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nuoH nuoH fdoI fdoI hybO hybO hybA hybA hybB hybB hybC hybC hycB hycB hycC hycC hycD hycD hycE hycE hycF hycF hyfG hyfG hyfF hyfF hyfE hyfE hyfD hyfD hyfC hyfC hyfB hyfB nuoC nuoC nuoE nuoE cyoC cyoC cydA cydA dmsA dmsA dmsB dmsB dmsC dmsC hyaA hyaA hyaB hyaB hyaC hyaC appC appC appB appB torA torA yceJ yceJ cybB cybB fdnI fdnI ynfH ynfH ydhU ydhU dld dld nuoN nuoN nuoM nuoM nuoL nuoL nuoK nuoK nuoI nuoI nuoG nuoG
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:
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)
fdoIFormate dehydrogenase-O, cytochrome b556 subunit; Function experimentally demonstrated in the studied species; carrier. (211 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)
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)
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. (479 aa)
hyfCHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (315 aa)
hyfBHydrogenase 4, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (672 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)
nuoENADH:ubiquinone oxidoreductase, chain E; Function experimentally demonstrated in the studied species; carrier. (166 aa)
cyoCCytochrome o ubiquinol oxidase subunit III; Function experimentally demonstrated in the studied species; carrier. (204 aa)
cydACytochrome d terminal oxidase, subunit I; Function experimentally demonstrated in the studied species; carrier. (522 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)
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)
hyaCHydrogenase 1, b-type cytochrome subunit; Function experimentally demonstrated in the studied species; carrier. (235 aa)
appCCytochrome bd-II oxidase, subunit I; Function experimentally demonstrated in the studied species; carrier. (514 aa)
appBCytochrome bd-II oxidase, subunit II; Function experimentally demonstrated in the studied species; carrier. (378 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)
yceJPutative cytochrome b561; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (188 aa)
cybBCytochrome b561; Function experimentally demonstrated in the studied species; carrier. (176 aa)
fdnIFormate dehydrogenase-N, cytochrome B556 (gamma) subunit, nitrate-inducible; Function experimentally demonstrated in the studied species; carrier. (217 aa)
ynfHOxidoreductase, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (284 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)
dldD-lactate dehydrogenase, FAD-binding, NADH independent; Catalyzes the oxidation of D-lactate to pyruvate. Belongs to the quinone-dependent D-lactate dehydrogenase family. (571 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. (425 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)
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)
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)
Your Current Organism:
Escherichia coli UMN026
NCBI taxonomy Id: 585056
Other names: E. coli UMN026
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