STRINGSTRING
coxB coxB coxA coxA PSEEN0058 PSEEN0058 PSEEN0059 PSEEN0059 PSEEN0063 PSEEN0063 cyoE1 cyoE1 ppa ppa cyoA cyoA cyoB cyoB cyoC cyoC cyoD cyoD cyoE cyoE ccoP-2 ccoP-2 ccoQ-2 ccoQ-2 ccoO-2 ccoO-2 ccoN-2 ccoN-2 ccoP-1 ccoP-1 ccoQ-1 ccoQ-1 ccoO-1 ccoO-1 ccoN-1 ccoN-1 PSEEN2040 PSEEN2040 cioA-2 cioA-2 cioB-2 cioB-2 PSEEN2617 PSEEN2617 PSEEN2681 PSEEN2681 nuoA nuoA nuoB nuoB nuoC nuoC nuoE nuoE nuoF nuoF nuoG nuoG nuoH nuoH nuoI nuoI nuoJ nuoJ nuoK nuoK nuoL nuoL nuoM nuoM nuoN nuoN sdhB sdhB sdhA sdhA sdhD sdhD sdhC sdhC petC petC petB petB petA petA ndh ndh cioB cioB cioA cioA ppk2 ppk2 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.
Node Color
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). (375 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. (529 aa)
PSEEN0058Putative cytochrome c oxidase assembly protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; factor. (185 aa)
PSEEN0059Putative cytochrome c oxidase, subunit III; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. (295 aa)
PSEEN0063Putative cytochrome oxidase assembly protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; membrane component. (357 aa)
cyoE1Putative protoheme 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. (299 aa)
ppaInorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (175 aa)
cyoACytochrome o ubiquinol oxidase subunit II; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (314 aa)
cyoBCytochrome o ubiquinol oxidase subunit I; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the heme-copper respiratory oxidase family. (673 aa)
cyoCCytochrome o ubiquinol oxidase subunit III; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (207 aa)
cyoDCytochrome o ubiquinol oxidase, subunit IV; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (110 aa)
cyoEProtoheme IX farnesyltransferase (heme O biosynthesis); 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. (295 aa)
ccoP-2Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (325 aa)
ccoQ-2Cytochrome c oxidase, cbb3-type, CcoQ subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (63 aa)
ccoO-2Cytochrome c oxidase, cbb3-type, subunit II; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (202 aa)
ccoN-2Cytochrome c oxidase, cbb3-type, subunit I; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the heme-copper respiratory oxidase family. (480 aa)
ccoP-1Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (313 aa)
ccoQ-1Cytochrome c oxidase, cbb3-type, CcoQ subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (64 aa)
ccoO-1Cytochrome c oxidase, cbb3-type, subunit II; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (202 aa)
ccoN-1Cytochrome c oxidase, cbb3-type, subunit I; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the heme-copper respiratory oxidase family. (474 aa)
PSEEN2040Putative pyridine nucleotide-disulphide oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. (400 aa)
cioA-2Ubiquinol oxidase subunit I, cyanide insensitive; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (463 aa)
cioB-2Ubiquinol oxidase subunit II, cyanide insensitive; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (338 aa)
PSEEN2617Putative NADH dehydrogenase, PNDR family; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. (430 aa)
PSEEN2681Conserved hypothetical protein; Homologs of previously reported genes of unknown function. (272 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. (137 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. (225 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. (593 aa)
nuoENADH dehydrogenase I chain E; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (165 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. (454 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. 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. (904 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. (335 aa)
nuoINADH dehydrogenase I chain I, 2Fe-2S ferredoxin-related; 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)
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. 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)
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. (102 aa)
nuoLNADH dehydrogenase I chain L; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (617 aa)
nuoMNADH dehydrogenase I chain M, membrane subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (510 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. (489 aa)
sdhBSuccinate dehydrogenase, iron-sulfur subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (234 aa)
sdhASuccinate dehydrogenase, flavoprotein subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (590 aa)
sdhDSuccinate dehydrogenase, hydrophobic membrane anchor protein; Membrane-anchoring subunit of succinate dehydrogenase (SDH). (122 aa)
sdhCSuccinate dehydrogenase, cytochrome b556 subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (128 aa)
petCUbiquinol--cytochrome c reductase, cytochrome c1; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (259 aa)
petBUbiquinol--cytochrome c reductase, cytochrome b; 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. (403 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)
ndhNADH dehydrogenase II; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (431 aa)
cioBUbiquinol oxidase subunit II, cyanide insensitive; Function of strongly homologous gene; enzyme. (335 aa)
cioAUbiquinol oxidase subunit I, cyanide insensitive; Function of strongly homologous gene; enzyme. (478 aa)
ppk2Polyphosphate kinase 2; Function of strongly homologous gene; enzyme. (336 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)
atpCATP synthase F1, epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (139 aa)
atpDATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. (458 aa)
atpGATP synthase F1, gamma subunit; 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. (286 aa)
atpAATP synthase F1, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family. (514 aa)
atpHATP synthase F1, delta subunit; 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; Belongs to the ATPase delta chain family. (178 aa)
atpFATP synthase F0, B subunit; 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. (156 aa)
atpEATP synthase F0, C subunit; 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 F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (289 aa)
Your Current Organism:
Pseudomonas entomophila
NCBI taxonomy Id: 384676
Other names: P. entomophila L48, Pseudomonas entomophila L48, Pseudomonas entomophila str. L48, Pseudomonas entomophila strain L48
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.