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ydeP ydeP ndh ndh efeO efeO efeU efeU rutA rutA torA torA torC torC ssuE ssuE ssuD ssuD dmsC dmsC dmsB dmsB dmsA dmsA trxB trxB yeiT yeiT yeiA yeiA nrdA nrdA nrdB nrdB glpA glpA glpB glpB nuoN nuoN nuoM nuoM nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoE nuoE nuoC nuoC nuoB nuoB nuoA nuoA hyfD hyfD hyfF hyfF hyfG hyfG hyfI hyfI hcaE hcaE hcaF hcaF hcaC hcaC hcaD hcaD yfhL yfhL nrdE nrdE nrdF nrdF hycG hycG hycE hycE ygcU ygcU fdoG fdoG fdoH fdoH fdoI fdoI xdhA xdhA xdhB xdhB xdhC xdhC gcvP gcvP gcvH gcvH gcvT gcvT glcE glcE glcD glcD gltB gltB gltD gltD glpD glpD guaC guaC aceE aceE aceF aceF lpd lpd folK folK cyoC cyoC cyoD cyoD tauD tauD ykgC ykgC ahpC ahpC ahpF ahpF sdhC sdhC sdhA sdhA sucA sucA sucB sucB hcr hcr gdhA gdhA ynfH ynfH ynfG ynfG ynfE ynfE narG narG narH narH narI narI ydbK ydbK narY narY narZ narZ fdnG fdnG fdnH fdnH fdnI fdnI
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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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
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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ydePPutative oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (759 aa)
ndhRespiratory NADH dehydrogenase 2/cupric reductase; Function experimentally demonstrated in the studied species; enzyme. (434 aa)
efeOFerrous iron transport binding protein; Function experimentally demonstrated in the studied species; transporter. (375 aa)
efeUFerrous iron permease; Function of homologous gene experimentally demonstrated in an other organism; transporter. (279 aa)
rutAMonooxygenase of the alternative pyrimidine degradation pathway; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily. (331 aa)
torATrimethylamine N-oxide (TMAO) reductase I, catalytic subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (848 aa)
torCTrimethylamine N-oxide (TMAO) reductase I, cytochrome c-type subunit; Function experimentally demonstrated in the studied species; carrier; Belongs to the TorC/TorY family. (390 aa)
ssuENAD(P)H-dependent FMN reductase; Function experimentally demonstrated in the studied species; enzyme. (191 aa)
ssuDAlkanesulfonate monooxygenase, FMNH(2)-dependent; Catalyzes the desulfonation of aliphatic sulfonates. Belongs to the SsuD family. (381 aa)
dmsCDimethyl sulfoxide reductase, anaerobic, subunit C; Function experimentally demonstrated in the studied species; enzyme. (287 aa)
dmsBDimethyl sulfoxide reductase, anaerobic, subunit B; Function experimentally demonstrated in the studied species; enzyme. (205 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)
trxBThioredoxin reductase, FAD/NAD(P)-binding; Function experimentally demonstrated in the studied species; enzyme. (321 aa)
yeiTPutative Fe-S cluster containing oxidoreductase subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (412 aa)
yeiAPutative oxidoreductase subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (411 aa)
nrdARibonucleoside diphosphate reductase 1, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. (761 aa)
nrdBRibonucleoside diphosphate reductase 1, beta subunit, ferritin-like; Function experimentally demonstrated in the studied species; carrier. (376 aa)
glpASn-glycerol-3-phosphate dehydrogenase (anaerobic), large subunit, FAD/NAD(P)-binding; Function experimentally demonstrated in the studied species; enzyme; Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family. (542 aa)
glpBSn-glycerol-3-phosphate dehydrogenase (anaerobic), membrane anchor subunit; Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor. (419 aa)
nuoNNADH:ubiquinone oxidoreductase, membrane subunit N; 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; Belongs to the complex I subunit 2 family. (485 aa)
nuoMNADH:ubiquinone oxidoreductase, membrane subunit M; Function experimentally demonstrated in the studied species; membrane component. (509 aa)
nuoLNADH:ubiquinone oxidoreductase, membrane subunit L; Function experimentally demonstrated in the studied species; membrane component. (613 aa)
nuoKNADH:ubiquinone oxidoreductase, membrane subunit K; 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; Belongs to the complex I subunit 4L family. (100 aa)
nuoJNADH:ubiquinone oxidoreductase, membrane subunit J; 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. (184 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)
nuoHNADH:ubiquinone oxidoreductase, membrane subunit H; 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. This subunit may bind ubiquinone. (325 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)
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)
nuoENADH:ubiquinone oxidoreductase, chain E; Function experimentally demonstrated in the studied species; carrier. (166 aa)
nuoCNADH:ubiquinone oxidoreductase, chain C,D; 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family. (600 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)
nuoANADH:ubiquinone oxidoreductase, membrane subunit A; 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; Belongs to the complex I subunit 3 family. (147 aa)
hyfDHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (479 aa)
hyfFHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (526 aa)
hyfGHydrogenase 4, subunit; Function experimentally demonstrated in the studied species; carrier. (555 aa)
hyfIHydrogenase 4, Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (252 aa)
hcaE3-phenylpropionate dioxygenase, large (alpha) subunit; Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3- phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid- dihydrodiol (CI-dihydrodiol), respectively; Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family. (453 aa)
hcaF3-phenylpropionate dioxygenase, small (beta) subunit; Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3- phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid- dihydrodiol (CI-dihydrodiol), respectively. (172 aa)
hcaC3-phenylpropionate dioxygenase, putative ferredoxin subunit; Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid- dihydrodiol (CI-dihydrodiol), respectively. This protein seems to be a 2Fe-2S ferredoxin. (106 aa)
hcaDPhenylpropionate dioxygenase, ferredoxin reductase subunit; Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid- dihydrodiol (CI-dihydrodiol), respectively. (400 aa)
yfhLFerredoxin (4Fe-4S cluster-containing protein) (fdx-like); Function of strongly homologous gene; carrier. (86 aa)
nrdERibonucleoside-diphosphate reductase 2, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. (714 aa)
nrdFRibonucleoside-diphosphate reductase 2, beta subunit, ferritin-like; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides; Belongs to the ribonucleoside diphosphate reductase small chain family. (319 aa)
hycGHydrogenase 3 and formate hydrogenase complex, HycG subunit; Function experimentally demonstrated in the studied species; enzyme. (255 aa)
hycEHydrogenase 3, large subunit; Function experimentally demonstrated in the studied species; enzyme. (569 aa)
ygcUPutative FAD containing dehydrogenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (484 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)
fdoIFormate dehydrogenase-O, cytochrome b556 subunit; Function experimentally demonstrated in the studied species; carrier. (211 aa)
xdhAXanthine dehydrogenase, molybdenum binding subunit; Function experimentally demonstrated in the studied species; enzyme. (752 aa)
xdhBXanthine dehydrogenase, FAD-binding subunit; Function experimentally demonstrated in the studied species; enzyme. (292 aa)
xdhCXanthine dehydrogenase, Fe-S binding subunit; Function experimentally demonstrated in the studied species; carrier. (159 aa)
gcvPGlycine decarboxylase, PLP-dependent, subunit (protein P) of glycine cleavage complex; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. (957 aa)
gcvHGlycine cleavage complex lipoylprotein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. (129 aa)
gcvTAminomethyltransferase, tetrahydrofolate-dependent, subunit (T protein) of glycine cleavage complex; The glycine cleavage system catalyzes the degradation of glycine. (364 aa)
glcEGlycolate oxidase FAD binding subunit; Function experimentally demonstrated in the studied species; enzyme. (350 aa)
glcDGlycolate oxidase subunit, FAD-linked; Function experimentally demonstrated in the studied species; enzyme. (499 aa)
gltBGlutamate synthase, large subunit; Function experimentally demonstrated in the studied species; enzyme. (1517 aa)
gltDGlutamate synthase, 4Fe-4S protein, small subunit; Function experimentally demonstrated in the studied species; carrier. (472 aa)
glpDSn-glycerol-3-phosphate dehydrogenase, aerobic, FAD/NAD(P)-binding; Function experimentally demonstrated in the studied species; enzyme; Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family. (501 aa)
guaCGMP reductase; Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. (347 aa)
aceEPyruvate dehydrogenase, decarboxylase component E1, thiamin-binding; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (887 aa)
aceFPyruvate dehydrogenase, dihydrolipoyltransacetylase component E2; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). (630 aa)
lpdLipoamide dehydrogenase, E3 component is part of three enzyme complexes; Function experimentally demonstrated in the studied species; enzyme. (474 aa)
folK2-amino-4-hydroxy-6-hydroxymethyldihyropteridine pyrophosphokinase; Function experimentally demonstrated in the studied species; enzyme. (159 aa)
cyoCCytochrome o ubiquinol oxidase subunit III; Function experimentally demonstrated in the studied species; carrier. (204 aa)
cyoDCytochrome o ubiquinol oxidase subunit IV; Function experimentally demonstrated in the studied species; carrier. (109 aa)
tauDTaurine dioxygenase, 2-oxoglutarate-dependent; Function of strongly homologous gene; enzyme. (375 aa)
ykgCPutative pyridine nucleotide-disulfide oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (441 aa)
ahpCAlkyl hydroperoxide reductase, C22 subunit; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. (187 aa)
ahpFAlkyl hydroperoxide reductase, F52a subunit, FAD/NAD(P)-binding; Function experimentally demonstrated in the studied species; enzyme. (521 aa)
sdhCSuccinate dehydrogenase, membrane subunit, binds cytochrome b556; Function experimentally demonstrated in the studied species; membrane component. (129 aa)
sdhASuccinate dehydrogenase, flavoprotein subunit; Function experimentally demonstrated in the studied species; carrier; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (588 aa)
sucA2-oxoglutarate decarboxylase, thiamin-requiring; Function experimentally demonstrated in the studied species; enzyme. (933 aa)
sucBDihydrolipoyltranssuccinase; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). (405 aa)
hcrHCP oxidoreductase, NADH-dependent; Function experimentally demonstrated in the studied species; enzyme. (322 aa)
gdhAGlutamate dehydrogenase, NADP-specific; Function experimentally demonstrated in the studied species; enzyme; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. (447 aa)
ynfHOxidoreductase, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (284 aa)
ynfGOxidoreductase, Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (205 aa)
ynfEOxidoreductase subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (808 aa)
narGNitrate reductase 1, alpha subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1247 aa)
narHNitrate reductase 1, beta (Fe-S) subunit; Function experimentally demonstrated in the studied species; carrier. (512 aa)
narINitrate reductase 1, gamma (cytochrome b(NR)) subunit; Function experimentally demonstrated in the studied species; carrier. (225 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)
narYNitrate reductase 2 (NRZ), beta subunit; Function experimentally demonstrated in the studied species; carrier. (514 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)
fdnGFormate dehydrogenase-N, alpha subunit, nitrate-inducible; Function experimentally demonstrated in the studied genus; enzyme. (1015 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)
fdnIFormate dehydrogenase-N, cytochrome B556 (gamma) subunit, nitrate-inducible; Function experimentally demonstrated in the studied species; carrier. (217 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
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