STRINGSTRING
coxB coxB coxA coxA coxG coxG coxC coxC BAN45789.1 BAN45789.1 cyoE cyoE ppa ppa cioA cioA cioB cioB ccoN2 ccoN2 ndh ndh petA petA petB petB petC petC BAN47187.1 BAN47187.1 sdhC sdhC sdhD sdhD sdhA sdhA sdhB sdhB BAN48115.1 BAN48115.1 nuoN nuoN nuoM nuoM nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoE nuoE nuoC nuoC nuoB nuoB nuoA nuoA coxM coxM coxN coxN coxO coxO coxP coxP coxQ coxQ coxB-2 coxB-2 coxA-2 coxA-2 BAN48797.1 BAN48797.1 ccoN1 ccoN1 ccoO1 ccoO1 ccoQ2 ccoQ2 ccoP1 ccoP1 ccoN2-2 ccoN2-2 ccoO2 ccoO2 ccoQ2-2 ccoQ2-2 ccoP2 ccoP2 ppk ppk atpC atpC atpD atpD atpG atpG atpA atpA atpH atpH atpF atpF atpE atpE atpB atpB
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:
coxBCytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (367 aa)
coxACytochrome 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. (540 aa)
coxGCytochrome c oxidase assembly protein. (183 aa)
coxCCytochrome c oxidase subunit III. (295 aa)
BAN45789.1Hypothetical protein. (361 aa)
cyoEProtoheme 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. (301 aa)
ppaInorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (175 aa)
cioAUbiquinol oxidase subunit I. (479 aa)
cioBUbiquinol oxidase subunit II. (335 aa)
ccoN2Cbb3-type cytochrome c oxidase subunit CcoN2; Belongs to the heme-copper respiratory oxidase family. (491 aa)
ndhNADH dehydrogenase. (432 aa)
petAUbiquinol--cytochrome c reductase iron-sulfur subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (197 aa)
petBUbiquinol--cytochrome c reductase cytochrome b subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (404 aa)
petCUbiquinol--cytochrome c reductase cytochrome c1 subunit. (260 aa)
BAN47187.1Hypothetical protein. (274 aa)
sdhCSuccinate dehydrogenase cytochrome b556 subunit. (86 aa)
sdhDSuccinate dehydrogenase hydrophobic membrane anchor subunit; Membrane-anchoring subunit of succinate dehydrogenase (SDH). (122 aa)
sdhASuccinate dehydrogenase flavoprotein subunit; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (590 aa)
sdhBSuccinate dehydrogenase iron-sulfur protein subunit. (238 aa)
BAN48115.1Putative oxidoreductase. (400 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 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. (486 aa)
nuoMNADH-quinone oxidoreductase subunit M. (508 aa)
nuoLNADH-quinone oxidoreductase subunit L. (615 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 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. (102 aa)
nuoJNADH-quinone 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. (166 aa)
nuoINADH-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. (182 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. (330 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. (902 aa)
nuoFNADH-quinone oxidoreductase subunit 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. (448 aa)
nuoENADH-quinone oxidoreductase subunit E. (164 aa)
nuoCNADH-quinone oxidoreductase subunit 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 C-terminal section; belongs to the complex I 49 kDa subunit family. (593 aa)
nuoBNADH-quinone oxidoreductase subunit 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. (225 aa)
nuoANADH-quinone 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 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. (137 aa)
coxMCytochrome c oxidase subunit II CoxM. (479 aa)
coxNCytochrome c oxidase subunit I CoxN; 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. (589 aa)
coxOCytochrome c oxidase subunit III CoxO. (224 aa)
coxPCytochrome c oxidase subunit III CoxP. (222 aa)
coxQPutative cytochrome oxidase subunit IV. (105 aa)
coxB-2Cytochrome c oxidase subunit II. (278 aa)
coxA-2Cytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. (843 aa)
BAN48797.1Putative oxidoreductase. (400 aa)
ccoN1Cbb3-type cytochrome c oxidase subunit CcoN1; Belongs to the heme-copper respiratory oxidase family. (474 aa)
ccoO1Cbb3-type cytochrome c oxidase subunit CcoO1. (203 aa)
ccoQ2Cbb3-type cytochrome c oxidase subunit CcoQ2. (55 aa)
ccoP1Cbb3-type cytochrome c oxidase subunit CcoP1; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (311 aa)
ccoN2-2Cbb3-type cytochrome c oxidase subunit CcoN2; Belongs to the heme-copper respiratory oxidase family. (450 aa)
ccoO2Cbb3-type cytochrome c oxidase subunit CcoO2. (203 aa)
ccoQ2-2Cbb3-type cytochrome c oxidase subunit CcoQ2. (62 aa)
ccoP2Cbb3-type cytochrome c oxidase subunit CcoP2; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (324 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. (744 aa)
atpCATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. (141 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. (458 aa)
atpGATP synthase 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. (263 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. (514 aa)
atpHATP synthase 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. (178 aa)
atpFATP synthase 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. (156 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. (85 aa)
atpBATP synthase 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. (289 aa)
Your Current Organism:
Pseudomonas resinovorans NBRC106553
NCBI taxonomy Id: 1245471
Other names: P. resinovorans NBRC 106553, Pseudomonas resinovorans NBRC 106553
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