-08,"Dihydropteroate_synth-like","Homologous_superfamily","Dihydropteroate synthase-like","Biological Process: cellular metabolic process (GO:0044237)"]
[null,"IPR010207","HAMAP","MF_00463","RsxB_RnfB",7,197,0.669014,27.894,"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",7,101,0.330986,{"v":2.3E-21,"d":"2.30E-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",47,80,0.116197,7.9e-10,"4Fe-4S_dom","Domain","4Fe-4S domain","Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"IPR007202","PROFILE","PS51656","4FE4S",35,95,0.211268,23.818,"4Fe-4S_dom","Domain","4Fe-4S domain","Molecular Function: iron-sulfur cluster binding (GO:0051536)"]
[null,"_","_","G3DSA:3.30.70.20","_",212,278,0.232394,1.5e-07,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",149,196,0.165493,1.9E-13,"_","_","_","-"]
[null,"_","_","SSF54862","_",136,271,0.475352,{"v":3.31e-18,"d":"3.31E-18"},"_","_","_","-"]
[null,"_","_","cd10549","_",138,269,0.461268,{"v":6.51463e-21,"d":"6.51E-21"},"_","_","_","-"]
[null,"_","_","PTHR43560","_",7,269,0.922535,{"v":5e-50,"d":"5.00E-50"},"_","_","_","-"]
[]
["AZ49_01095","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",2,191,0.989529,24.067,"Ion_transpt_RnfA/RsxA","Family","Ion-translocating oxidoreductase complex, subunit  RnfA/RsxA","Biological Process: electron transport chain (GO:0022900)"]
[null,"IPR011293","TIGRFAMs","TIGR01943","rnfA",2,191,0.989529,{"v":7.6e-76,"d":"7.60E-76"},"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":1.9e-52,"d":"1.90E-52"},"NqrDE/RnfAE","Family","NqrDE/RnfAE","Cellular Component: membrane (GO:0016020)"]
[null,"IPR003667","PIRSF","PIRSF006102","NQR_DE",1,191,0.994764,{"v":3.6E-51,"d":"3.60E-51"},"NqrDE/RnfAE","Family","NqrDE/RnfAE","Cellular Component: membrane (GO:0016020)"]
[null,"_","_","PTHR30335","_",2,191,0.989529,{"v":4.4e-75,"d":"4.40E-75"},"_","_","_","-"]
[null,"_","_","PTHR30335:SF0","_",2,191,0.989529,{"v":4.4e-75,"d":"4.40E-75"},"_","_","_","-"]
[]
["AZ49_01100","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR010968","TIGRFAMs","TIGR01948","rnfE",5,193,0.908213,{"v":6.4e-68,"d":"6.40E-68"},"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":2.2e-58,"d":"2.20E-58"},"NqrDE/RnfAE","Family","NqrDE/RnfAE","Cellular Component: membrane (GO:0016020)"]
[null,"IPR003667","PIRSF","PIRSF006102","NQR_DE",1,204,0.980676,{"v":4.8E-67,"d":"4.80E-67"},"NqrDE/RnfAE","Family","NqrDE/RnfAE","Cellular Component: membrane (GO:0016020)"]
[null,"_","_","PTHR30586","_",4,199,0.942029,{"v":7.5e-68,"d":"7.50E-68"},"_","_","_","-"]
[]
["AZ49_01105","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",6,179,0.945355,20.829,"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",8,178,0.928962,{"v":1.3e-37,"d":"1.30E-37"},"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",1,182,0.989071,{"v":1.1e-34,"d":"1.10E-34"},"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",15,176,0.879781,{"v":1.3e-32,"d":"1.30E-32"},"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",89,174,0.464481,{"v":3e-19,"d":"3.00E-19"},"FMN-bd","Domain","FMN-binding","Molecular Function: FMN binding (GO:0010181); Cellular Component: membrane (GO:0016020)"]
[null,"IPR007329","SMART","SM00900","FMN_bind",89,177,0.480874,{"v":6e-26,"d":"6.00E-26"},"FMN-bd","Domain","FMN-binding","Molecular Function: FMN binding (GO:0010181); Cellular Component: membrane (GO:0016020)"]
[null,"_","_","PS51257","_",1,25,0.131148,5,"_","_","_","-"]
[]
["AZ49_01110","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",22,339,0.921512,24.762,"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",21,341,0.930233,{"v":3.2e-105,"d":"3.20E-105"},"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",27,337,0.901163,{"v":2.3e-97,"d":"2.30E-97"},"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",21,341,0.930233,{"v":3.2e-105,"d":"3.20E-105"},"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",24,337,0.909884,{"v":1.5E-111,"d":"1.50E-111"},"NqrB/RnfD","Family","Ion-translocating oxidoreductase NqrB/RnfD","Cellular Component: membrane (GO:0016020); Biological Process: transmembrane transport (GO:0055085)"]
[]
["AZ49_01115","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",134,283,0.330377,3.6e-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":6.54e-58,"d":"6.54E-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":9.1e-33,"d":"9.10E-33"},"RnfC_N","Domain","RnfC Barrel sandwich hybrid domain","-"]
[null,"IPR019554","PFAM","PF10531","SLBB",288,335,0.104213,3e-14,"Soluble_ligand-bd","Domain","Soluble ligand binding domain","-"]
[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,"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,"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":8e-47,"d":"8.00E-47"},"Nuo51_FMN-bd","Domain","NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain","-"]
[null,"IPR010208","HAMAP","MF_00461","RsxC_RnfC",1,451,0.997783,146.142,"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",1,448,0.991131,{"v":2.5E-156,"d":"2.50E-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":5.6e-162,"d":"5.60E-162"},"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",322,431,0.241685,3.27E-17,"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,"_","_","_","-"]

{"sheet":"PSortB","index":13,"n_rows":38,"n_cols":4,"rows_kept":38}
["CDS","PsortB Localization","Score","Gram"]
["AZ49_00320","Cytoplasmic",7.5,"+"]
["AZ49_00330","CytoplasmicMembrane",10,"+"]
["AZ49_04210","CytoplasmicMembrane",10,"+"]
["AZ49_00515","Cytoplasmic",7.5,"+"]
["AZ49_11470","Cytoplasmic",9.97,"+"]
["AZ49_01710","Unknown",2.5,"+"]
["AZ49_05490","Cytoplasmic",7.5,"+"]
["AZ49_06970","Unknown",2.5,"+"]
["AZ49_06950","Cytoplasmic",9.97,"+"]
["AZ49AM_0981","Cytoplasmic",7.5,"+"]
["AZ49_00050","Cytoplasmic",9.64,"+"]
["AZ49_02525","Cytoplasmic",9.97,"+"]
["AZ49_03535","Cytoplasmic",7.5,"+"]
["AZ49_05685","Cytoplasmic",9.97,"+"]
["AZ49_05690","Cytoplasmic",9.97,"+"]
["AZ49_10655","Cytoplasmic",7.5,"+"]
["AZ49_00555","Cytoplasmic",7.5,"+"]
["AZ49_00545","Cytoplasmic",7.5,"+"]
["AZ49_00550","Cytoplasmic",7.5,"+"]
["AZ49_02170","Unknown",2.5,"+"]
["AZ49_02175","Cytoplasmic",7.5,"+"]
["AZ49_00650","Cytoplasmic",9.97,"+"]
["AZ49_02755","Cytoplasmic",9.97,"+"]
["AZ49_02760","Cytoplasmic",7.5,"+"]
["AZ49_04240","Cytoplasmic",9.97,"+"]
["AZ49_06245","Cytoplasmic",9.97,"+"]
["AZ49_06555","Cytoplasmic",9.97,"+"]
["AZ49_06560","Cytoplasmic",7.5,"+"]
["AZ49_06565","Cytoplasmic",7.5,"+"]
["AZ49_07320","Unknown",2.5,"+"]
["AZ49_07325","Cytoplasmic",7.5,"+"]
["AZ49_01090","Cytoplasmic",9.97,"+"]
["AZ49_01095","CytoplasmicMembrane",10,"+"]
["AZ49_01100","CytoplasmicMembrane",10,"+"]
["AZ49_01105","Unknown",3.33,"+"]
["AZ49_01110","CytoplasmicMembrane",10,"+"]
["AZ49_01115","Cytoplasmic",7.5,"+"]