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AEE14668.1 AEE14668.1 AEE14670.1 AEE14670.1 nuoN nuoN AEE15350.1 AEE15350.1 nuoK nuoK AEE15356.1 AEE15356.1 nuoH nuoH nuoC nuoC nuoA nuoA nuoI nuoI nuoD nuoD nuoB nuoB
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AEE14668.1COGs: COG1905 NADH:ubiquinone oxidoreductase 24 kD subunit; InterPro IPR002023; KEGG: ssm:Spirs_3691 NADH-quinone oxidoreductase, E subunit; PFAM: NADH:ubiquinone oxidoreductase, 24kDa subunit; SPTR: NADH-quinone oxidoreductase, E subunit; IMG reference gene:2504784436; PFAM: Respiratory-chain NADH dehydrogenase 24 Kd subunit. (156 aa)
AEE14670.1NADH dehydrogenase (quinone); COGs: COG1894 NADH:ubiquinone oxidoreductase NADH-binding (51 kD) subunit; InterPro IPR011538:IPR019554:IPR019575; KEGG: dth:DICTH_0769 NADH:ubiquinone oxidoreductase, nadh-binding (51 kd) subunit; PFAM: NADH:ubiquinone oxidoreductase, 51kDa subunit; Soluble ligand binding domain; NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding; PRIAM: NADH dehydrogenase (quinone); SPTR: NADH:ubiquinone oxidoreductase, nadh-binding (51 kd) subunit; IMG reference gene:2504784438; PFAM: NADH-ubiquinone oxidoreductase-F iron-sulfur binding region; Respiratory- [...] (537 aa)
nuoNNAD(P)H-quinone oxidoreductase subunit 2; 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 a menaquinone. 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. (458 aa)
AEE15350.1Proton-translocating NADH-quinone oxidoreductase, chain M; COGs: COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M); InterPro IPR010227:IPR001750; KEGG: tye:THEYE_A0920 NADH-quinone oxidoreductase chain M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; PRIAM: NADH dehydrogenase (quinone); SPTR: NADH-quinone oxidoreductase chain m; TIGRFAM: NADH-quinone oxidoreductase, chain M; IMG reference gene:2504785160; PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M. (501 aa)
nuoKNAD(P)H-quinone oxidoreductase subunit 4L; 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 a menaquinone. 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. (100 aa)
AEE15356.1NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. (171 aa)
nuoHNAD(P)H-quinone oxidoreductase subunit 1; 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. (333 aa)
nuoCNAD(P)H-quinone oxidoreductase subunit J; 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 a menaquinone. 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. (178 aa)
nuoANAD(P)H-quinone oxidoreductase subunit 3; 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 a menaquinone. 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. (130 aa)
nuoINAD(P)H-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. (192 aa)
nuoDNAD(P)H-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 a menaquinone. 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. (419 aa)
nuoBNAD(P)H-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 a menaquinone. 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. (178 aa)
Your Current Organism:
Thermodesulfobium narugense
NCBI taxonomy Id: 747365
Other names: T. narugense DSM 14796, Thermodesulfobium narugense DSM 14796, Thermodesulfobium narugense Na82, Thermodesulfobium narugense str. DSM 14796, Thermodesulfobium narugense strain DSM 14796, sulfate-reducing bacterium Na82
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