STRINGSTRING
AGB44214.1 AGB44214.1 AGB42639.1 AGB42639.1 AGB42640.1 AGB42640.1 AGB43890.1 AGB43890.1 AGB44661.1 AGB44661.1 azoR azoR AGB45000.1 AGB45000.1 nuoD nuoD nuoA nuoA nuoB nuoB nuoC nuoC nuoD-2 nuoD-2 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 AGB45968.1 AGB45968.1 AGB45969.1 AGB45969.1
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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Your Input:
AGB44214.1Putative NADPH-quinone reductase (modulator of drug activity B); PFAM: Flavodoxin-like fold. (290 aa)
AGB42639.1NADH:ubiquinone oxidoreductase, NADH-binding (51 kD) subunit. (518 aa)
AGB42640.1Formate dehydrogenase, alpha subunit, archaeal-type; PFAM: Molybdopterin oxidoreductase; Molydopterin dinucleotide binding domain; Molybdopterin oxidoreductase Fe4S4 domain; TIGRFAM: formate dehydrogenase, alpha subunit, archaeal-type; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (970 aa)
AGB43890.1Putative NAD(P)H quinone oxidoreductase, PIG3 family; PFAM: Alcohol dehydrogenase GroES-like domain; Zinc-binding dehydrogenase; TIGRFAM: putative NAD(P)H quinone oxidoreductase, PIG3 family. (336 aa)
AGB44661.1PFAM: NADPH-dependent FMN reductase. (205 aa)
azoRAcyl carrier protein phosphodiesterase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity; Belongs to the azoreductase type 1 family. (211 aa)
AGB45000.1PFAM: NADPH-dependent FMN reductase. (363 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)
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)
AGB45968.1Putative NADPH-quinone reductase (modulator of drug activity B); PFAM: Flavodoxin-like fold. (193 aa)
AGB45969.1Putative NADPH-quinone reductase (modulator of drug activity B); PFAM: Flavodoxin-like fold. (195 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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