node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AGK52940.1 | AGK56008.1 | B1NLA3E_05880 | B1NLA3E_21350 | Cytochrome caa3 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). | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). | 0.984 |
AGK52940.1 | AGK56009.1 | B1NLA3E_05880 | B1NLA3E_21355 | Cytochrome caa3 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). | COG1009 NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunit. | 0.450 |
AGK52940.1 | AGK56015.1 | B1NLA3E_05880 | B1NLA3E_21385 | Cytochrome caa3 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). | COG0852 NADH:ubiquinone oxidoreductase 27 kD subunit. | 0.997 |
AGK52940.1 | AGK56050.1 | B1NLA3E_05880 | B1NLA3E_21560 | Cytochrome caa3 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). | Putative polyferredoxin; COG1145 Ferredoxin. | 0.968 |
AGK52940.1 | nuoA | B1NLA3E_05880 | B1NLA3E_21395 | Cytochrome caa3 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). | NADH dehydrogenase subunit 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 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. | 0.965 |
AGK52940.1 | nuoB | B1NLA3E_05880 | B1NLA3E_21390 | Cytochrome caa3 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). | 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. | 0.995 |
AGK52940.1 | nuoD | B1NLA3E_05880 | B1NLA3E_21380 | Cytochrome caa3 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). | 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. | 0.997 |
AGK52940.1 | nuoH | B1NLA3E_05880 | B1NLA3E_21375 | Cytochrome caa3 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). | NADH:ubiquinone 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 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. | 0.981 |
AGK52940.1 | nuoN | B1NLA3E_05880 | B1NLA3E_21345 | Cytochrome caa3 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). | NADH:ubiquinone oxidoreductase subunit 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 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. | 0.965 |
AGK56008.1 | AGK52940.1 | B1NLA3E_21350 | B1NLA3E_05880 | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). | Cytochrome caa3 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). | 0.984 |
AGK56008.1 | AGK56009.1 | B1NLA3E_21350 | B1NLA3E_21355 | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). | COG1009 NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunit. | 0.998 |
AGK56008.1 | AGK56011.1 | B1NLA3E_21350 | B1NLA3E_21365 | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). | NADH:ubiquinone oxidoreductase subunit 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. | 0.998 |
AGK56008.1 | AGK56015.1 | B1NLA3E_21350 | B1NLA3E_21385 | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). | COG0852 NADH:ubiquinone oxidoreductase 27 kD subunit. | 0.999 |
AGK56008.1 | AGK56050.1 | B1NLA3E_21350 | B1NLA3E_21560 | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). | Putative polyferredoxin; COG1145 Ferredoxin. | 0.953 |
AGK56008.1 | nuoA | B1NLA3E_21350 | B1NLA3E_21395 | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). | NADH dehydrogenase subunit 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 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. | 0.998 |
AGK56008.1 | nuoB | B1NLA3E_21350 | B1NLA3E_21390 | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (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. | 0.999 |
AGK56008.1 | nuoD | B1NLA3E_21350 | B1NLA3E_21380 | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (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 |
AGK56008.1 | nuoH | B1NLA3E_21350 | B1NLA3E_21375 | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). | NADH:ubiquinone 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 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. | 0.999 |
AGK56008.1 | nuoN | B1NLA3E_21350 | B1NLA3E_21345 | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). | NADH:ubiquinone oxidoreductase subunit 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 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. | 0.999 |
AGK56009.1 | AGK52940.1 | B1NLA3E_21355 | B1NLA3E_05880 | COG1009 NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunit. | Cytochrome caa3 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). | 0.450 |