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atpC atpC atpD atpD atpG atpG atpA atpA atpH atpH atpF atpF atpE atpE atpB atpB sdhA sdhA SdhB2 SdhB2 SdhC1 SdhC1 SdhD SdhD SdhA1 SdhA1 SdhB1 SdhB1 Ndh2 Ndh2 CydB2 CydB2 CydA2 CydA2 Ndh1 Ndh1 NuoF2 NuoF2 PvdS PvdS CtaA CtaA ctaB ctaB qcrB qcrB qcrA qcrA QcrC QcrC ctaE ctaE ctaD1_1 ctaD1_1 ctaC ctaC ctaD1_2 ctaD1_2 SdhB3 SdhB3 sdhA-2 sdhA-2 SdhC2 SdhC2 CydA1 CydA1 CydB1 CydB1 Ndh3 Ndh3 nuoA nuoA nuoB1 nuoB1 nuoC nuoC nuoD2 nuoD2 NuoE NuoE nuoF nuoF NuoG1 NuoG1 nuoH_2 nuoH_2 nuoI1 nuoI1 NuoJ1 NuoJ1 nuoK2 nuoK2 nuoL nuoL NuoM1 NuoM1 nuoN_1 nuoN_1 NuoA2 NuoA2 nuoB2 nuoB2 nuoH_1 nuoH_1 NuoI2 NuoI2 NuoJ2 NuoJ2 nuoK1 nuoK1 NuoL2 NuoL2 NuoM2 NuoM2 nuoN_2 nuoN_2 ppa ppa nuoD1 nuoD1 KUN50999.1 KUN50999.1 ppk ppk
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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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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
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atpCATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. (124 aa)
atpDATP 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. (478 aa)
atpGATP synthase F0F1 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. (305 aa)
atpAATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (529 aa)
atpHATP synthase F0F1 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. (273 aa)
atpFATP synthase F0F1 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. (180 aa)
atpEATP synthase 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. (80 aa)
atpBATP synthase F0F1 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. (269 aa)
sdhAPart of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; Derived by automated computational analysis using gene prediction method: Protein Homology. (667 aa)
SdhB2Catalyzes the fumarate and succinate interconversion; fumarate reductase is used under anaerobic conditions with glucose or glycerol as carbon source; Derived by automated computational analysis using gene prediction method: Protein Homology. (258 aa)
SdhC1Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (114 aa)
SdhDSuccinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (160 aa)
SdhA1Part of four member fumarate reductase enzyme complex FrdABCD which catalyzes the reduction of fumarate to succinate during anaerobic respiration; FrdAB are the catalytic subcomplex consisting of a flavoprotein subunit and an iron-sulfur subunit, respectively; FrdCD are the membrane components which interact with quinone and are involved in electron transfer; the catalytic subunits are similar to succinate dehydrogenase SdhAB; Derived by automated computational analysis using gene prediction method: Protein Homology. (584 aa)
SdhB1Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (257 aa)
Ndh2NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (435 aa)
CydB2Cytochrome BD oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (349 aa)
CydA2Cytochrome BD ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (498 aa)
Ndh1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (453 aa)
NuoF2NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (607 aa)
PvdSPolyphosphate kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. (267 aa)
CtaADerived by automated computational analysis using gene prediction method: Protein Homology. (335 aa)
ctaBProtoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (285 aa)
qcrBUbiquinol-cytochrome c reductase cytochrome b subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (548 aa)
qcrAUbiquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (357 aa)
QcrCCystathionine beta-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. (269 aa)
ctaEDerived by automated computational analysis using gene prediction method: Protein Homology. (206 aa)
ctaD1_1Cytochrome ubiquinol oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (579 aa)
ctaCCytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (319 aa)
ctaD1_2Cytochrome ubiquinol oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (563 aa)
SdhB3Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (249 aa)
sdhA-2Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; Derived by automated computational analysis using gene prediction method: Protein Homology. (649 aa)
SdhC2Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (223 aa)
CydA1Cytochrome BD ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (502 aa)
CydB1Cytochrome C oxidase assembly protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (334 aa)
Ndh3NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (454 aa)
nuoANADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (119 aa)
nuoB1NADH 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. (184 aa)
nuoCNADH 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 30 kDa subunit family. (248 aa)
nuoD2NADH 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. (443 aa)
NuoENADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (287 aa)
nuoFNADH dehydrogenase; 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. (448 aa)
NuoG1NADH-quinone oxidoreductase subunit 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. (834 aa)
nuoH_2NADH-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. (454 aa)
nuoI1Hypothetical protein; 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. (200 aa)
NuoJ1NADH:ubiquinone oxidoreductase 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. (280 aa)
nuoK2NADH:ubiquinone 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. (99 aa)
nuoLNADH:ubiquinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (634 aa)
NuoM1NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (532 aa)
nuoN_1NADH:ubiquinone 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. (549 aa)
NuoA2NADH-ubiquinone oxidoreductase subunit 3; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (146 aa)
nuoB2Hydroxyacid 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. (203 aa)
nuoH_1NADH 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 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. (322 aa)
NuoI2NADH-quinone oxidoreductase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (216 aa)
NuoJ2NADH dehydrogenase; 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. (207 aa)
nuoK1NADH-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. (129 aa)
NuoL2NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (663 aa)
NuoM2NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (527 aa)
nuoN_2NADH-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. (499 aa)
ppaInorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (163 aa)
nuoD1NADH-quinone oxidoreductase subunit 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 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. (383 aa)
KUN50999.1Oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (396 aa)
ppkPolyphosphate kinase; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Belongs to the polyphosphate kinase 1 (PPK1) family. (743 aa)
Your Current Organism:
Streptomyces avermitilis
NCBI taxonomy Id: 33903
Other names: ATCC 31267, DSM 46492, JCM 5070, NBRC 14893, NCIMB 12804, NRRL 8165, S. avermitilis, Streptomyces avermectinius, Streptomyces avermectinius Takahashi et al. 2002, strain MA-4680
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