STRINGSTRING
nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoC nuoC nuoB nuoB hyfG hyfG nuoA nuoA hyfB hyfB hyfD hyfD hycC hycC wrbA wrbA yabF yabF hyfI hyfI nuoN nuoN nuoM nuoM nuoL nuoL nuoK nuoK nuoJ nuoJ hycE hycE hycG hycG acpD acpD mdaB mdaB yieF yieF yheR yheR
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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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
Your Input:
nuoINADH dehydrogenase I 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 dehydrogenase I chain 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 dehydrogenase I chain G; 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 (By similarity). (910 aa)
nuoFNADH dehydrogenase I 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)
nuoCNADH dehydrogenase I 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 dehydrogenase I 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)
hyfGHydrogenase 4 subunit; Residues 1 to 571 of 571 are 96.84 pct identical to residues 1 to 555 of 555 from Escherichia coli K-12 Strain MG1655: B2487. (571 aa)
nuoANADH dehydrogenase I chain 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)
hyfBHydrogenase 4 membrane subunit; Residues 1 to 672 of 672 are 98.95 pct identical to residues 1 to 672 of 672 from Escherichia coli K-12 Strain MG1655: B2482. (672 aa)
hyfDHydrogenase 4 membrane subunit; Residues 1 to 479 of 479 are 99.58 pct identical to residues 1 to 479 of 479 from Escherichia coli K-12 Strain MG1655: B2484. (479 aa)
hycCMembrane-spanning protein of hydrogenase 3 (part of FHL complex); Residues 1 to 608 of 608 are 99.17 pct identical to residues 1 to 608 of 608 from Escherichia coli K-12 Strain MG1655: B2723. (608 aa)
wrbATrp repressor binding protein; Residues 1 to 181 of 181 are 98.89 pct identical to residues 18 to 198 of 198 from Escherichia coli K-12 Strain MG1655: B1004. (181 aa)
yabFPutative NAD(P)H oxidoreductase; 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)
hyfIHydrogenase 4 Fe-S subunit; Residues 1 to 252 of 252 are 99.20 pct identical to residues 1 to 252 of 252 from Escherichia coli K-12 Strain MG1655: B2489. (252 aa)
nuoNNADH dehydrogenase I chain 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 dehydrogenase I chain M; 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 (By similarity); Belongs to the complex I subunit 4 family. (509 aa)
nuoLNADH dehydrogenase I chain L; Residues 1 to 613 of 613 are 99.83 pct identical to residues 1 to 613 of 613 from Escherichia coli K-12 Strain MG1655: B2278. (613 aa)
nuoKNADH dehydrogenase I chain 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 dehydrogenase I chain J; 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 (By similarity); Belongs to the complex I subunit 6 family. (184 aa)
hycELarge subunit of hydrogenase 3 (part of FHL complex); Residues 1 to 569 of 569 are 99.82 pct identical to residues 1 to 569 of 569 from Escherichia coli K-12 Strain MG1655: B2721. (569 aa)
hycGHydrogenase activity; Residues 1 to 255 of 255 are 99.60 pct identical to residues 1 to 255 of 255 from Escherichia coli K-12 Strain MG1655: B2719. (255 aa)
acpDAcyl carrier protein phosphodiesterase; 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)
mdaBModulator of drug activity B; NADPH-specific quinone reductase. (193 aa)
yieFOrf, hypothetical protein; Catalyzes the reduction of quinones. Acts by simultaneous two-electron transfer, avoiding formation of highly reactive semiquinone intermediates and producing quinols that promote tolerance of H(2)O(2). Quinone reduction is probably the primary biological role of ChrR. Can also reduce toxic chromate to insoluble and less toxic Cr(3+). Catalyzes the transfer of three electrons to Cr(6+) producing Cr(3+) and one electron to molecular oxygen without producing the toxic Cr(5+) species and only producing a minimal amount of reactive oxygen species (ROS). Chromate [...] (188 aa)
yheRPutative NAD(P)H oxidoreductase; Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefB. (184 aa)
Your Current Organism:
Escherichia coli O157H7 EDL933
NCBI taxonomy Id: 155864
Other names: E. coli O157:H7 str. EDL933, Escherichia coli O157:H7 EDL933, Escherichia coli O157:H7 str. EDL933, Escherichia coli O157:H7 strain EDL933
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