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napA napA pflA pflA hyaA hyaA ydeM ydeM nuoF nuoF nuoB nuoB ispG ispG yfgB yfgB cysI cysI ygcF ygcF aslB aslB ilvD ilvD fdoG fdoG fdoH fdoH fdnH fdnH fdnG fdnG hemN hemN rumA rumA sdaB sdaB yggW yggW hybO hybO ygiQ ygiQ tdcG tdcG nirB nirB gntY gntY cutD cutD thiH thiH thiC thiC fdhF fdhF phnJ phnJ fumB fumB yjeK yjeK frdB frdB yjeS yjeS narZ narZ ydbK ydbK ydaO ydaO acnA acnA narG narG ynfE ynfE ynfF ynfF fumA fumA rsxB rsxB rsxC rsxC nth nth sdaA sdaA edd edd rumB rumB yliG yliG dinG dinG moaA moaA bioB bioB nadA nadA CAR16834.1 CAR16834.1 sdhB sdhB miaB miaB lipA lipA acnB acnB leuC leuC ispH ispH nuoG nuoG nuoI nuoI dmsA dmsA
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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napANitrate reductase, periplasmic, large subunit; Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite. (828 aa)
pflAPyruvate formate lyase activating enzyme 1; Activation of pyruvate formate-lyase under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine; Belongs to the organic radical-activating enzymes family. (246 aa)
hyaAHydrogenase 1, small subunit; Function experimentally demonstrated in the studied species; enzyme. (372 aa)
ydeMConserved hypothetical protein; Homologs of previously reported genes of unknown function; putative regulator. (385 aa)
nuoFNADH:ubiquinone oxidoreductase, chain F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. (445 aa)
nuoBNADH:ubiquinone oxidoreductase, chain B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (220 aa)
ispG1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family. (372 aa)
yfgBPutative Fe-S containing enzyme; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. (384 aa)
cysISulfite reductase, beta subunit, NAD(P)-binding, heme-binding; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. (570 aa)
ygcFConserved hypothetical protein; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. (223 aa)
aslBRegulator of arylsulfatase activity; Function of homologous gene experimentally demonstrated in an other organism; putative regulator. (411 aa)
ilvDDihydroxyacid dehydratase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the IlvD/Edd family. (616 aa)
fdoGFormate dehydrogenase-O, large subunit; Function experimentally demonstrated in the studied genus; enzyme. (1016 aa)
fdoHFormate dehydrogenase-O, Fe-S subunit; The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers. (300 aa)
fdnHFormate dehydrogenase-N, Fe-S (beta) subunit, nitrate-inducible; The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers. (294 aa)
fdnGFormate dehydrogenase-N, alpha subunit, nitrate-inducible; Function experimentally demonstrated in the studied genus; enzyme. (1015 aa)
hemNCoproporphyrinogen III oxidase, SAM and NAD(P)H dependent, oxygen-independent; Function experimentally demonstrated in the studied species; enzyme; Belongs to the anaerobic coproporphyrinogen-III oxidase family. (457 aa)
rumA23S rRNA (uracil-5)-methyltransferase; Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA; Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmD subfamily. (433 aa)
sdaBL-serine deaminase II; Function experimentally demonstrated in the studied species; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. (455 aa)
yggWPutative oxidoreductase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. (378 aa)
hybOHydrogenase 2, small subunit; Function experimentally demonstrated in the studied species; enzyme. (372 aa)
ygiQConserved hypothetical protein; Homologs of previously reported genes of unknown function. (739 aa)
tdcGL-serine dehydratase 3; Function experimentally demonstrated in the studied species; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. (454 aa)
nirBNitrite reductase, large subunit, NAD(P) H-binding; Function experimentally demonstrated in the studied species; enzyme; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. (847 aa)
gntYPutative gluconate transport associated protein; Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. (191 aa)
cutDPutative pyruvate formate-lyase activating enzyme; Catalyzes activation of the choline trimethylamine-lyase CutC under anaerobic conditions by generation of an organic free radical on a glycine residue, via an homolytic cleavage of S-adenosyl-L-methionine (SAM). (315 aa)
thiHThiamin biosynthesis ThiGH complex subunit; Function experimentally demonstrated in the studied species; enzyme. (377 aa)
thiCThiamin (pyrimidine moiety) biosynthesis protein; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. (631 aa)
fdhFFormate dehydrogenase-H, selenopolypeptide subunit; Function experimentally demonstrated in the studied genus; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (715 aa)
phnJCarbon-phosphorus lyase complex subunit; Catalyzes the breakage of the C-P bond in alpha-D-ribose 1- methylphosphonate 5-phosphate (PRPn) forming alpha-D-ribose. Belongs to the PhnJ family. (281 aa)
fumBAnaerobic class I fumarate hydratase (fumarase B); Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. (548 aa)
yjeKPutative lysine aminomutase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (342 aa)
frdBFumarate reductase (anaerobic), Fe-S subunit; Function experimentally demonstrated in the studied species; carrier; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (244 aa)
yjeSPutative Fe-S electron transport protein; Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr); Belongs to the QueG family. (379 aa)
narZNitrate reductase 2 (NRZ), alpha subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1246 aa)
ydbKPutative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (1174 aa)
ydaOPutative C32 tRNA thiolase; Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. (311 aa)
acnAAconitate hydratase 1; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate. (891 aa)
narGNitrate reductase 1, alpha subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1247 aa)
ynfEOxidoreductase subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (808 aa)
ynfFOxidoreductase subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (807 aa)
fumAFumarate hydratase (fumarase A), aerobic Class I; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. (548 aa)
rsxBPutative iron-sulfur protein; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR; Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily. (192 aa)
rsxCPutative 4Fe-4S ferredoxin-type protein fused with unknown protein; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR; Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC subfamily. (740 aa)
nthDNA glycosylase and apyrimidinic (AP) lyase (endonuclease III); DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. (211 aa)
sdaAL-serine deaminase I; Function experimentally demonstrated in the studied species; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. (454 aa)
edd6-phosphogluconate dehydratase; Catalyzes the dehydration of 6-phospho-D-gluconate to 2- dehydro-3-deoxy-6-phospho-D-gluconate; Belongs to the IlvD/Edd family. (603 aa)
rumB23S rRNA m(5)U747 methyltransferase; Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA; Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmC subfamily. (375 aa)
yliGPutative AdoMet-dependent methyltransferase, UPF0004 family; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. (441 aa)
dinGATP-dependent DNA helicase; DNA-dependent ATPase and 5'-3' DNA helicase. (716 aa)
moaAMolybdopterin biosynthesis protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. (329 aa)
bioBBiotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family. (346 aa)
nadAQuinolinate synthase, subunit A; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate; Belongs to the quinolinate synthase A family. Type 1 subfamily. (347 aa)
CAR16834.1Fumarate hydratase class I, beta subunit, aerobic (Fumarase); Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. (550 aa)
sdhBSuccinate dehydrogenase, FeS subunit; Function experimentally demonstrated in the studied species; carrier; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (238 aa)
miaBIsopentenyl-adenosine A37 tRNA methylthiolase; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. (474 aa)
lipALipoate synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. (321 aa)
acnBBifunctional aconitate hydratase 2 and 2-methylisocitrate dehydratase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the aconitase/IPM isomerase family. (865 aa)
leuC3-isopropylmalate isomerase subunit, dehydratase component; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (466 aa)
ispH1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase, 4Fe-4S protein; Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. (316 aa)
nuoGNADH:ubiquinone oxidoreductase, chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. (910 aa)
nuoINADH:ubiquinone oxidoreductase, chain I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (180 aa)
dmsADimethyl sulfoxide reductase, anaerobic, subunit A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (814 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
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