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ANB04239.1 ANB04239.1 ANB04383.1 ANB04383.1 ANB04489.1 ANB04489.1 ANB04730.1 ANB04730.1 ctaD ctaD ANB05772.1 ANB05772.1 ctaB ctaB qcrB qcrB qcrA qcrA qcrC qcrC ctaE ctaE ctaD-2 ctaD-2 ctaC ctaC ANB06823.1 ANB06823.1 ppk ppk ANB07201.1 ANB07201.1 cydB cydB cydA cydA ppa ppa nuoD nuoD nuoA nuoA nuoB nuoB nuoC nuoC nuoD-2 nuoD-2 ANB07901.1 ANB07901.1 nuoF nuoF nuoG nuoG nuoH nuoH nuoI nuoI ANB07906.1 ANB07906.1 nuoK nuoK nuoL nuoL nuoM nuoM nuoN nuoN ANB07947.1 ANB07947.1 nuoB-2 nuoB-2 nuoH-2 nuoH-2 nuoI-2 nuoI-2 ANB07952.1 ANB07952.1 nuoK-2 nuoK-2 ANB07954.1 ANB07954.1 ANB07955.1 ANB07955.1 nuoN-2 nuoN-2 sdhB sdhB sdhA sdhA ANB08158.1 ANB08158.1 ANB08159.1 ANB08159.1 ANB08358.1 ANB08358.1 ANB08359.1 ANB08359.1 atpB atpB atpE atpE atpF atpF atpH atpH atpA atpA atpG atpG atpD atpD atpC atpC ANB09905.1 ANB09905.1 ANB09906.1 ANB09906.1 ANB09907.1 ANB09907.1 ANB10263.1 ANB10263.1
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
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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
Others
textmining
co-expression
protein homology
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ANB04239.1Oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (396 aa)
ANB04383.1Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (576 aa)
ANB04489.1Oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (398 aa)
ANB04730.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (457 aa)
ctaDCytochrome C 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. (549 aa)
ANB05772.1Derived by automated computational analysis using gene prediction method: Protein Homology. (354 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. (545 aa)
qcrAUbiquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (352 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)
ctaD-2Cytochrome C 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. (577 aa)
ctaCCytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (319 aa)
ANB06823.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (444 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. (746 aa)
ANB07201.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (458 aa)
cydBCytochrome C oxidase assembly protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (334 aa)
cydACytochrome BD ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (501 aa)
ppaInorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (163 aa)
nuoDNADH-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)
nuoANADH 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 subunit 3 family. (119 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. (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. (251 aa)
nuoD-2NADH 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. (444 aa)
ANB07901.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (290 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. (449 aa)
nuoGNADH-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)
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. (462 aa)
nuoI(4Fe-4S)-binding 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. (213 aa)
ANB07906.1NADH: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. (285 aa)
nuoKNADH: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. (654 aa)
nuoMNADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (523 aa)
nuoNNADH: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)
ANB07947.1NADH-ubiquinone oxidoreductase subunit 3; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (138 aa)
nuoB-2Hypothetical 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 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. (199 aa)
nuoH-2NADH 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)
nuoI-2NADH-quinone oxidoreductase subunit 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. (230 aa)
ANB07952.1NADH 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. (268 aa)
nuoK-2NADH-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. (130 aa)
ANB07954.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (664 aa)
ANB07955.1NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (532 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. (515 aa)
sdhBSuccinate 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)
sdhAPart 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)
ANB08158.1Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (162 aa)
ANB08159.1Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (114 aa)
ANB08358.1Catalyzes 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. (255 aa)
ANB08359.1Part 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. (645 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. (279 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. (74 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. (182 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. (271 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)
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)
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. (482 aa)
atpCATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. (124 aa)
ANB09905.1Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (223 aa)
ANB09906.1Part 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)
ANB09907.1Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (249 aa)
ANB10263.1Polyphosphate kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. (335 aa)
Your Current Organism:
Streptomyces ambofaciens
NCBI taxonomy Id: 1889
Other names: ATCC 23877, BCRC 11857, CBS 616.68, CCRC 11857, CCRC:11857, CECT 3101, DSM 40053, IFO 12836, ISP 5053, JCM 4204, JCM 4618, KCTC 9111, NBRC 12836, NRRL 2420, NRRL B-2516, NRRL-ISP 5053, S. ambofaciens
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