{"text_format":"3","workbook":"xlsx","n_sheets":15,"sheets":["reactions","instruction","start","gene features","protein features","MaGe-Curated annotations","SwissProt","UniFIRE ","PRIAM EC number","COG","EGGNOG","FigFam","InterProScan","Sheet1","PSortB"],"not_rendered":{"defined_names":1},"read":"whole","date_system":"1900"}

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

{"sheet":"instruction","index":1,"n_rows":14,"n_cols":2,"rows_kept":14,"merged":[[0,0,0,1]]}
["Additional file 11. Functional annotations of strain Pseudoramibacter alactolyticus ATCC 23263"]
["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":17,"n_cols":13,"rows_kept":17}
["CDS","Strand","length","Begin","End","AMIGene Start","AMIGene Lpcod","AMIGene Apcod","Matrix","Prodigal Begin","Prodigal End","Glimmer Begin","Glimmer End"]
["AEQN01_210010","R",1281,1455276,1456556,1456556,0.995094,0.995094,1,1455276,1456556,1455276,1456556]
["AEQN01_210007","R",1554,1451968,1453611,1453611,0.921484,0.921484,1,1451968,1453521,1451968,1453521]
["AEQN01_180010","R",954,1384153,1385139,1385139,0.946193,0.946193,1,1384153,1385106,1384153,1385106]
["AEQN01_90013","D",3513,508582,512109,508582,0.908342,0.908342,2,508597,512109,508597,512109]
["AEQN01_230157","D",3513,1804563,1808075,1804563,0.973184,0.973184,1,1804563,1808075,1804563,1808075]
["AEQN01_220120","R",846,1586349,1587194,1587053,0.804386,0.937495,1,1586349,1587194,1586349,1587194]
["AEQN01_220121","R",777,1587271,1588047,1588047,0.93696,0.93696,1,1587271,1588047,1587271,1588047]
["AEQN01_220122","R",1185,1588077,1589303,1589174,0.852001,0.929741,1,1588077,1589261,1588077,1589261]
["AEQN01_70057","D",954,365116,366153,365296,0.801346,0.933926,1,365200,366153,365200,366153]
["AEQN01_300005","D",1341,2127786,2129126,2127786,0.98323,0.98323,1,2127786,2129126,2127786,2129126]
["AEQN01_210004","R",1143,1447463,1448605,1448605,0.928957,0.928957,1,1447463,1448605,1447463,1448605]
["AEQN01_220142","D",1146,1608505,1609650,1608505,0.96755,0.96755,1,1608505,1609650,1608505,1609650]
["AEQN01_250027","D",1152,1889242,1890432,1889242,0.955467,0.955467,1,1889281,1890432,1889281,1890432]
["AEQN01_230141","R",1920,1789068,1790987,1790987,0.973962,0.973962,1,1789068,1790987,1789068,1790987]
["AEQN01_220164","D",801,1628561,1629421,1628561,0.948738,0.948738,1,1628621,1629421,1628621,1629421]
["AEQN01_220165","D",1008,1629437,1630444,1629437,0.857189,0.857189,1,1629437,1630444,1629437,1630444]

{"sheet":"gene features","index":3,"n_rows":17,"n_cols":8,"rows_kept":17}
["CDS","GC Content","GC1 Content","GC2 Content","GC3 Content","CAI","GCskew","R/Y ratio"]
["AEQN01_210010",55.35,59.25,37.94,68.85,0.78,-0.069,1.212]
["AEQN01_210007",57.08,50.39,45.37,75.48,0.74,-0.067,0.95]
["AEQN01_180010",60.27,61.95,38.99,79.87,0.74,-0.061,1.047]
["AEQN01_90013",48.59,53.37,40.48,51.92,0.72,-0.062,1.087]
["AEQN01_230157",56.31,56.11,41.42,71.39,0.77,2E-3,1.097]
["AEQN01_220120",51.3,59.93,34.75,59.22,0.8,-0.092,1.215]
["AEQN01_220121",54.57,58.3,39,66.41,0.83,-0.066,1.201]
["AEQN01_220122",53.42,58.73,43.04,58.48,0.75,-0.134,1.166]
["AEQN01_70057",48.95,53.77,38.05,55.03,0.7,-0.028,1.065]
["AEQN01_300005",56.52,57.49,39.6,72.48,0.78,-0.079,1.122]
["AEQN01_210004",51.97,57.22,40.16,58.53,0.76,-0.074,1.125]
["AEQN01_220142",61.43,64.4,43.46,76.44,0.76,-0.043,1.195]
["AEQN01_250027",57.03,56.51,39.32,75.26,0.77,-0.059,1.165]
["AEQN01_230141",60.78,60.62,42.03,79.69,0.78,0.08,1.038]
["AEQN01_220164",51.94,60.67,37.83,57.3,0.74,0.019,1.13]
["AEQN01_220165",58.13,64.58,44.64,65.18,0.76,0.079,0.969]

{"sheet":"protein features","index":4,"n_rows":17,"n_cols":14,"rows_kept":17}
["CDS","Mw (Da)","Hydrophobicity","Tiny","Small","Aliphatic","Aromatic","Non Polar","Polar","Charged","Basic","Acidic","pI","Oxyphobic Index"]
["AEQN01_210010",45597.24,-0.04,31.92,53.52,22.77,7.75,57.28,42.72,26.29,11.97,14.32,4.95,9.19]
["AEQN01_210007",53586.99,1.02,38.3,56.09,30.95,8.51,71.57,28.43,8.9,5.42,3.48,9.07,8.19]
["AEQN01_180010",34206.98,0.22,30.28,51.42,27.13,9.46,62.15,37.85,22.71,11.04,11.67,5.32,9.22]
["AEQN01_90013",128201.24,-0.24,32.31,53.08,18.63,11.88,56.24,43.76,24.87,11.97,12.91,5.25,9.36]
["AEQN01_230157",128258.1,-0.29,32.91,53.16,17.86,11.88,55.9,44.1,24.87,12.39,12.48,5.53,9.6]
["AEQN01_220120",30103.64,0.08,29.54,51.6,25.27,6.41,59.79,40.21,26.33,12.1,14.23,5.02,9.34]
["AEQN01_220121",27890.96,-0.06,31.01,50.78,20.54,6.98,59.69,40.31,26.74,12.02,14.73,4.94,9.77]
["AEQN01_220122",41806.5,0.04,33.76,56.6,22.84,5.33,61.42,38.58,23.35,11.17,12.18,5.29,10.14]
["AEQN01_70057",34533.87,-0.05,30.28,51.42,23.34,9.78,56.78,43.22,21.45,9.78,11.67,4.94,8.85]
["AEQN01_300005",49274.9,-0.25,28.92,55.38,20.18,11.66,56.5,43.5,26.01,12.56,13.45,5.27,9.72]
["AEQN01_210004",41183.25,-0.14,32.89,51.58,18.95,8.95,58.16,41.84,25.53,10.79,14.74,4.73,9.86]
["AEQN01_220142",40193.49,0.02,36.22,52.76,21,6.82,61.94,38.06,24.93,11.55,13.39,5.1,9.61]
["AEQN01_250027",42091.4,-0.13,32.11,50.91,20.1,9.66,55.87,44.13,26.37,12.01,14.36,4.98,9.73]
["AEQN01_230141",68596.87,-0.15,32.39,51.96,20.81,9.08,60.09,39.91,23.94,12.52,11.42,6.75,9.34]
["AEQN01_220164",28824.82,-0.22,28.95,52.63,23.68,4.89,54.51,45.49,30.08,12.41,17.67,4.64,9.25]
["AEQN01_220165",35231.54,0.01,34.93,59.1,23.58,7.16,59.7,40.3,23.88,10.45,13.43,4.79,9.57]

{"sheet":"MaGe-Curated annotations","index":5,"n_rows":479,"n_cols":26,"rows_kept":479}
["AEQN01_210010","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_3221",null,"Clostridiales BL-6","larA","Lactate racemase","LACTATE-RACEMASE-RXN ; RHEA:10963 ;",1,1,63.85,0,1,1,"_","5.1.2.1","2 : Cytoplasmic","_","e : enzyme",24710389,"2a : Function from experimental evidences in other organisms",1,425,426,1,425,426]
[null,"CLOSTRIBL3_v1_11116",null,"Clostridiaceae BL-3","larA","Lactate racemase","LACTATE-RACEMASE-RXN ; RHEA:10960 ;",0.98357,0.98821,54.18,{"v":2E-155,"d":"2.00E-155"},1,1,"4.S.107 : L-lactate ;","5.1.2.1","2 : Cytoplasmic","_","e : enzyme",24710389,"1c : Function from experimental evidences in the studied genus",5,423,426,6,424,424]
[null,"CD630_11700",null,"Clostridium difficile 630","_","Conserved hypothetical protein","_",0.99061,0.99528,50.95,{"v":1e-147,"d":"1.00E-147"},1,1,"_","_","1 : Unknown","_","u : unknown","_","4 : Unknown function but conserved in other organisms",1,422,426,2,423,424]
[]
["AEQN01_210007","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","_",0.98646,1.00394,49.8,{"v":3E-176,"d":"3.00E-176"},1,1,"4.S.98 : lactate ;","_","11 : Membrane","_","t : transporter",10508058,"2a : Function from experimental evidences in other organisms",6,514,517,7,506,508]
[null,"CLOSTRIBL6_v1_3223",null,"Clostridiales BL-6","lctP","L-lactate permease","_",0.96325,0.96325,51.81,{"v":8e-168,"d":"8.00E-168"},1,1,"_","_","11 : Membrane","_","t : transporter",10508058,"2a : Function from experimental evidences in other organisms",8,502,517,6,503,517]
[null,"ECED1_5018","_","Escherichia coli ED1a","_","L-lactate permease","_",0.96718,0.96905,40.52,{"v":6e-127,"d":"6.00E-127"},1,1,"_","_","1 : Unknown","7 : Transport and binding proteins ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,505,517,7,507,518]
[null,"HELPY_0143","_","Helicobacter pylori B38","_","Putative L-lactate permease, LctP family; putative membrane protein","_",0.96189,1.02515,35.28,{"v":1e-96,"d":"1.00E-96"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ; 4.2.A.14 : The Lactate Permease (LctP) Family ; 6.1 : Membrane ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","7.3 : Carbohydrates, organic alcohols, and acids ;","t : transporter","11785976, 8407843","3 : Putative function from multiple computational evidences",7,511,517,19,544,551]
[null,"PP_4735",null,"Pseudomonas putida KT2440","lldP","L-lactate permease","_",0.94964,1.02128,35.42,{"v":1e-90,"d":"1.00E-90"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ; 6.1 : Membrane ; 7.3 : Inner membrane ;","_","5 : Inner membrane protein","7.3 : Carbohydrates, organic alcohols, and acids ; 16.1 : Circulate ;","t : transporter","19196979, 22408166, 614007, 11785976","1b : Function from experimental evidences in the studied species",7,506,517,19,541,556]
[]
["AEQN01_180010","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_2205","_","Clostridiales BL-4","ldh","L-lactate dehydrogenase","L-LACTATE-DEHYDROGENASE-RXN ; RHEA:23444 ;",0.97161,0.98089,54.22,{"v":7e-120,"d":"7.00E-120"},1,1,"_","1.1.1.27","2 : Cytoplasmic","_","e : enzyme",15007569,"2a : Function from experimental evidences in other organisms",5,312,317,3,309,314]
[null,"BSU03050","_","Bacillus subtilis 168","lctE","L-lactate dehydrogenase","L-LACTATE-DEHYDROGENASE-RXN ; RHEA:23444 ;",0.96262,0.97476,48.54,{"v":7e-100,"d":"7.00E-100"},1,1,"_","1.1.1.27","2 : Cytoplasmic","16.10 : Respire ;","e : enzyme","10809684, 16207915, 19383131","1a : Function from experimental evidences in the studied strain",5,312,317,5,311,321]
[null,"SSV_v1_1093","_","Streptococcus sanguinis 2908","ldh","L-lactate dehydrogenase","L-LACTATE-DEHYDROGENASE-RXN ;",0.95122,0.98423,48.4,{"v":2e-97,"d":"2.00E-97"},1,1,"_","1.1.1.27","2 : Cytoplasmic","16.10 : Respire ;","e : enzyme","10809684, 16207915","2a : Function from experimental evidences in other organisms",7,313,317,8,314,328]
[null,"BN424_462","_","Carnobacterium maltaromaticum LMA28 v1","ldh1","L-lactate dehydrogenase 1","L-LACTATE-DEHYDROGENASE-RXN ; RHEA:23444 ;",0.96885,0.98107,46.3,{"v":1e-96,"d":"1.00E-96"},1,1,"_","1.1.1.27","2 : Cytoplasmic","6.8 : Glycolysis/gluconeogenesis ;","e : enzyme","6411465, 1768113","2a : Function from experimental evidences in other organisms",7,316,317,10,318,321]
[null,"BTCD_v1_2573","_","Brochothrix thermosphacta CD337","lctE","L-lactate dehydrogenase","L-LACTATE-DEHYDROGENASE-RXN ; RHEA:23444 ;",0.97476,0.99677,47.9,{"v":3e-94,"d":"3.00E-94"},1,1,"_","1.1.1.27","2 : Cytoplasmic","16.10 : Respire ;","e : enzyme","10809684, 16207915, 19383131, 10644484, 16085862, 15644899","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,315,317,7,309,310]
[null,"AZOLI_2908","_","Azospirillum lipoferum 4B","ldh","L-lactate dehydrogenase","_",0.97792,0.98101,44.19,{"v":2e-86,"d":"2.00E-86"},1,1,"_","1.1.1.27","10 : Secreted","6.8 : Glycolysis/gluconeogenesis ;","e : enzyme",10809684,"2a : Function from experimental evidences in other organisms",8,316,317,2,309,316]
[null,"CLOSTRIBL6_v1_2713","_","Clostridiales BL-6","ldh","L-lactate dehydrogenase","L-LACTATE-DEHYDROGENASE-RXN ; RHEA:23444 ;",0.95899,0.95899,45.07,{"v":9e-86,"d":"9.00E-86"},1,1,"_","1.1.1.27","2 : Cytoplasmic","16.10 : Respire ;","e : enzyme","10809684, 16207915, 19383131","2a : Function from experimental evidences in other organisms",7,309,317,6,308,317]
[null,"BN10v3_10012","_","Tetrasphaera elongata Lp2","ldh","L-lactate dehydrogenase","_",0.95584,0.9619,39.93,{"v":8E-73,"d":"8.00E-73"},1,1,"_","1.1.1.27","2 : Cytoplasmic","6.7 : Fermentation ;","e : enzyme","10809684, 16207915","2a : Function from experimental evidences in other organisms",8,309,317,7,307,315]
[null,"CLOSTRIBL3_v1_10012","_","Clostridiaceae BL-3","ldh2","L-lactate dehydrogenase 2","RHEA:23444 ;",0.92812,0.93691,38.38,{"v":4E-70,"d":"4.00E-70"},1,1,"_","1.1.1.27","2 : Cytoplasmic","_","e : enzyme",11466286,"1c : Function from experimental evidences in the studied genus",8,300,317,7,301,320]
[null,"Ent638_2002","_","Enterobacter sp. 638","ldh","L-lactate dehydrogenase 2 (L-LDH 2)","_",0.90323,0.97161,35.39,{"v":1e-66,"d":"1.00E-66"},1,1,"_","1.1.1.27","2 : Cytoplasmic","6.8 : Glycolysis/gluconeogenesis ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,312,317,33,337,341]
[]
["AEQN01_90013","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_10343","_","Clostridiaceae BL-3","pfo","Pyruvate-flavodoxin oxidoreductase","PYFLAVOXRE-RXN ; RHEA:12765 ;",1.00171,1.00342,63.14,0,1,1,"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",1,1167,1170,1,1163,1168]
[null,"CD630_26820","_","Clostridium difficile 630","pfo","Pyruvate-ferredoxin oxidoreductase","_",1.00254,1.01026,62.52,0,1,1,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"1c : Function from experimental evidences in the studied genus",1,1167,1170,1,1176,1179]
[null,"SBF1_v1_1620011","_","Desulfosporosinus sp. SbF1","pfoA_2","pyruvate synthase","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.99744,1.00085,61.83,0,1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,1165,1170,1,1166,1174]
[null,"CLOSTRIBL6_v1_0279","_","Clostridiales BL-6","PFOF","Pyruvate:ferredoxin oxidoreductase","PYRUFLAVREDUCT-RXN ; RHEA:12768 ;",0.99747,1.01026,57.95,0,1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme","8620891, 7608066, 9495749","2a : Function from experimental evidences in other organisms",1,1163,1170,1,1177,1185]
[null,"BN11v3_340013",null,"Tetrasphaera australiensis Ben110","_","putative pyruvate-flavodoxin oxidoreductase","_",0.98994,1.0094,46.06,0,1,2,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",8352652,"3 : Putative function from multiple computational evidences",6,1165,1170,7,1174,1193]
[null,"SBF1_v1_1030024",null,"Desulfosporosinus sp. SbF1","pfoA_3a","fragment of pyruvate synthase (part 1/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.58803,0.97589,62.94,0,3,1,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",4,686,1170,3,688,705]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.39145,0.97447,66.38,0,2,1,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"2a : Function from experimental evidences in other organisms",1,458,1170,1,458,470]
[null,"SBF1_v1_1030023",null,"Desulfosporosinus sp. SbF1","pfoA_3b","fragment of pyruvate synthase (part 2/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.39402,0.98715,57.48,{"v":3e-178,"d":"3.00E-178"},4,1,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",711,1165,1170,1,457,467]
[null,"NBG4_v1_230036","_","Candidatus Sulfobium mesophilum","nifJ","Pyruvate:ferredoxin oxidoreductase","PYRUFLAVREDUCT-RXN ;",0.23162,0.99632,56.83,{"v":1E-100,"d":"1.00E-100"},1,1,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","1 : Unknown","6 : Energy metabolism ;","e : enzyme",11167002,"2a : Function from experimental evidences in other organisms",1,271,1170,1,271,272]
[]
["AEQN01_230157","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL3_v1_20129",null,"Clostridiaceae BL-3","pfo","Pyruvate-flavodoxin oxidoreductase","PYRUFLAVREDUCT-RXN ; RHEA:12765 ;",0.99658,0.99658,58.92,0,3,2,"1.3 : Energy metabolism (carbon) ;","1.2.7.1","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","8620891, 7608066, 9495749","1c : Function from experimental evidences in the studied genus",8,1166,1170,11,1169,1170]
[null,"CLOSTRIBL4_v1_0841","_","Clostridiales BL-4","PFOF","Pyruvate:ferredoxin oxidoreductase","PYRUFLAVREDUCT-RXN ; RHEA:12768 ;",1.00084,1.01282,57.3,0,1,1,"_","1.2.7.1","2 : Cytoplasmic","_","e : enzyme",18631365,"2a : Function from experimental evidences in other organisms",2,1167,1170,3,1182,1184]
[null,"CLOAM0324","_","Candidatus Cloacamonas acidaminovorans Evry","_","putative pyruvate-ferredoxin oxidoreductase (por-like) or pyruvate-flavodoxin oxidoreductase (ydbK-like), 4Fe-4S domain","_",1.00426,1.00684,52.38,0,1,1,"1.7.1 : Unassigned reversible reactions ; 1.1.2.3 : Propionate degradation ; 1.3.5 : Fermentation ;","1.2.7.1","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",6,1166,1170,7,1171,1173]
[null,"AZOLI_p30297","_","Azospirillum lipoferum 4B","_","putative pyruvate-ferredoxin/flavodoxin oxidoreductase","_",0.99915,1.00085,49.36,0,1,1,"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",8,1158,1170,1,1160,1172]
[null,"BN11v3_340013","_","Tetrasphaera australiensis Ben110","_","putative pyruvate-flavodoxin oxidoreductase","_",0.9891,1.00855,46.36,0,1,1,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",8352652,"3 : Putative function from multiple computational evidences",8,1169,1170,9,1181,1193]
[null,"ECK1374","_","Escherichia coli K12","ydbK","putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; 4Fe-4S cluster binding protein","PYRUFLAVREDUCT-RXN ;",1.00426,1.00769,47.58,0,1,1,"1.7.1 : Unassigned reversible reactions ;","_","1 : Unknown","16.11 : Scavenge (Catabolism) ; 5 : Central intermediary metabolism ;","e : enzyme",9025293,"3 : Putative function from multiple computational evidences",8,1170,1170,4,1169,1174]
[null,"BN874v1_1210009","_","Candidatus Contendobacter odensis Run_B_J11","_","putative pyruvate-flavodoxin oxidoreductase (nifJ)","_",1.0067,1.02735,46.01,0,1,1,"_","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",3,1168,1170,4,1183,1194]
[null,"Ent638_2136","_","Enterobacter sp. 638","ydbK","Putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; 4Fe-4S cluster binding protein","_",1.00341,1.00684,47.03,0,1,1,"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)",8,1170,1170,4,1169,1174]
[null,"Spro_2604","_","Serratia proteamaculans 568","_","Putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; 4Fe-4S cluster binding protein (NifJ)","_",1.0034,1.0094,46.74,0,1,1,"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",9,1168,1170,5,1170,1177]
[null,"BN873v1_150048","_","Candidatus Competibacter denitrificans Run_A_D11","_","putative pyruvate-flavodoxin oxidoreductase (nifJ)","_",1.00335,1.02308,45.95,0,1,1,"_","1.2.7.-","1 : Unknown","5 : Central intermediary metabolism ; 5.6 : Nitrogen fixation ;","e : enzyme","11167002, 21317262, 8415612","3 : Putative function from multiple computational evidences",3,1168,1170,4,1183,1193]
[null,"FRAAL3253","_","Frankia alni ACN14a","_","Pyruvate-flavodoxin oxidoreductase","_",0.9983,1.00256,46.89,0,1,1,"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)",8,1162,1170,6,1159,1175]
[null,"SBF1_v1_1030024",null,"Desulfosporosinus sp. SbF1","pfoA_3a","fragment of pyruvate synthase (part 1/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.59744,0.99149,60.66,0,3,2,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",4,696,1170,3,698,705]
[null,"VCA0530","_","Vibrio cholerae N16961","_","putative Pyruvate-flavodoxin oxidoreductase","_",0.94444,1.0241,39.28,0,1,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",7,1098,1170,4,1072,1079]
[null,"BN1095v2_250042",null,"Clostridium difficile MID11 7032989","pfo","Pyruvate-ferredoxin oxidoreductase","_",0.39145,0.97447,61.57,0,2,2,"_","1.2.7.-","2 : Cytoplasmic","_","e : enzyme",10486982,"2a : Function from experimental evidences in other organisms",1,458,1170,1,458,470]
[null,"SBF1_v1_1030023",null,"Desulfosporosinus sp. SbF1","pfoA_3b","fragment of pyruvate synthase (part 2/2)","PYRUFLAVREDUCT-RXN ; PYFLAVOXRE-RXN ; RHEA:12768 ;",0.39829,0.99786,56.22,{"v":5e-173,"d":"5.00E-173"},4,2,"1.7.1 : Unassigned reversible reactions ;","1.2.7.1","2 : Cytoplasmic","5 : Central intermediary metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",9025293,"2a : Function from experimental evidences in other organisms",711,1169,1170,1,464,467]
[]
["AEQN01_220120","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL4_v1_1869",null,"Clostridiales BL-4","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",1,1.00717,71.53,{"v":1e-140,"d":"1.00E-140"},1,1,"_","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,281,281,1,279,279]
[null,"CLOSTRIBL6_v1_0126",null,"Clostridiales BL-6","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.99644,1.00719,67.5,{"v":2e-134,"d":"2.00E-134"},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",1,280,281,1,278,278]
[null,"CLOSTRIBL3_v1_20313",null,"Clostridiaceae BL-3","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",1,1.00356,62.06,{"v":5e-114,"d":"5.00E-114"},1,1,"_","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286, 8001771","1c : Function from experimental evidences in the studied genus",2,281,281,3,282,282]
[null,"CD630_10580",null,"Clostridium difficile 630","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",1.00712,1.00712,56.18,{"v":7e-101,"d":"7.00E-101"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","6 : Energy metabolism ;","e : enzyme","15991056, 18060402, 7576770","1c : Function from experimental evidences in the studied genus",1,281,281,1,281,281]
[null,"NBG4_v1_200002",null,"Candidatus Sulfobium mesophilum","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:22432 ;",0.99645,1,49.47,{"v":7e-87,"d":"7.00E-87"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",23468890,"2a : Function from experimental evidences in other organisms",2,279,281,5,281,282]
[null,"MGMSRv2_1554","_","Magnetospirillum gryphiswaldense MSR-1 v2","mmgB","3-hydroxybutyryl-CoA dehydrogenase,containing NAD(P)-binding domain","_",0.92739,1,48.75,{"v":7e-85,"d":"7.00E-85"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",8759838,"2b : Function from indirect experimental evidences (e.g. phenotypes)",2,280,281,17,295,303]
[null,"AZOLI_p50301","_","Azospirillum lipoferum 4B","hbdA1","3-hydroxybutyryl-CoA dehydrogenase","_",0.96575,1.00356,46.81,{"v":7e-84,"d":"7.00E-84"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.1.1.157","2 : Cytoplasmic","3.1 : Biosynthesis ;","e : enzyme","11466286, 12597275, 8655474, 8759838, 8969508","2a : Function from experimental evidences in other organisms",2,281,281,6,285,292]
[null,"BN381v2_100132","_","Candidatus Microthrix parvicella RN1","_","putative dehydrogenase","_",0.93069,1.00356,46.45,{"v":8e-84,"d":"8.00E-84"},1,1,"_","_","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","12846838, 8001771, 1699931","3 : Putative function from multiple computational evidences",2,281,281,24,303,303]
[null,"BSU24160",null,"Bacillus subtilis 168","mmgB","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.97561,0.99644,48.21,{"v":9e-84,"d":"9.00E-84"},1,1,"2.4 : Metabolism of lipids ;","1.1.1.157","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8759838, 18461320, 28956599","1a : Function from experimental evidences in the studied strain",2,279,281,5,282,287]
[null,"BRADO3444",null,"Bradyrhizobium sp. ORS278","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.99293,1,48.75,{"v":3e-83,"d":"3.00E-83"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","2 : Cytoplasmic","16.7 : Manage energy ;","e : enzyme",1444364,"2a : Function from experimental evidences in other organisms",3,281,281,5,283,283]
[null,"AZCBGv1_p190002","_","Azospirillum brasilense CBG497","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.96575,1.00356,47.52,{"v":7e-82,"d":"7.00E-82"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.1.1.157","2 : Cytoplasmic","3.1 : Biosynthesis ;","e : enzyme","11466286, 12597275, 8655474, 8759838, 8969508","2a : Function from experimental evidences in other organisms",2,281,281,6,285,292]
[null,"RALTA_A0220","_","Cupriavidus taiwanensis LMG19424","_","3-HYDROXYBUTYRYL-COA DEHYDROGENASE","_",0.98944,1,47.33,{"v":2e-80,"d":"2.00E-80"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","1 : Unknown","3.2 : Degradation ;  6 : Energy metabolism ;","e : enzyme",8655474,"2b : Function from indirect experimental evidences (e.g. phenotypes)",3,281,281,6,284,284]
[null,"PSEEN3198",null,"Pseudomonas entomophila L48","paaH","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.98577,1.00727,47.65,{"v":4e-80,"d":"4.00E-80"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,279,281,1,275,275]
[null,"CMR15v5_0701","_","Ralstonia solanacearum CMR15","_","3-HYDROXYBUTYRYL-COA DEHYDROGENASE","_",0.98944,1,46.62,{"v":6e-80,"d":"6.00E-80"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","1 : Unknown","3.2 : Degradation ; 6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,281,281,6,284,284]
[null,"BBta_4257","_","Bradyrhizobium sp. BTAi1","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.97153,1.00738,47.62,{"v":5E-79,"d":"5.00E-79"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","2 : Cytoplasmic","16.7 : Manage energy ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",11,281,281,1,271,271]
[null,"Rmet_0212","_","Cupriavidus metallidurans CH34","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.98944,1,46.62,{"v":1E-78,"d":"1.00E-78"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.5 : Building block biosynthesis ; 1.5.4 : Fatty acid and phosphatidic acid ;","1.1.1.157","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,281,281,6,284,284]
[null,"BDBv6_40067",null,"Blood disease bacterium R229","_","3-HYDROXYBUTYRYL-COA DEHYDROGENASE","_",0.98944,1,45.91,{"v":2E-78,"d":"2.00E-78"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","1 : Unknown","3.2 : Degradation ; 6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,281,281,6,284,284]
[null,"PSHAa0399","_","Pseudoalteromonas haloplanktis TAC125","bhbD","3-hydroxybutyryl-CoA dehydrogenase (Beta- hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",1.00356,1.00356,46.1,{"v":3e-78,"d":"3.00E-78"},1,1,"_","1.1.1.157","unknown","_","e : enzyme",8001771,"2a : Function from experimental evidences in other organisms",1,279,281,1,281,281]
[null,"Mchl_1824","_","Methylobacterium extorquens CM4","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.95222,0.99288,46.59,{"v":1e-74,"d":"1.00E-74"},1,1,"_","1.1.1.157","1 : Unknown","_","e : enzyme","2687255, 8655474","2a : Function from experimental evidences in other organisms",3,279,281,8,284,293]
[null,"METDI2209","_","Methylobacterium extorquens DM4","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.92079,0.99288,46.59,{"v":2e-74,"d":"2.00E-74"},1,1,"_","1.1.1.157","1 : Unknown","_","e : enzyme","2687255, 8655474","2a : Function from experimental evidences in other organisms",3,279,281,18,294,303]
[null,"BN10v3_1170022","_","Tetrasphaera elongata Lp2","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD))","_",0.47208,0.99288,45.88,{"v":8e-74,"d":"8.00E-74"},1,1,"_","1.1.1.157","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,279,281,315,591,591]
[null,"BN11v3_1490005","_","Tetrasphaera australiensis Ben110","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD)","_",0.47128,0.99288,45.16,{"v":2E-73,"d":"2.00E-73"},1,1,"_","1.1.1.157","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",1444364,"3 : Putative function from multiple computational evidences",3,279,281,315,591,592]
[null,"BN12v2_1150036","_","Tetrasphaera japonica T1-X7","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD))","_",0.47297,0.99644,41.79,{"v":5e-73,"d":"5.00E-73"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,279,281,7,284,592]
[null,"NIDE3117",null,"Candidatus Nitrospira defluvii","paaH","3-hydroxybutyryl-CoA dehydrogenase","_",0.94898,0.99288,42.65,{"v":1e-72,"d":"1.00E-72"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","1.1.1.157","1 : Unknown","6 : Energy metabolism ; 3.2 : Degradation ;","e : enzyme","10766858, 12846838, 2204034, 8001771, 9748275","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,279,281,9,285,294]
[null,"RM41v1_680007","_","Sinorhizobium sp. Rm41","hbdA","3-hydroxybutyryl-CoA dehydrogenase (Beta- hydroxybutyryl-CoA dehydrogenase) (BHBD)","_",0.96207,0.99288,42.65,{"v":2e-72,"d":"2.00E-72"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 7.1 : Cytoplasm ;","1.1.1.157","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",8655474,"2b : Function from indirect experimental evidences (e.g. phenotypes)",3,279,281,5,281,290]
[null,"ADVE02_v2_10866","_","Methylosinus trichosporium OB3b","hbdA","3-hydroxybutyryl-CoA dehydrogenase","_",0.96246,1.00356,44.68,{"v":4e-72,"d":"4.00E-72"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,279,281,7,284,293]
[null,"BN13v1_460001","_","Tetrasphaera jenkinsii Ben74","_","putative 3-hydroxyacyl-CoA dehydrogenase (Beta-hydroxybutyryl-CoA dehydrogenase (hbd, mmgB, BHBD))","_",0.47128,0.99288,43.01,{"v":2e-69,"d":"2.00E-69"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,279,281,315,591,592]
[null,"BN873v1_210050",null,"Candidatus Competibacter denitrificans Run_A_D11","_","putative hydroxyacyl/hydroxybutyrl -CoA dehydrogenase","_",0.94295,1,41.28,{"v":2e-69,"d":"2.00E-69"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,280,281,5,283,298]
[null,"FRAAL5917","_","Frankia alni ACN14a","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.43417,0.98577,42.96,{"v":1e-68,"d":"1.00E-68"},1,1,"1.7.1 : Unassigned reversible reactions ;","1.1.1.157","1 : Unknown","16.2 : Construct biomass (Anabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,279,281,1,275,638]
[null,"Npun_R3442","_","Nostoc punctiforme ATCC 29133; PCC 73102","_","3-hydroxybutyryl-CoA dehydrogenase","_",0.97569,1,42.35,{"v":3E-68,"d":"3.00E-68"},1,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,280,281,7,285,288]
[null,"BN874v1_720038",null,"Candidatus Contendobacter odensis Run_B_J11","_","putative hydroxyacyl/hydroxybutyrl -CoA dehydrogenase","RXN0-2044 ;",0.94295,1,40.93,{"v":7e-68,"d":"7.00E-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",2,280,281,5,283,298]
[null,"NIDE3103",null,"Candidatus Nitrospira defluvii","_","putative 3-hydroxyacyl-CoA dehydrogenase","_",0.69042,1,41.99,{"v":3e-64,"d":"3.00E-64"},2,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.4 : Anaerobic fatty acid oxidation pathway ; 1.1.2.6 : Aerobic fatty acid oxidation pathway ;","1.1.1.35","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","12535077, 15229654","3 : Putative function from multiple computational evidences",2,280,281,5,281,407]
[null,"BN42v3_20192","_","Mycobacterium canettii STB-K","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98601,1.00356,38.3,{"v":6e-63,"d":"6.00E-63"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,279,281,7,286,286]
[null,"BN44v3_10518","_","Mycobacterium canettii STB-D","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98601,1.00356,37.94,{"v":3e-62,"d":"3.00E-62"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,279,281,7,286,286]
[null,"BN43v3_10507","_","Mycobacterium canettii STB-L","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98601,1.00356,37.94,{"v":3e-62,"d":"3.00E-62"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,279,281,7,286,286]
[null,"BN45v3_10517","_","Mycobacterium canettii STB-J","fadB","Putative 3-hydroxybutyryl-CoA dehydrogenase FadB2 (beta-hydroxybutyryl-coa dehydrogenase) (BHBD)","_",0.98601,1.00356,37.59,{"v":5e-62,"d":"5.00E-62"},1,1,"1 : lipid metabolism ;","1.1.1.157","1 : Unknown","_","e : enzyme","11271494, 12081975, 12657046, 15525680","3 : Putative function from multiple computational evidences",2,279,281,7,286,286]
[null,"SCFA_v1_130011",null,"Ca. Phosphitivorax anaerolimi F81","paaF","Enoyl-CoA hydratase/isomerase family (3-hydroxybutyryl-CoA dehydratase (Crotonase))","RXN-11667 ;",0.43161,1.01068,41.9,{"v":2e-60,"d":"2.00E-60"},3,1,"_","4.2.1.17, 5.1.2.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,280,281,6,284,658]
[null,"MGMSRv2_3175",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaH","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.55446,0.99644,39.29,{"v":3e-58,"d":"3.00E-58"},3,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",3,279,281,10,287,505]
[null,"PP_3282",null,"Pseudomonas putida KT2440","paaH","3-hydroxyadipyl-CoA dehydrogenase","RXN0-2044 ; RHEA:16199 ;",0.56238,1.01068,38.73,{"v":2e-57,"d":"2.00E-57"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.35","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","12846838, 15137080, 20660314, 10766858, 22961985, 22398448, 21247899, 9748275","2a : Function from experimental evidences in other organisms",1,281,281,8,289,505]
[null,"CLOSTRIBL6_v1_0555",null,"Clostridiales BL-6","hbd","3-hydroxybutyryl-CoA dehydrogenase","RXN-12705 ; RHEA:16200 ;",0.94649,1.00712,36.04,{"v":7e-57,"d":"7.00E-57"},2,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 25112316","2a : Function from experimental evidences in other organisms",5,280,281,11,292,299]
[null,"PSEEN2793",null,"Pseudomonas entomophila L48","paaC","3-hydroxyacyl-CoA dehydrogenase phaC","_",0.55512,1.00356,36.88,{"v":2e-56,"d":"2.00E-56"},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",2,280,281,12,291,508]
[null,"SCFA_v1_100019",null,"Ca. Phosphitivorax anaerolimi F81","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.74406,1.00356,39.36,{"v":3e-56,"d":"3.00E-56"},4,1,"_","1.1.1.157","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,280,281,5,282,379]
[null,"SCFA_v1_3390003",null,"Ca. Phosphitivorax butyraticus R76","hbd","3-hydroxybutyryl-CoA dehydrogenase (modular protein)","_",0.43161,1.01068,39.79,{"v":1e-55,"d":"1.00E-55"},3,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,280,281,6,284,658]
[null,"CLOSTRIBL4_v1_1158",null,"Clostridiales BL-4","hbd","3-hydroxybutyryl-CoA dehydrogenase","RXN-12570 ; RHEA:16200 ;",0.9596,1.01423,36.14,{"v":1e-55,"d":"1.00E-55"},2,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",3,280,281,9,292,297]
[null,"ABAYE2368",null,"Acinetobacter baumannii AYE","paaH","3-hydroxybutyryl-CoA dehydrogenase, phenylacetic acid degradation","_",0.55273,1.00712,35.69,{"v":4E-55,"d":"4.00E-55"},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",2,281,281,10,290,512]
[null,"MARHY2087","_","Marinobacter hydrocarbonoclasticus ATCC 49840","fadB","bifunctional enzyme (PBE) (PBFE) [Includes: Enoyl-CoA hydratase ; 3,2-trans-enoyl-CoA isomerase ; 3-hydroxyacyl-CoA dehydrogenase ]","_",0.40057,0.99644,38.21,{"v":1E-54,"d":"1.00E-54"},1,1,"_","5.3.3.8, 4.2.1.17, 1.1.1.35","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","4019459, 8549802","2a : Function from experimental evidences in other organisms",2,279,281,293,567,699]
[null,"AZOLI_p40260",null,"Azospirillum lipoferum 4B","paaH","3-hydroxybutyryl-CoA dehydrogenase","_",0.51083,1.00712,37.81,{"v":5e-54,"d":"5.00E-54"},1,1,"1.1.1 : carbon compounds ; 1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.-","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9748275,"2a : Function from experimental evidences in other organisms",3,280,281,10,288,554]
[null,"XDD1v4_1792","_","Xenorhabdus doucetiae FRM16","xcnB","3-hydroxyacyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",1.00702,1.02135,36.93,{"v":2e-53,"d":"2.00E-53"},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",1,280,281,1,281,285]
[null,"THI_3559","_","Thiomonas sp. 3As","_","putative 3-hydroxybutyryl-CoA dehydrogenase PaaH","_",0.55512,1.00356,38.65,{"v":5E-52,"d":"5.00E-52"},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",2,279,281,10,288,508]
[null,"XDD1v4_3925",null,"Xenorhabdus doucetiae FRM16","paaH","protein PaaH; 3-hydroxybutyryl-CoA dehydrogenase","_",0.51188,0.99644,38.21,{"v":1E-51,"d":"1.00E-51"},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",3,279,281,10,287,547]
[null,"AZOLI_p30575","_","Azospirillum lipoferum 4B","pimF","Enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase","_",0.39745,1,40.93,{"v":2E-51,"d":"2.00E-51"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17, 1.1.1.35","2 : Cytoplasmic","3.2 : Degradation ; 16.11 : Scavenge (Catabolism) ;","e : enzyme",15758219,"2a : Function from experimental evidences in other organisms",2,279,281,307,581,707]
[null,"CLOSTRIBL3_v1_13113",null,"Clostridiaceae BL-3","hbd","3-hydroxybutyryl-CoA dehydrogenase","3-HYDROXYBUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:16197 ;",0.99306,1.01779,38.46,{"v":2E-51,"d":"2.00E-51"},2,1,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","8655474, 25112316","1c : Function from experimental evidences in the studied genus",2,279,281,5,287,288]
[null,"NVIE_010920","_","Nitrososphaera viennensis EN76","_","hydroxyacyl-CoA dehydrogenase","_",0.73438,1.00356,35.82,{"v":3E-51,"d":"3.00E-51"},1,1,"_","1.1.1.35","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,279,281,9,287,384]
[null,"Rmet_4582","_","Cupriavidus metallidurans CH34","fadB","multifunctional: 3-hydroxybutyryl-CoA epimerase, delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase, enoyl-CoA hydratase (N-terminal); 3-hydroxyacyl-CoA dehydrogenase (C-terminal)","_",0.40374,1,39.86,{"v":6E-51,"d":"6.00E-51"},1,1,"_","1.1.1.35, 4.2.1.17","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,279,281,297,570,696]
[null,"THI_0464",null,"Thiomonas sp. 3As","_","putative 3-hydroxybutyryl-CoA dehydrogenase","_",0.56375,1.00712,35.34,{"v":3e-50,"d":"3.00E-50"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",2,281,281,12,291,502]
[null,"Spro_1832",null,"Serratia proteamaculans 568","paaH","3-hydroxyacyl-CoA dehydrogenase, NAD-binding","_",0.54617,0.98932,37.77,{"v":4E-50,"d":"4.00E-50"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","1.1.1.157","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,277,281,11,286,509]
[null,"MARHY2411",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","fadJ","Fatty acid oxidation complex subunit alpha","_",0.39944,1.01779,37.41,{"v":5e-50,"d":"5.00E-50"},2,1,"_","4.2.1.17, 1.1.1.35, 5.1.2.3","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,279,281,317,598,716]
[null,"ABAYE2306",null,"Acinetobacter baumannii AYE","dcaH","dehydrogenase","_",0.55227,0.99644,35.71,{"v":5e-49,"d":"5.00E-49"},3,1,"1.1.1 : carbon compounds ;","1.1.1.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",3,279,281,8,285,507]
[null,"ACIAD1690",null,"Acinetobacter baylyi ADP1","dcaH","dehydrogenase","1.1.1.259-RXN ; METHELENE-THMPT-OXI-RXN ; RXN0-2044 ;",0.55644,1,35.94,{"v":6E-49,"d":"6.00E-49"},1,1,"_","1.1.1.-","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921, 11571189","1a : Function from experimental evidences in the studied strain",2,279,281,7,285,505]
[null,"RALTA_A1467",null,"Cupriavidus taiwanensis LMG19424","fadB","multifunctional: 3-hydroxybutyryl-CoA epimerase, delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase, enoyl-CoA hydratase (N-terminal); 3-hydroxyacyl-CoA dehydrogenase (C-terminal)","_",0.40693,1.00356,38.3,{"v":4e-48,"d":"4.00E-48"},3,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","4.2.1.17, 5.3.3.8, 1.1.1.35, 5.1.2.3","1 : Unknown","3.2 : Degradation ;","e : enzyme",8549802,"2a : Function from experimental evidences in other organisms",2,279,281,294,567,693]
[null,"IBTHAUMv1_1140010","_","Ianthella basta symbiont thaum","hbd","3-hydroxybutyryl-CoA dehydrogenase","_",0.84698,0.92969,37.82,{"v":7e-48,"d":"7.00E-48"},1,1,"1.3 : Energy metabolism (carbon) ;","1.1.1.157","2 : Cytoplasmic","_","e : enzyme",11772643,"2b : Function from indirect experimental evidences (e.g. phenotypes)",3,237,281,6,242,256]
[null,"SCFA_v1_1540002",null,"Ca. Phosphitivorax butyraticus R76","_","Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase / 3-hydroxyacyl-CoA dehydrogenase","_",0.38584,0.95018,36.7,{"v":9e-48,"d":"9.00E-48"},4,1,"_","1.1.1.35, 4.2.1.17, 5.1.2.3, 5.3.3.8","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,266,281,324,587,692]
[null,"Rmet_1855",null,"Cupriavidus metallidurans CH34","fadB","fused 3-hydroxybutyryl-CoA epimerase and delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase and enoyl-CoA hydratase ; 3-hydroxyacyl-CoA dehydrogenase","_",0.40548,1,36.3,{"v":2E-46,"d":"2.00E-46"},3,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","5.3.3.8, 4.2.1.17, 5.1.2.3, 1.1.1.35","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",2,279,281,294,567,693]
[null,"ACIAD2989",null,"Acinetobacter baylyi ADP1","_","putative 3-hydroxybutyryl-CoA epimerase","OHBUTYRYL-COA-EPIM-RXN ;",0.40225,1.01779,36.71,{"v":1e-45,"d":"1.00E-45"},2,1,"_","5.1.2.3","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,279,281,316,597,711]
[null,"BN11v3_4910008",null,"Tetrasphaera australiensis Ben110","fadJ","fused enoyl-CoA hydratase and epimerase and isomerase ; 3-hydroxyacyl-CoA dehydrogenase","_",0.38164,0.94662,36.84,{"v":1e-44,"d":"1.00E-44"},2,1,"_","4.2.1.17, 5.3.3.8, 5.1.2.3, 1.1.1.35","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","12270828, 12535077","2a : Function from experimental evidences in other organisms",2,265,281,341,601,697]
[null,"CMR15v5_2681",null,"Ralstonia solanacearum CMR15","fadB","fused 3-hydroxybutyryl-CoA epimerase, delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase, enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase","_",0.40404,0.99644,37.86,{"v":2e-44,"d":"2.00E-44"},3,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","4.2.1.17, 5.3.3.8, 1.1.1.35, 5.1.2.3","1 : Unknown","3.2 : Degradation ;","e : enzyme",8549802,"2a : Function from experimental evidences in other organisms",3,279,281,295,567,693]
[null,"BRADO0981",null,"Bradyrhizobium sp. ORS278","pimF","Enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase","_",0.40172,0.99644,36.43,{"v":1e-43,"d":"1.00E-43"},4,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17, 1.1.1.35","1 : Unknown","16.11 : Scavenge (Catabolism) ;","e : enzyme",15758219,"2a : Function from experimental evidences in other organisms",2,279,281,297,564,697]
[null,"VCR9J2v1_150068",null,"Vibrio crassostreae J2-9","fadB","Putative 3-hydroxybutyryl-CoA epimerase","OHBUTYRYL-COA-EPIM-RXN ; RHEA:21760 ;",0.39415,1.00712,35.69,{"v":1e-43,"d":"1.00E-43"},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",2,281,281,319,597,718]
[null,"BN13v1_130026",null,"Tetrasphaera jenkinsii Ben74","fadJ","Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase ; 3-hydroxyacyl-CoA dehydrogenase]","_",0.38362,0.95018,37.45,{"v":1e-43,"d":"1.00E-43"},2,1,"_","4.2.1.17, 5.1.2.3, 1.1.1.35","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","12270828, 12535077","2a : Function from experimental evidences in other organisms",2,265,281,339,599,696]
[null,"BN10v3_810004",null,"Tetrasphaera elongata Lp2","_","fused enoyl-CoA hydratase and epimerase and isomerase ; 3-hydroxyacyl-CoA dehydrogenase","_",0.38559,0.97153,35.16,{"v":3e-41,"d":"3.00E-41"},2,1,"_","4.2.1.17, 5.3.3.8, 5.1.2.3, 1.1.1.35","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","12270828, 12535077","2a : Function from experimental evidences in other organisms",2,272,281,339,606,708]
[null,"FRAAL2096",null,"Frankia alni ACN14a","_","fatty acid oxidation complex alpha-subunit","_",0.38322,0.97509,35.4,{"v":5e-40,"d":"5.00E-40"},3,1,"1.1.5.4 : Beta-ketoadipate pathway ;","5.1.2.3","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,272,281,344,612,715]
[]
["AEQN01_220121","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_1868",null,"Clostridiales BL-4","crt","Short-chain-enoyl-CoA hydratase","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; RHEA:17852 ;",1,1,67.44,{"v":1e-123,"d":"1.00E-123"},1,1,"_","4.2.1.55","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286, 5057466","2a : Function from experimental evidences in other organisms",1,258,258,1,258,258]
[null,"CLOSTRIBL3_v1_20308",null,"Clostridiaceae BL-3","crt","Short-chain-enoyl-CoA hydratase","ENOYL-COA-HYDRAT-RXN ; RHEA:16105 ;",0.97683,0.98062,60.08,{"v":4e-101,"d":"4.00E-101"},1,1,"_","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 5057466","1c : Function from experimental evidences in the studied genus",7,258,258,9,259,259]
[null,"CLOSTRIBL6_v1_0134",null,"Clostridiales BL-6","ldeF","methylglutaconyl-CoA hydratase","METHYLGLUTACONYL-COA-HYDRATASE-RXN ; RHEA:21536 ;",1,1.00775,54.62,{"v":2e-96,"d":"2.00E-96"},1,1,"_","4.2.1.18","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",19935659,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,258,258,1,260,260]
[null,"CD630_08000","_","Clostridium difficile 630","crt1","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.98462,0.99225,49.22,{"v":2E-78,"d":"2.00E-78"},1,1,"1.6 : Macromolecules (cellular constituent) biosynthesis ;","4.2.1.55","1 : Unknown","6 : Energy metabolism ;","e : enzyme","8001771, 16346566, 11263873","2a : Function from experimental evidences in other organisms",4,258,258,7,260,260]
[null,"CD630_10570",null,"Clostridium difficile 630","crt2","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.93962,0.96512,51.41,{"v":1e-72,"d":"1.00E-72"},2,1,"_","4.2.1.55","1 : Unknown","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",4,251,258,12,259,265]
[null,"SCFA_v1_1190005","_","Ca. Phosphitivorax anaerolimi F81","crt","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.9845,1.00395,49.61,{"v":1E-70,"d":"1.00E-70"},1,1,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,251,258,1,247,253]
[null,"IBTHAUMv1_18460003","_","Ianthella basta symbiont thaum","crt","3-hydroxybutyryl-CoA dehydratase","_",0.92248,0.94444,47.48,{"v":5e-68,"d":"5.00E-68"},1,1,"1.1 : Carbon compound utilization ;","4.2.1.55","2 : Cytoplasmic","5.2 : One-carbon metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",15,251,258,14,251,252]
[null,"LEPBIa0927","_","Leptospira biflexa serovar Patoc Patoc 1","crt","3-hydroxybutyryl-CoA dehydratase (Crotonase)","_",0.97674,0.99213,46.03,{"v":1e-67,"d":"1.00E-67"},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",1,251,258,1,251,254]
[null,"BSU18220",null,"Bacillus subtilis 168","ldeF","methylglutaconyl-CoA hydratase (leucine degradation)","METHYLGLUTACONYL-COA-HYDRATASE-RXN ; RHEA:21536 ;",0.93846,0.94574,45.08,{"v":4e-65,"d":"4.00E-65"},1,1,"_","4.2.1.18","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",19935659,"2b : Function from indirect experimental evidences (e.g. phenotypes)",12,251,258,14,254,260]
[null,"NVIE_008340","_","Nitrososphaera viennensis EN76","_","3-hydroxybutyryl-CoA dehydratase","_",0.94314,1.09302,40.07,{"v":3e-61,"d":"3.00E-61"},1,1,"_","4.2.1.55","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,251,258,17,298,299]
[null,"CLOSTRIBL6_v1_0558",null,"Clostridiales BL-6","crt","Short-chain-enoyl-CoA hydratase","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; RHEA:52667 ;",0.96565,0.98062,45.85,{"v":1e-60,"d":"1.00E-60"},2,1,"_","4.2.1.150, 4.2.1.55","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","8655474, 11466286, 5057466","2a : Function from experimental evidences in other organisms",4,250,258,8,255,262]
[null,"CLOSTRIBL3_v1_13112",null,"Clostridiaceae BL-3","crt","Short-chain-enoyl-CoA hydratase","RXN-11667 ; RHEA:52664 ;",0.97674,0.98824,42.46,{"v":3e-59,"d":"3.00E-59"},2,1,"_","4.2.1.150","2 : Cytoplasmic","_","e : enzyme","8655474, 5057466","1c : Function from experimental evidences in the studied genus",1,251,258,1,249,255]
[null,"CLOSTRIBL4_v1_1161",null,"Clostridiales BL-4","crt","Short-chain-enoyl-CoA hydratase","ENOYL-COA-HYDRAT-RXN ; RHEA:16108 ;",0.9058,0.96899,43.2,{"v":7e-58,"d":"7.00E-58"},2,1,"1 : Metabolism ;","4.2.1.50, 4.2.17.150","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","8655474, 11466286, 5057466","2a : Function from experimental evidences in other organisms",4,250,258,22,269,276]
[null,"BN44v3_11186",null,"Mycobacterium canettii STB-D","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",0.94961,0.95331,43.67,{"v":8e-58,"d":"8.00E-58"},1,1,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",7,250,258,9,250,257]
[null,"BN43v3_30123",null,"Mycobacterium canettii STB-L","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",0.94961,0.95331,43.67,{"v":8e-58,"d":"8.00E-58"},1,1,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",7,250,258,9,250,257]
[null,"BN45v3_30109",null,"Mycobacterium canettii STB-J","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",0.94961,0.95331,43.67,{"v":5e-57,"d":"5.00E-57"},1,1,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",7,250,258,9,250,257]
[null,"BN42v3_20918",null,"Mycobacterium canettii STB-K","echA","Putative enoyl-CoA hydratase EchA8 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",0.94961,0.95331,43.27,{"v":5e-57,"d":"5.00E-57"},1,1,"1 : lipid metabolism ;","4.2.1.17","1 : Unknown","_","e : enzyme","10768780, 11271494, 11929527, 12657046","3 : Putative function from multiple computational evidences",7,250,258,9,250,257]
[null,"PSEEN3545",null,"Pseudomonas entomophila L48","fadB1x","enoyl-CoA hydratase, FadB1x","_",0.93798,0.968,43.8,{"v":9e-57,"d":"9.00E-57"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","4.2.1.-","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",11251808,"2a : Function from experimental evidences in other organisms",12,251,258,7,244,250]
[null,"THI_0338","_","Thiomonas sp. 3As","fadB","enoyl-CoA hydratase-isomerase","_",0.94636,0.95736,43.72,{"v":2e-56,"d":"2.00E-56"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",7,251,258,12,255,261]
[null,"NIDE3102",null,"Candidatus Nitrospira defluvii","paaF","putative Enoyl-CoA hydratase","_",0.87786,0.89147,44.78,{"v":1e-55,"d":"1.00E-55"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.1 : Carbohydrates/Carbon compounds ; 1.1.3 : Amino acids ;","4.2.1.17","1 : Unknown","3.2 : Degradation ; 6.2 : Amino acids and amines ; 6.11 : Sugars ;","e : enzyme","10766858, 11263873, 12445775, 12846838, 9748275","3 : Putative function from multiple computational evidences",24,251,258,28,256,262]
[null,"RALSYv5_1694","_","Ralstonia syzygii R24","_","Enoyl-CoA hydratase/isomerase (paaF like)","_",0.96169,0.97287,39.04,{"v":2E-55,"d":"2.00E-55"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,250,258,4,254,261]
[null,"Rmet_3162","_","Cupriavidus metallidurans CH34","paaF","enoyl-CoA hydratase-isomerase","_",0.99225,0.99225,42.19,{"v":2E-55,"d":"2.00E-55"},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",7,258,258,9,258,258]
[null,"BDBv6_60063",null,"Blood disease bacterium R229","paaF","enoyl-CoA hydratase-isomerase","_",0.95349,0.95349,43.5,{"v":4E-55,"d":"4.00E-55"},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",7,251,258,9,252,258]
[null,"Rru_A3801","_","Rhodospirillum rubrum ATCC 11170","fadB","short chain enoyl-CoA hydratase","_",0.95736,0.95736,42.51,{"v":7e-55,"d":"7.00E-55"},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)",7,251,258,9,252,258]
[null,"ABAYE3764","_","Acinetobacter baumannii AYE","_","putative Enoyl-CoA hydratase","_",0.95349,0.9572,41.46,{"v":1E-54,"d":"1.00E-54"},1,1,"_","4.2.1.17","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",7,251,258,9,251,257]
[null,"FRAAL5882","_","Frankia alni ACN14a","echA","enoyl-CoA hydratase-isomerase","_",0.96124,0.96124,41.13,{"v":2e-54,"d":"2.00E-54"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","4.2.1.17","1 : Unknown","16.2 : Construct biomass (Anabolism) ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,247,258,1,246,258]
[null,"BN13v1_100067","_","Tetrasphaera jenkinsii Ben74","_","putative enoyl-CoA hydratase echA8","_",0.96139,0.96512,41.37,{"v":5e-54,"d":"5.00E-54"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,249,258,4,249,259]
[null,"CMR15v5_1457","_","Ralstonia solanacearum CMR15","paaF","enoyl-CoA hydratase-isomerase","_",0.95349,0.95349,43.9,{"v":5e-54,"d":"5.00E-54"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme",9748275,"2a : Function from experimental evidences in other organisms",7,251,258,9,252,258]
[null,"BN873v1_210051",null,"Candidatus Competibacter denitrificans Run_A_D11","_","putative enoyl-CoA hydratase-isomerase","_",0.96124,0.96124,41.94,{"v":1E-53,"d":"1.00E-53"},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",4,250,258,6,251,258]
[null,"MGMSRv2_2895","_","Magnetospirillum gryphiswaldense MSR-1 v2","paaF","enoyl-CoA hydratase-isomerase","_",0.94961,0.94961,42.04,{"v":3e-53,"d":"3.00E-53"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",7,250,258,9,251,258]
[null,"ACIAD1608",null,"Acinetobacter baylyi ADP1","FadB","Enoyl-CoA hydratase (valine degradation) (valine degradation)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; ENOYL-COA-HYDRAT-RXN ; METHYLACYLYLCOA-HYDROXY-RXN ; RXN-902 ; TIGLYLCOA-HYDROXY-RXN ; RHEA:31178 ;",0.94961,0.95331,40.41,{"v":3e-53,"d":"3.00E-53"},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",7,250,258,9,250,257]
[null,"BN874v1_720037",null,"Candidatus Contendobacter odensis Run_B_J11","_","putative enoyl-CoA hydratase-isomerase","_",0.9845,0.9845,41.73,{"v":9e-53,"d":"9.00E-53"},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",4,253,258,6,254,258]
[null,"SCFA_v1_100018",null,"Ca. Phosphitivorax anaerolimi F81","_","Enoyl-CoA hydratase","_",0.96899,0.97656,40,{"v":1E-52,"d":"1.00E-52"},2,1,"_","4.2.1.17","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,251,258,9,250,256]
[null,"AZOLI_3178","_","Azospirillum lipoferum 4B","paaF1","Enoyl-CoA hydratase-isomerase","_",0.96512,0.96512,42.97,{"v":2E-52,"d":"2.00E-52"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",7,251,258,9,252,258]
[null,"BN11v3_3200006","_","Tetrasphaera australiensis Ben110","_","putative enoyl-CoA hydratase echA8","_",0.95367,0.95736,39.68,{"v":7e-52,"d":"7.00E-52"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,249,258,4,249,259]
[null,"RM41v1_60029","_","Sinorhizobium sp. Rm41","_","Putative enoyl-CoA hydratase","_",0.95736,0.96109,39.68,{"v":1E-51,"d":"1.00E-51"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","1743516, 2204034, 2806264, 7815937","3 : Putative function from multiple computational evidences",7,253,258,9,253,257]
[null,"BRADO2663","_","Bradyrhizobium sp. ORS278","_","Putative enoyl-CoA hydratase","_",0.94361,0.97287,39.84,{"v":2E-51,"d":"2.00E-51"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","1743516, 2204034, 2806264, 7815937","3 : Putative function from multiple computational evidences",7,251,258,17,260,266]
[null,"PSEEN2791",null,"Pseudomonas entomophila L48","phaA","enoyl-CoA hydratase/isomerase PhaA","_",0.93798,0.94163,41.32,{"v":3E-51,"d":"3.00E-51"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","Cytoplasmic","6 : Energy metabolism ;","e : enzyme","12534466, 15474299, 9600981","2a : Function from experimental evidences in other organisms",10,250,258,12,250,257]
[null,"RALTA_A2759","_","Cupriavidus taiwanensis LMG19424","badK","cyclohex-1-ene-1-carboxyl-CoA hydratase","_",0.96124,0.96124,40.73,{"v":8e-51,"d":"8.00E-51"},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)",7,250,258,9,251,258]
[null,"HEAR0207","_","Herminiimonas arsenicoxydans","ech","Enoyl-CoA hydratase","_",0.93023,0.93023,41.67,{"v":4E-50,"d":"4.00E-50"},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",12,250,258,14,251,258]
[null,"ABAYE2304",null,"Acinetobacter baumannii AYE","dcaE","enoyl-CoA hydratase","_",0.8893,0.93411,39.42,{"v":2e-49,"d":"2.00E-49"},2,1,"1.1.1 : carbon compounds ;","4.2.1.17","1 : Unknown","_","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921","2a : Function from experimental evidences in other organisms",12,251,258,28,265,271]
[null,"SCFA_v1_130011",null,"Ca. Phosphitivorax anaerolimi F81","paaF","Enoyl-CoA hydratase/isomerase family (3-hydroxybutyryl-CoA dehydratase (Crotonase))","RXN-11667 ;",0.37082,0.94574,40.98,{"v":7e-49,"d":"7.00E-49"},3,2,"_","4.2.1.17, 5.1.2.3","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",10,251,258,411,652,658]
[null,"BN12v2_350029","_","Tetrasphaera japonica T1-X7","_","putative enoyl-CoA hydratase echA8","_",0.95038,0.96512,40.16,{"v":2e-48,"d":"2.00E-48"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,248,258,5,251,262]
[null,"PP_3284",null,"Pseudomonas putida KT2440","paaF","enoyl-CoA hydratase-isomerase","RXN0-6513 ; RHEA:34866 ;",0.93411,0.93774,40.66,{"v":3e-48,"d":"3.00E-48"},2,1,"_","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","12846838, 15137080, 18437357","2a : Function from experimental evidences in other organisms",12,251,258,14,251,257]
[null,"XDD1v4_3923",null,"Xenorhabdus doucetiae FRM16","paaF","protein PaaF; enoyl-CoA hydratase-isomerase","_",0.92248,0.92607,38.24,{"v":4e-48,"d":"4.00E-48"},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",15,251,258,17,251,257]
[null,"VIBNIv4_A2696","_","Vibrio nigripulchritudo SFn1","_","putative Enoyl-CoA hydratase","_",0.86957,0.93023,36.25,{"v":5e-48,"d":"5.00E-48"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",12,250,258,17,256,276]
[null,"BN10v3_570010","_","Tetrasphaera elongata Lp2","_","putative enoyl-CoA hydratase echA8","_",0.96512,0.96512,39.76,{"v":5e-48,"d":"5.00E-48"},1,1,"_","4.2.1.17","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,251,258,5,252,258]
[null,"ACIAD1692",null,"Acinetobacter baylyi ADP1","dcaE","Enoyl-CoA hydratase (branched-chain amino acid degradation)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; ENOYL-COA-HYDRAT-RXN ; METHYLACYLYLCOA-HYDROXY-RXN ; RXN-2425 ; RXN-902 ; TIGLYLCOA-HYDROXY-RXN ; RXN0-6513 ; RXN-7838 ; RHEA:16107 ; RHEA:17850 ; RHEA:31178 ; RHEA:31122 ;",0.92337,0.93411,39,{"v":8e-48,"d":"8.00E-48"},2,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme","2298704, 8002591, 8063101, 8181753, 8331077, 8449410, 9515921, 11571189","1a : Function from experimental evidences in the studied strain",12,251,258,18,255,261]
[null,"MGMSRv2_3173",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaF","enoyl-CoA hydratase-isomerase","_",0.91892,0.92248,40.34,{"v":1E-46,"d":"1.00E-46"},3,1,"1.1.5.1 : Phenylacetic acid degradation ;","4.2.1.17","1 : Unknown","6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 9748275","2a : Function from experimental evidences in other organisms",15,251,258,19,253,259]
[null,"PSHAa0882","_","Pseudoalteromonas haloplanktis TAC125","paaF","putative enoyl-CoA hydratase-isomerase","_",0.9387,0.94961,37.55,{"v":8e-46,"d":"8.00E-46"},1,1,"2 : Intermediary metabolism ;","4.2.1.17","unknown","_","e : enzyme",9748275,"3 : Putative function from multiple computational evidences",15,258,258,21,261,261]
[null,"SCFA_v1_3390003",null,"Ca. Phosphitivorax butyraticus R76","hbd","3-hydroxybutyryl-CoA dehydrogenase (modular protein)","_",0.37082,0.94574,39.34,{"v":1e-45,"d":"1.00E-45"},2,2,"_","1.1.1.157","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",10,251,258,411,652,658]
[null,"AZCBGv1_p1100088","_","Azospirillum brasilense CBG497","_","enoyl-CoA hydratase-isomerase","_",0.90566,0.93023,38.75,{"v":4e-45,"d":"4.00E-45"},1,1,"1.1.5.1 : Phenylacetic acid degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","e : enzyme","1743516, 2204034, 2806264, 7815937","2b : Function from indirect experimental evidences (e.g. phenotypes)",12,250,258,22,258,265]
[null,"BN381v2_10064","_","Candidatus Microthrix parvicella RN1","_","putative enoyl-CoA hydratase-isomerase","_",0.9304,0.9845,37.4,{"v":6e-45,"d":"6.00E-45"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","8655474, 10727085, 2204034, 1743516","3 : Putative function from multiple computational evidences",14,256,258,18,267,273]
[null,"RALTA_B1107","_","Cupriavidus taiwanensis LMG19424","_","putative ENOYL-COA HYDRATASE ISOMERASE; similar to paaF (E.coli)","_",0.93411,0.94141,36.93,{"v":2e-44,"d":"2.00E-44"},1,1,"1 : Metabolism ;","4.2.1.-","2 : Cytoplasmic","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",12,250,258,10,249,256]
[null,"CMR15v5_mp0937","_","Ralstonia solanacearum CMR15","_","putative enoyl-CoA hydratase/isomerase (paaF)","_",0.90602,0.93411,38.59,{"v":2e-42,"d":"2.00E-42"},1,1,"1 : Metabolism ;","4.2.1.-","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",12,250,258,12,251,266]
[null,"MARHY1100","_","Marinobacter hydrocarbonoclasticus ATCC 49840","paaF","enoyl-CoA hydratase-isomerase","_",0.96525,0.96899,37.2,{"v":5E-42,"d":"5.00E-42"},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",4,251,258,5,253,259]
[null,"ECS88_4526","_","Escherichia coli S88","_","putative Enoyl-CoA hydratase/carnithine racemase","_",0.96525,0.96899,35.2,{"v":9e-41,"d":"9.00E-41"},1,1,"_","4.2.1.17","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",4,251,258,6,253,259]
[null,"Rmet_5150","_","Cupriavidus metallidurans CH34","_","enoyl-CoA hydratase","_",0.98485,1.00775,35.38,{"v":2e-40,"d":"2.00E-40"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","4.2.1.17","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,251,258,3,259,264]
[null,"AGR4A_v2_Lc60051","_","Agrobacterium genomosp. 4 B6","_","putative enoyl-CoA hydratase/isomerase","_",0.96139,0.96512,36.55,{"v":3e-40,"d":"3.00E-40"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",4,250,258,6,251,259]
[null,"BDBv6_60062",null,"Blood disease bacterium R229","paaG","acyl-CoA hydratase, phenylacetic acid degradation","_",0.93511,0.94961,35.51,{"v":5e-39,"d":"5.00E-39"},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",10,250,258,12,255,262]
[null,"SCFA_v1_230003",null,"Ca. Phosphitivorax anaerolimi F81","echA","enoyl-CoA hydratase Echa16 (enoyl hydrase) (unsaturated acyl-CoA hydratase) (crotonase)","_",0.89147,0.96234,35.65,{"v":3e-35,"d":"3.00E-35"},6,1,"_","4.2.1.17","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,232,258,5,230,239]
[null,"NBG4_v1_200001",null,"Candidatus Sulfobium mesophilum","echA","3-hydroxybutyryl-CoA dehydratase (fragment)","3-HYDROXBUTYRYL-COA-DEHYDRATASE-RXN ; RHEA:17849 ;",0.50775,0.92908,45.8,{"v":2e-29,"d":"2.00E-29"},1,1,"_","4.2.1.55","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",2,131,258,10,138,141]
[]
["AEQN01_220122","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL4_v1_1867",null,"Clostridiales BL-4","thlA","acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.92417,0.98985,60.26,{"v":2E-174,"d":"2.00E-174"},1,1,"_","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","7867955, 11075929","2a : Function from experimental evidences in other organisms",1,389,394,27,416,422]
[null,"CLOSTRIBL3_v1_12838","_","Clostridiaceae BL-3","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.98985,0.9949,60.26,{"v":2E-170,"d":"2.00E-170"},1,1,"_","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","7867955, 11075929, 11466286, 1685080","2a : Function from experimental evidences in other organisms",3,391,394,2,391,392]
[null,"CLOSTRIBL6_v1_0127",null,"Clostridiales BL-6","phaA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99747,1,58.38,{"v":3e-165,"d":"3.00E-165"},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",1,391,394,1,394,395]
[null,"CD630_10590",null,"Clostridium difficile 630","thlA1","Acetoacetyl-CoA thiolase 1","_",0.98223,0.98977,55.81,{"v":1e-159,"d":"1.00E-159"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","11075929, 2191949","1c : Function from experimental evidences in the studied genus",3,389,394,2,388,391]
[null,"RALTA_A1351","_","Cupriavidus taiwanensis LMG19424","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.97716,0.97964,55.32,{"v":5e-149,"d":"5.00E-149"},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",4,387,394,3,387,393]
[null,"Rmet_1357",null,"Cupriavidus metallidurans CH34","phaA","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.97716,0.97964,55.06,{"v":2e-148,"d":"2.00E-148"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,387,394,3,387,393]
[null,"PSEEN4635","_","Pseudomonas entomophila L48","phbA","acetyl-CoA acetyltransferase","_",0.94595,0.97716,54.81,{"v":4e-147,"d":"4.00E-147"},1,1,"5.6.2 : Detoxification (xenobiotic metabolism) ;","2.3.1.9","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",4,387,394,17,401,407]
[null,"AZOLI_2388","_","Azospirillum lipoferum 4B","phbA3","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.97462,0.9821,55.99,{"v":3e-145,"d":"3.00E-145"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.9","2 : Cytoplasmic","3.1 : Biosynthesis ;","e : enzyme","7582015, 12788722, 12039753","1c : Function from experimental evidences in the studied genus",4,387,394,3,385,391]
[null,"CMR15v5_2547","_","Ralstonia solanacearum CMR15","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.97716,0.97964,53.51,{"v":2e-144,"d":"2.00E-144"},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",4,387,394,3,387,393]
[null,"PP_4636","_","Pseudomonas putida KT2440","yqeF","acetyl-CoA acetyltransferase","METHYLACETOACETYLCOATHIOL-RXN ; RXN-12561 ; ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",0.97716,0.98214,53.51,{"v":9E-143,"d":"9.00E-143"},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",4,387,394,3,387,392]
[null,"HEAR0577","_","Herminiimonas arsenicoxydans","phbA","acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.96491,0.97716,50.65,{"v":7e-142,"d":"7.00E-142"},1,1,"1.3 : Energy metabolism (carbon) ; 7.1 : Cytoplasm ;","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","1396692, 2670935","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,387,394,10,394,399]
[null,"MARHY3102","_","Marinobacter hydrocarbonoclasticus ATCC 49840","phbA","acetyl-CoA acetyltransferase with thiolase domain, PHB biosynthesis","_",0.9797,0.98469,52.59,{"v":8e-141,"d":"8.00E-141"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",1396692,"2a : Function from experimental evidences in other organisms",3,387,394,2,387,392]
[null,"BRADO0562","_","Bradyrhizobium sp. ORS278","phbA","acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98223,0.98223,53.23,{"v":1e-140,"d":"1.00E-140"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.9","1 : Unknown","16.2 : Construct biomass (Anabolism) ;","e : enzyme",7582015,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,387,394,3,388,394]
[null,"THI_1641","_","Thiomonas sp. 3As","phbA1","acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.98731,0.99235,51.93,{"v":3e-139,"d":"3.00E-139"},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",4,391,394,3,391,392]
[null,"METDI4272","_","Methylobacterium extorquens DM4","phaA","beta-ketothiolase","_",0.99492,0.99492,51.79,{"v":4e-139,"d":"4.00E-139"},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",2,393,394,4,394,394]
[null,"BN873v1_100077","_","Candidatus Competibacter denitrificans Run_A_D11","phaA","Acetyl-CoA acetyltransferase","_",0.9797,0.98219,50.52,{"v":7e-137,"d":"7.00E-137"},1,1,"_","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ; 6 : Energy metabolism ; 16.14 : Store ;","e : enzyme","1685080, 1755959, 7867955, 9904","2a : Function from experimental evidences in other organisms",3,387,394,2,387,393]
[null,"VIBNIv4_B1306","_","Vibrio nigripulchritudo SFn1","phbA","acetyl-CoA acetyltransferase","_",0.98753,1.00508,50.51,{"v":6e-136,"d":"6.00E-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",3,389,394,2,397,401]
[null,"MGMSRv2_1838","_","Magnetospirillum gryphiswaldense MSR-1 v2","phbA","acetyl-CoA acetyltransferase containing thiolase domain (Acetoacetyl-CoA thiolase)","_",0.97462,0.98462,50.78,{"v":1E-135,"d":"1.00E-135"},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)",4,387,394,3,385,390]
[null,"BN874v1_850028","_","Candidatus Contendobacter odensis Run_B_J11","phaA","Acetyl-CoA acetyltransferase","_",0.9797,0.98219,48.7,{"v":7e-133,"d":"7.00E-133"},1,1,"1.3 : Energy metabolism (carbon) ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ; 6 : Energy metabolism ; 16.14 : Store ;","e : enzyme","1685080, 1755959, 7867955, 9904","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,387,394,2,387,393]
[null,"Rmet_1362",null,"Cupriavidus metallidurans CH34","bktB","acetyl-CoA acetyltransferase","_",1.00254,1.00254,48.61,{"v":1e-131,"d":"1.00E-131"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",1,393,394,1,394,394]
[null,"RM41v1_110012","_","Sinorhizobium sp. Rm41","phbA","acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98731,0.98982,50.13,{"v":2E-131,"d":"2.00E-131"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 1.7 : Central intermediary metabolism ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ; 16.2 : Construct biomass (Anabolism) ;","e : enzyme",7582015,"1b : Function from experimental evidences in the studied species",5,393,394,6,393,393]
[null,"AZOLI_p10676","_","Azospirillum lipoferum 4B","phbA2","Acetyl-CoA acetyltransferase with thiolase domain (Beta-ketothiolase)","_",1.00254,1.00509,47.85,{"v":5e-131,"d":"5.00E-131"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.9","1 : Unknown","3.1 : Biosynthesis ; 3 : Fatty acid and phospholipid metabolism ;","e : enzyme","12534463, 9851987","2a : Function from experimental evidences in other organisms",1,393,394,1,393,393]
[null,"NT26v4_3604","_","Rhizobium sp. NT-26","phbA","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",0.98223,0.98473,49.87,{"v":6e-131,"d":"6.00E-131"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ; 1.3 : Energy metabolism (carbon) ; 7.1 : Cytoplasm ;","2.3.1.9","1 : Unknown","16.2 : Construct biomass (Anabolism) ; 6 : Energy metabolism ;","e : enzyme",7582015,"2b : Function from indirect experimental evidences (e.g. phenotypes)",5,391,394,6,391,393]
[null,"NBG4_v1_200004",null,"Candidatus Sulfobium mesophilum","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.98481,0.98731,48.59,{"v":3e-130,"d":"3.00E-130"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.9","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",23468890,"2a : Function from experimental evidences in other organisms",1,389,394,7,392,395]
[null,"Spro_0592","_","Serratia proteamaculans 568","atoB","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.96259,0.9797,49.48,{"v":1e-129,"d":"1.00E-129"},1,1,"1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,387,394,10,395,401]
[null,"RPSI07_1730",null,"Ralstonia solanacearum PSI07","phaA","acetyl-CoA acetyltransferase, thiolase-like","_",1.00254,1.00254,48.86,{"v":4e-129,"d":"4.00E-129"},2,1,"1.7 : Central intermediary metabolism ;","2.3.1.9","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,393,394,1,394,394]
[null,"VS_II0585","_","Vibrio tasmaniensis LGP32","_","Acetyl-CoA C acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.99504,1.01777,47.63,{"v":7e-129,"d":"7.00E-129"},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",3,394,394,2,402,403]
[null,"ECK2842","_","Escherichia coli K12","yqeF","Acetyl-CoA acetyltransferase","_",0.97716,0.97964,48.83,{"v":2e-128,"d":"2.00E-128"},1,1,"1.7 : Central intermediary metabolism ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",7763384,"2a : Function from experimental evidences in other organisms",3,387,394,2,386,393]
[null,"HELPY_0683","_","Helicobacter pylori B38","atoB","Acetyl coenzyme A acetyltransferase","_",0.98477,0.99233,48.2,{"v":2e-127,"d":"2.00E-127"},1,1,"1.1.2.7 : Acetoacetate degradation ;","2.3.1.9","2 : Cytoplasmic","3.1 : General ;","e : enzyme",3025185,"2a : Function from experimental evidences in other organisms",4,391,394,3,389,391]
[null,"CLOSTRIBL3_v1_13111",null,"Clostridiaceae BL-3","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.98985,0.99744,46.15,{"v":1e-126,"d":"1.00E-126"},2,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","7867955, 11075929, 11466286, 1685080","1c : Function from experimental evidences in the studied genus",3,391,394,2,390,391]
[null,"CLOSTRIBL6_v1_0556",null,"Clostridiales BL-6","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",1.00504,1.01269,46.62,{"v":1E-125,"d":"1.00E-125"},2,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","7867955, 11075929, 11466286, 1685080","2a : Function from experimental evidences in other organisms",1,393,394,1,397,397]
[null,"CLOSTRIBL4_v1_1159",null,"Clostridiales BL-4","thlA","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",1.00504,1.01269,46.87,{"v":3e-125,"d":"3.00E-125"},2,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","7867955, 11075929, 11466286, 1685080","2a : Function from experimental evidences in other organisms",1,393,394,1,397,397]
[null,"PSEEN3197",null,"Pseudomonas entomophila L48","_","putative Acetoacetyl-CoA thiolase","_",0.99239,0.99239,46.04,{"v":2E-121,"d":"2.00E-121"},2,1,"1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.9","Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,393,394,5,394,394]
[null,"BN424_3179","_","Carnobacterium maltaromaticum LMA28 v1","thlA","Acetoacetyl-CoA thiolase","METHYLACETOACETYLCOATHIOL-RXN ; RXN-12561 ; ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.98985,1.00257,47.44,{"v":7e-121,"d":"7.00E-121"},1,1,"_","2.3.1.9","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,391,394,2,387,389]
[null,"SCFA_v1_120020",null,"Ca. Phosphitivorax anaerolimi F81","yqeF","Acetyl-CoA acetyltransferase","_",0.98477,0.9898,46.65,{"v":4e-120,"d":"4.00E-120"},3,1,"1.7 : Central intermediary metabolism ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",7763384,"2a : Function from experimental evidences in other organisms",3,389,394,2,388,392]
[null,"NIDE3116",null,"Candidatus Nitrospira defluvii","atoB","Acetyl-CoA acetyltransferase","_",0.9797,0.9797,46.89,{"v":1e-118,"d":"1.00E-118"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1.2.7 : Acetoacetate degradation ; 1.1.2 : Fatty acids (fatty acid oxidation) ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","15229654, 1685080, 1755959, 7867955, 9904","2a : Function from experimental evidences in other organisms",6,391,394,8,393,394]
[null,"METUNv2_520573","_","Methyloversatilis universalis FAM5","phbA","Acetyl-CoA acetyltransferase","_",0.99241,0.99492,44.9,{"v":8e-118,"d":"8.00E-118"},1,1,"1 : Metabolism ; 1.1.1 : Carbohydrates/Carbon compounds ;","2.3.1.9","2 : Cytoplasmic","15.11 : Biosynthesis of natural products ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,393,394,5,395,395]
[null,"ACIAD0694","_","Acinetobacter baylyi ADP1","fadA","3-ketoacyl-CoA thiolase, Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RXN-11246 ; RXN-12561 ; RXN0-6512 ; RXN-12565 ; KETOACYLCOATHIOL-RXN ; RHEA:21039 ; RHEA:21567 ;",0.97462,0.9821,45.83,{"v":4e-117,"d":"4.00E-117"},1,1,"1.1.5.1 : Phenylacetic acid degradation ;","2.3.1.16, 2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ; 16.11 : Scavenge (Catabolism) ;","e : enzyme","11075929, 18246303, 21209787","2a : Function from experimental evidences in other organisms",4,387,394,3,385,391]
[null,"PSHAa1586","_","Pseudoalteromonas haloplanktis TAC125","atoB","acetyl-CoA acetyltransferase with thiolase domain, Acetoacetyl-CoA thiolase","_",0.95355,0.98985,44.87,{"v":7e-117,"d":"7.00E-117"},1,1,"_","2.3.1.9","cytoplasm (undefined)","_","e : enzyme",7867955,"2a : Function from experimental evidences in other organisms",5,393,394,21,409,409]
[null,"BSU24170",null,"Bacillus subtilis 168","mmgA","degradative acetoacetyl-CoA thiolase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.9797,0.98219,45.85,{"v":2e-115,"d":"2.00E-115"},1,1,"2.4 : Metabolism of lipids ;","2.3.1.9","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","16352833, 18246303, 19016856, 28956599","1a : Function from experimental evidences in the studied strain",3,387,394,2,387,393]
[null,"BTCD_v1_1714","_","Brochothrix thermosphacta CD337","mevB","Acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21036 ;",0.9797,0.99485,47.15,{"v":5e-115,"d":"5.00E-115"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme",7763384,"2a : Function from experimental evidences in other organisms",3,387,394,2,382,388]
[null,"LEPBIa0355","_","Leptospira biflexa serovar Patoc Patoc 1","thiL1","Putative acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.99239,0.99491,45.01,{"v":4e-113,"d":"4.00E-113"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","2 : Cytoplasmic","16.2 : Construct biomass (Anabolism) ;","e : enzyme",15733928,"2a : Function from experimental evidences in other organisms",3,392,394,2,390,393]
[null,"ACIAD1612",null,"Acinetobacter baylyi ADP1","_","putative acetyl-CoA C-acetyltransferase with thiolase domain","_",0.98477,0.98728,44.07,{"v":1e-110,"d":"1.00E-110"},2,1,"1.1.1 : carbon compounds ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,387,394,1,387,393]
[null,"PP_2215",null,"Pseudomonas putida KT2440","_","acetyl-CoA acetyltransferase","ACETYL-COA-ACETYLTRANSFER-RXN ; RHEA:21039 ;",0.98237,0.98985,44.1,{"v":5E-110,"d":"5.00E-110"},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",5,393,394,8,396,397]
[null,"SCFA_v1_3830001",null,"Ca. Phosphitivorax butyraticus R76","atoB","fragment of acetyl-CoA acetyltransferase (part 2)","ACETYL-COA-ACETYLTRANSFER-RXN ;",0.93677,1.01523,47,{"v":6e-110,"d":"6.00E-110"},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",3,376,394,28,427,427]
[null,"PSEEN3547",null,"Pseudomonas entomophila L48","fadAx","acetyl-CoA acetyltransferase with thiolase domain FadAx","_",0.98237,0.98985,43.59,{"v":2E-109,"d":"2.00E-109"},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)",5,393,394,8,396,397]
[null,"AZOLI_p10029",null,"Azospirillum lipoferum 4B","atoB","acetyl-CoA acetyltransferase with thiolase domain","_",1,1.00254,43.15,{"v":8e-108,"d":"8.00E-108"},2,1,"1.1.2.1 : Degradation of short-chain fatty acids ; 1.1 : Carbon compound utilization ; 1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ; 6.2 : Amino acids and amines ;","e : enzyme",7867955,"2a : Function from experimental evidences in other organisms",1,393,394,1,393,393]
[null,"VIBNIv4_A1234","_","Vibrio nigripulchritudo SFn1","phbA","Acetyl-CoA acetyltransferase","_",0.97462,0.97462,41.93,{"v":3e-107,"d":"3.00E-107"},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",4,387,394,5,387,394]
[null,"pRALTA_0081","_","Cupriavidus taiwanensis LMG19424","_","acetyl-CoA acetyltransferase","_",0.9675,0.98223,43.41,{"v":3e-107,"d":"3.00E-107"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,387,394,9,394,400]
[null,"Atu3475",null,"Agrobacterium tumefaciens C58","fadAx","acetyl-CoA C-acetyltransferase","_",0.93204,0.97462,45.31,{"v":6e-107,"d":"6.00E-107"},1,1,"1 : Metabolism ;","_","2 : Cytoplasmic","_","e : enzyme",11251808,"2b : Function from indirect experimental evidences (e.g. phenotypes)",5,387,394,32,406,412]
[null,"ACIAD2516",null,"Acinetobacter baylyi ADP1","atoB","acetyl-CoA acetyltransferase with thiolase domain","ACETYL-COA-ACETYLTRANSFER-RXN ; METHYLACETOACETYLCOATHIOL-RXN ; RXN-12561 ; RHEA:21039 ;",0.97462,0.97462,42.45,{"v":2e-106,"d":"2.00E-106"},3,1,"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",4,387,394,5,387,394]
[null,"NIDE3104",null,"Candidatus Nitrospira defluvii","fadA","3-ketoacyl-CoA thiolase","_",1,1.00508,43.43,{"v":6e-105,"d":"6.00E-105"},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)",3,393,394,2,396,396]
[null,"BN12v2_3170003","_","Tetrasphaera japonica T1-X7","phaA","acetyl-CoA acetyltransferase (fadA) (Acetoacetyl-CoA thiolase) (beta-ketothiolase)","_",0.97487,0.98477,44.85,{"v":2e-102,"d":"2.00E-102"},1,1,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",6,389,394,7,392,398]
[null,"RALTA_B1528","_","Cupriavidus taiwanensis LMG19424","_","putative acetyl-CoA acetyltransferase with thiolase domain","_",0.99502,1.01523,40.75,{"v":5e-101,"d":"5.00E-101"},1,1,"1.7 : Central intermediary metabolism ;","2.3.1.9","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,391,394,2,400,402]
[null,"MGMSRv2_3177",null,"Magnetospirillum gryphiswaldense MSR-1 v2","paaE","beta-ketoadipyl CoA thiolase","_",0.99751,1.01523,42,{"v":1E-99,"d":"1.00E-99"},3,1,"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",4,393,394,3,401,401]
[null,"BN381v2_150043","_","Candidatus Microthrix parvicella RN1","phaA","acetyl-CoA acetyltransferase","_",0.9797,0.98219,43.78,{"v":1E-99,"d":"1.00E-99"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","18246303, 10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",6,389,394,5,389,393]
[null,"AZOLI_p40026","_","Azospirillum lipoferum 4B","pcaF","Beta-ketoadipyl CoA thiolase","_",0.98522,1.01523,41.5,{"v":1E-99,"d":"1.00E-99"},1,1,"1.1 : Carbon compound utilization ;","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",9582432,"2a : Function from experimental evidences in other organisms",3,393,394,9,406,406]
[null,"THI_0462",null,"Thiomonas sp. 3As","pcaF1","Beta-ketoadipyl CoA thiolase","_",0.9975,1.01269,41.35,{"v":4e-99,"d":"4.00E-99"},3,1,"1 : Metabolism ;","2.3.1.-","2 : Cytoplasmic","5 : Central intermediary metabolism ;","e : enzyme",7961399,"2a : Function from experimental evidences in other organisms",4,393,394,3,400,400]
[null,"BN45v3_30404","_","Mycobacterium canettii STB-J","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.9797,0.99229,44.3,{"v":5e-99,"d":"5.00E-99"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",6,389,394,1,385,389]
[null,"BN13v1_460011","_","Tetrasphaera jenkinsii Ben74","_","putative Acetyl-CoA acetyltransferase (beta-ketothiolase) (phaA)","_",0.97487,0.98477,44.59,{"v":6e-99,"d":"6.00E-99"},1,1,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","3 : Putative function from multiple computational evidences",6,389,394,7,392,398]
[null,"ABAYE2367",null,"Acinetobacter baumannii AYE","paaJ","beta-ketoadipyl CoA thiolase with thiolase-like domain, phenylacetic acid degradation","_",1,1.0203,43.28,{"v":9e-99,"d":"9.00E-99"},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)",3,393,394,2,401,402]
[null,"BN42v3_21228","_","Mycobacterium canettii STB-K","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.9797,0.99229,44.3,{"v":2e-98,"d":"2.00E-98"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",6,389,394,1,385,389]
[null,"BN44v3_11488","_","Mycobacterium canettii STB-D","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.9797,0.99229,44.04,{"v":8e-98,"d":"8.00E-98"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",6,389,394,1,385,389]
[null,"BN43v3_30420","_","Mycobacterium canettii STB-L","fadA","Putative Acetyl-CoA acetyltransferase FadA4 (Acetoacetyl-CoA Thiolase)","_",0.9797,0.99229,44.04,{"v":8e-98,"d":"8.00E-98"},1,1,"1 : lipid metabolism ;","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11271494, 12010964, 12657046, 17443846","3 : Putative function from multiple computational evidences",6,389,394,1,385,389]
[null,"Pars_0309","_","Pyrobaculum arsenaticum DSM 13514","thlA","Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)","_",0.95332,0.98477,44.07,{"v":1e-96,"d":"1.00E-96"},1,1,"_","2.3.1.9","2 : Cytoplasmic","_","e : enzyme","11075929, 11466286, 1685080, 7867955","2a : Function from experimental evidences in other organisms",4,387,394,15,401,407]
[null,"ECK1394",null,"Escherichia coli K12","paaE","beta-ketoadipyl CoA thiolase","RXN-3641 ; RXN0-6512 ;",1,1.01777,40.65,{"v":3e-96,"d":"3.00E-96"},3,1,"1.1.5.1 : Phenylacetic acid degradation ;","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ; 6 : Energy metabolism ;","e : enzyme","10766858, 12846838, 17259607, 9748275","1a : Function from experimental evidences in the studied strain",3,393,394,2,401,401]
[null,"FRAAL5910","_","Frankia alni ACN14a","atoB","acetyl-CoA acetyltransferase with thiolase domain","_",0.97975,0.98223,43.15,{"v":3e-96,"d":"3.00E-96"},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)",6,389,394,5,389,395]
[null,"AZOLI_p40258",null,"Azospirillum lipoferum 4B","paaJ","beta-ketoadipyl CoA thiolase","_",1,1.0203,40.55,{"v":4e-93,"d":"4.00E-93"},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",3,393,394,2,402,402]
[null,"BN11v3_1860009","_","Tetrasphaera australiensis Ben110","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",0.97494,0.98731,42.67,{"v":1e-92,"d":"1.00E-92"},1,1,"_","2.3.1.9","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",6,389,394,8,393,399]
[null,"Rmet_1853",null,"Cupriavidus metallidurans CH34","atoB","acetyl-CoA acetyltransferase / thiolase","_",1.0203,1.02551,40.55,{"v":1E-91,"d":"1.00E-91"},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",4,393,394,3,392,392]
[null,"RALTA_A1469",null,"Cupriavidus taiwanensis LMG19424","_","putative 3-ketoacyl-CoA thiolase / acetyl-CoA acetyltransferase","_",1.0203,1.02551,40.05,{"v":2E-91,"d":"2.00E-91"},4,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16, 2.3.1.9","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,393,394,3,392,392]
[null,"ABAYE2307",null,"Acinetobacter baumannii AYE","dcaF","beta-ketoadipyl CoA thiolase","_",0.99002,1.00761,37.78,{"v":1e-90,"d":"1.00E-90"},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",7,393,394,6,400,401]
[null,"CMR15v5_2683",null,"Ralstonia solanacearum CMR15","_","acetyl-CoA acetyltransferase","_",1.02284,1.02806,39.7,{"v":1e-90,"d":"1.00E-90"},3,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16","1 : Unknown","3.2 : Degradation ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",4,391,394,3,390,392]
[null,"Rmet_3669","_","Cupriavidus metallidurans CH34","pcaF","acetyl-CoA acetyltransferase","_",0.9975,1.01269,39.1,{"v":7e-90,"d":"7.00E-90"},1,1,"1.1.2.7 : Acetoacetate degradation ;","_","1 : Unknown","_","c : carrier","_","2a : Function from experimental evidences in other organisms",4,393,394,3,400,400]
[null,"AZOLI_p30161","_","Azospirillum lipoferum 4B","phbA4","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",1.00508,1.01799,40.15,{"v":1E-89,"d":"1.00E-89"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","2.3.1.9","2 : Cytoplasmic","3.1 : Biosynthesis ;","e : enzyme","7582015, 1396692","2a : Function from experimental evidences in other organisms",1,391,394,1,387,389]
[null,"PSEEN2795",null,"Pseudomonas entomophila L48","pcaF-2","beta-ketoadipyl CoA thiolase","_",0.98768,1.01777,39.4,{"v":2e-89,"d":"2.00E-89"},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",6,393,394,10,406,406]
[null,"XDD1v4_3927",null,"Xenorhabdus doucetiae FRM16","paaJ","protein PaaJ; Beta-ketoadipyl-CoA thiolase","_",0.98762,1.01269,38.6,{"v":5e-89,"d":"5.00E-89"},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",7,393,394,6,403,404]
[null,"ACIAD1689",null,"Acinetobacter baylyi ADP1","dcaF","beta-ketoadipyl CoA thiolase","2.3.1.155-RXN ; KETOACYLCOATHIOL-RXN ; RXN-3641 ;",0.99002,1.00761,37.53,{"v":8e-89,"d":"8.00E-89"},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",7,393,394,6,400,401]
[null,"PP_3280",null,"Pseudomonas putida KT2440","paaJ","3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase","RXN0-6512 ; RXN-3641 ; RHEA:34441 ; RHEA:19483 ;",0.98522,1.01523,38,{"v":1e-88,"d":"1.00E-88"},5,1,"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",4,393,394,8,406,406]
[null,"XPG1v4_0713","_","Xenorhabdus poinarii G6","pcaF","Beta-ketoadipyl-CoA thiolase","_",0.98,0.99492,38.52,{"v":9e-87,"d":"9.00E-87"},1,1,"_","2.3.1.174","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",12,393,394,11,400,400]
[null,"BN11v3_1360003",null,"Tetrasphaera australiensis Ben110","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase)","_",0.99746,1.0155,38.93,{"v":2e-84,"d":"2.00E-84"},2,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme",17189250,"3 : Putative function from multiple computational evidences",3,393,394,4,387,387]
[null,"BN11v3_1350015",null,"Tetrasphaera australiensis Ben110","phaA","Acetyl-CoA acetyltransferase (beta-ketothiolase)","_",1.00246,1.03299,37.84,{"v":3e-82,"d":"3.00E-82"},3,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","10416645, 1987116, 2670936","2a : Function from experimental evidences in other organisms",4,393,394,3,405,406]
[null,"BRADO0983",null,"Bradyrhizobium sp. ORS278","pimB","Acetyl-CoA acetyltransferase with thiolase domain (Acetoacetyl-CoA thiolase)","_",1.02278,1.02538,38.61,{"v":1e-81,"d":"1.00E-81"},4,1,"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",4,394,394,3,395,395]
[null,"BBta_7072",null,"Bradyrhizobium sp. BTAi1","pimB","Acetyl-CoA acetyltransferase with thiolase domain","_",1.02278,1.02538,38.61,{"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","_","2a : Function from experimental evidences in other organisms",4,394,394,3,395,395]
[null,"AZCBGv1_p150132","_","Azospirillum brasilense CBG497","phaA","Beta-ketothiolase (acetyl-CoA acetyltransferase with thiolase domain)(Acetyl-CoA C-acyltransferase)","_",1,1.01809,37.06,{"v":2e-80,"d":"2.00E-80"},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",2,391,394,10,385,387]
[null,"BN42v3_20922",null,"Mycobacterium canettii STB-K","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",1.00741,1.03553,38.48,{"v":5E-80,"d":"5.00E-80"},2,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",4,393,394,3,404,405]
[null,"BN44v3_11190",null,"Mycobacterium canettii STB-D","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",1,1.04061,38.05,{"v":1E-79,"d":"1.00E-79"},2,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",4,393,394,8,409,410]
[null,"BN43v3_30127",null,"Mycobacterium canettii STB-L","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",1,1.04061,38.05,{"v":1E-79,"d":"1.00E-79"},2,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",4,393,394,8,409,410]
[null,"BN45v3_30114",null,"Mycobacterium canettii STB-J","fadA","Putative beta-ketoacyl CoA thiolase FadA3","_",0.99512,1.03553,38.24,{"v":2E-79,"d":"2.00E-79"},2,1,"1 : lipid metabolism ;","2.3.1.-","2 : Cytoplasmic","_","e : enzyme","10493122, 10510226, 12657046, 17443846","3 : Putative function from multiple computational evidences",4,393,394,8,409,410]
[null,"BN10v3_920035","_","Tetrasphaera elongata Lp2","_","Putative 3-ketoacyl-CoA thiolase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",1.02211,1.05584,37.02,{"v":1e-77,"d":"1.00E-77"},1,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",4,393,394,3,406,407]
[null,"MARHY2410",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","paaJ","ketoadipyl CoA thiolase subunit","_",1.03483,1.05584,36.54,{"v":8e-76,"d":"8.00E-76"},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)",1,393,394,1,402,402]
[null,"FRAAL2097",null,"Frankia alni ACN14a","fadA","3-ketoadipyl CoA thiolase","_",1.00506,1.00761,37.78,{"v":2e-74,"d":"2.00E-74"},5,1,"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)",5,392,394,1,384,395]
[null,"BN11v3_4910007",null,"Tetrasphaera australiensis Ben110","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",0.99752,1.0203,36.82,{"v":8E-73,"d":"8.00E-73"},4,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,392,394,6,393,403]
[null,"BN10v3_810005",null,"Tetrasphaera elongata Lp2","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",0.99752,1.0203,36.32,{"v":2e-72,"d":"2.00E-72"},3,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,392,394,6,393,403]
[null,"ACIAD2988",null,"Acinetobacter baylyi ADP1","_","putative thiolase; putative acyl-CoA thiolase","_",1.03483,1.05584,35.1,{"v":3e-72,"d":"3.00E-72"},8,1,"_","_","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,393,394,1,402,402]
[null,"BN13v1_130025",null,"Tetrasphaera jenkinsii Ben74","_","Putative acetyl-CoA C-acyltransferase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase (EC no 2.3.1.9)","_",1,1.02284,35.24,{"v":4E-70,"d":"4.00E-70"},4,1,"_","2.3.1.16","2 : Cytoplasmic","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,393,394,6,394,403]
[null,"RALSYv5_mp0378","_","Ralstonia syzygii R24","_","putative 3-ketoacyl-CoA thiolase / acetyl-CoA acetyltransferase (fragment)","_",0.43401,0.93443,43.27,{"v":4e-39,"d":"4.00E-39"},1,1,"1.1.2.1 : Degradation of short-chain fatty acids ;","2.3.1.16, 2.3.1.9","2 : Cytoplasmic","3.2 : Degradation ;","e : enzyme","_","3 : Putative function from multiple computational evidences",221,391,394,12,181,183]
[]
["AEQN01_300005","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_1873","_","Clostridiales BL-4","cat","Butyryl-CoA:acetate CoA-transferase","R11-RXN ;",0.99776,1,58.74,0,1,1,"_","2.8.3.-","2 : Cytoplasmic","_","e : enzyme","18218779, 8550525","2a : Function from experimental evidences in other organisms",1,445,446,1,446,447]
[null,"SCFA_v1_780005","_","Ca. Propionivorax syntrophicum F70","ACH1","Acetyl-CoA hydrolase","ACETYL-COA-HYDROLASE-RXN ; RHEA:20289 ;",1.00224,1.00903,52.57,{"v":2e-161,"d":"2.00E-161"},1,1,"_","3.1.2.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,446,446,1,443,443]
[null,"CLOSTRIBL3_v1_13110","_","Clostridiaceae BL-3","_","Butyryl-CoA:acetate CoA-transferase","_",0.97788,0.99103,51.13,{"v":3e-147,"d":"3.00E-147"},1,1,"_","2.8.3.-","2 : Cytoplasmic","_","e : enzyme","18218779, 8550525","2a : Function from experimental evidences in other organisms",6,445,446,10,449,452]
[null,"CD630_23390","_","Clostridium difficile 630","cat2","4-hydroxybutyrate CoA transferase","_",0.97758,1.0023,40.83,{"v":4E-95,"d":"4.00E-95"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","1385386, 11041350, 8550525","1c : Function from experimental evidences in the studied genus",1,436,446,1,429,435]
[]
["AEQN01_210004","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,"BN43v3_60289","_","Mycobacterium canettii STB-L","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.95373,0.97632,43.94,{"v":5e-101,"d":"5.00E-101"},1,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","10510226, 12775759, 15525680","3 : Putative function from multiple computational evidences",3,371,380,13,382,389]
[null,"CLOSTRIBL4_v1_2140",null,"Clostridiales BL-4","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47196 ;",0.59906,1.00263,45.14,{"v":7e-101,"d":"7.00E-101"},1,3,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286, 8399220, 7857927","2a : Function from experimental evidences in other organisms",1,379,380,1,380,636]
[null,"CLOSTRIBL3_v1_12502",null,"Clostridiaceae BL-3","bcd","Acyl-CoA dehydrogenase, short-chain specific","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47199 ; RHEA:24004 ;",0.6,1.00263,45.14,{"v":1E-100,"d":"1.00E-100"},3,4,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286, 8399220, 7857927","2a : Function from experimental evidences in other organisms",1,379,380,1,380,635]
[null,"CLOSTRIBL6_v1_1904",null,"Clostridiales BL-6","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47199 ;",0.6038,1.00263,45.67,{"v":1E-100,"d":"1.00E-100"},2,3,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,379,380,1,380,631]
[null,"CLOSTRIBL6_v1_3216",null,"Clostridiales BL-6","bud","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; RHEA:47199 ;",0.98158,0.98158,43.16,{"v":9e-100,"d":"9.00E-100"},3,4,"_","1.3.8.1","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 21398533","2a : Function from experimental evidences in other organisms",1,371,380,1,372,380]
[null,"BN12v2_410006","_","Tetrasphaera japonica T1-X7","_","acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.97416,0.99211,40.05,{"v":2E-95,"d":"2.00E-95"},1,1,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme",17189250,"2a : Function from experimental evidences in other organisms",3,377,380,10,386,387]
[null,"AZOLI_p40074","_","Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.95276,0.95526,43.53,{"v":6e-93,"d":"6.00E-93"},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)",19,379,380,19,379,381]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.96579,0.97347,40.87,{"v":2E-92,"d":"2.00E-92"},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",8,371,380,5,370,377]
[null,"BN13v1_920006","_","Tetrasphaera jenkinsii Ben74","_","putative acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.97927,0.99474,39.42,{"v":4e-91,"d":"4.00E-91"},1,1,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,377,380,8,385,386]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.94103,0.96579,40.05,{"v":2e-81,"d":"2.00E-81"},3,3,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",8,371,380,15,380,390]
[null,"BN381v2_250102","_","Candidatus Microthrix parvicella RN1","_","putative Acyl-CoA dehydrogenase","_",0.97561,1.05263,35.75,{"v":1e-67,"d":"1.00E-67"},1,1,"1.5.4 : Fatty acid and phosphatidic acid ;","1.3.8.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme",17189250,"3 : Putative function from multiple computational evidences",5,378,380,8,406,410]
[null,"AZOLI_p20054","_","Azospirillum lipoferum 4B","_","conserved protein of unknown function","_",0.18947,0.86747,37.5,0.024,1,1,"_","_","1 : Unknown","18 : Unknown function ;","u : unknown","_","4 : Unknown function but conserved in other organisms",32,94,380,3,74,83]
[]
["AEQN01_220142","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CD630_08030","_","Clostridium difficile 630","_","Putative acyl-CoA dehydrogenase","_",1,1.00263,57.48,{"v":1e-143,"d":"1.00E-143"},1,1,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,378,381,1,379,380]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.98688,0.99735,48.4,{"v":2e-122,"d":"2.00E-122"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","1.3.99.-","2 : Cytoplasmic","3.2 : Degradation ; 6.2 : Amino acids and amines ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",5,378,381,3,376,377]
[null,"RALSYv5_mp0315","_","Ralstonia syzygii R24","_","putative Butyryl-CoA dehydrogenase","_",0.99475,1.00531,48.28,{"v":4e-115,"d":"4.00E-115"},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",1,377,381,1,377,377]
[null,"BN873v1_590034","_","Candidatus Competibacter denitrificans Run_A_D11","_","putative acyl-CoA dehydrogenase","_",0.99475,1,47.23,{"v":2e-114,"d":"2.00E-114"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.8.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",3,379,381,1,377,379]
[null,"RSK60v3_mp750032","_","Ralstonia solanacearum K60","_","putative Butyryl-CoA dehydrogenase","_",0.99475,1.00531,48.81,{"v":1e-113,"d":"1.00E-113"},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",1,377,381,1,377,377]
[null,"CMR15v5_mp0941","_","Ralstonia solanacearum CMR15","_","putative Butyryl-CoA dehydrogenase","_",0.99475,1.00531,48.28,{"v":2E-113,"d":"2.00E-113"},1,1,"1 : Metabolism ;","1.3.99.2","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",1,377,381,1,377,377]
[null,"MGMSRv2_0193","_","Magnetospirillum gryphiswaldense MSR-1 v2","_","Acyl-CoA dehydrogenase","_",0.99475,0.99737,46.97,{"v":9e-112,"d":"9.00E-112"},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",3,379,381,1,377,380]
[null,"ACIAD1607","_","Acinetobacter baylyi ADP1","acads","Acyl-CoA dehydrogenase, short-chain specific","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; RXN0-2301 ; RHEA:24007 ; RHEA:12277 ;",0.979,0.99467,47.72,{"v":1e-111,"d":"1.00E-111"},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",7,377,381,5,375,375]
[null,"CMR15v5_0672",null,"Ralstonia solanacearum CMR15","_","putative acyl CoA dehydrogenase oxidoreductase protein","_",0.9895,1.00266,45.09,{"v":3e-110,"d":"3.00E-110"},1,1,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,377,381,1,375,376]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.9895,1.00266,44.3,{"v":8e-110,"d":"8.00E-110"},1,1,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",3,377,381,1,375,376]
[null,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.9895,1.00533,45.89,{"v":1E-107,"d":"1.00E-107"},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",3,377,381,1,375,375]
[null,"RALTA_B1110","_","Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.9685,1.00545,47.15,{"v":2E-107,"d":"2.00E-107"},1,1,"1 : Metabolism ;","1.3.99.-","2 : Cytoplasmic","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",11,377,381,1,367,367]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.9895,1.00266,42.97,{"v":1e-106,"d":"1.00E-106"},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)",3,377,381,1,375,376]
[null,"MARHY1099","_","Marinobacter hydrocarbonoclasticus ATCC 49840","_","acyl-CoA dehydrogenase","_",0.98196,1,39.11,{"v":2E-91,"d":"2.00E-91"},1,1,"_","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,378,381,1,379,388]
[null,"BRADO3138","_","Bradyrhizobium sp. ORS278","_","acyl-CoA dehydrogenase","_",1,1,41.47,{"v":2e-89,"d":"2.00E-89"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ; 1.1.3 : Amino acids ;","1.3.99.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",10524212,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,378,381,1,377,381]
[null,"BN10v3_1070026","_","Tetrasphaera elongata Lp2","_","putative short chain acyl-CoA dehydrogenase (Putative Butyryl-CoA dehydrogenase)","_",0.9601,1.0105,38.96,{"v":5e-89,"d":"5.00E-89"},1,1,"_","1.3.99.-","1 : Unknown","6 : Energy metabolism ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,378,381,10,394,401]
[null,"Rmet_4427","_","Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase(Butyryl-CoA dehydrogenase)","_",0.99227,1.0105,39.74,{"v":7e-86,"d":"7.00E-86"},1,1,"_","_","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,378,381,4,383,388]
[null,"THI_3281",null,"Thiomonas sp. 3As","ivd","Isovaleryl-CoA dehydrogenase","_",0.97449,1.00262,39.27,{"v":1E-83,"d":"1.00E-83"},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)",5,379,381,10,389,392]
[null,"BRADO1447",null,"Bradyrhizobium sp. ORS278","ivd2","isovaleryl-CoA dehydrogenase","_",0.95641,0.979,38.61,{"v":4e-83,"d":"4.00E-83"},2,2,"1.1.3.12 : Leucine degradation ;","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",5,375,381,13,383,390]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.95641,0.979,37.53,{"v":1e-82,"d":"1.00E-82"},3,2,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",5,375,381,13,383,390]
[null,"MARHY1166",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","ivdA","Isovaleryl-coenzyme A dehydrogenase","_",0.9768,0.99475,38.52,{"v":6e-82,"d":"6.00E-82"},2,2,"1.1.3 : Amino acids ;","1.3.99.10","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",14612443,"2a : Function from experimental evidences in other organisms",5,381,381,12,388,388]
[null,"CMR15v5_0667",null,"Ralstonia solanacearum CMR15","_","putative acyl-CoA dehydrogenase oxidoreductase","_",0.97201,1.00262,37.43,{"v":4E-78,"d":"4.00E-78"},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",5,379,381,11,390,393]
[null,"MARHY1169",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","fadE","long chain acyl coenzyme A dehydrogenase","_",0.93717,0.93963,39.11,{"v":3e-77,"d":"3.00E-77"},4,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.99.13","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",24,378,381,25,380,382]
[null,"RALTA_A0110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL-COA DEHYDROGENASE OXIDOREDUCTASE","_",0.97201,1.00262,37.96,{"v":3e-77,"d":"3.00E-77"},3,2,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,379,381,11,390,393]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.97201,1.00262,37.43,{"v":3e-76,"d":"3.00E-76"},3,2,"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",5,379,381,11,390,393]
[null,"SCFA_v1_1630002","_","Ca. Propionivorax syntrophicum F70","acdB","Acyl-CoA dehydrogenase, short-chain specific","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47196 ; RHEA:24004 ;",0.94898,0.97638,37.1,{"v":3e-76,"d":"3.00E-76"},1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",6,376,381,18,388,392]
[null,"BN381v2_80083","_","Candidatus Microthrix parvicella RN1","_","putative acyl-CoA dehydrogenase","ACYLCOADEHYDROG-RXN ; BUTYRYL-COA-DEHYDROGENASE-RXN ; LONG-CHAIN-ACYL-COA-DEHYDROGENASE-RXN ;",0.98953,0.99213,36.24,{"v":4e-75,"d":"4.00E-75"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","1.3.8.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",4,377,381,5,380,382]
[null,"METDI3005","_","Methylobacterium extorquens DM4","msd","methylsuccinyl-CoA dehydrogenase","_",0.68861,1.01575,39.28,{"v":3e-70,"d":"3.00E-70"},1,1,"_","1.3.8.4","2 : Cytoplasmic","_","e : enzyme","16856937, 17548827","1c : Function from experimental evidences in the studied genus",5,378,381,177,560,562]
[null,"META1_2223","_","Methylobacterium extorquens AM1","mcd","methylsuccinyl-CoA dehydrogenase, putative isobutyryl-CoA dehydrogenase","_",0.68861,1.01575,39.28,{"v":4E-70,"d":"4.00E-70"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","16856937, 17548827","2a : Function from experimental evidences in other organisms",5,378,381,177,560,562]
[null,"NBG4_v1_200003","_","Candidatus Sulfobium mesophilum","acdA","Acyl-CoA dehydrogenase","RHEA:47196 ; RHEA:24004 ;",0.94087,0.96063,37.16,{"v":1e-67,"d":"1.00E-67"},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",18,378,381,30,386,389]
[null,"BRADO1442",null,"Bradyrhizobium sp. ORS278","_","acyl-CoA dehydrogenase","_",0.86598,0.88189,37.2,{"v":3e-64,"d":"3.00E-64"},4,1,"1.1.3.12 : Leucine degradation ;","1.3.99.10","2 : Cytoplasmic","_","e : enzyme",9535763,"2a : Function from experimental evidences in other organisms",38,358,381,39,362,388]
[null,"BN43v3_20455",null,"Mycobacterium canettii STB-L","fadE","Putative acyl-CoA dehydrogenase FadE13","_",0.9267,0.92913,35.03,{"v":5e-61,"d":"5.00E-61"},6,3,"1 : lipid metabolism ;","1.3.99.-","1 : Unknown","_","e : enzyme",12657046,"3 : Putative function from multiple computational evidences",19,368,381,19,369,382]
[null,"BN43v3_20452",null,"Mycobacterium canettii STB-L","fadE","Acyl-CoA dehydrogenase FadE12","_",0.82474,0.8399,35.31,{"v":6e-50,"d":"6.00E-50"},8,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",43,358,381,46,362,388]
[null,"Rmet_6103","_","Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase-like protein (fragment)","_",0.56693,1.00935,36.57,{"v":4E-41,"d":"4.00E-41"},1,1,"1.1.2 : Fatty acids (fatty acid oxidation) ;","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",169,378,381,1,209,214]
[]
["AEQN01_250027","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","_",0.96907,0.98172,44.41,{"v":2E-107,"d":"2.00E-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",1,375,383,1,375,388]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.97911,0.99734,38.93,{"v":5e-87,"d":"5.00E-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)",5,377,383,2,375,376]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.97911,0.99734,38.13,{"v":3e-86,"d":"3.00E-86"},1,5,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,377,383,2,375,376]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.9765,0.99204,39.57,{"v":2E-85,"d":"2.00E-85"},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",6,377,383,3,375,377]
[null,"CMR15v5_0672",null,"Ralstonia solanacearum CMR15","_","putative acyl CoA dehydrogenase oxidoreductase protein","_",0.97911,0.99734,37.6,{"v":5E-80,"d":"5.00E-80"},1,5,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,377,383,2,375,376]
[null,"ABAYE2315",null,"Acinetobacter baumannii AYE","dcaA","acyl-CoA dehydrogenase","_",0.96867,0.96867,37.74,{"v":3e-73,"d":"3.00E-73"},4,4,"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",13,379,383,11,380,383]
[null,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.97911,1,36.27,{"v":2e-72,"d":"2.00E-72"},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",5,377,383,2,375,375]
[null,"RALTA_B0350","_","Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.93095,0.95039,37.91,{"v":3e-72,"d":"3.00E-72"},1,1,"1.4 : Energy production/transport ;","1.3.99.-","1 : Unknown","6.5 : Electron transport ;","e : enzyme","_","3 : Putative function from multiple computational evidences",17,379,383,20,381,391]
[null,"THI_3281",null,"Thiomonas sp. 3As","ivd","Isovaleryl-CoA dehydrogenase","_",0.97704,1,36.55,{"v":4e-72,"d":"4.00E-72"},2,3,"1.1.3.12 : Leucine degradation ;","1.3.99.10","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme","10677295, 12477932, 12665801, 1310317, 2318964, 7640268, 8468053, 921428","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,377,383,7,387,392]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.92821,0.94517,35.64,{"v":6e-72,"d":"6.00E-72"},3,5,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",18,377,383,25,385,390]
[null,"CMR15v5_0667",null,"Ralstonia solanacearum CMR15","_","putative acyl-CoA dehydrogenase oxidoreductase","_",0.97201,0.99739,35.86,{"v":1e-71,"d":"1.00E-71"},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",4,377,383,9,388,393]
[null,"RALTA_A0110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL-COA DEHYDROGENASE OXIDOREDUCTASE","_",0.96692,0.99217,35.26,{"v":4e-69,"d":"4.00E-69"},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",4,377,383,9,388,393]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.9313,0.95561,35.25,{"v":2e-67,"d":"2.00E-67"},3,3,"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",18,377,383,23,388,393]
[]
["AEQN01_230141","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_2140",null,"Clostridiales BL-4","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47196 ;",1,1.00472,77,0,1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286, 8399220, 7857927","2a : Function from experimental evidences in other organisms",1,638,639,1,635,636]
[null,"CLOSTRIBL6_v1_1904",null,"Clostridiales BL-6","bcd","Butyryl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47199 ;",1.00156,1.01426,73.28,0,1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,638,639,1,630,631]
[null,"CLOSTRIBL3_v1_12502",null,"Clostridiaceae BL-3","bcd","Acyl-CoA dehydrogenase, short-chain specific","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:47199 ; RHEA:24004 ;",1.00156,1.00787,71.09,0,1,1,"_","1.3.8.1","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286, 8399220, 7857927","2a : Function from experimental evidences in other organisms",1,638,639,1,634,635]
[null,"CD630_10540","_","Clostridium difficile 630","bcd2","Butyryl-CoA dehydrogenase","_",0.58372,0.98677,58.45,{"v":3e-145,"d":"3.00E-145"},1,1,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",6,378,639,5,377,378]
[null,"BSU24150","_","Bacillus subtilis 168","mmgC","propionyl-CoA dehydrogenase subunit","_",0.58685,0.98945,55.47,{"v":4e-141,"d":"4.00E-141"},1,1,"2.4 : Metabolism of lipids ;","1.3.99.-","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme",28956599,"1a : Function from experimental evidences in the studied strain",5,379,639,3,377,379]
[null,"SCFA_v1_1080002","_","Ca. Phosphitivorax butyraticus R76","acdA","Acyl-CoA dehydrogenase","_",0.59311,0.98956,50.13,{"v":1e-121,"d":"1.00E-121"},1,1,"_","1.3.8.-","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,380,639,3,381,383]
[null,"SCFA_v1_190035","_","Ca. Phosphitivorax anaerolimi F81","bcd","acyl-CoA dehydrogenase, short-chain specific (Butyryl-CoA dehydrogenase)","_",0.59468,0.99476,48.95,{"v":7e-119,"d":"7.00E-119"},1,1,"_","1.3.8.1","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,379,639,1,380,382]
[null,"PSEEN3546","_","Pseudomonas entomophila L48","fadFx","acyl-CoA dehydrogenase protein FadFx","_",0.58372,0.99467,46.65,{"v":5e-113,"d":"5.00E-113"},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",5,377,639,3,375,375]
[null,"PP_2216","_","Pseudomonas putida KT2440","acd","short-chain acyl-CoA dehydrogenase","BUTYRYL-COA-DEHYDROGENASE-RXN ; RHEA:24007 ;",0.58372,0.99467,46.65,{"v":8e-112,"d":"8.00E-112"},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",5,377,639,3,375,375]
[null,"AZOLI_p10028",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.58529,0.99204,45.45,{"v":2E-107,"d":"2.00E-107"},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",5,378,639,3,376,377]
[null,"RALTA_A0115",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL COA DEHYDROGENASE OXIDOREDUCTASE PROTEIN","_",0.58372,0.99202,45.04,{"v":5e-107,"d":"5.00E-107"},1,2,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,377,639,3,375,376]
[null,"Rmet_0108",null,"Cupriavidus metallidurans CH34","_","acyl-CoA dehydrogenase, short-chain specific","_",0.58372,0.99202,44.77,{"v":3e-106,"d":"3.00E-106"},1,2,"_","1.3.99.2","1 : Unknown","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",5,377,639,3,375,376]
[null,"CMR15v5_0672",null,"Ralstonia solanacearum CMR15","_","putative acyl CoA dehydrogenase oxidoreductase protein","_",0.58372,0.99202,43.43,{"v":3E-103,"d":"3.00E-103"},1,2,"1 : Metabolism ;","1.3.99.-","1 : Unknown","18.1 : Enzymes of unknown specificity ;","e : enzyme","_","3 : Putative function from multiple computational evidences",5,377,639,3,375,376]
[null,"BN45v3_60311","_","Mycobacterium canettii STB-J","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.59155,0.97172,44.97,{"v":3e-101,"d":"3.00E-101"},1,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","10510226, 12775759, 15525680","3 : Putative function from multiple computational evidences",2,378,639,12,388,389]
[null,"BN44v3_70065","_","Mycobacterium canettii STB-D","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.59155,0.97172,44.97,{"v":3e-101,"d":"3.00E-101"},1,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","10510226, 12775759, 15525680","3 : Putative function from multiple computational evidences",2,378,639,12,388,389]
[null,"BN42v3_41331","_","Mycobacterium canettii STB-K","fadE","Putative acyl-CoA dehydrogenase FadE25","_",0.59155,0.97172,44.97,{"v":3e-101,"d":"3.00E-101"},1,1,"1 : lipid metabolism ;","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","10510226, 12775759, 15525680","3 : Putative function from multiple computational evidences",2,378,639,12,388,389]
[null,"THI_3277",null,"Thiomonas sp. 3As","bcd","Short-chain specific acyl-CoA dehydrogenase (SCAD) (Butyryl-CoA dehydrogenase)","_",0.58372,0.99467,43.43,{"v":3E-98,"d":"3.00E-98"},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",5,377,639,3,375,375]
[null,"BN13v1_430010","_","Tetrasphaera jenkinsii Ben74","_","putative acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.61033,0.98985,43.85,{"v":1E-97,"d":"1.00E-97"},1,1,"_","1.3.99.-","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,377,639,1,390,394]
[null,"MARHY1166","_","Marinobacter hydrocarbonoclasticus ATCC 49840","ivdA","Isovaleryl-coenzyme A dehydrogenase","_",0.58685,0.96649,41.87,{"v":1e-96,"d":"1.00E-96"},1,1,"1.1.3 : Amino acids ;","1.3.99.10","1 : Unknown","5 : Central intermediary metabolism ;","e : enzyme",14612443,"2a : Function from experimental evidences in other organisms",3,377,639,10,384,388]
[null,"BRADO1447","_","Bradyrhizobium sp. ORS278","ivd2","isovaleryl-CoA dehydrogenase","_",0.59155,0.96923,41.8,{"v":1e-95,"d":"1.00E-95"},1,1,"1.1.3.12 : Leucine degradation ;","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,380,639,11,388,390]
[null,"AZOLI_p10030",null,"Azospirillum lipoferum 4B","_","acyl-CoA dehydrogenase","_",0.58685,0.96154,40.27,{"v":1e-92,"d":"1.00E-92"},2,1,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","_","2a : Function from experimental evidences in other organisms",3,377,639,11,385,390]
[null,"BN12v2_410044","_","Tetrasphaera japonica T1-X7","_","putative acyl-CoA dehydrogenase (putative Butyryl-CoA dehydrogenase (EC no. 1.3.99.2))","_",0.60407,0.98721,42.75,{"v":2E-92,"d":"2.00E-92"},1,1,"_","1.3.99.-","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",2,377,639,1,386,391]
[null,"VIBNIv4_B0452","_","Vibrio nigripulchritudo SFn1","_","putative Acyl-CoA dehydrogenase","_",0.58842,0.97409,41.76,{"v":2E-90,"d":"2.00E-90"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","3 : Putative function from multiple computational evidences",7,378,639,10,380,386]
[null,"lpg1824","_","Legionella pneumophila subsp. pneumophila Philadelphia 1","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.58685,0.96401,39.73,{"v":7e-89,"d":"7.00E-89"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,377,639,10,384,389]
[null,"lpl1788","_","Legionella pneumophila Lens","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.58685,0.96401,39.73,{"v":7e-89,"d":"7.00E-89"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,377,639,10,384,389]
[null,"lpp1787","_","Legionella pneumophila Paris","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.58685,0.96401,39.73,{"v":7e-89,"d":"7.00E-89"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,377,639,10,384,389]
[null,"LPVv2_2096","_","Legionella pneumophila subsp. pneumophila HL06041035","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.58685,0.9715,39.73,{"v":7e-89,"d":"7.00E-89"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,377,639,7,381,386]
[null,"LPC_1268","_","Legionella pneumophila Corby","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.58685,0.9715,39.73,{"v":7e-89,"d":"7.00E-89"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,377,639,7,381,386]
[null,"Rmet_0103",null,"Cupriavidus metallidurans CH34","ivd1","isovaleryl-CoA dehydrogenase","_",0.59937,0.97455,40.47,{"v":1e-88,"d":"1.00E-88"},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",3,380,639,9,391,393]
[null,"LPOv2_1885","_","Legionella pneumophila subsp. pneumophila Lorraine","ivd","Isovaleryl-CoA dehydrogenase 2, mitochondrial precursor (IVD 2)","_",0.58685,0.9715,39.47,{"v":3e-88,"d":"3.00E-88"},1,1,"_","1.3.99.10","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",3,377,639,7,381,386]
[null,"CMR15v5_0667",null,"Ralstonia solanacearum CMR15","_","putative acyl-CoA dehydrogenase oxidoreductase","_",0.59468,0.96692,39.21,{"v":9e-87,"d":"9.00E-87"},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",3,377,639,9,388,393]
[null,"THI_3281",null,"Thiomonas sp. 3As","ivd","Isovaleryl-CoA dehydrogenase","_",0.59937,0.97704,38.64,{"v":1e-85,"d":"1.00E-85"},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)",3,380,639,8,390,392]
[null,"RALTA_A0110",null,"Cupriavidus taiwanensis LMG19424","_","putative ACYL-COA DEHYDROGENASE OXIDOREDUCTASE","_",0.59937,0.97455,39.43,{"v":2E-85,"d":"2.00E-85"},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",3,380,639,9,391,393]
[null,"VIBNIv4_A0948","_","Vibrio nigripulchritudo SFn1","ACAD8","Isobutyryl-CoA dehydrogenase","_",0.59311,0.98698,41.69,{"v":4e-83,"d":"4.00E-83"},1,1,"1.1.3.14 : Valine degradation ;","1.3.99.-","1 : Unknown","6.2 : Amino acids and amines ;","e : enzyme","10524212, 11013134, 14702039, 15489334, 10235267, 14752098, 12359132, 15505379, 16857760","2a : Function from experimental evidences in other organisms",1,378,639,1,377,384]
[null,"Npun_R3440","_","Nostoc punctiforme ATCC 29133; PCC 73102","_","putative acyl-CoA dehydrogenase","_",0.58842,0.95431,36.44,{"v":5e-69,"d":"5.00E-69"},1,1,"_","1.3.99.2","1 : Unknown","_","e : enzyme","_","3 : Putative function from multiple computational evidences",1,374,639,1,370,394]
[null,"METDI5267","_","Methylobacterium extorquens DM4","_","putative acyl-CoA dehydrogenase","_",0.61972,0.97059,37.12,{"v":2E-66,"d":"2.00E-66"},1,1,"_","1.3.99.-","2 : Cytoplasmic","3 : Fatty acid and phospholipid metabolism ;","e : enzyme","11812788, 2777793, 8759838","3 : Putative function from multiple computational evidences",6,384,639,20,408,408]
[null,"XNC1_1707","_","Xenorhabdus nematophila ATCC19061","xcnE","Acyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",0.58685,0.97911,36.8,{"v":2E-66,"d":"2.00E-66"},1,1,"_","1.3.99.2","1 : Unknown","_","e : enzyme","16349198, 1955881","1a : Function from experimental evidences in the studied strain",17,389,639,14,379,383]
[null,"XDD1v4_1795","_","Xenorhabdus doucetiae FRM16","xcnE","Acyl-CoA dehydrogenase involved in xenocoumacin synthesis","_",0.58685,0.97911,36.8,{"v":3e-66,"d":"3.00E-66"},1,1,"_","1.3.8.1","1 : Unknown","_","e : enzyme","16349198, 1955881","2a : Function from experimental evidences in other organisms",17,389,639,14,379,383]
[null,"NMA1201",null,"Neisseria meningitidis Z2491","rubA","rubredoxin (Rd)","_",0.07355,0.83929,48.94,2e-11,2,3,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",590,636,639,3,49,56]
[]
["AEQN01_220164","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","_",1,1.00752,66.04,{"v":2e-122,"d":"2.00E-122"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme",9694853,"2a : Function from experimental evidences in other organisms",1,266,266,1,268,268]
[null,"CD630_08040",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein beta-subunit, core","_",0.98872,0.99621,54.37,{"v":9e-85,"d":"9.00E-85"},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",1,260,266,1,258,264]
[null,"CLOSTRIBL3_v1_12011",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1.00376,1.01908,48.69,{"v":1e-76,"d":"1.00E-76"},2,1,"1.3 : Energy metabolism (carbon) ;","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,266,266,1,262,262]
[null,"CD630_04000",null,"Clostridium difficile 630","etfB1","Beta-subunit of electron transfer flavoprotein","_",0.98496,1.00383,48.85,{"v":1e-76,"d":"1.00E-76"},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",1,262,266,1,258,261]
[null,"SBF1_v1_470015",null,"Desulfosporosinus sp. SbF1","fixA","electron-transferring flavoprotein, subunit FixA","_",0.96751,1.00752,44.4,{"v":1e-72,"d":"1.00E-72"},1,1,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,266,266,1,266,277]
[null,"CLOSTRIBL3_v1_20311",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.98496,1.01158,45.42,{"v":2E-70,"d":"2.00E-70"},3,1,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286, 9694853","2a : Function from experimental evidences in other organisms",1,262,266,1,256,259]
[null,"CLOSTRIBL6_v1_0136",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein subunit beta","_",0.98496,1.01158,46.18,{"v":7e-69,"d":"7.00E-69"},2,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,262,266,1,256,259]
[null,"MGMSRv2_1063",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.94604,0.98872,45.25,{"v":1e-67,"d":"1.00E-67"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",1,256,266,1,261,278]
[null,"MGMSRv2_0362",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixA","Electron transfer flavoprotein, beta-subunit","_",0.87324,0.93233,44.76,{"v":6e-67,"d":"6.00E-67"},2,1,"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",1,244,266,1,247,284]
[null,"CLOSTRIBL3_v1_11115",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.98496,1,43.51,{"v":9e-66,"d":"9.00E-66"},4,1,"_","_","2 : Cytoplasmic","_","c : carrier","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,260,266,1,256,262]
[null,"CLOSTRIBL3_v1_20124",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",0.99248,0.99623,41.67,{"v":9e-66,"d":"9.00E-66"},5,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,261,266,1,257,265]
[null,"AZOLI_0535",null,"Azospirillum lipoferum 4B","fixA","electron transfer flavoprotein beta subunit","_",0.92933,0.98872,43.35,{"v":1e-64,"d":"1.00E-64"},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",1,259,266,1,261,283]
[null,"CD630_11710",null,"Clostridium difficile 630","etfB","Electron transfer flavoprotein subunit alpha","_",0.99248,0.99623,44.32,{"v":1e-64,"d":"1.00E-64"},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",1,262,266,4,261,265]
[null,"SBF1_v1_6700003",null,"Desulfosporosinus sp. SbF1","etfB_2","electron-transferring flavoprotein, beta subunit EtfB (lutD-associated)","_",0.96241,1.01186,42.58,{"v":4e-64,"d":"4.00E-64"},2,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",1,254,266,1,249,253]
[null,"BRADO5386",null,"Bradyrhizobium sp. ORS278","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.94662,1,42.48,{"v":1E-62,"d":"1.00E-62"},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)",1,262,266,1,265,281]
[null,"CD630_10550",null,"Clostridium difficile 630","etfB","Electron transfer flavoproteins subunit beta","_",0.98872,0.99245,42.59,{"v":3e-62,"d":"3.00E-62"},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",1,262,266,6,262,265]
[null,"CLOSTRIBL3_v1_11488",null,"Clostridiaceae BL-3","etfB","Electron transfer flavoprotein subunit beta","_",1.01128,1.01509,43.87,{"v":3e-61,"d":"3.00E-61"},6,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,266,266,1,264,265]
[null,"CLOSTRIBL4_v1_1871",null,"Clostridiales BL-4","etfB","Electron transfer flavoprotein subunit beta","_",1.01504,1.01504,41.11,{"v":2e-59,"d":"2.00E-59"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,266,266,1,266,266]
[null,"RM41v1_psym670028",null,"Sinorhizobium sp. Rm41","fixA","protein fixA; electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.83219,0.91353,44.44,{"v":7e-59,"d":"7.00E-59"},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)",1,239,266,1,242,292]
[null,"pRALTA_0381",null,"Cupriavidus taiwanensis LMG19424","fixA","Electron transfer flavoprotein beta-subunit","_",0.95035,1.00752,41.04,{"v":5e-57,"d":"5.00E-57"},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",1,262,266,1,260,282]
[null,"CLOSTRIBL6_v1_2821",null,"Clostridiales BL-6","etfB","Electron transfer flavoprotein, beta subunit","_",1.01504,1.01504,40,{"v":1E-56,"d":"1.00E-56"},3,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,266,266,1,266,266]
[null,"BURPHP2_0599",null,"Burkholderia phymatum STM815","fixA","protein fixA, electron transfer flavoprotein beta-subunit (Beta-ETF)","_",0.84752,0.8985,43.1,{"v":2E-55,"d":"2.00E-55"},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",1,235,266,1,237,282]
[null,"SCFA_v1_130010",null,"Ca. Phosphitivorax anaerolimi F81","etfB","Electron transfer flavoprotein subunit beta","_",0.98872,1.01938,36.12,{"v":8e-43,"d":"8.00E-43"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,259,266,1,247,258]
[null,"SCFA_v1_3390002","_","Ca. Phosphitivorax butyraticus R76","etfB","Electron transfer flavoprotein subunit beta","_",0.98496,1.0155,35.5,{"v":1E-42,"d":"1.00E-42"},1,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,259,266,1,247,258]
[null,"SCFA_v1_1630003","_","Ca. Propionivorax syntrophicum F70","FixA","Electron transfer flavoproteins subunit beta","_",0.96241,0.9697,37.5,{"v":2e-42,"d":"2.00E-42"},1,1,"_","_","1 : Unknown","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,253,266,1,248,264]
[null,"BN77v1_0452","_","Rhizobium mesoamericanum STM3625","etfB","Electron transfer flavoprotein beta-subunit (Beta-ETF) (Electron transfer flavoprotein small subunit) (ETFSS)","_",0.65038,0.865,38.73,{"v":5e-25,"d":"5.00E-25"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier",10026281,"2a : Function from experimental evidences in other organisms",1,172,266,34,199,200]
[]
["AEQN01_220165","Label","Synteny","Organism","Gene","Product","Reaction","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Roles","EC number","Localization","BioProcess","Product Type","PubMedId","Class","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"CLOSTRIBL6_v1_3217",null,"Clostridiales BL-6","etfA","Electron transfer flavoprotein subunit alpha","_",0.99701,1,72.75,{"v":1E-176,"d":"1.00E-176"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme",9694853,"2a : Function from experimental evidences in other organisms",1,334,335,1,333,334]
[null,"CLOSTRIBL3_v1_12010",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.97917,0.98209,53.5,{"v":4e-123,"d":"4.00E-123"},1,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",6,334,335,7,334,336]
[null,"CLOSTRIBL3_v1_20312",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.98209,0.98799,54.41,{"v":7e-121,"d":"7.00E-121"},2,1,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","c : carrier","17189250, 20059546, 21398533, 8655474, 11466286","2a : Function from experimental evidences in other organisms",6,334,335,7,333,333]
[null,"CD630_04010",null,"Clostridium difficile 630","etfA1","Alpha-subunit of electron transfer flavoprotein","_",0.95072,0.9791,52.74,{"v":2e-117,"d":"2.00E-117"},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",6,333,335,11,336,345]
[null,"CLOSTRIBL6_v1_0137",null,"Clostridiales BL-6","etfA","electron transfer flavoprotein (alpha subunit)","_",0.95665,0.98806,51.06,{"v":7e-115,"d":"7.00E-115"},2,1,"_","_","2 : Cytoplasmic","16.11 : Scavenge (Catabolism) ;","e : enzyme","17189250, 20059546, 21398533","2a : Function from experimental evidences in other organisms",6,335,335,14,341,346]
[null,"CLOSTRIBL4_v1_1872",null,"Clostridiales BL-4","etfA","Electron transfer flavoprotein subunit alpha","_",0.96739,1.06269,47.75,{"v":7e-107,"d":"7.00E-107"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",6,335,335,13,366,368]
[null,"CD630_08050",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein alpha-subunit","_",0.96176,0.97612,50.46,{"v":2e-105,"d":"2.00E-105"},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",8,332,335,18,340,340]
[null,"SBF1_v1_470014",null,"Desulfosporosinus sp. SbF1","fixB","electron-transferring flavoprotein, subunit FixB","_",0.73363,0.97015,50.77,{"v":3E-103,"d":"3.00E-103"},1,1,"_","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",8,332,335,113,435,443]
[null,"CD630_10560",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.94048,0.94328,49.05,{"v":5e-97,"d":"5.00E-97"},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",21,334,335,16,328,336]
[null,"CLOSTRIBL3_v1_20125",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.98507,0.99099,44.55,{"v":4E-95,"d":"4.00E-95"},4,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",6,334,335,2,329,333]
[null,"MGMSRv2_1064",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.89617,0.9791,45.43,{"v":2e-94,"d":"2.00E-94"},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)",8,332,335,31,357,366]
[null,"BURPHP2_0598",null,"Burkholderia phymatum STM815","fixB","Protein fixB, Electron transfer flavoprotein, alpha subunit","_",0.86898,0.97015,46.15,{"v":3e-93,"d":"3.00E-93"},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",8,329,335,35,358,374]
[null,"pRALTA_0380",null,"Cupriavidus taiwanensis LMG19424","fixB","Electron transfer flavoprotein, alpha subunit","_",0.872,0.97612,44.95,{"v":1e-90,"d":"1.00E-90"},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",6,329,335,33,358,375]
[null,"MGMSRv2_0361",null,"Magnetospirillum gryphiswaldense MSR-1 v2","fixB","Electron transfer flavoprotein, alpha subunit","_",0.89674,0.98507,45.76,{"v":1E-89,"d":"1.00E-89"},2,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","5.6 : Nitrogen fixation ;","c : carrier","15028689, 3029021, 7875566, 8796346, 9163424, 8599534, 2503674","2a : Function from experimental evidences in other organisms",6,332,335,32,359,368]
[null,"BRADO5385",null,"Bradyrhizobium sp. ORS278","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.89402,0.98209,44.98,{"v":7e-86,"d":"7.00E-86"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","5.6 : Nitrogen fixation ;","c : carrier",15028689,"2b : Function from indirect experimental evidences (e.g. phenotypes)",6,331,335,29,355,368]
[null,"RM41v1_psym670029",null,"Sinorhizobium sp. Rm41","fixB","protein FixB; electron transfer flavoprotein alpha chain","_",0.92635,0.97612,42.81,{"v":1e-85,"d":"1.00E-85"},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",6,328,335,13,337,353]
[null,"BSU28520",null,"Bacillus subtilis 168","etfA","electron transfer flavoprotein (alpha subunit)","_",0.94925,0.97846,43.08,{"v":4e-83,"d":"4.00E-83"},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",17,333,335,13,321,325]
[null,"AZOLI_0536",null,"Azospirillum lipoferum 4B","fixB","electron transfer flavoprotein alpha chain","_",0.91086,0.97612,43.12,{"v":5e-82,"d":"5.00E-82"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","6.5 : Electron transport ; 5.6 : Nitrogen fixation ;","c : carrier",15028689,"2a : Function from experimental evidences in other organisms",6,329,335,22,347,359]
[null,"SCFA_v1_130009",null,"Ca. Phosphitivorax anaerolimi F81","etfA","Electron transfer flavoprotein subunit alpha","_",0.95224,0.99068,44.2,{"v":2e-77,"d":"2.00E-77"},1,1,"_","_","2 : Cytoplasmic","_","e : enzyme","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",18,334,335,13,321,322]
[null,"CLOSTRIBL3_v1_11114",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.83911,1.01194,38.64,{"v":2E-73,"d":"2.00E-73"},5,1,"_","_","2 : Cytoplasmic","_","c : carrier",17189250,"2a : Function from experimental evidences in other organisms",1,334,335,63,398,404]
[null,"CLOSTRIBL3_v1_11487",null,"Clostridiaceae BL-3","etfA","Electron transfer flavoprotein subunit alpha","_",0.99403,1.01524,41.74,{"v":5e-72,"d":"5.00E-72"},6,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",1,331,335,1,323,328]
[null,"LEPBIa1132",null,"Leptospira biflexa serovar Patoc Patoc 1","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.95224,1,42.01,{"v":1e-71,"d":"1.00E-71"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","16.10 : Respire ;","c : carrier","_","2a : Function from experimental evidences in other organisms",17,333,335,12,317,319]
[null,"SBF1_v1_6700004",null,"Desulfosporosinus sp. SbF1","etfA_2","electron-transferring flavoprotein, alpha subunit EtfA (lutD-associated)","_",0.84826,1.01791,38.42,{"v":2e-68,"d":"2.00E-68"},3,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2a : Function from experimental evidences in other organisms",6,335,335,68,397,402]
[null,"CD630_11720",null,"Clostridium difficile 630","etfA","Electron transfer flavoprotein subunit alpha","_",0.83251,1.00896,37.57,{"v":3e-67,"d":"3.00E-67"},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",6,334,335,66,394,406]
[null,"FRAAL5877",null,"Frankia alni ACN14a","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.98507,1.03125,38.48,{"v":5e-65,"d":"5.00E-65"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","16.1 : Circulate ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",7,335,335,3,319,320]
[null,"SCFA_v1_2400007","_","Ca. Phosphitivorax butyraticus R76","etfA","Electron transfer flavoprotein subunit alpha","_",1,1.00601,37.01,{"v":1e-64,"d":"1.00E-64"},1,1,"_","_","2 : Cytoplasmic","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",1,332,335,1,329,333]
[null,"MARHY1802",null,"Marinobacter hydrocarbonoclasticus ATCC 49840","etfA","electron transfer flavoprotein alpha-subunit","_",0.88358,0.94569,40.2,{"v":1E-62,"d":"1.00E-62"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6 : Energy metabolism ;","c : carrier",3415685,"2a : Function from experimental evidences in other organisms",39,333,335,29,312,313]
[null,"CLOSTRIBL6_v1_2820",null,"Clostridiales BL-6","etfA","Electron transfer flavoprotein subunit alpha","_",0.95522,0.97561,41.88,{"v":1e-60,"d":"1.00E-60"},3,1,"_","_","2 : Cytoplasmic","_","e : enzyme","8655474, 11466286","2a : Function from experimental evidences in other organisms",18,335,335,17,327,328]
[null,"HEAR0620",null,"Herminiimonas arsenicoxydans","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.87463,0.94822,41.3,{"v":4e-59,"d":"4.00E-59"},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",39,330,335,29,308,309]
[null,"NMV_2368",null,"Neisseria meningitidis NEM8013","etfA","electron transfer flavoprotein alpha-subunit (alpha-ETF; electron transfer flavoprotein large subunit; ETFLS)","_",0.87761,0.94534,42.18,{"v":5e-59,"d":"5.00E-59"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","f : factor","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",40,331,335,29,310,311]
[null,"CMR15v5_3436",null,"Ralstonia solanacearum CMR15","etfA","Electron transfer flavoprotein, alpha-subunit","_",0.87761,0.94534,41.84,{"v":8e-59,"d":"8.00E-59"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",39,330,335,29,310,311]
[null,"Rmet_0738",null,"Cupriavidus metallidurans CH34","etfA","Electron transfer flavoprotein subunit alpha (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.87761,0.94534,42.52,{"v":1E-58,"d":"1.00E-58"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",39,330,335,29,310,311]
[null,"Rmet_5518",null,"Cupriavidus metallidurans CH34","etfA","electron transfer flavoprotein, alpha subunit","_",0.87761,0.94839,41.16,{"v":2e-57,"d":"2.00E-57"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","_","c : carrier","10026281, 1576992, 8376381, 8599534","2a : Function from experimental evidences in other organisms",39,330,335,29,310,310]
[null,"BURPHK2_1883",null,"Burkholderia phymatum STM815","etfA","electron transfer flavoprotein, alpha subunit","_",0.89851,0.96474,39.53,{"v":3E-57,"d":"3.00E-57"},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",35,331,335,25,311,312]
[null,"BN45v3_60005",null,"Mycobacterium canettii STB-J","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.98507,1.03774,38.79,{"v":5e-57,"d":"5.00E-57"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",7,334,335,3,317,318]
[null,"BN44v3_60522",null,"Mycobacterium canettii STB-D","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.98507,1.03774,38.79,{"v":7e-57,"d":"7.00E-57"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",7,334,335,3,317,318]
[null,"BN43v3_60007",null,"Mycobacterium canettii STB-L","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.98507,1.03774,38.79,{"v":7e-57,"d":"7.00E-57"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",7,334,335,3,317,318]
[null,"RALTA_A0796",null,"Cupriavidus taiwanensis LMG19424","etfA","ELECTRON TRANSFER FLAVOPROTEIN, ALPHA-SUBUNIT","_",0.87761,0.94534,40.82,{"v":9e-57,"d":"9.00E-57"},1,1,"1.4.3 : Electron carrier ;","_","1 : Unknown","6.5 : Electron transport ;","c : carrier","_","2b : Function from indirect experimental evidences (e.g. phenotypes)",39,330,335,29,310,311]
[null,"AZOLI_p50300",null,"Azospirillum lipoferum 4B","etfA2","Electron transfer flavoprotein alpha-subunit","_",0.88657,0.95192,39.39,{"v":1E-56,"d":"1.00E-56"},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)",35,330,335,26,311,312]
[null,"BN42v3_41031",null,"Mycobacterium canettii STB-K","fixB","Putative electron transfer flavoprotein (alpha-subunit) FixB (alpha-ETF) (electron transfer flavoprotein large subunit) (ETFLS)","_",0.98507,1.03774,38.48,{"v":8e-56,"d":"8.00E-56"},1,1,"7 : intermediary metabolism and respiration ;","_","_","_","_","10493122, 10510226, 10768780, 11271494, 15525680","3 : Putative function from multiple computational evidences",7,334,335,3,317,318]
[null,"PSHAa1617",null,"Pseudoalteromonas haloplanktis TAC125","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.88657,0.96429,36.36,{"v":9e-55,"d":"9.00E-55"},1,1,"2.5.4 : Menaquinone and ubiquinone ;","_","unknown","_","u : unknown",8599534,"2a : Function from experimental evidences in other organisms",35,330,335,25,308,308]
[null,"PSEEN3657",null,"Pseudomonas entomophila L48","etfA","electron transfer flavoprotein alpha-subunit","_",0.86269,1.0471,40.14,{"v":1E-54,"d":"1.00E-54"},1,1,"1.4.3 : Electron carrier ;","_","Unknown","6 : Energy metabolism ;","c : carrier","_","2a : Function from experimental evidences in other organisms",45,330,335,2,276,276]
[null,"THI_1679",null,"Thiomonas sp. 3As","etfA","electron transfer flavoprotein alpha-subunit (Alpha-ETF)(Electron transfer flavoprotein large subunit) (ETFLS)","_",0.86866,0.93871,41.24,{"v":2e-54,"d":"2.00E-54"},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",45,333,335,35,310,310]
[null,"AZCBGv1_p190001","_","Azospirillum brasilense CBG497","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.8597,0.92903,39.58,{"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)",45,330,335,33,307,310]
[null,"Mchl_1823",null,"Methylobacterium extorquens CM4","etfA","electron transfer flavoprotein alpha subunit","_",0.95522,1.00946,37.5,{"v":2e-53,"d":"2.00E-53"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","15188393, 16926146, 8599534","2a : Function from experimental evidences in other organisms",17,334,335,11,315,317]
[null,"METDI2208",null,"Methylobacterium extorquens DM4","etfA","electron transfer flavoprotein, NAD/FAD-binding domain and ETFP adenine nucleotide-binding domain-like","_",0.95522,1.00946,38.12,{"v":2e-53,"d":"2.00E-53"},1,1,"1.1.1 : Carbohydrates/Carbon compounds ;","_","1 : Unknown","_","e : enzyme","15188393, 16926146, 8599534","2a : Function from experimental evidences in other organisms",17,334,335,11,315,317]
[null,"ACIAD2654",null,"Acinetobacter baylyi ADP1","etfA","electron transfer flavoprotein alpha-subunit","_",0.89254,0.96141,39.8,{"v":9e-53,"d":"9.00E-53"},1,1,"1.4.3 : electron carrier ;","_","1 : Unknown","_","f : factor","_","2a : Function from experimental evidences in other organisms",35,330,335,25,311,311]
[null,"NT26v4_3414",null,"Rhizobium sp. NT-26","etfA","Electron transfer flavoprotein alpha-subunit (Alpha-ETF) (Electron transfer flavoprotein large subunit) (ETFLS)","_",0.87761,0.95146,38.44,{"v":4E-52,"d":"4.00E-52"},1,1,"1.4.3 : Electron carrier ;","_","2 : Cytoplasmic","_","c : carrier",8599534,"2b : Function from indirect experimental evidences (e.g. phenotypes)",39,330,335,29,309,309]
[null,"VIBNIv4_A0954",null,"Vibrio nigripulchritudo SFn1","etfA","Electron transfer flavoprotein subunit alpha","_",0.86866,0.94175,37.11,{"v":4E-52,"d":"4.00E-52"},1,1,"1.4.1 : Electron donor ;","_","2 : Cytoplasmic","5.8 : Electron carrier regeneration ;","c : carrier","8599534, 12597275","2a : Function from experimental evidences in other organisms",45,330,335,35,309,309]
[null,"VIBNIv4_B0455",null,"Vibrio nigripulchritudo SFn1","etfA","Electron transfer flavoprotein subunit alpha","_",0.86269,0.93226,38.41,{"v":6E-51,"d":"6.00E-51"},1,1,"1.4.1 : Electron donor ;","_","1 : Unknown","5.8 : Electron carrier regeneration ;","c : carrier","8599534, 12597275","2a : Function from experimental evidences in other organisms",46,331,335,34,308,310]

{"sheet":"SwissProt","index":6,"n_rows":234,"n_cols":22,"rows_kept":234}
["AEQN01_210010","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"D9TQ02","IPMed?",0.98592,0.98592,53.81,{"v":5e-153,"d":"5.00E-153"},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)","_",5,424,426,6,425,426]
[null,"F9USS9","IPMed?",0.98357,0.98821,52.74,{"v":4e-142,"d":"4.00E-142"},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",4,422,426,5,423,424]
[null,"Q6ZFH6","IPMed?",0.24578,0.30751,25.95,0.44,3,1,"RCN11","Beta-1,2-xylosyltransferase RCN11","2.4.2.-","Complete proteome, Glycoprotein, Glycosyltransferase, Golgi apparatus, Membrane, Reference proteome, Signal-anchor, Stress response, Transferase, Transmembrane, Transmembrane helix","16100779, 18089549, 24280374, 15604706, 26025522","Oryza sativa subsp. japonica","cv. Nipponbare / cv. Nipponbare / cv. Nipponbare / cv. Nipponbare",278,398,426,163,277,533]
[]
["AEQN01_210007","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?",0.88008,0.95992,43.96,{"v":6e-131,"d":"6.00E-131"},1,1,"lctP","L-lactate permease","_","Cell membrane, Membrane, Transmembrane, Transmembrane helix, Transport",10508058,"Streptococcus iniae","_",7,460,517,5,449,474]
[null,"Q46839","IPMed?",0.94821,1.02708,34.46,{"v":6e-91,"d":"6.00E-91"},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",7,506,517,19,546,560]
[null,"Q8ZL63","_",0.96189,1.02515,33.58,{"v":2E-85,"d":"2.00E-85"},3,1,"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",7,506,517,19,538,551]
[null,"P33231","IPMed?",0.96189,1.02515,33.58,{"v":3e-85,"d":"3.00E-85"},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",7,506,517,19,538,551]
[null,"P71067","IPMed?",0.95915,1.04449,31.85,{"v":4e-85,"d":"4.00E-85"},5,1,"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",7,507,517,19,548,563]
[null,"P65253","_",0.96189,1.02515,33.4,{"v":7e-85,"d":"7.00E-85"},6,1,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Transmembrane, Transmembrane helix, Transport",12471157,"Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","CFT073 / ATCC 700928 / UPEC",7,506,517,19,538,551]
[null,"P65254","_",0.96189,1.02515,33.4,{"v":7e-85,"d":"7.00E-85"},6,1,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport","11206551, 11258796","Escherichia coli O157:H7","O157:H7 / EDL933 / ATCC 700927 / EHEC / O157:H7 / Sakai / RIMD 0509952 / EHEC",7,506,517,19,538,551]
[null,"Q8Z2E3","_",0.96189,1.02515,33.4,{"v":3e-84,"d":"3.00E-84"},7,1,"lldP","L-lactate permease","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Transmembrane, Transmembrane helix, Transport","11677608, 12644504","Salmonella typhi","CT18 / ATCC 700931 / Ty2",7,506,517,19,538,551]
[null,"Q9K5Z9","_",0.99237,1.0058,32.12,{"v":2e-81,"d":"2.00E-81"},8,1,"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",3,513,517,13,523,524]
[null,"P55910","IPMed?",0.99445,1.04062,31.04,{"v":6E-79,"d":"6.00E-79"},9,1,"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",4,515,517,14,541,541]
[null,"Q57251","_",1.02068,1.05029,25.41,{"v":2e-39,"d":"2.00E-39"},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",4,510,517,2,525,532]
[null,"Q9HU16","IPMed?",0.37331,0.45199,25.91,1E-3,11,1,"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",9,193,517,216,407,427]
[null,"P0ABP3","IPMed?",0.33075,0.37093,22.22,0.026,12,1,"dcuC","Anaerobic C4-dicarboxylate transporter DcuC","_","Cell inner membrane, Cell membrane, Complete proteome, Membrane, Reference proteome, Transmembrane, Transmembrane helix, Transport","8955408, 8905232, 9278503, 16738553, 10368146, 15919996","Escherichia coli (strain K12)","K12 / AN387 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / AN387 / K12 / MG1655 / ATCC 47076",342,502,517,273,443,461]
[null,"Q8NHS3","IPMed?",0.40927,0.41006,24.53,0.082,13,1,"MFSD8","Major facilitator superfamily domain-containing protein 8","_","Alternative splicing, Complete proteome, Disease mutation, Glycoprotein, Lysosome, Membrane, Neurodegeneration, Neuronal ceroid lipofuscinosis, Polymorphism, Reference proteome, Transmembrane, Transmembrane helix, Transport","14702039, 15815621, 15489334, 17897319, 20406422, 17564970, 19201763, 19177532, 18850119, 19277732, 22612257, 21990111, 25227500","Homo sapiens","_",159,353,517,147,345,518]
[null,"P42194","IPMed?",0.44101,0.76768,23.68,0.19,14,2,"pecM","Protein PecM","_","Cell membrane, Complete proteome, Membrane, Reference proteome, Repeat, Transmembrane, Transmembrane helix, Transport","8022282, 21217001","Dickeya dadantii (strain 3937)","3937 / 3937",4,224,517,87,274,297]
[null,"Q06496","IPMed?",0.22763,0.28046,27.59,0.26,15,2,"Slc34a1","Sodium-dependent phosphate transport protein 2A","_","Cell membrane, Complete proteome, Disulfide bond, Glycoprotein, Ion transport, Membrane, Phosphoprotein, Reference proteome, Sodium, Sodium transport, Symport, Transmembrane, Transmembrane helix, Transport","8327470, 15489334, 8691716, 9058191, 9465116, 10198426, 10370077, 10926678, 22673903","Rattus norvegicus","_",375,511,517,356,490,637]
[]
["AEQN01_180010","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"Q97MD1","_",0.97161,0.98403,51.62,{"v":4e-114,"d":"4.00E-114"},1,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome",11466286,"Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",8,315,317,6,312,313]
[null,"B0K226","_",0.98423,1.00322,51.6,{"v":3e-113,"d":"3.00E-113"},2,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","_","Thermoanaerobacter sp. (strain X514)","_",6,317,317,1,311,311]
[null,"B0KDA4","_",0.98423,1.00322,51.6,{"v":3e-113,"d":"3.00E-113"},2,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","_","Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E)","_",6,317,317,1,311,311]
[null,"B1L1N3","_",0.9717,0.97476,50.49,{"v":2e-112,"d":"2.00E-112"},3,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",18060065,"Clostridium botulinum (strain Loch Maree / Type A3)","Loch Maree / Type A3",5,313,317,6,313,318]
[null,"C1FMZ1","_",0.9717,0.97476,50.49,{"v":3e-112,"d":"3.00E-112"},4,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","_","Clostridium botulinum (strain Kyoto / Type A2)","_",5,313,317,6,313,318]
[null,"A7GDK3","_",0.9717,0.97476,50.49,{"v":3e-112,"d":"3.00E-112"},4,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","_","Clostridium botulinum (strain Langeland / NCTC 10281 / Type F)","_",5,313,317,6,313,318]
[null,"Q7X5C9","IPMed?",0.98423,1.00322,52.56,{"v":4e-112,"d":"4.00E-112"},5,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",15007569,"Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485)","DSM 8691 / JW/SL-YS485",6,317,317,1,311,311]
[null,"Q892U0","_",0.97792,0.98101,50.32,{"v":6e-112,"d":"6.00E-112"},6,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome",12552129,"Clostridium tetani (strain Massachusetts / E88)","Massachusetts / E88",8,317,317,7,315,316]
[null,"B1IKX1","_",0.9717,0.97476,50.49,{"v":7e-112,"d":"7.00E-112"},7,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",18060065,"Clostridium botulinum (strain Okra / Type B1)","Okra / Type B1",5,313,317,6,313,318]
[null,"A7FU32","_",0.9717,0.97476,50.16,{"v":9e-112,"d":"9.00E-112"},8,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",18060065,"Clostridium botulinum (strain ATCC 19397 / Type A)","ATCC 19397 / Type A",5,313,317,6,313,318]
[null,"A5I1Z6","_",0.9717,0.97476,50.16,{"v":9e-112,"d":"9.00E-112"},8,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","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",5,313,317,6,313,318]
[null,"C3KVF0","_",0.9717,0.97476,49.84,{"v":3e-111,"d":"3.00E-111"},9,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","_","Clostridium botulinum (strain 657 / Type Ba4)","_",5,313,317,6,313,318]
[null,"Q8KQC4","_",0.98423,0.98423,52.56,{"v":4e-111,"d":"4.00E-111"},10,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Complete proteome, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein, Reference proteome","_","Hungateiclostridium thermocellum (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)","_",6,317,317,7,317,317]
[null,"P10655","IPMed?",0.9653,0.9653,50.33,{"v":8e-105,"d":"8.00E-105"},11,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","3675869, 3297694","Bacillus caldotenax","_",8,312,317,8,311,317]
[null,"Q59244","IPMed?",0.9653,0.9653,49.67,{"v":3E-103,"d":"3.00E-103"},12,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",3675869,"Bacillus caldolyticus","_",8,312,317,8,311,317]
[null,"P00344","IPMed?",0.9653,0.9653,48.37,{"v":2E-100,"d":"2.00E-100"},13,1,"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",8,312,317,8,311,317]
[null,"P00345","IPMed?",0.95283,0.95584,48.18,{"v":2E-99,"d":"2.00E-99"},14,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","3122782, 3118900","Bacillus megaterium","DSM 090",7,309,317,10,310,318]
[null,"Q60009","IPMed?",0.94207,0.97476,49.51,{"v":8e-99,"d":"8.00E-99"},15,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",7765475,"Streptococcus thermophilus","M-192",7,313,317,8,314,328]
[null,"P13714","IPMed?",0.96562,0.97476,48.54,{"v":1E-97,"d":"1.00E-97"},16,1,"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",5,312,317,4,310,320]
[null,"P20619","IPMed?",0.97179,0.97792,48.71,{"v":2e-97,"d":"2.00E-97"},17,1,"ldh2","L-lactate dehydrogenase 2","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein",2334516,"Bacillus psychrosaccharolyticus","_",5,313,317,5,312,319]
[null,"D8KFT1","IPMed?",0.98738,0.99682,47.28,{"v":5e-97,"d":"5.00E-97"},18,1,"ldh","L-lactate dehydrogenase","1.1.1.27","Allosteric enzyme, Cytoplasm, NAD, Oxidoreductase, Phosphoprotein","12867459, 20639323","Lactococcus lactis subsp. cremoris (strain NZ9000)","NZ9000 / NZ9000",4,315,317,3,313,314]
[null,"P04034","IPMed?",0.96308,0.98738,47.6,{"v":1e-96,"d":"1.00E-96"},19,1,"ldh1","L-lactate dehydrogenase 1","1.1.1.27","Allosteric enzyme, Cytoplasm, Direct protein sequencing, NAD, Oxidoreductase, Phosphoprotein","8081494, 9023947, 518918","Lactococcus lactis subsp. cremoris","ML1 / AM4 / US3",1,313,317,1,311,325]
[]
["AEQN01_90013","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P19543","IPMed?",1.00597,1.00855,59.58,0,1,1,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Plasmid, Repeat, Transport","2504647, 1708766","Enterobacter agglomerans","333 / 333",1,1167,1170,1,1169,1173]
[null,"Q2RMD6","IPMed?",1.00512,1.00598,58.71,0,2,1,"_","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",1,1167,1170,1,1167,1171]
[null,"P03833","IPMed?",1.00085,1.00171,57.51,0,3,1,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","3062178, 3060860, 8483412, 6306580","Klebsiella pneumoniae","_",1,1165,1170,1,1164,1171]
[null,"P94692","IPMed?",0.9513,1.00171,56.48,0,4,1,"por","Pyruvate:ferredoxin oxidoreductase","1.2.7.1","3D-structure, 4Fe-4S, Calcium, Cytoplasm, Direct protein sequencing, Disulfide bond, Electron transport, Iron, Iron-sulfur, Magnesium, Metal-binding, Oxidoreductase, Pyruvate, Thiamine pyrophosphate, Transport","9294422, 7612653, 10048931, 11752578, 16472741","Desulfocurvibacter africanus","ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi / ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi",1,1163,1170,1,1161,1232]
[null,"Q94IN5","IPMed?",0.65003,1.00171,47.95,0,5,1,"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",7,1165,1170,71,1229,1803]
[null,"Q968X7","IPMed?",0.63961,1.05726,47.29,0,6,1,"PFOR","Pyruvate dehydrogenase [NADP(+)]","1.2.1.51","4Fe-4S, Electron transport, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NADP, Oxidoreductase, Repeat, Thiamine pyrophosphate, Transport",11319255,"Cryptosporidium parvum","KSU-1",8,1163,1170,7,1235,1934]
[null,"P52965","_",0.98165,1.00598,48.17,0,7,2,"nifJ","Putative pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8590279, 8905231","Synechocystis sp. (strain PCC 6803 / Kazusa)","ATCC 27184 / PCC 6803 / N-1 / PCC 6803 / Kazusa",7,1165,1170,8,1169,1199]
[null,"Q3M8N0","IPMed?",0.99664,1.01368,47.64,0,8,2,"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",2,1165,1170,3,1179,1190]
[null,"Q06879","IPMed?",1.00334,1.02821,46.63,0,9,2,"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",1,1165,1170,1,1193,1199]
[null,"Q53046","IPMed?",0.98908,1.00684,46.43,0,10,2,"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",3,1162,1170,4,1171,1191]
[null,"P52647","IPMed?",1.00426,1.00769,46.14,0,11,2,"ydbK","Probable pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","9097039, 9278503, 16738553, 9025293","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",5,1163,1170,1,1159,1174]
[]
["AEQN01_230157","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P19543","IPMed?",1.00341,1.00598,58.03,0,1,2,"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",4,1167,1170,4,1172,1173]
[null,"Q2RMD6","IPMed?",1.00171,1.00256,58.06,0,2,2,"_","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",8,1166,1170,6,1169,1171]
[null,"P03833","IPMed?",1.00512,1.00598,56.58,0,3,2,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Repeat, Transport","3062178, 3060860, 8483412, 6306580","Klebsiella pneumoniae","_",1,1169,1170,1,1171,1171]
[null,"P94692","IPMed?",0.94805,0.99829,53,0,4,2,"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",1,1160,1170,1,1161,1232]
[null,"P52965","_",0.98332,1.00769,48.94,0,5,1,"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",6,1168,1170,7,1175,1199]
[null,"Q3M8N0","IPMed?",1.00252,1.01966,48.95,0,6,1,"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",2,1169,1170,3,1186,1190]
[null,"Q06879","IPMed?",1.00751,1.03248,47.6,0,7,1,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8415612, 11759840","Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)","PCC 7120 / SAG 25.82 / UTEX 2576",1,1168,1170,1,1199,1199]
[null,"Q94IN5","IPMed?",0.64781,0.99829,47.43,0,8,2,"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",8,1162,1170,72,1229,1803]
[null,"Q968X7","IPMed?",0.64064,1.05897,46.97,0,9,2,"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",7,1160,1170,6,1235,1934]
[null,"Q53046","IPMed?",0.99496,1.01282,47.17,0,10,1,"nifJ","Pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Nitrogen fixation, Oxidoreductase, Reference proteome, Repeat, Transport","8736535, 21886856","Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)","ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1",3,1166,1170,4,1178,1191]
[null,"P52647","IPMed?",1.00426,1.00769,47.58,0,11,1,"ydbK","Probable pyruvate-flavodoxin oxidoreductase","1.2.7.-","4Fe-4S, Complete proteome, Electron transport, Iron, Iron-sulfur, Metal-binding, Oxidoreductase, Reference proteome, Repeat, Transport","9097039, 9278503, 16738553, 9025293","Escherichia coli (strain K12)","K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12",8,1170,1170,4,1169,1174]
[]
["AEQN01_220120","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?",1,1.00356,62.77,{"v":2e-114,"d":"2.00E-114"},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",2,281,281,3,282,282]
[null,"Q0AVM2","IPMed?",1,1.00717,58.36,{"v":2e-106,"d":"2.00E-106"},2,1,"_","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.35","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, NAD, Oxidoreductase, Reference proteome","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",1,279,281,1,279,279]
[null,"P77851","_",0.99644,0.99644,56.79,{"v":2e-103,"d":"2.00E-103"},3,1,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",2,279,281,3,280,281]
[null,"P45364","IPMed?",1.00712,1.00712,55.48,{"v":6e-96,"d":"6.00E-96"},4,1,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase",8001771,"Clostridioides difficile","E",1,281,281,1,281,281]
[null,"Q9RVG1","_",1,1.01079,51.6,{"v":2e-89,"d":"2.00E-89"},5,1,"hbd","Probable 3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome",10567266,"Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)","ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422",1,279,281,1,278,278]
[null,"P45856","IPMed?",0.97561,0.99644,48.21,{"v":1e-81,"d":"1.00E-81"},6,1,"mmgB","Probable 3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",2,279,281,5,282,287]
[null,"Q45223","_",0.95563,0.99644,46.07,{"v":5E-74,"d":"5.00E-74"},7,1,"hbdA","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome",12597275,"Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110",2,279,281,7,284,293]
[null,"Q16836","IPMed?",0.91083,1.01779,44.76,{"v":2e-65,"d":"2.00E-65"},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","_",3,279,281,30,313,314]
[null,"P00348","IPMed?",0.91083,1.01779,41.96,{"v":4e-64,"d":"4.00E-64"},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","_",3,279,281,30,313,314]
[null,"Q9WVK7","IPMed?",0.90764,1.01423,43.51,{"v":5e-64,"d":"5.00E-64"},10,1,"Hadh","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","Acetylation, Complete proteome, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide",10064895,"Rattus norvegicus","Sprague-Dawley",3,279,281,30,313,314]
[null,"Q61425","IPMed?",0.90764,1.01423,43.51,{"v":7e-64,"d":"7.00E-64"},11,1,"Hadh","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","Acetylation, Complete proteome, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide","7642117, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J",3,279,281,30,313,314]
[null,"P9WNP7","IPMed?",0.98601,1.00356,37.94,{"v":5e-60,"d":"5.00E-60"},12,1,"fadB2","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","9634230, 11489128, 12081975, 20378648, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",2,279,281,7,286,286]
[null,"P76083","IPMed?",0.58947,0.99644,36.79,{"v":4E-51,"d":"4.00E-51"},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",3,279,281,8,285,475]
[]
["AEQN01_220121","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?",0.96935,0.98062,56.13,{"v":3e-97,"d":"3.00E-97"},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",7,258,258,9,261,261]
[null,"Q0AVM1","IPMed?",0.94615,0.95349,56.91,{"v":1E-89,"d":"1.00E-89"},2,1,"_","Crotonyl-CoA hydratase","4.2.1.150","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",7,251,258,9,254,260]
[null,"O34893","IPMed?",0.93846,0.94574,45.08,{"v":6e-63,"d":"6.00E-63"},3,1,"yngF","Putative enoyl-CoA hydratase/isomerase YngF","_","Complete proteome, Lyase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",12,251,258,14,254,260]
[null,"A4YI89","IPMed?",0.91892,0.92248,46.64,{"v":7e-61,"d":"7.00E-61"},4,1,"_","3-hydroxypropionyl-coenzyme A dehydratase","4.2.1.116","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","18083856, 19429610","Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)","ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2",15,251,258,17,253,259]
[null,"Q1ZXF1","_",0.89531,0.96124,43.55,{"v":5E-56,"d":"5.00E-56"},5,1,"echs1","Probable enoyl-CoA hydratase, mitochondrial","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide",15875012,"Dictyostelium discoideum","AX4",7,250,258,29,270,277]
[null,"P9WNN9","_",0.94961,0.95331,43.67,{"v":1e-55,"d":"1.00E-55"},6,1,"echA8","Probable enoyl-CoA hydratase echA8","4.2.1.17","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","9634230, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",7,250,258,9,250,257]
[null,"P9WNN8","_",0.94961,0.95331,43.67,{"v":1e-55,"d":"1.00E-55"},6,1,"echA8","Probable enoyl-CoA hydratase echA8","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase",12218036,"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","CDC 1551 / Oshkosh",7,250,258,9,250,257]
[null,"P64017","_",0.94961,0.95331,43.67,{"v":1e-55,"d":"1.00E-55"},6,1,"echA8","Probable enoyl-CoA hydratase echA8","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase","12788972, 28385856","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97",7,250,258,9,250,257]
[null,"Q8BH95","_",0.83793,0.94186,43.21,{"v":3e-55,"d":"3.00E-55"},7,1,"Echs1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Phosphoprotein, Reference proteome, Transit peptide","16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / C57BL/6J",12,251,258,47,284,290]
[null,"P14604","IPMed?",0.83793,0.94186,42.8,{"v":3e-54,"d":"3.00E-54"},8,1,"Echs1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide","2806264, 15489334, 7883013, 8895557, 9480773, 11851409, 12445775","Rattus norvegicus","_",12,251,258,47,284,290]
[null,"Q58DM8","_",0.84138,0.94574,43.44,{"v":9e-54,"d":"9.00E-54"},9,1,"ECHS1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","Acetylation, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Reference proteome, Transit peptide",16305752,"Bos taurus","_",12,251,258,47,284,290]
[null,"P30084","IPMed?",0.83103,0.93411,42.74,{"v":5E-53,"d":"5.00E-53"},10,1,"ECHS1","Enoyl-CoA hydratase, mitochondrial","4.2.1.17","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Disease mutation, Fatty acid metabolism, Lipid metabolism, Lyase, Mitochondrion, Neurodegeneration, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","8012501, 9073515, 15164054, 15489334, 1286669, 11271497, 19608861, 21269460, 25125611, 24275569, 25393721, 25944712, 26000322, 26251176, 27221955, 26741492","Homo sapiens","_",12,251,258,47,284,290]
[null,"Q52995","IPMed?",0.95736,0.96109,39.68,{"v":1e-49,"d":"1.00E-49"},11,1,"fadB1","Probable enoyl-CoA hydratase","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","7751302, 11481430, 11474104","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",7,253,258,9,253,257]
[null,"F4JML5","IPMed?",0.7907,0.92248,39.08,{"v":2e-48,"d":"2.00E-48"},12,1,"_","Probable enoyl-CoA hydratase 2, mitochondrial","4.2.1.17","Complete proteome, Fatty acid metabolism, Hydrolase, Lipid metabolism, Lyase, Mitochondrion, Protease, Reference proteome, Transit peptide","9461215, 10617198, 27862469, 14593172, 10929101","Arabidopsis thaliana","cv. Columbia / cv. Columbia / cv. Columbia / cv. Columbia",15,251,258,58,295,301]
[null,"P94549","IPMed?",0.9845,0.9845,39.76,{"v":2e-48,"d":"2.00E-48"},13,1,"fadB","Probable enoyl-CoA hydratase","4.2.1.17","Complete proteome, Fatty acid metabolism, Lipid degradation, Lipid metabolism, Lyase, Reference proteome","8969504, 9384377, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",1,251,258,1,252,258]
[null,"P76082","IPMed?",0.92248,0.93333,38.66,{"v":6e-47,"d":"6.00E-47"},14,1,"paaF","2,3-dehydroadipyl-CoA hydratase","4.2.1.17","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Lyase, Reference proteome","9748275, 9097039, 9278503, 16738553, 10766858, 12846838, 20660314","Escherichia coli (strain K12)","W / ATCC 11105 / DSM 1900 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911",14,250,258,14,248,255]
[]
["AEQN01_220122","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?",0.98731,0.99235,61.7,{"v":3e-170,"d":"3.00E-170"},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",3,391,394,2,390,392]
[null,"Q0AVM3","IPMed?",1.00253,1.00761,57.43,{"v":3E-158,"d":"3.00E-158"},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",1,393,394,1,396,396]
[null,"Q18AR0","_",0.98223,0.98977,55.81,{"v":2e-157,"d":"2.00E-157"},3,1,"thlA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Cytoplasm, Reference proteome, Transferase",16804543,"Peptoclostridium difficile (strain 630)",630,3,389,394,2,388,391]
[null,"Q9ZHI1","IPMed?",0.97716,0.98214,53.25,{"v":2e-148,"d":"2.00E-148"},4,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, PHA biosynthesis, Reference proteome, Transferase","14500782, 10427049","Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)","ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757 / ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757",4,387,394,2,386,392]
[null,"P14611","IPMed?",0.97716,0.97964,55.84,{"v":3E-148,"d":"3.00E-148"},5,1,"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",4,387,394,3,387,393]
[null,"Q9I2A8","_",0.9797,0.98219,52.59,{"v":6e-143,"d":"6.00E-143"},6,1,"atoB","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase",10984043,"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1",3,387,394,2,387,393]
[null,"P45369","IPMed?",1,1,50.25,{"v":3e-138,"d":"3.00E-138"},7,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, PHB biosynthesis, Reference proteome, Transferase","1396692, 22675582, 1476773","Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)","ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D / ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D",1,393,394,1,394,394]
[null,"P44873","_",0.99492,0.99746,51.53,{"v":4E-136,"d":"4.00E-136"},8,1,"atoB","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase",7542800,"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","ATCC 51907 / DSM 11121 / KW20 / Rd",3,393,394,2,393,393]
[null,"P45363","IPMed?",1,1,50,{"v":1E-135,"d":"1.00E-135"},9,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase","7763384, 1476773","Thiocystis violacea","2311 / DSM 208",1,393,394,1,394,394]
[null,"P54810","IPMed?",0.98223,0.98977,50.65,{"v":2E-131,"d":"2.00E-131"},10,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase",8566717,"Paracoccus denitrificans","_",4,387,394,3,385,391]
[null,"P50174","IPMed?",0.98731,0.98982,50.13,{"v":2e-129,"d":"2.00E-129"},11,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","Acyltransferase, Complete proteome, Cytoplasm, PHB biosynthesis, Reference proteome, Transferase","7582015, 11481430, 11474104","Rhizobium meliloti (strain 1021)","41 / 1021 / 1021",5,393,394,6,393,393]
[null,"P07097","IPMed?",0.99746,1.00255,49.11,{"v":2e-128,"d":"2.00E-128"},12,1,"phaA","Acetyl-CoA acetyltransferase","2.3.1.9","3D-structure, Acyltransferase, Cytoplasm, PHB biosynthesis, Transferase","2878929, 2670935, 1673680, 1476773, 10764581, 10545327, 12501183","Zoogloea ramigera","ATCC 19623 / I-16-M / NCIB 10340 / NCTC 10482",1,393,394,1,392,392]
[null,"Q0KBP1","IPMed?",1.00254,1.00254,47.59,{"v":4e-124,"d":"4.00E-124"},13,1,"bktB","Beta-ketothiolase BktB","2.3.1.16, 2.3.1.9","3D-structure, Acyltransferase, Complete proteome, Direct protein sequencing, Reference proteome, Transferase","9555876, 16964242","Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)","ATCC 17699 / H16 / DSM 428 / Stanier 337 / ATCC 17699 / H16 / DSM 428 / Stanier 337",1,393,394,1,394,394]
[]
["AEQN01_70057","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P41938","_",0.99369,1.01942,27.3,{"v":6e-38,"d":"6.00E-38"},1,2,"_","Probable 3-hydroxyacyl-CoA dehydrogenase B0272.3","1.1.1.35","Complete proteome, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome",9851916,"Caenorhabditis elegans","Bristol N2",3,317,317,22,309,309]
[null,"Q16836","IPMed?",0.99369,1.00318,29.21,{"v":9e-38,"d":"9.00E-38"},2,2,"HADH","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","3D-structure, Acetylation, Alternative splicing, Complete proteome, Disease mutation, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Polymorphism, Reference proteome, Transit peptide","8687463, 15815621, 15489334, 19608861, 21269460, 24275569, 25944712, 10231530, 10840044, 16176262, 11489939","Homo sapiens","_",3,317,317,27,314,314]
[null,"Q9WVK7","IPMed?",0.99369,1.00318,28.57,{"v":2e-37,"d":"2.00E-37"},3,2,"Hadh","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","Acetylation, Complete proteome, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide",10064895,"Rattus norvegicus","Sprague-Dawley",3,317,317,27,314,314]
[null,"P00348","IPMed?",0.99369,1.00318,28.25,{"v":6E-37,"d":"6.00E-37"},4,2,"HADH","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","3D-structure, Acetylation, Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide","9593854, 7409145, 10064895, 3479790, 10548046","Sus scrofa","_",3,317,317,27,314,314]
[null,"Q61425","IPMed?",0.99369,1.00318,28.25,{"v":2e-36,"d":"2.00E-36"},5,2,"Hadh","Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial","1.1.1.35","Acetylation, Complete proteome, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome, Transit peptide","7642117, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J",3,317,317,27,314,314]
[null,"P45364","IPMed?",1,1.12811,28.71,{"v":4E-35,"d":"4.00E-35"},6,2,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase",8001771,"Clostridioides difficile","E",5,316,317,2,279,281]
[null,"P52041","IPMed?",0.99369,1.11702,28.89,{"v":4e-32,"d":"4.00E-32"},7,2,"hbd","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",3,316,317,1,280,282]
[null,"P34439","_",0.99685,1.0604,26.9,{"v":2e-30,"d":"2.00E-30"},9,2,"_","Probable 3-hydroxyacyl-CoA dehydrogenase F54C8.1","1.1.1.35","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, Mitochondrion, NAD, Oxidoreductase, Reference proteome","7906398, 9851916","Caenorhabditis elegans","Bristol N2 / Bristol N2",2,317,317,10,297,298]
[null,"Q45223","_",0.99685,1.0785,27.22,{"v":2e-30,"d":"2.00E-30"},8,2,"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",3,317,317,5,285,293]
[null,"Q9RVG1","_",0.98738,1.1259,27.16,{"v":4e-30,"d":"4.00E-30"},10,2,"hbd","Probable 3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome",10567266,"Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)","ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422",5,316,317,2,278,278]
[null,"P45856","IPMed?",1,1.10453,28.08,{"v":6e-30,"d":"6.00E-30"},11,2,"mmgB","Probable 3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",1,316,317,1,282,287]
[null,"Q0AVM2","IPMed?",0.98738,1.12186,27.16,{"v":9e-30,"d":"9.00E-30"},12,2,"_","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.35","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, NAD, Oxidoreductase, Reference proteome","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",5,316,317,2,279,279]
[null,"P9WNP7","IPMed?",0.99685,1.1049,25.95,{"v":2e-25,"d":"2.00E-25"},13,2,"fadB2","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157","3D-structure, Complete proteome, Fatty acid metabolism, Lipid metabolism, NADP, Oxidoreductase, Reference proteome","9634230, 11489128, 12081975, 20378648, 21969609","Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","ATCC 25618 / H37Rv / ATCC 25618 / H37Rv",3,316,317,5,286,286]
[null,"Q9F0Y7","IPMed?",0.42524,0.97792,23.87,{"v":3e-21,"d":"3.00E-21"},14,3,"fadB","Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase / 3-hydroxyacyl-CoA dehydrogenase","4.2.1.17, 5.1.2.3, 5.3.3.8, 1.1.1.35","Fatty acid metabolism, Isomerase, Lipid degradation, Lipid metabolism, Lyase, Multifunctional enzyme, NAD, Oxidoreductase",11097912,"Enterobacter cloacae","A-11 / 501R3",8,317,317,318,593,729]
[]
["AEQN01_300005","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"B0MC58","_",1,1,65.92,0,1,1,"_","Butyryl-CoA:acetate CoA-transferase","2.8.3.-","Complete proteome, Fatty acid metabolism, Lipid metabolism, Transferase",16385128,"Anaerostipes caccae (strain DSM 14662 / NCIMB 13811 / L1-92)","DSM 14662 / NCIMB 13811 / L1-92",1,445,446,1,446,446]
[null,"G2SYC0","_",1,1,63,0,2,1,"_","Butyryl-CoA:acetate CoA-transferase","2.8.3.-","Complete proteome, Direct protein sequencing, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","16385128, 26543119","Roseburia hominis (strain DSM 16839 / NCIMB 14029 / A2-183)","DSM 16839 / NCIMB 14029 / A2-183 / DSM 16839 / NCIMB 14029 / A2-183",1,445,446,1,446,446]
[null,"Q0AVM5","IPMed?",0.99105,0.99327,51.69,{"v":6E-152,"d":"6.00E-152"},3,1,"_","Probable butyrate:acetyl-CoA coenzyme A-transferase","2.8.3.-","Complete proteome, Cytoplasm, Fatty acid metabolism, Lipid metabolism, Reference proteome, Transferase","21966920, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",4,445,446,6,445,447]
[null,"P38942","IPMed?",0.97534,1.01399,38.85,{"v":3e-87,"d":"3.00E-87"},4,2,"cat2","4-hydroxybutyrate coenzyme A transferase","2.8.3.-","Complete proteome, Reference proteome, Transferase","18218779, 8550525","Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)","ATCC 8527 / DSM 555 / NCIMB 10680",1,431,446,1,422,429]
[null,"P83773","IPMed?",0.92366,1.0852,23.14,{"v":1e-17,"d":"1.00E-17"},5,1,"ACH1","Acetyl-CoA hydrolase","3.1.2.1","Complete proteome, Cytoplasm, Direct protein sequencing, Hydrolase, Reference proteome","15123810, 17419877, 24025428, 15378761","Candida albicans (strain SC5314 / ATCC MYA-2876)","SC5314 / ATCC MYA-2876 / SC5314 / ATCC MYA-2876 / SC5314 / ATCC MYA-2876 / SC5314 / ATCC MYA-2876",7,430,446,14,476,524]
[null,"P38946","IPMed?",0.72677,0.87668,23.27,1e-15,6,1,"cat1","Succinyl-CoA:coenzyme A transferase","2.8.3.-","Complete proteome, Reference proteome, Transferase","8550525, 18218779","Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)","ATCC 8527 / DSM 555 / NCIMB 10680",88,431,446,137,503,538]
[null,"P15937","IPMed?",0.65333,0.76906,24.78,1e-12,7,1,"acu-8","Acetyl-CoA hydrolase","3.1.2.1","Complete proteome, Cytoplasm, Hydrolase, Reference proteome","2140429, 12712197, 1357077","Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)","ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987",117,420,446,143,470,525]
[null,"P52043","IPMed?",0.97358,1.07399,23.59,1e-12,8,1,"scpC","Propionyl-CoA:succinate CoA transferase","2.8.3.-","Complete proteome, Reference proteome, Transferase","9278503, 16738553, 10769117","Escherichia coli (strain K12)","K12 / MG1655 / ATCC 47076 / K12 / W3110 / ATCC 27325 / DSM 5911 / K12 / MG1655 / ATCC 47076",13,430,446,9,458,492]
[null,"P32316","IPMed?",0.91255,1.07623,23.54,5e-12,9,1,"ACH1","Acetyl-CoA hydrolase","3.1.2.1","Acetylation, Complete proteome, Cytoplasm, Direct protein sequencing, Glycoprotein, Hydrolase, Phosphoprotein, Reference proteome","1970569, 1441754, 7813418, 24374639, 11502169, 14562106, 17761666, 22814378","Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 204508 / S288c / ATCC 201238 / W303-1B / ATCC 76625 / YPH499",7,427,446,16,475,526]
[null,"B3EY95","IPMed?",0.4396,0.49776,25.68,3e-07,10,3,"_","Succinyl-CoA:acetate CoA-transferase","2.8.3.18","3D-structure, Transferase","18502856, 23030530","Acetobacter aceti","1023 / 1023 / 1023",211,430,446,261,466,505]
[]
["AEQN01_210004","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?",0.98695,0.99474,46.56,{"v":2e-105,"d":"2.00E-105"},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","_",1,372,380,1,377,383]
[null,"O34421","IPMed?",0.99737,0.99737,42.74,{"v":1e-101,"d":"1.00E-101"},2,3,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,377,380,1,379,380]
[null,"P41367","IPMed?",0.90736,1.00526,44.24,{"v":2e-101,"d":"2.00E-101"},3,1,"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","_",2,380,380,38,419,421]
[null,"P45867","IPMed?",0.98158,0.98417,45.58,{"v":2e-101,"d":"2.00E-101"},4,4,"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",1,371,380,1,372,379]
[null,"P45857","IPMed?",0.98947,0.99208,42.55,{"v":2e-101,"d":"2.00E-101"},5,5,"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",5,378,380,3,377,379]
[null,"Q8HXY8","_",0.90736,1.00526,43.46,{"v":2E-99,"d":"2.00E-99"},6,1,"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","_","Macaca fascicularis","_",2,380,380,38,419,421]
[null,"P11310","IPMed?",0.90736,1.00526,42.93,{"v":2E-99,"d":"2.00E-99"},7,1,"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","_",2,380,380,38,419,421]
[null,"Q3SZB4","_",0.90736,1.00526,43.72,{"v":3e-99,"d":"3.00E-99"},8,1,"ACADM","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","_","Bos taurus","_",2,380,380,38,419,421]
[null,"P52042","IPMed?",0.98158,0.98417,44.77,{"v":4e-99,"d":"4.00E-99"},9,4,"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",1,371,380,1,372,379]
[null,"A5A6I0","_",0.90736,1.00526,42.67,{"v":5e-99,"d":"5.00E-99"},10,1,"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",17574350,"Pan troglodytes","_",2,380,380,38,419,421]
[null,"P45952","IPMed?",0.90736,1.00526,43.19,{"v":7e-99,"d":"7.00E-99"},11,2,"Acadm","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","7829081, 1438358, 21183079, 23806337, 23576753","Mus musculus","BALB/cJ",2,380,380,38,419,421]
[null,"P08503","IPMed?",0.90736,1.00526,42.67,{"v":3e-97,"d":"3.00E-97"},12,2,"Acadm","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","Acetylation, Complete proteome, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","3611054, 2029527","Rattus norvegicus","_",2,380,380,38,419,421]
[null,"Q22347","IPMed?",0.91847,1.00789,40.99,{"v":5e-95,"d":"5.00E-95"},13,1,"acdh-10","Probable medium-chain specific acyl-CoA dehydrogenase 10, mitochondrial","1.3.8.7","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Reference proteome, Transit peptide","9851916, 18522834","Caenorhabditis elegans","Bristol N2",1,380,380,27,409,417]
[]
["AEQN01_220142","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"G3KIM8","IPMed?",0.96701,1,52.76,{"v":2e-133,"d":"2.00E-133"},1,1,"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",1,378,381,14,392,394]
[null,"P45867","IPMed?",0.9895,0.99472,51.19,{"v":2E-119,"d":"2.00E-119"},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",1,375,381,1,375,379]
[null,"P45857","IPMed?",0.99213,0.99736,49.74,{"v":1E-117,"d":"1.00E-117"},3,2,"mmgC","Acyl-CoA dehydrogenase","1.3.99.-","3D-structure, Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",5,380,381,3,378,379]
[null,"P52042","IPMed?",0.98688,0.99208,46.28,{"v":1e-112,"d":"1.00E-112"},4,2,"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",1,374,381,1,374,379]
[null,"H6LGM6","IPMed?",0.97638,0.98153,48.66,{"v":7e-104,"d":"7.00E-104"},5,2,"carC","Caffeyl-CoA reductase-Etf complex subunit CarC","1.3.1.108","3D-structure, Complete proteome, Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",6,374,381,4,373,379]
[null,"O34421","IPMed?",1,1.00263,45.41,{"v":5e-103,"d":"5.00E-103"},6,2,"yngJ","Probable acyl-CoA dehydrogenase YngJ","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","9387222, 9384377","Bacillus subtilis (strain 168)","168 / 168",1,378,381,1,379,380]
[null,"Q3ZBF6","IPMed?",0.91019,0.98425,46.4,{"v":7e-103,"d":"7.00E-103"},7,2,"ACADS","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide",6712627,"Bos taurus","_",2,374,381,31,403,412]
[null,"Q5RF40","_",0.86806,0.98425,45.07,{"v":5e-102,"d":"5.00E-102"},8,1,"ACADSB","Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.5","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","_","Pongo abelii","_",6,379,381,58,430,432]
[null,"P45954","IPMed?",0.86806,0.98425,44.8,{"v":2e-101,"d":"2.00E-101"},9,1,"ACADSB","Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.5","3D-structure, Acetylation, Alternative splicing, Complete proteome, Disease mutation, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Polymorphism, Reference proteome, Transit peptide","7698750, 11013134, 14702039, 15164054, 15489334, 17974005, 19608861, 21269460, 24275569, 25944712, 10832746, 16317551","Homo sapiens","_",6,379,381,58,430,432]
[null,"Q07417","IPMed?",0.91019,0.98425,44.53,{"v":2e-101,"d":"2.00E-101"},10,2,"Acads","Short-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.1","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","8276399, 16141072, 15489334, 21183079, 23806337, 23576753","Mus musculus","C57BL/6J / FVB/N",2,374,381,31,403,412]
[null,"P70584","IPMed?",0.86806,0.98425,44.53,{"v":6e-101,"d":"6.00E-101"},11,1,"Acadsb","Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.5","Acetylation, Complete proteome, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide","8660691, 6874697","Rattus norvegicus","Sprague-Dawley",6,379,381,58,430,432]
[]
["AEQN01_250027","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P45857","IPMed?",0.97389,0.98417,46.92,{"v":2e-105,"d":"2.00E-105"},1,3,"mmgC","Acyl-CoA dehydrogenase","1.3.99.-","3D-structure, Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",6,375,383,3,373,379]
[null,"P45867","IPMed?",0.97911,0.98945,45.87,{"v":2e-102,"d":"2.00E-102"},2,3,"acdA","Acyl-CoA dehydrogenase","1.3.99.-","Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid degradation, Lipid metabolism, Oxidoreductase, Reference proteome","9353933, 9384377, 17189250","Bacillus subtilis (strain 168)","168 / 168 / 168",3,375,383,2,375,379]
[null,"Q06319","IPMed?",1,1,46.48,{"v":7e-102,"d":"7.00E-102"},3,4,"_","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","_",3,379,383,2,383,383]
[null,"P08503","IPMed?",0.90974,1,42.56,{"v":8e-102,"d":"8.00E-102"},4,1,"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","_",4,382,383,39,420,421]
[null,"P45952","IPMed?",0.90974,1,42.56,{"v":1e-101,"d":"1.00E-101"},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",4,382,383,39,420,421]
[null,"P41367","IPMed?",0.90974,1,43.34,{"v":5e-100,"d":"5.00E-100"},6,2,"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","_",4,382,383,39,420,421]
[null,"P11310","IPMed?",0.90974,1,41.78,{"v":4e-98,"d":"4.00E-98"},7,2,"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","_",4,382,383,39,420,421]
[null,"A5A6I0","_",0.90974,1,41.78,{"v":4e-98,"d":"4.00E-98"},7,2,"ACADM","Medium-chain specific acyl-CoA dehydrogenase, mitochondrial","1.3.8.7","Acetylation, Complete proteome, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Mitochondrion, Oxidoreductase, Phosphoprotein, Reference proteome, Transit peptide",17574350,"Pan troglodytes","_",4,382,383,39,420,421]
[null,"P52042","IPMed?",0.99217,1.00264,43.16,{"v":7e-98,"d":"7.00E-98"},8,5,"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",3,379,383,2,379,379]
[null,"P46703","_",0.97172,0.98695,43.12,{"v":1E-97,"d":"1.00E-97"},9,3,"fadE25","Probable acyl-CoA dehydrogenase fadE25","1.3.99.-","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","7489918, 11234002","Mycobacterium leprae (strain TN)","TN",4,379,383,13,389,389]
[null,"Q3SZB4","_",0.90974,1,42.3,{"v":5e-97,"d":"5.00E-97"},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","_","Bos taurus","_",4,382,383,39,420,421]
[null,"G3KIM8","IPMed?",0.96701,0.99478,44.36,{"v":2e-96,"d":"2.00E-96"},11,4,"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",3,380,383,15,394,394]
[null,"Q2LQN9","IPMed?",0.90338,0.9765,40.91,{"v":2e-88,"d":"2.00E-88"},12,2,"_","Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase","1.3.8.10","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome",23667239,"Syntrophus aciditrophicus (strain SB)","_",6,377,383,37,410,414]
[]
["AEQN01_230141","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"P52042","IPMed?",0.58998,0.99472,56.76,{"v":5e-140,"d":"5.00E-140"},1,1,"bcd","Acyl-CoA dehydrogenase, short-chain specific","1.3.8.1","Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome","8655474, 11466286","Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)","ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 / ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787",1,377,639,1,377,379]
[null,"P45857","IPMed?",0.58685,0.98945,55.47,{"v":7E-139,"d":"7.00E-139"},2,1,"mmgC","Acyl-CoA dehydrogenase","1.3.99.-","3D-structure, Complete proteome, FAD, Flavoprotein, Oxidoreductase, Reference proteome, Sporulation","8759838, 8969508, 9384377, 19383706","Bacillus subtilis (strain 168)","168 / MB24 / 168 / JH642 / 168",5,379,639,3,377,379]
[null,"P45867","IPMed?",0.58998,0.99472,54.91,{"v":4e-128,"d":"4.00E-128"},3,1,"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",1,377,639,1,377,379]
[null,"Q06319","IPMed?",0.59781,0.99739,51.05,{"v":3e-119,"d":"3.00E-119"},4,1,"_","Acyl-CoA dehydrogenase, short-chain specific","1.3.8.1","3D-structure, Direct protein sequencing, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Oxidoreductase","8399220, 7857927","Megasphaera elsdenii","_",1,378,639,1,382,383]
[null,"O34421","IPMed?",0.59311,0.99737,50.66,{"v":8e-119,"d":"8.00E-119"},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",1,378,639,1,379,380]
[null,"Q07417","IPMed?",0.58685,0.91019,51.73,{"v":2E-116,"d":"2.00E-116"},6,1,"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",4,378,639,33,407,412]
[null,"P15651","IPMed?",0.58685,0.91019,51.73,{"v":3e-116,"d":"3.00E-116"},7,1,"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","_",4,378,639,33,407,412]
[null,"Q3ZBF6","IPMed?",0.58685,0.91019,50.93,{"v":5e-114,"d":"5.00E-114"},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",6712627,"Bos taurus","_",4,378,639,33,407,412]
[null,"Q5RAS0","_",0.58685,0.91019,51.2,{"v":1e-112,"d":"1.00E-112"},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","_","Pongo abelii","_",4,378,639,33,407,412]
[null,"P16219","IPMed?",0.58685,0.91019,50.93,{"v":1e-111,"d":"1.00E-111"},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","_",4,378,639,33,407,412]
[null,"H6LGM6","IPMed?",0.58842,0.99208,49.2,{"v":4E-109,"d":"4.00E-109"},11,1,"carC","Caffeyl-CoA reductase-Etf complex subunit CarC","1.3.1.108","3D-structure, Complete proteome, Cytoplasm, FAD, Flavoprotein, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",6,380,639,4,379,379]
[]
["AEQN01_220164","PB id","Exp","maxLrap","minLrap","Ident %","Eval","OrderQ","OrderB","Gene","Description","EC number","Keywords","PubMedId","Organism","Strain","BeginQ","EndQ","LengthQ","BeginB","EndB","LengthB"]
[null,"O85691","IPMed?",0.94444,0.95865,50.2,{"v":7e-82,"d":"7.00E-82"},1,1,"etfB","Electron transfer flavoprotein subunit beta","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",1,253,266,1,255,270]
[null,"H6LGM7","IPMed?",1,1.01527,45.86,{"v":2e-75,"d":"2.00E-75"},2,1,"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",1,266,266,1,262,262]
[null,"P97089","_",1.01128,1.03462,50.56,{"v":6e-75,"d":"6.00E-75"},3,1,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",1,266,266,1,260,260]
[null,"P52040","IPMed?",0.98496,1.01158,48.85,{"v":3e-74,"d":"3.00E-74"},4,1,"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",1,262,266,1,256,259]
[null,"P26482","IPMed?",0.86121,0.90977,44.63,{"v":2e-62,"d":"2.00E-62"},5,1,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Reference proteome, Transport","1850088, 3216855","Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)","_",1,238,266,1,241,281]
[null,"Q53210","_",0.92632,0.99248,42.05,{"v":2e-61,"d":"2.00E-61"},6,1,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Transport","8796346, 9163424, 19376903","Sinorhizobium fredii (strain NBRC 101917 / NGR234)","NBRC 101917 / NGR234 / NBRC 101917 / NGR234",1,260,266,1,262,285]
[null,"P53577","IPMed?",0.91667,0.99248,42.05,{"v":8e-61,"d":"8.00E-61"},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",1,260,266,1,262,288]
[null,"Q05559","IPMed?",0.94624,0.99248,42.8,{"v":4e-59,"d":"4.00E-59"},8,1,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport",8369342,"Rhizobium leguminosarum bv. phaseoli","_",1,260,266,1,260,279]
[null,"P09818","IPMed?",0.83219,0.91353,44.44,{"v":6E-57,"d":"6.00E-57"},9,1,"fixA","Protein FixA","_","Complete proteome, Electron transport, Nitrogen fixation, Plasmid, Reference proteome, Transport","3029021, 11481432, 11474104, 6317191","Rhizobium meliloti (strain 1021)","1021 / 1021 / 1021",1,239,266,1,242,292]
[null,"P53576","_",0.9395,0.99248,42.8,{"v":2e-56,"d":"2.00E-56"},10,1,"fixA","Protein FixA","_","Electron transport, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",1,258,266,1,259,281]
[null,"G3KIM7","IPMed?",1.00375,1.00752,39.18,{"v":1E-52,"d":"1.00E-52"},11,1,"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",1,262,266,1,264,267]
[null,"Q9DCW4","IPMed?",0.9812,1.02353,32.95,{"v":2e-33,"d":"2.00E-33"},12,1,"Etfb","Electron transfer flavoprotein subunit beta","_","Acetylation, Complete proteome, Direct protein sequencing, Electron transport, Methylation, Mitochondrion, Nucleotide-binding, Phosphoprotein, Reference proteome, Transport","16141072, 15489334, 21183079, 23806337, 23576753, 25023281","Mus musculus","C57BL/6J / FVB/N",1,259,266,4,252,255]
[null,"P64098","IPMed?",0.98496,0.98496,31.3,{"v":1e-32,"d":"1.00E-32"},13,1,"etfB","Electron transfer flavoprotein subunit beta","_","Complete proteome, Electron transport, FAD, Flavoprotein, Transport","12788972, 28385856, 16006064","Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","ATCC BAA-935 / AF2122/97 / ATCC BAA-935 / AF2122/97 / BCG / Pasteur",2,256,266,3,260,266]
[]
["AEQN01_220165","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","_",0.98209,0.99697,56.84,{"v":3e-123,"d":"3.00E-123"},1,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Electron transport, FAD, Flavoprotein, Reference proteome, Transport","_","Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814)","_",6,334,335,5,330,330]
[null,"P53578","IPMed?",0.9791,0.98204,54.27,{"v":4e-118,"d":"4.00E-118"},2,1,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Transport",7875566,"Clostridium saccharobutylicum","ATCC BAA-117 / DSM 13864 / NCP 262",6,333,335,7,330,334]
[null,"O85692","IPMed?",0.94675,0.95522,51.88,{"v":2E-109,"d":"2.00E-109"},3,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Electron transport, FAD, Flavoprotein, Transport",9694853,"Megasphaera elsdenii","ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927",17,334,335,17,335,338]
[null,"H6LGM8","IPMed?",0.82828,0.9791,50.3,{"v":8e-108,"d":"8.00E-108"},4,1,"carE","Caffeyl-CoA reductase-Etf complex subunit CarE","1.3.1.108","3D-structure, 4Fe-4S, Complete proteome, Cytoplasm, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NAD, Oxidoreductase, Reference proteome",23479729,"Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)","ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1",6,333,335,69,394,396]
[null,"P52039","IPMed?",0.9881,0.99104,50.3,{"v":6e-106,"d":"6.00E-106"},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",6,335,335,7,333,336]
[null,"G3KIM6","IPMed?",0.97003,1.06269,47.75,{"v":8e-106,"d":"8.00E-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",6,334,335,12,365,367]
[null,"P26483","IPMed?",0.8916,0.98209,44.98,{"v":5e-86,"d":"5.00E-86"},7,1,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Reference proteome, Transport",1850088,"Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)","_",6,331,335,30,356,369]
[null,"P09819","IPMed?",0.92635,0.97612,42.81,{"v":1E-83,"d":"1.00E-83"},8,1,"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",6,328,335,13,337,353]
[null,"P53574","_",0.91667,0.98507,44.85,{"v":3e-83,"d":"3.00E-83"},9,1,"fixB","Protein FixB","_","Electron transport, FAD, Flavoprotein, Nitrogen fixation, Transport","_","Azotobacter vinelandii","_",6,331,335,23,350,360]
[null,"Q53209","_",0.88618,0.97612,42.81,{"v":4e-82,"d":"4.00E-82"},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",6,329,335,30,354,369]
[null,"P10449","IPMed?",0.8916,0.98209,41.95,{"v":1E-79,"d":"1.00E-79"},11,1,"fixB","Protein FixB","_","Complete proteome, Electron transport, FAD, Flavoprotein, Nitrogen fixation, Reference proteome, Transport","8599534, 11157954, 12597275, 2503674","Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)","USDA 3I1b110 / USDA 110spc4 / JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110 / USDA 110spc4",6,331,335,30,356,369]
[null,"Q0AZ33","IPMed?",0.97612,1.03155,39.45,{"v":9e-73,"d":"9.00E-73"},12,1,"etfA","Electron transfer flavoprotein subunit alpha","_","Complete proteome, Cytoplasm, Electron transport, FAD, Fatty acid metabolism, Flavoprotein, Lipid metabolism, Reference proteome, Transport","21966920, 19648244, 23468890","Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)","DSM 2245B / Goettingen",9,332,335,5,317,317]
[null,"P13803","IPMed?",0.89851,0.9039,36.88,{"v":1E-52,"d":"1.00E-52"},13,1,"Etfa","Electron transfer flavoprotein subunit alpha, mitochondrial","_","Acetylation, Complete proteome, Direct protein sequencing, Electron transport, FAD, Flavoprotein, Mitochondrion, Phosphoprotein, Reference proteome, Transit peptide, Transport","3415685, 15489334, 7334008, 22673903","Rattus norvegicus","_",35,332,335,44,332,333]

{"sheet":"UniFIRE ","index":7,"n_rows":91,"n_cols":8,"rows_kept":91}
["AEQN01_180010","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000103159","catalytic activity","(S)-lactate + NAD(+) = pyruvate + NADH","_","_","MF_00488","HAMAP"]
[null,"UR000103159","gene name","ldh","_","_","MF_00488","HAMAP"]
[null,"UR000103159","GO","GO:0005737","_","_","MF_00488","HAMAP"]
[null,"UR000103159","GO","GO:0006096","_","_","MF_00488","HAMAP"]
[null,"UR000103159","GO","GO:0004459","_","_","MF_00488","HAMAP"]
[null,"UR000000418","keyword","Oxidoreductase","_","_","RU003369","RuleBase"]
[null,"UR000103159","keyword","Cytoplasm","_","_","MF_00488","HAMAP"]
[null,"UR000103159","keyword","NAD","_","_","MF_00488","HAMAP"]
[null,"UR000103159","keyword","Oxidoreductase","_","_","MF_00488","HAMAP"]
[null,"UR000103159","nucleotide binding","NAD",15,43,"MF_00488","HAMAP"]
[null,"UR000103159","pathway","Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1","_","_","MF_00488","HAMAP"]
[null,"UR000103159","product - EC number","1.1.1.27","_","_","MF_00488","HAMAP"]
[null,"UR000103159","product name","L-lactate dehydrogenase","_","_","MF_00488","HAMAP"]
[null,"UR000103159","product name","L-LDH","_","_","MF_00488","HAMAP"]
[null,"UR000000418","similarity","Belongs to the LDH/MDH superfamily","_","_","RU003369","RuleBase"]
[null,"UR000103159","similarity","Belongs to the LDH/MDH superfamily. LDH family","_","_","MF_00488","HAMAP"]
[null,"UR000103159","site actif","Proton acceptor",178,178,"MF_00488","HAMAP"]
[null,"UR000103159","site binding","Substrate",91,91,"MF_00488","HAMAP"]
[null,"UR000103159","site binding","NAD or substrate",123,123,"MF_00488","HAMAP"]
[null,"UR000103159","site binding","Substrate",154,154,"MF_00488","HAMAP"]
[null,"UR000103159","site binding","Substrate",233,233,"MF_00488","HAMAP"]
[null,"UR000103159","subcellular location","Cytoplasm","_","_","MF_00488","HAMAP"]
[null,"UR000103159","subunit","Homotetramer","_","_","MF_00488","HAMAP"]
[]
["AEQN01_90013","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"]
[]
["AEQN01_230157","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"]
[]
["AEQN01_220120","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"SAAS00649305","keyword","Oxidoreductase"]
[]
["AEQN01_220121","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000000628","similarity","Belongs to the enoyl-CoA hydratase/isomerase family","_","_","RU003707","RuleBase"]
[]
["AEQN01_220122","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"]
[]
["AEQN01_210004","UniRule","Annotation type","Annotation value","Begin","End","UniRule Source","UniRule Method"]
[null,"UR000170765","cofactor","Name=FAD; Xref=ChEBI:CHEBI:57692","_","_","RU362125","RuleBase"]
[null,"UR000170765","GO","GO:0050660","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Oxidoreductase","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","Flavoprotein","_","_","RU362125","RuleBase"]
[null,"UR000170765","keyword","FAD","_","_","RU362125","RuleBase"]
[null,"UR000170765","similarity","Belongs to the acyl-CoA dehydrogenase family","_","_","RU362125","RuleBase"]
[]
["AEQN01_220142","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"]
[]
["AEQN01_250027","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"]
[]
["AEQN01_230141","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"]
[null,"SAAS00804701","keyword","Electron transport"]
[null,"SAAS00804703","keyword","Iron"]
[null,"SAAS00804711","keyword","Metal-binding"]
[null,"SAAS00804702","keyword","Transport"]

{"sheet":"PRIAM EC number","index":8,"n_rows":86,"n_cols":15,"rows_kept":86}
["AEQN01_180010","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.1.1.27","high",1,321,{"v":1E-125,"d":"1.00E-125"},55,4,315,312,"L-lactate dehydrogenase","L-lactic acid dehydrogenase. L-lactic dehydrogenase","(S)-lactate + NAD(+) = pyruvate + NADH","_","-!- Also oxidizes other (S)-2-hydroxymonocarboxylic acids. -!- NADP(+) acts, more slowly, with the animal, but not the bacterial, enzyme"]
[null,"1.1.1.37","no",1,302,{"v":2e-49,"d":"2.00E-49"},30,37,315,279,"Malate dehydrogenase","Malic dehydrogenase","(S)-malate + NAD(+) = oxaloacetate + NADH","_","-!- Also oxidizes some other 2-hydroxydicarboxylic acids"]
[null,"1.1.1.82","no",1,322,{"v":5e-19,"d":"5.00E-19"},21,8,288,281,"Malate dehydrogenase (NADP(+))","NADP-linked malate dehydrogenase","(S)-malate + NADP(+) = oxaloacetate + NADPH","_","-!- Activated by light"]
[]
["AEQN01_90013","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.2.1.51","high",1,1928,0,47,8,1165,1158,"Pyruvate dehydrogenase (NADP(+))","Pyruvate:NADP(+) oxidoreductase","Pyruvate + CoA + NADP(+) = acetyl-CoA + CO(2) + NADPH","_","-!- The Euglena enzyme can also use FAD or methylviologen as acceptor, more slowly. -!- Inhibited by oxygen"]
[null,"1.16.1.5","no",1,1803,0,47,7,1165,1159,"Aquacobalamin reductase (NADPH)","Aquacobalamin (reduced nicotinamide adenine dinucleotide phosphate) reductase. NADPH-linked aquacobalamin reductase. NADPH:aquacob(III)alamin oxidoreductase","2 cob(II)alamin + NADP(+) + 2 H(2)O = 2 aquacob(III)alamin + NADPH","Flavoprotein","-!- Acts on aquacob(III)alamin and hydroxycobalamin, but not on cyanocobalamin. -!- Formerly EC 1.6.99.11"]
[null,"1.2.7.1","no",3,395,{"v":2E-50,"d":"2.00E-50"},31,10,385,376,"Pyruvate synthase","2-oxobutyrate synthase. 2-oxobutyrate-ferredoxin oxidoreductase. Alpha-ketobutyrate synthase. Alpha-ketobutyrate-ferredoxin oxidoreductase. Pyruvate oxidoreductase. Pyruvate synthetase. Pyruvic-ferredoxin oxidoreductase","Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+)","Iron-sulfur; Thiamine diphosphate","-!- The enzyme also decarboxylates 2-oxobutanoate with lower efficiency, but shows no activity with 2-oxoglutarate. -!- This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to fo"]
[null,"1.2.7.7","no",4,328,{"v":7e-26,"d":"7.00E-26"},24,10,329,320,"3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)","2-ketoisovalerate ferredoxin reductase. 2-oxoisovalerate ferredoxin reductase. 3-methyl-2-oxobutanoate synthase (ferredoxin). Branched-chain ketoacid ferredoxin reductase. Branched-chain oxo acid ferredoxin reductase. Keto-valine-ferredoxin oxidoreductase. Ketoisovalerate ferredoxin reductase. Ketoisovalerate oxidoreductase. VOR","3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO(2) + 2 reduced ferredoxin + H(+)","Iron-sulfur; Tungstopterin","-!- The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. -!- Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo- pentanoate, and 2-oxobutanoate. -!"]
[]
["AEQN01_230157","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"1.2.1.51","high",1,1928,0,45,8,1162,1155,"Pyruvate dehydrogenase (NADP(+))","Pyruvate:NADP(+) oxidoreductase","Pyruvate + CoA + NADP(+) = acetyl-CoA + CO(2) + NADPH","_","-!- The Euglena enzyme can also use FAD or methylviologen as acceptor, more slowly. -!- Inhibited by oxygen"]
[null,"1.16.1.5","no",1,1803,0,47,8,1162,1155,"Aquacobalamin reductase (NADPH)","Aquacobalamin (reduced nicotinamide adenine dinucleotide phosphate) reductase. NADPH-linked aquacobalamin reductase. NADPH:aquacob(III)alamin oxidoreductase","2 cob(II)alamin + NADP(+) + 2 H(2)O = 2 aquacob(III)alamin + NADPH","Flavoprotein","-!- Acts on aquacob(III)alamin and hydroxycobalamin, but not on cyanocobalamin. -!- Formerly EC 1.6.99.11"]
[null,"1.2.7.1","no",3,395,{"v":1e-48,"d":"1.00E-48"},28,5,392,388,"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":5e-26,"d":"5.00E-26"},23,10,329,320,"3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)","2-ketoisovalerate ferredoxin reductase. 2-oxoisovalerate ferredoxin reductase. 3-methyl-2-oxobutanoate synthase (ferredoxin). Branched-chain ketoacid ferredoxin reductase. Branched-chain oxo acid ferredoxin reductase. Keto-valine-ferredoxin oxidoreductase. Ketoisovalerate ferredoxin reductase. Ketoisovalerate oxidoreductase. VOR","3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO(2) + 2 reduced ferredoxin + H(+)","Iron-sulfur; Tungstopterin","-!- The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. -!- Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo- pentanoate, and 2-oxobutanoate. -!"]
[null,"1.2.7.1","no",1,184,5e-14,26,421,608,188,"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"]
[]
["AEQN01_220120","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":3e-96,"d":"3.00E-96"},52,1,279,279,"3-hydroxybutyryl-CoA dehydrogenase","Beta-hydroxybutyryl-CoA dehydrogenase. BHBD","(S)-3-hydroxybutanoyl-CoA + NADP(+) = 3-acetoacetyl-CoA + NADPH","_","_"]
[null,"1.1.1.35","no",1,301,{"v":6e-74,"d":"6.00E-74"},36,2,281,280,"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":2e-57,"d":"2.00E-57"},32,2,279,278,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"1.1.1.211","no",1,763,{"v":2e-37,"d":"2.00E-37"},33,3,279,277,"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)"]
[]
["AEQN01_220121","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":2e-81,"d":"2.00E-81"},56,7,258,252,"3-hydroxybutyryl-CoA dehydratase","Crotonase","(3R)-3-hydroxybutanoyl-CoA = crotonoyl-CoA + H(2)O","_","-!- Also acts on crotonoyl thioesters of pantetheine and acyl-carrier protein"]
[null,"4.2.1.17","no",1,264,{"v":6e-59,"d":"6.00E-59"},39,9,251,243,"Enoyl-CoA hydratase","Enoyl hydrase. Unsaturated acyl-CoA hydratase","(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O","_","-!- Acts in the reverse direction. -!- With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74)"]
[null,"4.2.1.18","no",1,276,{"v":3e-46,"d":"3.00E-46"},38,12,251,240,"Methylglutaconyl-CoA hydratase","_","(S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA + H(2)O","_","_"]
[null,"5.1.2.3","no",1,707,{"v":3E-43,"d":"3.00E-43"},42,10,197,188,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"5.3.3.8","no",1,265,{"v":3e-41,"d":"3.00E-41"},40,10,208,199,"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":2e-37,"d":"2.00E-37"},35,4,251,248,"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":2e-27,"d":"2.00E-27"},30,12,251,240,"Transferred entry: 7.2.4.3","_","_","_","_"]
[null,"1.1.1.211","no",1,763,{"v":2e-24,"d":"2.00E-24"},33,4,198,195,"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-23,"d":"4.00E-23"},33,4,191,188,"3-hydroxyisobutyryl-CoA hydrolase","_","3-hydroxy-2-methylpropanoyl-CoA + H(2)O = CoA + 3-hydroxy-2- methylpropanoate","_","-!- Also hydrolyzes 3-hydroxypropanoyl-CoA"]
[null,"2.3.1.48","no",43,544,5e-14,23,14,253,240,"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"]
[null,"4.2.1.100","no",1,258,1E-13,28,35,250,216,"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"]
[]
["AEQN01_220122","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-145,"d":"1.00E-145"},56,6,391,386,"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-104,"d":"1.00E-104"},39,3,393,391,"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-99,"d":"4.00E-99"},41,3,391,389,"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"]
[]
["AEQN01_70057","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":3e-39,"d":"3.00E-39"},28,5,316,312,"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":3E-32,"d":"3.00E-32"},25,2,316,315,"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":2e-24,"d":"2.00E-24"},24,3,316,314,"3-hydroxybutyryl-CoA epimerase","_","(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA","_","_"]
[null,"1.1.1.211","no",1,763,{"v":9e-16,"d":"9.00E-16"},22,2,317,316,"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)"]
[]
["AEQN01_300005","PRIAM EC number","Evidence","Profile","Profile Length","Eval","Ident %","Begin","End","Match Length","Enzyme Description","Alternative Name","Catalysed Reaction","Reaction Cofactor","Comments"]
[null,"3.1.2.1","high",1,525,{"v":4e-18,"d":"4.00E-18"},26,109,430,322,"Acetyl-CoA hydrolase","Acetyl-CoA acylase. Acetyl-CoA deacylase","Acetyl-CoA + H(2)O = CoA + acetate","_","_"]
[]
["AEQN01_210004","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"},44,1,373,373,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":4e-98,"d":"4.00E-98"},44,2,380,379,"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-77,"d":"1.00E-77"},35,4,379,376,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":1E-54,"d":"1.00E-54"},33,4,377,374,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":1e-43,"d":"1.00E-43"},30,4,371,368,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":4E-35,"d":"4.00E-35"},31,39,377,339,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":8e-18,"d":"8.00E-18"},22,71,374,304,"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)"]
[]
["AEQN01_220142","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-101,"d":"1.00E-101"},49,1,374,374,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":4e-81,"d":"4.00E-81"},37,2,375,374,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":5E-80,"d":"5.00E-80"},39,2,378,377,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":7e-61,"d":"7.00E-61"},35,4,378,375,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":8e-50,"d":"8.00E-50"},29,5,377,373,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":3e-47,"d":"3.00E-47"},34,1,378,378,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":7e-25,"d":"7.00E-25"},23,44,378,335,"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)"]
[]
["AEQN01_250027","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-100,"d":"1.00E-100"},43,3,379,377,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":2e-94,"d":"2.00E-94"},42,4,381,378,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":6e-71,"d":"6.00E-71"},33,5,377,373,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":2E-55,"d":"2.00E-55"},34,18,377,360,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":7e-40,"d":"7.00E-40"},28,6,375,370,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":1e-36,"d":"1.00E-36"},31,3,377,375,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":1e-17,"d":"1.00E-17"},22,93,375,283,"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)"]
[]
["AEQN01_230141","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-139,"d":"1.00E-139"},54,1,378,378,"Transferred entry: 1.3.8.1","_","_","_","_"]
[null,"1.3.99.10","no",1,404,{"v":1e-86,"d":"1.00E-86"},37,7,377,371,"Transferred entry: 1.3.8.4","_","_","_","_"]
[null,"1.3.99.3","no",1,408,{"v":4e-76,"d":"4.00E-76"},37,3,380,378,"Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9","_","_","_","_"]
[null,"1.3.99.7","no",1,405,{"v":1E-62,"d":"1.00E-62"},34,4,379,376,"Transferred entry: 1.3.8.6","_","_","_","_"]
[null,"1.3.99.13","no",1,430,{"v":3e-60,"d":"3.00E-60"},35,9,378,370,"Transferred entry: 1.3.8.8","_","_","_","_"]
[null,"1.3.99.21","no",1,406,{"v":1e-37,"d":"1.00E-37"},29,1,378,378,"Transferred entry: 1.3.8.3","_","_","_","_"]
[null,"1.3.3.6","no",1,494,{"v":9e-28,"d":"9.00E-28"},21,10,378,369,"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":23,"n_cols":7,"rows_kept":23}
["CDS","COG id","Score","Begin","End","Classes","Function"]
["AEQN01_210010","COG3875",307,38,344,"S","Uncharacterized conserved protein"]
["AEQN01_210007","COG1620",512,4,515,"C","L-lactate permease"]
["AEQN01_180010","COG0039",317,1,317,"C","Malate/lactate dehydrogenases"]
["AEQN01_90013","COG0674",411,1,411,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
[null,"COG1014",383,414,796,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
[null,"COG1013",374,797,1170,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
["AEQN01_230157","COG0674",410,1,410,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit"]
[null,"COG1014",384,414,797,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, gamma subunit"]
[null,"COG1013",371,798,1168,"C","Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit"]
["AEQN01_220120","COG1250",281,1,281,"I","3-hydroxyacyl-CoA dehydrogenase"]
["AEQN01_220121","COG1024",258,1,258,"I","Enoyl-CoA hydratase/carnithine racemase"]
["AEQN01_220122","COG0183",394,1,394,"I","Acetyl-CoA acetyltransferase"]
["AEQN01_70057","COG1250",317,1,317,"I","3-hydroxyacyl-CoA dehydrogenase"]
["AEQN01_300005","COG0427",436,4,439,"C","Acetyl-CoA hydrolase"]
["AEQN01_210004","COG1960",380,1,380,"I","Acyl-CoA dehydrogenases"]
["AEQN01_220142","COG1960",381,1,381,"I","Acyl-CoA dehydrogenases"]
["AEQN01_250027","COG1960",383,1,383,"I","Acyl-CoA dehydrogenases"]
["AEQN01_230141","COG1960",397,1,397,"I","Acyl-CoA dehydrogenases"]
[null,"COG2025",174,398,571,"C","Electron transfer flavoprotein, alpha subunit"]
[null,"COG1773",50,590,639,"C","Rubredoxin"]
["AEQN01_220164","COG2086",266,1,266,"C","Electron transfer flavoprotein, beta subunit"]
["AEQN01_220165","COG2025",330,6,335,"C","Electron transfer flavoprotein, alpha subunit"]

{"sheet":"EGGNOG","index":10,"n_rows":17,"n_cols":7,"rows_kept":17}
["CDS","OG ID","Score","Eval","Class ID","OG function","KEGG map"]
["AEQN01_210010","05QUH","841.6",{"v":5.8e-242,"d":"5.80E-242"},"S","Domain of unknown function (DUF2088)","-"]
["AEQN01_210007","05DAA","958",{"v":6.8e-277,"d":"6.80E-277"},"C","L-lactate","-"]
["AEQN01_180010","05C80","622.1",{"v":5.4e-176,"d":"5.40E-176"},"C","Catalyzes the reversible oxidation of malate to oxaloacetate (By similarity)","00010, 00020, 00270, 00620, 00630, 00640, 00680, 00710, 00720, 01100, 01110, 01120"]
["AEQN01_90013","05D95","2370.5",0,"C","Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (By similarity)","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 00910, 01100, 01120"]
["AEQN01_230157","05D95","2376.3",0,"C","Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (By similarity)","00010, 00020, 00620, 00633, 00640, 00650, 00680, 00720, 00910, 01100, 01120"]
["AEQN01_220120","05DYT","547.7",{"v":1.1E-153,"d":"1.10E-153"},"I","3-hydroxyacyl-CoA dehydrogenase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00640, 00650, 00720, 00903, 00930, 01040, 01100, 01110, 01120"]
["AEQN01_220121","05E39","509.6",{"v":3.2e-142,"d":"3.20E-142"},"I","Enoyl-CoA hydratase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00627, 00630, 00640, 00650, 00720, 00903, 00930, 01100, 01110, 01120"]
["AEQN01_220122","05CHU","785.4",{"v":4.6e-225,"d":"4.60E-225"},"I","acetyl-coa acetyltransferase","00071, 00072, 00280, 00281, 00310, 00362, 00380, 00592, 00620, 00630, 00640, 00642, 00650, 00720, 00900, 01100, 01110, 01120, 02020"]
["AEQN01_70057","05DYT","624.8",{"v":8.3e-177,"d":"8.30E-177"},"I","3-hydroxyacyl-CoA dehydrogenase","00071, 00280, 00281, 00310, 00360, 00362, 00380, 00410, 00640, 00650, 00720, 00903, 00930, 01040, 01100, 01110, 01120"]
["AEQN01_300005","05CYC","909.8",{"v":1.8e-262,"d":"1.80E-262"},"C","Transferase","00620"]
["AEQN01_210004","05C1G","755",{"v":6.4e-216,"d":"6.40E-216"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["AEQN01_220142","05C1G","722.2",{"v":4.6e-206,"d":"4.60E-206"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["AEQN01_250027","05C1G","756.5",{"v":2.2e-216,"d":"2.20E-216"},"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["AEQN01_230141","05C1G","1270.4",0,"I","acyl-Coa dehydrogenase","00071, 00280, 00281, 00310, 00380, 00410, 00640, 01100, 01110, 03320"]
["AEQN01_220164","05BZJ","528.9",{"v":5.2e-148,"d":"5.20E-148"},"C","Electron transfer flavoprotein","00910"]
["AEQN01_220165","05C10","678.3",{"v":6.7e-193,"d":"6.70E-193"},"C","Electron transfer flavoprotein","00910"]

{"sheet":"FigFam","index":11,"n_rows":11,"n_cols":4,"rows_kept":11}
["CDS","FIGFAM id","FIGFAM Description","EC number"]
["AEQN01_180010","FIG000812","L-lactate dehydrogenase","1.1.1.27"]
["AEQN01_90013","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["AEQN01_230157","FIG001269","Pyruvate-flavodoxin oxidoreductase","1.2.7.-"]
["AEQN01_220122","FIG002604","Acetyl-CoA acetyltransferase","2.3.1.9"]
["AEQN01_70057","FIG000819","3-hydroxybutyryl-CoA dehydrogenase","1.1.1.157, 1.1.1.35"]
["AEQN01_210004","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["AEQN01_220142","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["AEQN01_230141","FIG009149","Butyryl-CoA dehydrogenase","1.3.8.1"]
["AEQN01_220164","FIG136866","Electron transfer flavoprotein, beta subunit","_"]
["AEQN01_220165","FIG000366","Electron transfer flavoprotein, alpha subunit","_"]

{"sheet":"InterProScan","index":12,"n_rows":245,"n_cols":13,"rows_kept":245}
["AEQN01_210010","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",8,212,0.478873,{"v":1.9E-62,"d":"1.90E-62"},"LarA-like_N","Domain","LarA-like, N-terminal","Molecular Function: lactate racemase activity (GO:0050043)"]
[null,"_","_","PTHR33171","_",2,421,0.983568,{"v":1.5e-97,"d":"1.50E-97"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.11440","_",33,268,0.551643,{"v":2.4E-147,"d":"2.40E-147"},"_","_","_","-"]
[null,"_","_","G3DSA:3.90.226.30","_",5,417,0.967136,{"v":2.4E-147,"d":"2.40E-147"},"_","_","_","-"]
[]
["AEQN01_210007","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",4,510,0.978723,{"v":3.7E-137,"d":"3.70E-137"},"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",5,509,0.974855,{"v":3.7e-131,"d":"3.70E-131"},"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",4,510,0.978723,{"v":2.4e-126,"d":"2.40E-126"},"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","_",4,510,0.978723,{"v":3.7E-137,"d":"3.70E-137"},"_","_","_","-"]
[]
["AEQN01_180010","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036291","SSF","SSF51735","SSF51735",4,147,0.451104,{"v":8.13e-55,"d":"8.13E-55"},"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR022383","PFAM","PF02866","Ldh_1_C",148,313,0.520505,{"v":2.8e-30,"d":"2.80E-30"},"Lactate/malate_DH_C","Domain","Lactate/malate dehydrogenase, C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR018177","PROSITE","PS00064","L_LDH",175,181,0.0189274,"_","L-lactate_DH_AS","Active_site","L-lactate dehydrogenase, active site","Molecular Function: L-lactate dehydrogenase activity (GO:0004459); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR015955","CATHGENE3D","G3DSA:3.90.110.10","G3DSA:3.90.110.10",148,316,0.529968,{"v":1E-58,"d":"1.00E-58"},"Lactate_DH/Glyco_Ohase_4_C","Homologous_superfamily","Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal","Molecular Function: catalytic activity (GO:0003824); Biological Process: carbohydrate metabolic process (GO:0005975); Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR015955","SSF","SSF56327","SSF56327",146,315,0.533123,{"v":5.11e-54,"d":"5.11E-54"},"Lactate_DH/Glyco_Ohase_4_C","Homologous_superfamily","Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal","Molecular Function: catalytic activity (GO:0003824); Biological Process: carbohydrate metabolic process (GO:0005975); Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011304","HAMAP","MF_00488","Lactate_dehydrog",6,316,0.977918,42.945,"L-lactate_DH","Family","L-lactate dehydrogenase","Molecular Function: L-lactate dehydrogenase activity (GO:0004459); Cellular Component: cytoplasm (GO:0005737); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011304","TIGRFAMs","TIGR01771","L-LDH-NAD",11,309,0.940063,{"v":5.6e-122,"d":"5.60E-122"},"L-lactate_DH","Family","L-lactate dehydrogenase","Molecular Function: L-lactate dehydrogenase activity (GO:0004459); Cellular Component: cytoplasm (GO:0005737); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001557","PIRSF","PIRSF000102","Lac_mal_DH",3,316,0.987382,{"v":2.6e-106,"d":"2.60E-106"},"L-lactate/malate_DH","Family","L-lactate/malate dehydrogenase","Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: carboxylic acid metabolic process (GO:0019752); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001557","PRINTS","PR00086","LLDHDRGNASE",33,57,0.0757098,{"v":3.7e-50,"d":"3.70E-50"},"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",8,32,0.0757098,{"v":3.7e-50,"d":"3.70E-50"},"L-lactate/malate_DH","Family","L-lactate/malate dehydrogenase","Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: carboxylic acid metabolic process (GO:0019752); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001557","PRINTS","PR00086","LLDHDRGNASE",143,161,0.0567823,{"v":3.7e-50,"d":"3.70E-50"},"L-lactate/malate_DH","Family","L-lactate/malate dehydrogenase","Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: carboxylic acid metabolic process (GO:0019752); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001557","PRINTS","PR00086","LLDHDRGNASE",119,139,0.0630915,{"v":3.7e-50,"d":"3.70E-50"},"L-lactate/malate_DH","Family","L-lactate/malate dehydrogenase","Molecular Function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616); Biological Process: carboxylic acid metabolic process (GO:0019752); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR001557","PRINTS","PR00086","LLDHDRGNASE",173,186,0.0410095,{"v":3.7e-50,"d":"3.70E-50"},"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",8,145,0.432177,{"v":5.1e-46,"d":"5.10E-46"},"Lactate/malate_DH_N","Domain","Lactate/malate dehydrogenase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","G3DSA:3.40.50.720","_",2,147,0.457413,{"v":3.2e-59,"d":"3.20E-59"},"_","_","_","-"]
[null,"_","_","PTHR43128","_",7,312,0.962145,{"v":2.1e-127,"d":"2.10E-127"},"_","_","_","-"]
[null,"_","_","PTHR43128:SF4","_",7,312,0.962145,{"v":2.1e-127,"d":"2.10E-127"},"_","_","_","-"]
[null,"_","_","cd05292","_",8,315,0.968454,0,"_","_","_","-"]
[]
["AEQN01_90013","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033412","PFAM","PF17147","PFOR_II",269,374,0.0897436,1.4e-15,"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",3,258,0.217949,{"v":5.89e-75,"d":"5.89E-75"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",788,1167,0.323932,{"v":1.68e-120,"d":"1.68E-120"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",425,609,0.157265,{"v":1.7e-32,"d":"1.70E-32"},"Pyrv/ketoisovalerate_OxRed_cat","Domain","Pyruvate/ketoisovalerate oxidoreductase, catalytic domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR019456","PFAM","PF10371","EKR",626,680,0.0461538,{"v":3.6e-19,"d":"3.60E-19"},"Pyrv-flavodox_OxRtase_EKR","Domain","Pyruvate-flavodoxin oxidoreductase, EKR domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR019456","SMART","SM00890","EKR",623,681,0.0495727,{"v":1.3e-19,"d":"1.30E-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,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",691,702,0.00940171,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",682,711,0.0247863,9.525,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",738,769,0.0264957,8.634,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR011895","PIRSF","PIRSF000159","NifJ",1,1169,0.998291,0,"Pyrv_flavodox_OxRed","Family","Pyruvate-flavodoxin oxidoreductase","Molecular Function: iron ion binding (GO:0005506); Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: electron transport chain (GO:0022900); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011895","TIGRFAMs","TIGR02176","pyruv_ox_red",5,1167,0.993162,0,"Pyrv_flavodox_OxRed","Family","Pyruvate-flavodoxin oxidoreductase","Molecular Function: iron ion binding (GO:0005506); Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: electron transport chain (GO:0022900); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011766","PFAM","PF02775","TPP_enzyme_C",959,1070,0.0948718,1.4E-11,"TPP_enzyme-bd_C","Domain","Thiamine pyrophosphate enzyme, C-terminal TPP-binding","Molecular Function: catalytic activity (GO:0003824); Molecular Function: thiamine pyrophosphate binding (GO:0030976)"]
[null,"IPR009014","CATHGENE3D","G3DSA:3.40.50.920","G3DSA:3.40.50.920",259,413,0.131624,{"v":3.9e-55,"d":"3.90E-55"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR009014","SSF","SSF52922","SSF52922",259,412,0.130769,{"v":4.57e-42,"d":"4.57E-42"},"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",17,246,0.195726,{"v":2.3E-75,"d":"2.30E-75"},"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",415,627,0.181197,{"v":6.4e-88,"d":"6.40E-88"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","SSF","SSF53323","SSF53323",416,661,0.209402,{"v":2.88e-80,"d":"2.88E-80"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PF13484","_",690,758,0.0581197,6.4e-09,"_","_","_","-"]
[null,"_","_","SSF54862","_",672,832,0.136752,1.81E-18,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",671,786,0.0982906,{"v":3.3e-43,"d":"3.30E-43"},"_","_","_","-"]
[null,"_","_","cd07034","_",10,173,0.139316,{"v":1.22139E-51,"d":"1.22E-51"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",2,258,0.218803,{"v":3.1e-105,"d":"3.10E-105"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",787,1170,0.32735,{"v":7.9e-157,"d":"7.90E-157"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",1,1167,0.996581,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",1,1167,0.996581,0,"_","_","_","-"]
[null,"_","_","cd03377","_",805,1167,0.309402,0,"_","_","_","-"]
[]
["AEQN01_230157","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033412","PFAM","PF17147","PFOR_II",269,370,0.0863248,3.3e-13,"PFOR_II","Domain","Pyruvate:ferredoxin oxidoreductase, core domain II","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",4,258,0.217094,{"v":4.71e-74,"d":"4.71E-74"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR029061","SSF","SSF52518","SSF52518",790,1167,0.322222,{"v":1.86e-123,"d":"1.86E-123"},"THDP-binding","Homologous_superfamily","Thiamin diphosphate-binding fold","-"]
[null,"IPR019752","PFAM","PF01558","POR",425,610,0.15812,{"v":1.7e-30,"d":"1.70E-30"},"Pyrv/ketoisovalerate_OxRed_cat","Domain","Pyruvate/ketoisovalerate oxidoreductase, catalytic domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR019456","PFAM","PF10371","EKR",625,680,0.0470085,{"v":4.1e-20,"d":"4.10E-20"},"Pyrv-flavodox_OxRtase_EKR","Domain","Pyruvate-flavodoxin oxidoreductase, EKR domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR019456","SMART","SM00890","EKR",623,681,0.0495727,{"v":2.2e-22,"d":"2.20E-22"},"Pyrv-flavodox_OxRtase_EKR","Domain","Pyruvate-flavodoxin oxidoreductase, EKR domain","Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",691,702,0.00940171,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017900","PROSITE","PS00198","4FE4S_FER_1",747,758,0.00940171,"_","4Fe4S_Fe_S_CS","Conserved_site","4Fe-4S ferredoxin, iron-sulphur binding, conserved site","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",738,769,0.0264957,9.76,"4Fe4S_Fe-S-bd","Domain","4Fe-4S ferredoxin-type, iron-sulphur binding domain","-"]
[null,"IPR017896","PROFILE","PS51379","4FE4S_FER_2",682,711,0.0247863,9.34,"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",7,1167,0.991453,0,"Pyrv_flavodox_OxRed","Family","Pyruvate-flavodoxin oxidoreductase","Molecular Function: iron ion binding (GO:0005506); Molecular Function: oxidoreductase activity, acting on the aldehyde or oxo group of donors (GO:0016903); Biological Process: electron transport chain (GO:0022900); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR011766","PFAM","PF02775","TPP_enzyme_C",953,1066,0.0965812,2.7E-11,"TPP_enzyme-bd_C","Domain","Thiamine pyrophosphate enzyme, C-terminal TPP-binding","Molecular Function: catalytic activity (GO:0003824); Molecular Function: thiamine pyrophosphate binding (GO:0030976)"]
[null,"IPR009014","CATHGENE3D","G3DSA:3.40.50.920","G3DSA:3.40.50.920",259,413,0.131624,{"v":1.8E-58,"d":"1.80E-58"},"Transketo_C/PFOR_II","Homologous_superfamily","Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR009014","SSF","SSF52922","SSF52922",259,414,0.132479,{"v":2.86e-47,"d":"2.86E-47"},"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",21,247,0.193162,{"v":3.8e-73,"d":"3.80E-73"},"Pyrv_Fd/Flavodoxin_OxRdtase_N","Domain","Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","CATHGENE3D","G3DSA:3.40.920.10","G3DSA:3.40.920.10",415,626,0.180342,{"v":2.1e-87,"d":"2.10E-87"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR002869","SSF","SSF53323","SSF53323",418,668,0.213675,{"v":9.15e-80,"d":"9.15E-80"},"Pyrv_flavodox_OxRed_cen","Homologous_superfamily","Pyruvate-flavodoxin oxidoreductase, central domain","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PF13484","_",690,759,0.0589744,3E-9,"_","_","_","-"]
[null,"_","_","SSF54862","_",667,834,0.142735,2.09E-19,"_","_","_","-"]
[null,"_","_","G3DSA:3.30.70.20","_",671,786,0.0982906,{"v":3.4e-43,"d":"3.40E-43"},"_","_","_","-"]
[null,"_","_","cd07034","_",10,173,0.139316,{"v":3.67411E-50,"d":"3.67E-50"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",2,258,0.218803,{"v":3.5E-105,"d":"3.50E-105"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.970","_",788,1169,0.325641,{"v":3.8E-162,"d":"3.80E-162"},"_","_","_","-"]
[null,"_","_","PTHR32154","_",3,1165,0.993162,0,"_","_","_","-"]
[null,"_","_","PTHR32154:SF0","_",3,1165,0.993162,0,"_","_","_","-"]
[null,"_","_","cd03377","_",806,1167,0.308547,0,"_","_","_","-"]
[]
["AEQN01_220120","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR036291","SSF","SSF51735","SSF51735",2,179,0.629893,{"v":3.81e-51,"d":"3.81E-51"},"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR022694","PIRSF","PIRSF000105","HCDH",1,281,0.996441,{"v":7.8e-86,"d":"7.80E-86"},"3-OHacyl-CoA_DH","Family","3-hydroxyacyl-CoA dehydrogenase","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Biological Process: oxidation-reduction process (GO:0055114); Molecular Function: NAD+ binding (GO:0070403)"]
[null,"IPR013328","CATHGENE3D","G3DSA:1.10.1040.10","G3DSA:1.10.1040.10",186,281,0.338078,{"v":1.8e-35,"d":"1.80E-35"},"6PGD_dom2","Homologous_superfamily","6-phosphogluconate dehydrogenase, domain 2","Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR008927","SSF","SSF48179","SSF48179",183,280,0.345196,{"v":7.14e-32,"d":"7.14E-32"},"6-PGluconate_DH-like_C_sf","Homologous_superfamily","6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily","Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006180","PROSITE","PS00067","3HCDH",180,204,0.0854093,"_","3-OHacyl-CoA_DH_CS","Conserved_site","3-hydroxyacyl-CoA dehydrogenase, conserved site","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006176","PFAM","PF02737","3HCDH_N",2,180,0.633452,{"v":4.3e-62,"d":"4.30E-62"},"3-OHacyl-CoA_DH_NAD-bd","Domain","3-hydroxyacyl-CoA dehydrogenase, NAD binding","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006108","PFAM","PF00725","3HCDH",183,279,0.341637,{"v":4.7E-35,"d":"4.70E-35"},"3HC_DH_C","Domain","3-hydroxyacyl-CoA dehydrogenase, C-terminal","Molecular Function: 3-hydroxyacyl-CoA dehydrogenase activity (GO:0003857); Biological Process: fatty acid metabolic process (GO:0006631); Molecular Function: oxidoreductase activity (GO:0016491); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","G3DSA:3.40.50.720","_",1,185,0.654804,{"v":1.2E-64,"d":"1.20E-64"},"_","_","_","-"]
[null,"_","_","PTHR43145","_",2,280,0.989324,{"v":6.1e-107,"d":"6.10E-107"},"_","_","_","-"]
[null,"_","_","PTHR43145:SF10","_",2,280,0.989324,{"v":6.1e-107,"d":"6.10E-107"},"_","_","_","-"]
[]
["AEQN01_220121","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR029045","SSF","SSF52096","SSF52096",1,253,0.976744,{"v":2.85e-86,"d":"2.85E-86"},"ClpP/crotonase-like_dom_sf","Homologous_superfamily","ClpP/crotonase-like domain superfamily","-"]
[null,"IPR018376","PROSITE","PS00166","ENOYL_COA_HYDRATASE",98,118,0.0775194,"_","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",198,257,0.228682,{"v":1.5E-19,"d":"1.50E-19"},"Enoyl-CoA_hydra_C","Homologous_superfamily","Enoyl-CoA hydratase, C-terminal","-"]
[null,"IPR001753","PFAM","PF00378","ECH_1",9,252,0.94186,{"v":7.1e-73,"d":"7.10E-73"},"Enoyl-CoA_hydra/iso","Family","Enoyl-CoA hydratase/isomerase","Molecular Function: catalytic activity (GO:0003824)"]
[null,"_","_","G3DSA:3.90.226.10","_",3,197,0.751938,{"v":2.1E-69,"d":"2.10E-69"},"_","_","_","-"]
[null,"_","_","cd06558","_",4,196,0.744186,{"v":2.98458e-75,"d":"2.98E-75"},"_","_","_","-"]
[null,"_","_","PTHR11941","_",9,252,0.94186,{"v":1.1e-79,"d":"1.10E-79"},"_","_","_","-"]
[null,"_","_","PTHR11941:SF140","_",9,252,0.94186,{"v":1.1e-79,"d":"1.10E-79"},"_","_","_","-"]
[]
["AEQN01_220122","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR020617","PFAM","PF02803","Thiolase_C",271,391,0.304569,{"v":1.4e-43,"d":"1.40E-43"},"Thiolase_C","Domain","Thiolase, C-terminal","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020616","PFAM","PF00108","Thiolase_N",5,262,0.652284,{"v":1.4E-100,"d":"1.40E-100"},"Thiolase_N","Domain","Thiolase, N-terminal","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR020610","PROSITE","PS00099","THIOLASE_3",374,387,0.0329949,"_","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",127,388,0.662437,{"v":8.3e-157,"d":"8.30E-157"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","CATHGENE3D","G3DSA:3.40.47.10","G3DSA:3.40.47.10",6,276,0.685279,{"v":8.3e-157,"d":"8.30E-157"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",271,391,0.304569,{"v":3.9e-40,"d":"3.90E-40"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR016039","SSF","SSF53901","SSF53901",4,270,0.675127,{"v":3.36e-91,"d":"3.36E-91"},"Thiolase-like","Homologous_superfamily","Thiolase-like","Molecular Function: catalytic activity (GO:0003824)"]
[null,"IPR002155","CDD","cd00751","thiolase",6,392,0.979695,0,"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":9.9e-130,"d":"9.90E-130"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"IPR002155","TIGRFAMs","TIGR01930","AcCoA-C-Actrans",7,391,0.974619,{"v":3.4e-143,"d":"3.40E-143"},"Thiolase","Family","Thiolase","Molecular Function: transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)"]
[null,"_","_","PTHR18919","_",2,391,0.98731,{"v":6.3e-158,"d":"6.30E-158"},"_","_","_","-"]
[null,"_","_","PTHR18919:SF107","_",2,391,0.98731,{"v":6.3e-158,"d":"6.30E-158"},"_","_","_","-"]
[]
["AEQN01_70057","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",1,212,0.665615,{"v":5.3e-34,"d":"5.30E-34"},"NAD(P)-bd_dom_sf","Homologous_superfamily","NAD(P)-binding domain superfamily","-"]
[null,"IPR022694","PIRSF","PIRSF000105","HCDH",1,89,0.277603,2.4e-07,"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,"IPR022694","PIRSF","PIRSF000105","HCDH",75,317,0.763407,{"v":1.9e-56,"d":"1.90E-56"},"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",220,317,0.305994,{"v":1.1E-24,"d":"1.10E-24"},"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",217,316,0.312303,1.45E-20,"6-PGluconate_DH-like_C_sf","Homologous_superfamily","6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily","Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006176","PFAM","PF02737","3HCDH_N",5,215,0.662461,{"v":1.8E-32,"d":"1.80E-32"},"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",218,316,0.309148,{"v":8.2e-20,"d":"8.20E-20"},"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","_",1,219,0.687697,{"v":5.8e-45,"d":"5.80E-45"},"_","_","_","-"]
[null,"_","_","PTHR43561","_",96,316,0.694006,{"v":1.4e-79,"d":"1.40E-79"},"_","_","_","-"]
[null,"_","_","PTHR43561","_",1,72,0.223975,{"v":1.4e-79,"d":"1.40E-79"},"_","_","_","-"]
[null,"_","_","PTHR43561:SF4","_",96,316,0.694006,{"v":1.4e-79,"d":"1.40E-79"},"_","_","_","-"]
[null,"_","_","PTHR43561:SF4","_",1,72,0.223975,{"v":1.4e-79,"d":"1.40E-79"},"_","_","_","-"]
[]
["AEQN01_300005","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR038460","CATHGENE3D","G3DSA:3.40.1080.20","G3DSA:3.40.1080.20",296,445,0.334081,{"v":1E-54,"d":"1.00E-54"},"AcetylCoA_hyd_C_sf","Homologous_superfamily","Acetyl-CoA hydrolase/transferase, C-terminal domain superfamily","-"]
[null,"IPR037171","SSF","SSF100950","SSF100950",4,226,0.497758,{"v":1.26e-34,"d":"1.26E-34"},"NagB/RpiA_transferase-like","Homologous_superfamily","NagB/RpiA transferase-like","-"]
[null,"IPR037171","SSF","SSF100950","SSF100950",193,440,0.553812,{"v":3.62e-57,"d":"3.62E-57"},"NagB/RpiA_transferase-like","Homologous_superfamily","NagB/RpiA transferase-like","-"]
[null,"IPR026888","PFAM","PF13336","AcetylCoA_hyd_C",278,432,0.345291,{"v":2.1E-59,"d":"2.10E-59"},"AcetylCoA_hyd_C","Domain","Acetyl-CoA hydrolase/transferase C-terminal domain","-"]
[null,"IPR023990","TIGRFAMs","TIGR03948","butyr_acet_CoA",3,445,0.991031,{"v":3.8e-227,"d":"3.80E-227"},"Butryl-CoA_acetate_CoA_Tfrase","Family","Butyryl-CoA:acetate CoA-transferase","-"]
[null,"IPR003702","PFAM","PF02550","AcetylCoA_hydro",5,182,0.396861,{"v":4.4e-20,"d":"4.40E-20"},"ActCoA_hydro","Family","Acetyl-CoA hydrolase/transferase","Molecular Function: catalytic activity (GO:0003824); Biological Process: acetyl-CoA metabolic process (GO:0006084)"]
[null,"_","_","G3DSA:3.30.750.70","_",191,294,0.230942,{"v":4.5e-33,"d":"4.50E-33"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.1080.10","_",2,185,0.410314,{"v":7.8e-58,"d":"7.80E-58"},"_","_","_","-"]
[null,"_","_","PTHR21432","_",4,437,0.970852,{"v":2.7e-106,"d":"2.70E-106"},"_","_","_","-"]
[]
["AEQN01_210004","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",1,114,0.297368,{"v":5.8e-29,"d":"5.80E-29"},"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",226,379,0.402632,{"v":4.35e-57,"d":"4.35E-57"},"AcylCo_DH-like_C","Homologous_superfamily","Acyl-CoA dehydrogenase-like, C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR013786","PFAM","PF02771","Acyl-CoA_dh_N",6,114,0.284211,{"v":1.1E-22,"d":"1.10E-22"},"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",4,240,0.621053,{"v":9.42e-75,"d":"9.42E-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",228,373,0.381579,{"v":3.9e-49,"d":"3.90E-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",120,216,0.252632,{"v":2.3e-25,"d":"2.30E-25"},"Acyl-CoA_Oxase/DH_cen-dom","Domain","Acyl-CoA oxidase/dehydrogenase, central domain","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00072","ACYL_COA_DH_1",122,134,0.0315789,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00073","ACYL_COA_DH_2",335,354,0.05,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PIRSF016578","_",4,366,0.952632,1.9e-15,"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",119,233,0.3,{"v":2.9e-44,"d":"2.90E-44"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",234,379,0.381579,{"v":2.9e-54,"d":"2.90E-54"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",3,377,0.984211,{"v":9.9e-133,"d":"9.90E-133"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",3,377,0.984211,{"v":9.9e-133,"d":"9.90E-133"},"_","_","_","-"]
[]
["AEQN01_220142","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",1,118,0.307087,{"v":2.5E-36,"d":"2.50E-36"},"AcylCoA_DH/ox_N_sf","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR036250","SSF","SSF47203","SSF47203",227,378,0.396325,{"v":9.99e-57,"d":"9.99E-57"},"AcylCo_DH-like_C","Homologous_superfamily","Acyl-CoA dehydrogenase-like, C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR013786","PFAM","PF02771","Acyl-CoA_dh_N",6,116,0.288714,{"v":6.4e-31,"d":"6.40E-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",3,242,0.627297,{"v":1.7E-76,"d":"1.70E-76"},"AcylCoA_DH/oxidase_NM_dom","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR009075","PFAM","PF00441","Acyl-CoA_dh_1",229,377,0.388451,{"v":6E-51,"d":"6.00E-51"},"AcylCo_DH/oxidase_C","Domain","Acyl-CoA dehydrogenase/oxidase C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006091","PFAM","PF02770","Acyl-CoA_dh_M",120,217,0.254593,{"v":1.3E-25,"d":"1.30E-25"},"Acyl-CoA_Oxase/DH_cen-dom","Domain","Acyl-CoA oxidase/dehydrogenase, central domain","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00072","ACYL_COA_DH_1",122,134,0.0314961,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00073","ACYL_COA_DH_2",336,355,0.0498688,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","PIRSF016578","_",2,379,0.989501,{"v":1.2E-23,"d":"1.20E-23"},"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",119,236,0.307087,{"v":2.2E-43,"d":"2.20E-43"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",237,380,0.375328,{"v":4.7e-54,"d":"4.70E-54"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",2,378,0.986877,{"v":4e-138,"d":"4.00E-138"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF12","_",2,378,0.986877,{"v":4e-138,"d":"4.00E-138"},"_","_","_","-"]
[]
["AEQN01_250027","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",1,118,0.305483,{"v":9.7e-30,"d":"9.70E-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",226,381,0.4047,2.58E-53,"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",7,117,0.287206,{"v":4.2e-23,"d":"4.20E-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",2,239,0.618799,{"v":7.59e-77,"d":"7.59E-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",228,377,0.389034,{"v":1.2e-45,"d":"1.20E-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",121,216,0.248042,{"v":2.8E-27,"d":"2.80E-27"},"Acyl-CoA_Oxase/DH_cen-dom","Domain","Acyl-CoA oxidase/dehydrogenase, central domain","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00072","ACYL_COA_DH_1",123,135,0.0313316,"_","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",336,355,0.0496084,"_","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","_",2,91,0.232376,0.00067,"_","_","_","-"]
[null,"_","_","PIRSF016578","_",126,227,0.263708,0.00046,"_","_","_","-"]
[null,"_","_","PIRSF016578","_",243,382,0.362924,8.5e-10,"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",120,233,0.295039,{"v":4.3e-46,"d":"4.30E-46"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",234,382,0.386423,{"v":2.8e-52,"d":"2.80E-52"},"_","_","_","-"]
[null,"_","_","PTHR43516","_",4,382,0.986945,{"v":2e-127,"d":"2.00E-127"},"_","_","_","-"]
[null,"_","_","PTHR43516:SF5","_",4,382,0.986945,{"v":2e-127,"d":"2.00E-127"},"_","_","_","-"]
[]
["AEQN01_230141","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",1,120,0.186228,{"v":6.1e-41,"d":"6.10E-41"},"AcylCoA_DH/ox_N_sf","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR036250","SSF","SSF47203","SSF47203",227,380,0.239437,{"v":9.99e-57,"d":"9.99E-57"},"AcylCo_DH-like_C","Homologous_superfamily","Acyl-CoA dehydrogenase-like, C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR029035","SSF","SSF52467","SSF52467",441,561,0.187793,{"v":7.94e-37,"d":"7.94E-37"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR024935","CDD","cd00730","rubredoxin",590,639,0.0766823,{"v":2.32119E-16,"d":"2.32E-16"},"Rubredoxin_dom","Domain","Rubredoxin domain","Molecular Function: iron ion binding (GO:0005506)"]
[null,"IPR024935","PFAM","PF00301","Rubredoxin",590,636,0.0719875,{"v":5.7e-17,"d":"5.70E-17"},"Rubredoxin_dom","Domain","Rubredoxin domain","Molecular Function: iron ion binding (GO:0005506)"]
[null,"IPR024935","PRINTS","PR00163","RUBREDOXIN",590,606,0.0250391,2.8e-06,"Rubredoxin_dom","Domain","Rubredoxin domain","Molecular Function: iron ion binding (GO:0005506)"]
[null,"IPR024935","PRINTS","PR00163","RUBREDOXIN",620,636,0.0250391,2.8e-06,"Rubredoxin_dom","Domain","Rubredoxin domain","Molecular Function: iron ion binding (GO:0005506)"]
[null,"IPR024934","PROFILE","PS50903","RUBREDOXIN_LIKE",588,639,0.0798122,12.183,"Rubredoxin-like_dom","Domain","Rubredoxin-like domain","Molecular Function: iron ion binding (GO:0005506)"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",443,524,0.126761,{"v":4.1e-25,"d":"4.10E-25"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR013786","PFAM","PF02771","Acyl-CoA_dh_N",6,117,0.173709,{"v":2.1e-37,"d":"2.10E-37"},"AcylCoA_DH/ox_N","Domain","Acyl-CoA dehydrogenase/oxidase, N-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Molecular Function: flavin adenine dinucleotide binding (GO:0050660); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR009100","SSF","SSF56645","SSF56645",3,242,0.374022,{"v":2.23e-87,"d":"2.23E-87"},"AcylCoA_DH/oxidase_NM_dom","Homologous_superfamily","Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR009075","PFAM","PF00441","Acyl-CoA_dh_1",229,376,0.230047,{"v":3.3E-48,"d":"3.30E-48"},"AcylCo_DH/oxidase_C","Domain","Acyl-CoA dehydrogenase/oxidase C-terminal","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006091","PFAM","PF02770","Acyl-CoA_dh_M",122,217,0.14867,{"v":3e-25,"d":"3.00E-25"},"Acyl-CoA_Oxase/DH_cen-dom","Domain","Acyl-CoA oxidase/dehydrogenase, central domain","Molecular Function: oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"IPR006089","PROSITE","PS00072","ACYL_COA_DH_1",124,136,0.0187793,"_","Acyl-CoA_DH_CS","Conserved_site","Acyl-CoA dehydrogenase, conserved site","Molecular Function: acyl-CoA dehydrogenase activity (GO:0003995); Biological Process: oxidation-reduction process (GO:0055114)"]
[null,"_","_","SSF57802","_",590,638,0.0751174,{"v":3.7E-16,"d":"3.70E-16"},"_","_","_","-"]
[null,"_","_","G3DSA:2.20.28.10","_",588,639,0.0798122,{"v":1.6E-18,"d":"1.60E-18"},"_","_","_","-"]
[null,"_","_","G3DSA:2.40.110.10","_",121,234,0.176839,{"v":5.7e-42,"d":"5.70E-42"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1220","_",438,570,0.206573,{"v":1e-43,"d":"1.00E-43"},"_","_","_","-"]
[null,"_","_","G3DSA:1.20.140.10","_",235,383,0.231612,{"v":1E-53,"d":"1.00E-53"},"_","_","_","-"]
[null,"_","_","PTHR43884","_",2,567,0.884194,{"v":3.6e-210,"d":"3.60E-210"},"_","_","_","-"]
[null,"_","_","PTHR43884:SF25","_",2,567,0.884194,{"v":3.6e-210,"d":"3.60E-210"},"_","_","_","-"]
[null,"_","_","cd01158","_",7,379,0.58216,0,"_","_","_","-"]
[]
["AEQN01_220164","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",2,209,0.778196,{"v":4.64915e-88,"d":"4.65E-88"},"ETF_beta_N","Domain","Electron transfer flavoprotein, beta subunit, N-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",24,212,0.706767,{"v":1.1E-42,"d":"1.10E-42"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",22,217,0.733083,{"v":7e-53,"d":"7.00E-53"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014729","CATHGENE3D","G3DSA:3.40.50.620","G3DSA:3.40.50.620",1,266,0.996241,{"v":8.3e-92,"d":"8.30E-92"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR012255","PANTHER","PTHR21294","PTHR21294",1,265,0.992481,{"v":1.2e-89,"d":"1.20E-89"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"IPR012255","PIRSF","PIRSF000090","Beta-ETF",1,266,0.996241,{"v":6.6e-87,"d":"6.60E-87"},"ETF_b","Family","Electron transfer flavoprotein, beta subunit","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"IPR000049","PROSITE","PS01065","ETF_BETA",161,181,0.075188,"_","ET-Flavoprotein_bsu_CS","Conserved_site","Electron transfer flavoprotein, beta-subunit, conserved site","Molecular Function: electron transfer activity (GO:0009055)"]
[null,"_","_","SSF52402","_",1,261,0.977444,{"v":7.67e-76,"d":"7.67E-76"},"_","_","_","-"]
[null,"_","_","PTHR21294:SF17","_",1,265,0.992481,{"v":1.2e-89,"d":"1.20E-89"},"_","_","_","-"]
[]
["AEQN01_220165","IP id","Method","Method id","Method Name","Begin","End","maxLrap","Eval/Score","IP name","IP type","IP Description","Gene Ontology"]
[null,"IPR033947","CDD","cd01715","ETF_alpha",9,186,0.528358,{"v":2.30088e-47,"d":"2.30E-47"},"ETF_alpha_N","Domain","Electron transfer flavoprotein, alpha subunit, N-terminal","-"]
[null,"IPR029035","SSF","SSF52467","SSF52467",208,330,0.364179,{"v":5.09e-48,"d":"5.09E-48"},"DHS-like_NAD/FAD-binding_dom","Homologous_superfamily","DHS-like NAD/FAD-binding domain superfamily","-"]
[null,"IPR018206","PROSITE","PS00696","ETF_ALPHA",274,300,0.0776119,"_","ETF_asu_C_CS","Conserved_site","Electron transfer flavoprotein subunit alpha, conserved site","-"]
[null,"IPR014731","PFAM","PF00766","ETF_alpha",210,293,0.247761,{"v":1e-34,"d":"1.00E-34"},"ETF_asu_C","Domain","Electron transfer flavoprotein, alpha subunit, C-terminal","-"]
[null,"IPR014730","PFAM","PF01012","ETF",9,187,0.531343,{"v":3.8e-46,"d":"3.80E-46"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014730","SMART","SM00893","ETF",8,198,0.567164,{"v":2.9E-46,"d":"2.90E-46"},"ETF_a/b_N","Domain","Electron transfer flavoprotein, alpha/beta-subunit, N-terminal","-"]
[null,"IPR014729","CATHGENE3D","G3DSA:3.40.50.620","G3DSA:3.40.50.620",4,206,0.602985,{"v":5.4e-73,"d":"5.40E-73"},"Rossmann-like_a/b/a_fold","Homologous_superfamily","Rossmann-like alpha/beta/alpha sandwich fold","-"]
[null,"IPR001308","PIRSF","PIRSF000089","Electra_flavoP_a",4,335,0.98806,{"v":9.2e-117,"d":"9.20E-117"},"ETF_a/FixB","Family","Electron transfer flavoprotein alpha subunit/FixB","Molecular Function: electron transfer activity (GO:0009055); Molecular Function: flavin adenine dinucleotide binding (GO:0050660)"]
[null,"_","_","SSF52402","_",7,188,0.540299,{"v":7.67e-50,"d":"7.67E-50"},"_","_","_","-"]
[null,"_","_","G3DSA:3.40.50.1220","_",207,335,0.38209,{"v":1.2E-56,"d":"1.20E-56"},"_","_","_","-"]
[null,"_","_","PTHR43153","_",3,334,0.98806,{"v":2.5e-131,"d":"2.50E-131"},"_","_","_","-"]
[null,"_","_","PTHR43153:SF9","_",3,334,0.98806,{"v":2.5e-131,"d":"2.50E-131"},"_","_","_","-"]

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

{"sheet":"PSortB","index":14,"n_rows":17,"n_cols":4,"rows_kept":17}
["CDS","PsortB Localization","Score","Gram"]
["AEQN01_210010","Cytoplasmic",7.5,"+"]
["AEQN01_210007","CytoplasmicMembrane",10,"+"]
["AEQN01_180010","Cytoplasmic",9.97,"+"]
["AEQN01_90013","Unknown",2.5,"+"]
["AEQN01_230157","Unknown",2.5,"+"]
["AEQN01_220120","Cytoplasmic",7.5,"+"]
["AEQN01_220121","Cytoplasmic",7.5,"+"]
["AEQN01_220122","Cytoplasmic",9.97,"+"]
["AEQN01_70057","Cytoplasmic",7.5,"+"]
["AEQN01_300005","Cytoplasmic",7.5,"+"]
["AEQN01_210004","Cytoplasmic",9.97,"+"]
["AEQN01_220142","Cytoplasmic",9.97,"+"]
["AEQN01_250027","Cytoplasmic",9.97,"+"]
["AEQN01_230141","Cytoplasmic",9.97,"+"]
["AEQN01_220164","Cytoplasmic",7.5,"+"]
["AEQN01_220165","Cytoplasmic",7.5,"+"]