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AGB43275.1 AGB43275.1 AGB43277.1 AGB43277.1 AGB43565.1 AGB43565.1 AGB43566.1 AGB43566.1 AGB43567.1 AGB43567.1 AGB43569.1 AGB43569.1 ppa ppa atpH atpH atpA atpA atpG atpG atpD atpD atpC atpC AGB44623.1 AGB44623.1 AGB44624.1 AGB44624.1 AGB44625.1 AGB44625.1 AGB44924.1 AGB44924.1 AGB44925.1 AGB44925.1 AGB44926.1 AGB44926.1 AGB44927.1 AGB44927.1 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 AGB45158.1 AGB45158.1 nuoD nuoD nuoA nuoA nuoB nuoB nuoC nuoC nuoD-2 nuoD-2 AGB45921.1 AGB45921.1 AGB45922.1 AGB45922.1 AGB45923.1 AGB45923.1 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 AGB46425.1 AGB46425.1 AGB46535.1 AGB46535.1 ctaA ctaA AGB46877.1 AGB46877.1 ppk ppk AGB47418.1 AGB47418.1 ctaG ctaG ctaB ctaB AGB47422.1 AGB47422.1 AGB47423.1 AGB47423.1 atpF atpF atpF-2 atpF-2 atpE atpE atpB atpB AGB47860.1 AGB47860.1 AGB47861.1 AGB47861.1 AGB47862.1 AGB47862.1 AGB47863.1 AGB47863.1 AGB48252.1 AGB48252.1
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
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textmining
co-expression
protein homology
Your Input:
AGB43275.1PFAM: Cytochrome oxidase subunit II; TIGRFAM: cytochrome d oxidase, subunit II (cydB). (334 aa)
AGB43277.1Cytochrome bd-type quinol oxidase, subunit 1; PFAM: Bacterial Cytochrome Ubiquinol Oxidase. (453 aa)
AGB43565.1Succinate dehydrogenase, cytochrome b556 subunit; PFAM: Succinate dehydrogenase/Fumarate reductase transmembrane subunit; TIGRFAM: succinate dehydrogenase, cytochrome b556 subunit. (138 aa)
AGB43566.1PFAM: Succinate dehydrogenase/Fumarate reductase transmembrane subunit; TIGRFAM: succinate dehydrogenase, hydrophobic membrane anchor protein. (131 aa)
AGB43567.1PFAM: domain; FAD binding domain; TIGRFAM: succinate dehydrogenase, flavoprotein subunit, E. coli/mitochondrial subgroup; succinate dehydrogenase or fumarate reductase, flavoprotein subunitGram-negative/mitochondrial subgroup; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (611 aa)
AGB43569.1TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (259 aa)
ppaInorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (177 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. (186 aa)
atpAProton translocating ATP 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. (509 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. (294 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. (531 aa)
atpCATP synthase, F1 epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (135 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)
AGB44924.1Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (287 aa)
AGB44925.1PFAM: Cbb3-type cytochrome oxidase component FixQ. (49 aa)
AGB44926.1PFAM: Cytochrome C oxidase, mono-heme subunit/FixO; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II. (243 aa)
AGB44927.1PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit I; Belongs to the heme-copper respiratory oxidase family. (565 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)
AGB45158.1PFAM: Succinate dehydrogenase/Fumarate reductase transmembrane subunit; TIGRFAM: succinate dehydrogenase, hydrophobic membrane anchor protein. (129 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)
AGB45923.1Hypothetical protein. (231 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)
AGB46425.1Cytochrome c, mono- and diheme variants family; PFAM: Cytochrome c; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit III. (177 aa)
AGB46535.1NADH dehydrogenase, FAD-containing subunit; PFAM: Pyridine nucleotide-disulphide oxidoreductase. (421 aa)
ctaAUncharacterized protein required for cytochrome oxidase assembly; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group; Belongs to the COX15/CtaA family. Type 2 subfamily. (363 aa)
AGB46877.1PFAM: Polyphosphate kinase 2 (PPK2); TIGRFAM: polyphosphate kinase 2, PA0141 family. (306 aa)
ppkPolyphosphate kinase 1; 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. (730 aa)
AGB47418.1Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III. (293 aa)
ctaGCytochrome oxidase assembly factor; Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I; Belongs to the COX11/CtaG family. (210 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. (314 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)
atpFF0F1-type ATP synthase, beta subunit; 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. (163 aa)
atpF-2F0F1-type ATP synthase, beta subunit; 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. (199 aa)
atpEF0F1-type ATP synthase, subunit c/archaeal/vacuolar-type H+-ATPase, subunit K; 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)
atpBF0F1-type ATP synthase, alpha subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (252 aa)
AGB47860.1Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (287 aa)
AGB47861.1PFAM: Cbb3-type cytochrome oxidase component FixQ. (49 aa)
AGB47862.1PFAM: Cytochrome C oxidase, mono-heme subunit/FixO; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II. (243 aa)
AGB47863.1PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit I; Belongs to the heme-copper respiratory oxidase family. (542 aa)
AGB48252.1PFAM: Polyphosphate kinase 2 (PPK2); TIGRFAM: polyphosphate kinase 2, PA0141 family. (302 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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