STRINGSTRING
AGB44399.1 AGB44399.1 AGB44623.1 AGB44623.1 AGB44624.1 AGB44624.1 AGB44625.1 AGB44625.1 AGB44981.1 AGB44981.1 AGB44982.1 AGB44982.1 AGB44983.1 AGB44983.1 AGB44984.1 AGB44984.1 AGB45024.1 AGB45024.1 AGB45025.1 AGB45025.1 AGB45026.1 AGB45026.1 AGB45027.1 AGB45027.1 AGB45157.1 AGB45157.1 nuoD nuoD nuoA nuoA nuoB nuoB nuoC nuoC nuoD-2 nuoD-2 AGB45921.1 AGB45921.1 AGB45922.1 AGB45922.1 AGB45924.1 AGB45924.1 nuoH nuoH nuoI nuoI AGB45927.1 AGB45927.1 nuoK nuoK AGB45929.1 AGB45929.1 AGB45930.1 AGB45930.1 nuoN nuoN AGB46422.1 AGB46422.1 AGB46423.1 AGB46423.1 AGB46424.1 AGB46424.1 AGB47418.1 AGB47418.1 AGB47422.1 AGB47422.1 AGB47423.1 AGB47423.1 AGB48120.1 AGB48120.1
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:
AGB44399.1Hypothetical protein. (259 aa)
AGB44623.1Ubiquinol-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. (186 aa)
AGB44624.1Cytochrome b subunit of the bc complex; 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. (433 aa)
AGB44625.1PFAM: Cytochrome C1 family. (290 aa)
AGB44981.1PFAM: Prokaryotic Cytochrome C oxidase subunit IV; TIGRFAM: cytochrome o ubiquinol oxidase subunit IV. (138 aa)
AGB44982.1Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III; TIGRFAM: cytochrome o ubiquinol oxidase, subunit III. (228 aa)
AGB44983.1PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome o ubiquinol oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family. (667 aa)
AGB44984.1PFAM: COX Aromatic Rich Motif; Cytochrome C oxidase subunit II, periplasmic domain; TIGRFAM: cytochrome o ubiquinol oxidase subunit II. (338 aa)
AGB45024.1PFAM: COX Aromatic Rich Motif; Cytochrome C oxidase subunit II, periplasmic domain; TIGRFAM: cytochrome o ubiquinol oxidase subunit II. (393 aa)
AGB45025.1PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome o ubiquinol oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family. (665 aa)
AGB45026.1PFAM: Cytochrome c oxidase subunit III; TIGRFAM: cytochrome o ubiquinol oxidase, subunit III. (208 aa)
AGB45027.1PFAM: Prokaryotic Cytochrome C oxidase subunit IV; TIGRFAM: cytochrome o ubiquinol oxidase subunit IV. (125 aa)
AGB45157.1Cytochrome 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. (552 aa)
nuoDNADH dehydrogenase I, D subunit; 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. (395 aa)
nuoANADH:ubiquinone oxidoreductase subunit 3 (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. (121 aa)
nuoBNADH-quinone oxidoreductase, B subunit; 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. (193 aa)
nuoCNADH/F420H2 dehydrogenase, 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)
nuoD-2NADH dehydrogenase I, D subunit; 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)
AGB45921.1PFAM: Respiratory-chain NADH dehydrogenase 24 Kd subunit; TIGRFAM: NADH-quinone oxidoreductase, E subunit. (337 aa)
AGB45922.1NADH-quinone oxidoreductase, F subunit; 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)
AGB45924.1NADH-quinone oxidoreductase, 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. (693 aa)
nuoHNADH:ubiquinone oxidoreductase subunit 1 (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. (347 aa)
nuoINADH-quinone oxidoreductase, chain 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)
AGB45927.1NADH:ubiquinone oxidoreductase subunit 6 (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. (206 aa)
nuoKNADH:ubiquinone oxidoreductase subunit 11 or 4L (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)
AGB45929.1Proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH dehydrogenase subunit 5 C-terminus; NADH-Ubiquinone/plastoquinone (complex I), various chains; NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L. (657 aa)
AGB45930.1Proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; NADH-ubiquinone oxidoreductase chain 4, amino terminus; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M. (501 aa)
nuoNProton-translocating NADH-quinone oxidoreductase, 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. (478 aa)
AGB46422.1Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III. (201 aa)
AGB46423.1Cytochrome 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. (658 aa)
AGB46424.1PFAM: Cytochrome c; Cytochrome C oxidase subunit II, periplasmic domain; TIGRFAM: cytochrome c oxidase, subunit II. (337 aa)
AGB47418.1Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III. (293 aa)
AGB47422.1Cytochrome 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. (550 aa)
AGB47423.1Cytochrome 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). (288 aa)
AGB48120.14Fe-4S protein. (64 aa)
Your Current Organism:
Mesorhizobium australicum
NCBI taxonomy Id: 754035
Other names: M. australicum WSM2073, Mesorhizobium australicum LMG 24608, Mesorhizobium australicum WSM2073, Mesorhizobium australicum str. WSM2073, Mesorhizobium australicum strain WSM2073, Mesorhizobium sp. WSM 2073, Mesorhizobium sp. WSM2073
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