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guaC guaC aceE aceE aceF aceF tauD tauD ahpF ahpF sdhC sdhC sucA sucA sucB sucB dmsA dmsA dmsB dmsB ssuD ssuD ssuE ssuE hyaA hyaA rutA rutA efeU efeU ndh ndh narG narG narH narH narI narI narV narV narY narY narZ narZ fdnI fdnI ynfF ynfF ynfG ynfG gdhA gdhA yeiT yeiT nrdA nrdA nrdB nrdB glpA glpA nuoF nuoF nuoE nuoE nuoC nuoC hyfG hyfG hyfI hyfI hcaE hcaE hcaF hcaF hcaC hcaC hcaD hcaD nrdE nrdE nrdF nrdF hycG hycG hycE hycE hycB hycB xdhA xdhA xdhB xdhB xdhC xdhC gcvP gcvP gcvH gcvH gcvT gcvT glcD glcD hybO hybO gltB gltB gltD gltD glpD glpD gpsA gpsA fdoI fdoI fdhF fdhF
Nodes:
Network nodes represent proteins
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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
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)
tauDTaurine dioxygenase, 2-oxoglutarate-dependent; Function experimentally demonstrated in the studied species; enzyme. (283 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)
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)
dmsADimethyl sulfoxide reductase, anaerobic, subunit A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (814 aa)
dmsBDimethyl sulfoxide reductase, anaerobic, subunit B; Function experimentally demonstrated in the studied species; enzyme. (205 aa)
ssuDAlkanesulfonate monooxygenase, FMNH(2)-dependent; Catalyzes the desulfonation of aliphatic sulfonates. Belongs to the SsuD family. (381 aa)
ssuENAD(P)H-dependent FMN reductase; Function experimentally demonstrated in the studied species; enzyme. (191 aa)
hyaAHydrogenase 1, small subunit; Function experimentally demonstrated in the studied species; enzyme. (372 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. (382 aa)
efeUFerrous iron permease; Function of homologous gene experimentally demonstrated in an other organism; transporter. (279 aa)
ndhRespiratory NADH dehydrogenase 2/cupric reductase; Function experimentally demonstrated in the studied species; enzyme. (434 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)
narVNitrate reductase 2 (NRZ), gamma subunit; Function experimentally demonstrated in the studied species; enzyme. (226 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)
fdnIFormate dehydrogenase-N, cytochrome B556 (gamma) subunit, nitrate-inducible; Function experimentally demonstrated in the studied species; carrier. (217 aa)
ynfFOxidoreductase subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (807 aa)
ynfGOxidoreductase, Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (205 aa)
gdhAGlutamate dehydrogenase, NADP-specific; Function experimentally demonstrated in the studied species; enzyme; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. (447 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)
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)
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)
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)
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)
hycBHydrogenase 3, Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (203 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)
glcDGlycolate oxidase subunit, FAD-linked; Function experimentally demonstrated in the studied species; enzyme. (499 aa)
hybOHydrogenase 2, small subunit; Function experimentally demonstrated in the studied species; enzyme. (372 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)
gpsAGlycerol-3-phosphate dehydrogenase (NAD+); Function experimentally demonstrated in the studied species; enzyme; Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family. (339 aa)
fdoIFormate dehydrogenase-O, cytochrome b556 subunit; Function experimentally demonstrated in the studied species; carrier. (211 aa)
fdhFFormate dehydrogenase-H, selenopolypeptide subunit; Function experimentally demonstrated in the studied genus; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (715 aa)
Your Current Organism:
Escherichia coli UMN026
NCBI taxonomy Id: 585056
Other names: E. coli UMN026
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