node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SDK93735.1 | SDL02378.1 | SAMN05216298_2122 | SAMN05216298_2324 | Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains. | Proton-translocating NADH-quinone oxidoreductase, chain M. | 0.809 |
SDK93735.1 | SDL37059.1 | SAMN05216298_2122 | SAMN05216298_3653 | Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains. | NADH-quinone oxidoreductase subunit C; 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 30 kDa subunit family. | 0.875 |
SDK93735.1 | acpP | SAMN05216298_2122 | SAMN05216298_0890 | Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains. | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. | 0.875 |
SDK93735.1 | nuoB | SAMN05216298_2122 | SAMN05216298_3631 | Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains. | NADH dehydrogenase 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 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. | 0.855 |
SDK93735.1 | nuoB-2 | SAMN05216298_2122 | SAMN05216298_3652 | Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains. | NADH dehydrogenase 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 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. | 0.855 |
SDK93735.1 | nuoC | SAMN05216298_2122 | SAMN05216298_3632 | Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains. | NADH 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 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. | 0.875 |
SDK93735.1 | nuoD | SAMN05216298_2122 | SAMN05216298_3350 | Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains. | NADH 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 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. | 0.864 |
SDK93735.1 | nuoD-2 | SAMN05216298_2122 | SAMN05216298_3633 | Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains. | NADH 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 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. | 0.864 |
SDK93735.1 | nuoI | SAMN05216298_2122 | SAMN05216298_3638 | Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains. | NADH dehydrogenase 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. | 0.867 |
SDK93735.1 | nuoI-2 | SAMN05216298_2122 | SAMN05216298_3768 | Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains. | NADH dehydrogenase 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. | 0.867 |
SDL02378.1 | SDK93735.1 | SAMN05216298_2324 | SAMN05216298_2122 | Proton-translocating NADH-quinone oxidoreductase, chain M. | Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains. | 0.809 |
SDL02378.1 | SDL37059.1 | SAMN05216298_2324 | SAMN05216298_3653 | Proton-translocating NADH-quinone oxidoreductase, chain M. | NADH-quinone oxidoreductase subunit C; 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 30 kDa subunit family. | 0.999 |
SDL02378.1 | acpP | SAMN05216298_2324 | SAMN05216298_0890 | Proton-translocating NADH-quinone oxidoreductase, chain M. | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. | 0.993 |
SDL02378.1 | nuoB | SAMN05216298_2324 | SAMN05216298_3631 | Proton-translocating NADH-quinone oxidoreductase, chain M. | NADH dehydrogenase 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 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. | 0.998 |
SDL02378.1 | nuoB-2 | SAMN05216298_2324 | SAMN05216298_3652 | Proton-translocating NADH-quinone oxidoreductase, chain M. | NADH dehydrogenase 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 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. | 0.998 |
SDL02378.1 | nuoC | SAMN05216298_2324 | SAMN05216298_3632 | Proton-translocating NADH-quinone oxidoreductase, chain M. | NADH 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 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. | 0.998 |
SDL02378.1 | nuoD | SAMN05216298_2324 | SAMN05216298_3350 | Proton-translocating NADH-quinone oxidoreductase, chain M. | NADH 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 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. | 0.999 |
SDL02378.1 | nuoD-2 | SAMN05216298_2324 | SAMN05216298_3633 | Proton-translocating NADH-quinone oxidoreductase, chain M. | NADH 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 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. | 0.998 |
SDL02378.1 | nuoI | SAMN05216298_2324 | SAMN05216298_3638 | Proton-translocating NADH-quinone oxidoreductase, chain M. | NADH dehydrogenase 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. | 0.997 |
SDL02378.1 | nuoI-2 | SAMN05216298_2324 | SAMN05216298_3768 | Proton-translocating NADH-quinone oxidoreductase, chain M. | NADH dehydrogenase 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. | 0.998 |