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nuoM nuoM yeiA yeiA pntA pntA pntB pntB azoR azoR ynaJ ynaJ ndh ndh wrbA wrbA ycaK ycaK guaC guaC kefF kefF hycC hycC queF queF mdaB mdaB kefG kefG yieF yieF sthA sthA hycE hycE qor qor hpaC hpaC hycF hycF hycG hycG hyfI hyfI hyfH hyfH hyfG hyfG hyfD hyfD hyfB hyfB nuoA nuoA nuoB nuoB nuoC nuoC nuoF nuoF nuoG nuoG nuoH nuoH nuoI nuoI nuoJ nuoJ nuoK nuoK nuoL nuoL nuoN nuoN
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.
Node Color
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:
nuoMNADH:ubiquinone oxidoreductase, membrane subunit M; Function experimentally demonstrated in the studied species; membrane component. (509 aa)
yeiAPutative oxidoreductase subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (411 aa)
pntAPyridine nucleotide transhydrogenase, alpha subunit; Function experimentally demonstrated in the studied species; enzyme. (510 aa)
pntBPyridine nucleotide transhydrogenase, beta subunit; Function experimentally demonstrated in the studied species; enzyme. (462 aa)
azoRNADH-azoreductase, FMN-dependent; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity; Belongs to the azoreductase type 1 family. (201 aa)
ynaJConserved hypothetical protein; Homologs of previously reported genes of unknown function; putative membrane component. (85 aa)
ndhRespiratory NADH dehydrogenase 2/cupric reductase; Function experimentally demonstrated in the studied species; enzyme. (434 aa)
wrbAPutative conserved flavoprotein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (198 aa)
ycaKPutative NAD(P)H oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (196 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)
kefFGlutathione-regulated potassium-efflux system ancillary protein KefF; Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC; Belongs to the NAD(P)H dehydrogenase (quinone) family. KefF subfamily. (176 aa)
hycCHydrogenase 3, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (608 aa)
queFNADPH-dependent 7-cyano-7-deazaguanine reductase; Catalyzes the NADPH-dependent reduction of 7-cyano-7- deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). (282 aa)
mdaBNADPH quinone reductase; Function experimentally demonstrated in the studied species; carrier. (193 aa)
kefGComponent of potassium effux complex with KefB; Function experimentally demonstrated in the studied species; transporter. (184 aa)
yieFChromate reductase, Class I, flavoprotein; Function experimentally demonstrated in the studied species; enzyme. (188 aa)
sthAPyridine nucleotide transhydrogenase, soluble; Function experimentally demonstrated in the studied species; enzyme. (466 aa)
hycEHydrogenase 3, large subunit; Function experimentally demonstrated in the studied species; enzyme. (569 aa)
qorQuinone oxidoreductase, NADPH-dependent; Function experimentally demonstrated in the studied species; enzyme. (327 aa)
hpaC4-hydroxyphenylacetate 3-monooxygenase small component, Flavin:NADH reductase; Catalyzes the reduction of free flavins (FMN, FAD and riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the large HpaB component or to other electron acceptors such as cytochrome c and Fe(3+) ion. (170 aa)
hycFFormate hydrogenlyase complex iron-sulfur protein; Function experimentally demonstrated in the studied species; carrier. (180 aa)
hycGHydrogenase 3 and formate hydrogenase complex, HycG subunit; Function experimentally demonstrated in the studied species; enzyme. (255 aa)
hyfIHydrogenase 4, Fe-S subunit; Function experimentally demonstrated in the studied species; carrier. (252 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)
hyfDHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (450 aa)
hyfBHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (672 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)
nuoBNADH:ubiquinone oxidoreductase, chain B; Function experimentally demonstrated in the studied species; carrier; Belongs to the complex I 20 kDa subunit family. (220 aa)
nuoCNADH:ubiquinone oxidoreductase, chain C,D; Function experimentally demonstrated in the studied species; carrier. (600 aa)
nuoFNADH:ubiquinone oxidoreductase, chain F; Function experimentally demonstrated in the studied species; carrier. (445 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)
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)
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)
nuoNNADH:ubiquinone oxidoreductase, membrane subunit N; Function experimentally demonstrated in the studied species; membrane component. (485 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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