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nuoA nuoA nuoB nuoB AOH47544.1 AOH47544.1 nuoD nuoD nuoH nuoH AOH47547.1 AOH47547.1 nuoK nuoK AOH47550.1 AOH47550.1 AOH47551.1 AOH47551.1 nuoN nuoN AOH47950.1 AOH47950.1 AOH48371.1 AOH48371.1 AOH48372.1 AOH48372.1 AOH48373.1 AOH48373.1 AOH48417.1 AOH48417.1 AOH48418.1 AOH48418.1 AOH48457.1 AOH48457.1 BCS37_09840 BCS37_09840 atpC atpC atpD atpD atpG atpG atpA atpA atpH atpH atpF atpF atpE atpE atpB atpB
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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
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nuoANADH:ubiquinone oxidoreductase 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 a menaquinone. 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. (117 aa)
nuoBNADH dehydrogenase; 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 a menaquinone. 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. (179 aa)
AOH47544.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (162 aa)
nuoDNADH dehydrogenase; 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 a menaquinone. 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 49 kDa subunit family. (366 aa)
nuoHNADH-quinone oxidoreductase 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. (348 aa)
AOH47547.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (227 aa)
nuoKNADH-quinone oxidoreductase 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 a menaquinone. 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. (101 aa)
AOH47550.1NADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (633 aa)
AOH47551.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (510 aa)
nuoNNADH-quinone oxidoreductase 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 a menaquinone. 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. (484 aa)
AOH47950.1Inorganic diphosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. (548 aa)
AOH48371.1Succinate dehydrogenase iron-sulfur subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (250 aa)
AOH48372.1Succinate dehydrogenase flavoprotein subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (603 aa)
AOH48373.1Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (210 aa)
AOH48417.1Cytochrome D ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (456 aa)
AOH48418.1Cytochrome d ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (338 aa)
AOH48457.1Pyridine nucleotide-disulfide oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (428 aa)
BCS37_09840(2Fe-2S)-binding protein; Incomplete; partial on complete genome; missing start; Derived by automated computational analysis using gene prediction method: Protein Homology. (289 aa)
atpCATP synthase F1 subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. (144 aa)
atpDF0F1 ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. (470 aa)
atpGATP synthase F1 subunit gamma; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. (283 aa)
atpAF0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (505 aa)
atpHATP synthase F1 subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (179 aa)
atpFATP synthase F0 subunit B; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. (174 aa)
atpEATP synthase F0 subunit C; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (83 aa)
atpBATP synthase F0 subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. (226 aa)
Your Current Organism:
Selenomonas
NCBI taxonomy Id: 1884263
Other names: S. sp. oral taxon 920, Selenomonas sp. oral taxon 920
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