node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SHK35221.1 | SHK59747.1 | SAMN04488087_0943 | SAMN04488087_1511 | NADH dehydrogenase. | Cytochrome c oxidase subunit 2; 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). | 0.860 |
SHK35221.1 | SHK81576.1 | SAMN04488087_0943 | SAMN04488087_2064 | NADH dehydrogenase. | NADH dehydrogenase subunit E. | 0.994 |
SHK35221.1 | SHK81626.1 | SAMN04488087_0943 | SAMN04488087_2066 | NADH dehydrogenase. | NADH dehydrogenase subunit F; 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. | 0.996 |
SHK35221.1 | SHK81680.1 | SAMN04488087_0943 | SAMN04488087_2068 | NADH dehydrogenase. | NADH dehydrogenase subunit G. | 0.997 |
SHK35221.1 | SHK87469.1 | SAMN04488087_0943 | SAMN04488087_2198 | NADH dehydrogenase. | Rieske [2Fe-2S] domain-containing protein. | 0.986 |
SHK35221.1 | SHL08754.1 | SAMN04488087_0943 | SAMN04488087_2690 | NADH dehydrogenase. | Zinc protease. | 0.879 |
SHK35221.1 | acpP | SAMN04488087_0943 | SAMN04488087_0840 | NADH dehydrogenase. | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.996 |
SHK35221.1 | nuoC | SAMN04488087_0943 | SAMN04488087_2062 | NADH dehydrogenase. | 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. 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. | 0.999 |
SHK35221.1 | nuoD | SAMN04488087_0943 | SAMN04488087_2063 | NADH dehydrogenase. | 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 |
SHK35221.1 | nuoI | SAMN04488087_0943 | SAMN04488087_2167 | NADH dehydrogenase. | NADH-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 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 |
SHK59747.1 | SHK35221.1 | SAMN04488087_1511 | SAMN04488087_0943 | Cytochrome c oxidase subunit 2; 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. | 0.860 |
SHK59747.1 | SHK81576.1 | SAMN04488087_1511 | SAMN04488087_2064 | Cytochrome c oxidase subunit 2; 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 E. | 0.955 |
SHK59747.1 | SHK81626.1 | SAMN04488087_1511 | SAMN04488087_2066 | Cytochrome c oxidase subunit 2; 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 F; 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. | 0.850 |
SHK59747.1 | SHK81680.1 | SAMN04488087_1511 | SAMN04488087_2068 | Cytochrome c oxidase subunit 2; 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 G. | 0.930 |
SHK59747.1 | SHK87469.1 | SAMN04488087_1511 | SAMN04488087_2198 | Cytochrome c oxidase subunit 2; 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). | Rieske [2Fe-2S] domain-containing protein. | 0.999 |
SHK59747.1 | SHL08754.1 | SAMN04488087_1511 | SAMN04488087_2690 | Cytochrome c oxidase subunit 2; 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). | Zinc protease. | 0.989 |
SHK59747.1 | acpP | SAMN04488087_1511 | SAMN04488087_0840 | Cytochrome c oxidase subunit 2; 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). | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.882 |
SHK59747.1 | nuoC | SAMN04488087_1511 | SAMN04488087_2062 | Cytochrome c oxidase subunit 2; 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-quinone oxidoreductase 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. | 0.962 |
SHK59747.1 | nuoD | SAMN04488087_1511 | SAMN04488087_2063 | Cytochrome c oxidase subunit 2; 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. | 0.982 |
SHK59747.1 | nuoI | SAMN04488087_1511 | SAMN04488087_2167 | Cytochrome c oxidase subunit 2; 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-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 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. | 0.954 |