STRINGSTRING
appC appC yjjI yjjI frdA frdA frdB frdB frdC frdC aspA aspA nrfC nrfC nrfB nrfB nrfA nrfA aceK aceK aceA aceA aceB aceB ppc ppc fdoG fdoG fdoH fdoH fdoI fdoI ubiE ubiE bisC bisC mdh mdh hybO hybO hybA hybA hybB hybB hybC hybC glcB glcB sdhB sdhB sdhA sdhA sdhD sdhD sdhC sdhC gltA gltA ylbE ylbE fdrA fdrA cyoB cyoB cyoC cyoC prpD prpD hycB hycB hycC hycC hycD hycD hycE hycE hycF hycF yfjG yfjG hyfH hyfH hyfG hyfG hyfF hyfF hyfE hyfE hyfD hyfD hyfC hyfC hyfB hyfB nuoC nuoC nuoE nuoE nuoG nuoG nuoH nuoH nuoI nuoI nuoK nuoK nuoL nuoL nuoM nuoM ynfF ynfF ynfE ynfE fdnI fdnI fdnH fdnH fdnG fdnG cybB cybB acnA acnA icd icd yceJ yceJ torA torA torC torC torT torT appB appB hyaC hyaC fumA fumA ydhU ydhU ydhX ydhX ydhY ydhY torZ torZ torY torY yodB yodB dld dld nuoN nuoN napC napC napB napB napG napG mqo mqo glpC glpC prpC prpC yahG yahG yahF yahF ykgE ykgE acnB acnB fumC fumC ynfH ynfH ynfG ynfG sucA sucA sucB sucB sucC sucC sucD sucD cydA cydA cydB cydB ybhJ ybhJ dmsA dmsA dmsB dmsB dmsC dmsC hyaA hyaA hyaB hyaB
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:
appCCytochrome bd-II oxidase, subunit I; Function experimentally demonstrated in the studied species; carrier. (514 aa)
yjjIConserved hypothetical protein; Homologs of previously reported genes of unknown function. (516 aa)
frdAFumarate reductase (anaerobic) catalytic and NAD/flavoprotein subunit; Function experimentally demonstrated in the studied species; enzyme. (602 aa)
frdBFumarate reductase (anaerobic), Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (244 aa)
frdCFumarate reductase (anaerobic), membrane anchor subunit; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. (131 aa)
aspAAspartate ammonia-lyase; Function experimentally demonstrated in the studied species; enzyme. (478 aa)
nrfCFormate-dependent nitrite reductase, 4Fe4S subunit; Function experimentally demonstrated in the studied species; carrier. (223 aa)
nrfBNitrite reductase, formate-dependent, penta-heme cytochrome c; Function experimentally demonstrated in the studied species; carrier. (188 aa)
nrfANitrite reductase, formate-dependent, cytochrome; Function experimentally demonstrated in the studied species; carrier; Belongs to the cytochrome c-552 family. (478 aa)
aceKIsocitrate dehydrogenase kinase/phosphatase; Function experimentally demonstrated in the studied species; enzyme. (578 aa)
aceAIsocitrate lyase; Function experimentally demonstrated in the studied species; enzyme. (434 aa)
aceBMalate synthase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the malate synthase family. (533 aa)
ppcPhosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle; Belongs to the PEPCase type 1 family. (883 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)
ubiEUbiquinone/menaquinone biosynthesis C-methyltransferase UbiE; Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3- methyl-6-methoxy-1,4-benzoquinol (DMQH2). (251 aa)
bisCBiotin sulfoxide reductase; Function experimentally demonstrated in the studied species; enzyme. (759 aa)
mdhMalate dehydrogenase, NAD(P)-binding; Catalyzes the reversible oxidation of malate to oxaloacetate. (312 aa)
hybOHydrogenase 2, small subunit; Function experimentally demonstrated in the studied species; enzyme. (372 aa)
hybAHydrogenase 2 4Fe-4S ferredoxin-type component; Function experimentally demonstrated in the studied species; putative carrier. (328 aa)
hybBFunction of strongly homologous gene; carrier. (392 aa)
hybCHydrogenase 2, large subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family. (567 aa)
glcBMalate synthase G; Function experimentally demonstrated in the studied species; enzyme. (723 aa)
sdhBSuccinate dehydrogenase, FeS subunit; Function experimentally demonstrated in the studied species; carrier. (238 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)
sdhDSuccinate dehydrogenase, membrane subunit, binds cytochrome b556; Membrane-anchoring subunit of succinate dehydrogenase (SDH). (115 aa)
sdhCSuccinate dehydrogenase, membrane subunit, binds cytochrome b556; Function experimentally demonstrated in the studied species; membrane component. (129 aa)
gltACitrate synthase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the citrate synthase family. (427 aa)
ylbEConserved hypothetical protein; Homologs of previously reported genes of unknown function. (419 aa)
fdrAPutative acyl-CoA synthetase with NAD(P)-binding Rossmann-fold domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (555 aa)
cyoBCytochrome o ubiquinol oxidase subunit I; Function experimentally demonstrated in the studied species; carrier. (663 aa)
cyoCCytochrome o ubiquinol oxidase subunit III; Function experimentally demonstrated in the studied species; carrier. (204 aa)
prpD2-methylcitrate dehydratase; Function experimentally demonstrated in the studied species; enzyme. (483 aa)
hycBHydrogenase 3, Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (203 aa)
hycCHydrogenase 3, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (608 aa)
hycDHydrogenase 3, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (307 aa)
hycEHydrogenase 3, large subunit; Function experimentally demonstrated in the studied species; enzyme. (569 aa)
hycFFormate hydrogenlyase complex iron-sulfur protein; Function experimentally demonstrated in the studied species; carrier. (180 aa)
yfjGConserved hypothetical protein; Homologs of previously reported genes of unknown function. (158 aa)
hyfHHydrogenase 4, Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (179 aa)
hyfGHydrogenase 4, subunit; Function experimentally demonstrated in the studied species; carrier. (555 aa)
hyfFHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (526 aa)
hyfEHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (216 aa)
hyfDHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (450 aa)
hyfCHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (322 aa)
hyfBHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (672 aa)
nuoCNADH:ubiquinone oxidoreductase, chain C,D; Function experimentally demonstrated in the studied species; carrier. (600 aa)
nuoENADH:ubiquinone oxidoreductase, chain E; Function experimentally demonstrated in the studied species; carrier. (166 aa)
nuoGNADH:ubiquinone oxidoreductase, chain G; Function experimentally demonstrated in the studied species; carrier. (910 aa)
nuoHNADH:ubiquinone oxidoreductase, membrane subunit H; Function experimentally demonstrated in the studied species; membrane component. (325 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)
nuoKNADH:ubiquinone oxidoreductase, membrane subunit K; Function experimentally demonstrated in the studied species; membrane component. (100 aa)
nuoLNADH:ubiquinone oxidoreductase, membrane subunit L; Function experimentally demonstrated in the studied species; membrane component. (613 aa)
nuoMNADH:ubiquinone oxidoreductase, membrane subunit M; Function experimentally demonstrated in the studied species; membrane component. (509 aa)
ynfFOxidoreductase subunit; Function experimentally demonstrated in the studied species; enzyme. (807 aa)
ynfEOxidoreductase subunit; Function experimentally demonstrated in the studied species; enzyme. (808 aa)
fdnIFormate dehydrogenase-N, cytochrome B556 (gamma) subunit, nitrate-inducible; Function experimentally demonstrated in the studied species; carrier. (217 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)
cybBCytochrome b561; Function experimentally demonstrated in the studied species; carrier. (176 aa)
acnAAconitate hydratase 1; Function experimentally demonstrated in the studied species; enzyme. (891 aa)
icdIsocitrate dehydrogenase, specific for NADP+; Function experimentally demonstrated in the studied species; extrachromosomal origin. (416 aa)
yceJPutative cytochrome b561; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (188 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)
torTPeriplasmic sensory protein associated with the TorRS two-component regulatory system; Function experimentally demonstrated in the studied species; regulator. (342 aa)
appBCytochrome bd-II oxidase, subunit II; Function experimentally demonstrated in the studied species; carrier. (378 aa)
hyaCHydrogenase 1, b-type cytochrome subunit; Function experimentally demonstrated in the studied species; carrier. (235 aa)
fumAFumarate hydratase (fumarase A), aerobic Class I; Function experimentally demonstrated in the studied species; enzyme. (548 aa)
ydhUPutative cytochrome b subunit of a reductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (261 aa)
ydhXPutative 4Fe-4S ferridoxin-type subunit of oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (222 aa)
ydhYPutative 4Fe-4S ferridoxin-type subunit of oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (208 aa)
torZTrimethylamine N-oxide reductase system III, catalytic subunit; Function experimentally demonstrated in the studied species; enzyme. (809 aa)
torYTMAO reductase III (TorYZ), cytochrome c-type subunit; Function experimentally demonstrated in the studied species; carrier; Belongs to the TorC/TorY family. (366 aa)
yodBPutative cytochrome; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (176 aa)
dldD-lactate dehydrogenase, FAD-binding, NADH independent; Function experimentally demonstrated in the studied species; enzyme. (571 aa)
nuoNNADH:ubiquinone oxidoreductase, membrane subunit N; Function experimentally demonstrated in the studied species; membrane component. (485 aa)
napCNitrate reductase, cytochrome c-type,periplasmic; Function experimentally demonstrated in the studied species; carrier. (200 aa)
napBNitrate reductase, small, cytochrome C550 subunit, periplasmic; Electron transfer subunit of the periplasmic nitrate reductase complex NapAB; Belongs to the NapB family. (149 aa)
napGFerredoxin-type protein NapG (Periplasmic nitrate reductase); Function experimentally demonstrated in the studied species; carrier. (231 aa)
mqoMalate dehydrogenase, FAD/NAD(P)-binding domain; Function experimentally demonstrated in the studied species; enzyme. (548 aa)
glpCSn-glycerol-3-phosphate dehydrogenase (anaerobic), small subunit; Function experimentally demonstrated in the studied species; enzyme. (396 aa)
prpC2-methylcitrate synthase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the citrate synthase family. (389 aa)
yahGConserved hypothetical protein; Homologs of previously reported genes of unknown function. (472 aa)
yahFPutative enzyme with acyl-CoA domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (515 aa)
ykgEPutative hydroxyacid oxidoreductase (Fe-S centre); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (239 aa)
acnBBifunctional aconitate hydratase 2 and 2-methylisocitrate dehydratase; Function experimentally demonstrated in the studied species; enzyme. (865 aa)
fumCFumarate hydratase (fumarase C),aerobic Class II; Function experimentally demonstrated in the studied species; enzyme. (467 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)
sucA2-oxoglutarate decarboxylase, thiamin-requiring; Function experimentally demonstrated in the studied species; enzyme. (933 aa)
sucBDihydrolipoyltranssuccinase; Function experimentally demonstrated in the studied species; enzyme. (405 aa)
sucCsuccinyl-CoA synthetase, beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (388 aa)
sucDsuccinyl-CoA synthetase, NAD(P)-binding, alpha subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. (289 aa)
cydACytochrome d terminal oxidase, subunit I; Function experimentally demonstrated in the studied species; carrier. (522 aa)
cydBCytochrome d terminal oxidase, subunit II; Function experimentally demonstrated in the studied species; carrier. (379 aa)
ybhJPutative enzyme; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (753 aa)
dmsADimethyl sulfoxide reductase, anaerobic, subunit A; Function experimentally demonstrated in the studied species; enzyme. (814 aa)
dmsBDimethyl sulfoxide reductase, anaerobic, subunit B; Function experimentally demonstrated in the studied species; enzyme. (205 aa)
dmsCDimethyl sulfoxide reductase, anaerobic, subunit C; Function experimentally demonstrated in the studied species; enzyme. (287 aa)
hyaAHydrogenase 1, small subunit; Function experimentally demonstrated in the studied species; enzyme. (372 aa)
hyaBHydrogenase 1, large subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family. (597 aa)
Your Current Organism:
Escherichia coli IAI1
NCBI taxonomy Id: 585034
Other names: E. coli IAI1, Escherichia coli str. IAI1, Escherichia coli strain IAI1
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