STRINGSTRING
petA petA AQS61156.1 AQS61156.1 AQS61157.1 AQS61157.1 AQS61338.1 AQS61338.1 CcoN CcoN CcoO CcoO AQS61827.1 AQS61827.1 CcoP CcoP NuoN NuoN AQS62024.1 AQS62024.1 AQS62025.1 AQS62025.1 nuoK nuoK AQS62027.1 AQS62027.1 nuoI nuoI nuoH nuoH AQS62030.1 AQS62030.1 nuoF nuoF AQS62032.1 AQS62032.1 nuoD nuoD nuoC nuoC nuoB nuoB nuoA nuoA AQS62059.1 AQS62059.1 ppk ppk AQS62464.1 AQS62464.1 AQS62465.1 AQS62465.1 ctaB ctaB ctaD ctaD CoxB CoxB AQS62510.1 AQS62510.1 AQS62511.1 AQS62511.1 atpE atpE atpB atpB Ppk2 Ppk2 CyoA CyoA cyoB cyoB cyoC cyoC CyoD CyoD cydX cydX CydB CydB AQS64083.1 AQS64083.1 AQS64179.1 AQS64179.1
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.
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:
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. (192 aa)
AQS61156.1Cytochrome 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. (427 aa)
AQS61157.1Cytochrome c1; Derived by automated computational analysis using gene prediction method: Protein Homology. (294 aa)
AQS61338.1FAD-dependent oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (421 aa)
CcoNCytochrome-c oxidase, cbb3-type subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (540 aa)
CcoOCytochrome c oxidase, cbb3-type subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (243 aa)
AQS61827.1Cbb3-type cytochrome C oxidase subunit 3; Derived by automated computational analysis using gene prediction method: Protein Homology. (50 aa)
CcoPCytochrome-c oxidase, cbb3-type subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. (287 aa)
NuoNNADH-quinone oxidoreductase subunit N; Derived by automated computational analysis using gene prediction method: Protein Homology. (480 aa)
AQS62024.1NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (503 aa)
AQS62025.1NADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (665 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)
AQS62027.1NADH: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. (204 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. (163 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)
AQS62030.1NADH-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. (693 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. (434 aa)
AQS62032.1NADH-quinone oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. (365 aa)
nuoDNADH dehydrogenase 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 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 49 kDa subunit family. (396 aa)
nuoCNADH-quinone oxidoreductase subunit C; 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 30 kDa subunit family. (200 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. (194 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. (121 aa)
AQS62059.1Heme A synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. (372 aa)
ppkRNA degradosome polyphosphate 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. (732 aa)
AQS62464.1Cytochrome c oxidase subunit 3; Derived by automated computational analysis using gene prediction method: Protein Homology. (291 aa)
AQS62465.1Cytochrome c oxidase assembly protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (205 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. (317 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. (566 aa)
CoxBCytochrome c oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (287 aa)
AQS62510.1ATP F0F1 synthase subunit B; Produces ATP from ADP in the presence of a proton gradient across the membrane. Subunit B is part of the membrane proton channel; Derived by automated computational analysis using gene prediction method: Protein Homology. (161 aa)
AQS62511.1F0F1 ATP synthase subunit B; Derived by automated computational analysis using gene prediction method: Protein Homology. (213 aa)
atpEATP F0F1 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. (75 aa)
atpBF0F1 ATP 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. (249 aa)
Ppk2Polyphosphate kinase 2; Derived by automated computational analysis using gene prediction method: Protein Homology. (295 aa)
CyoAUbiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (343 aa)
cyoBCytochrome o ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. (667 aa)
cyoCCytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. (208 aa)
CyoDCytochrome o ubiquinol oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology. (131 aa)
cydXCyd operon protein YbgT; Derived by automated computational analysis using gene prediction method: Protein Homology. (40 aa)
CydBCytochrome d ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (385 aa)
AQS64083.1Cytochrome d terminal oxidase subunit 1; Part of the aerobic respiratory chain; catalyzes the ubiquinol to ubiquinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (525 aa)
AQS64179.1F0F1 ATP synthase subunit A; Derived by automated computational analysis using gene prediction method: Protein Homology. (248 aa)
Your Current Organism:
Agrobacterium rhizogenes
NCBI taxonomy Id: 359
Other names: A. rhizogenes, ATCC 11325, Agrobacterium biovar 2, Agrobacterium genomic group 10, Agrobacterium genomic species 10, Agrobacterium genomosp. 10, Agrobacterium rhizogenes (RI plasmid PRI1724), Agrobacterium rhizogenes (RI plasmid PRI8196), Agrobacterium rhizogenes (RI plasmid PRIA4B), CFBP 5520, CIP 104328, DSM 30148, ICMP 5794, IFO 13257, JCM 20919, LMG 150, LMG:150, NBRC 13257, NCPPB 2991, Rhizobium rhizogenes, Rhizobium sp. LMG 9509
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