| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KML35734.1 | KML35994.1 | VL14_22615 | VL14_22155 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B; 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). | 0.998 |
| KML35734.1 | KML35995.1 | VL14_22615 | VL14_22160 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Quinol oxidase subunit 1; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | 0.994 |
| KML35734.1 | KML35997.1 | VL14_22615 | VL14_22170 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B6; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.924 |
| KML35734.1 | KML39826.1 | VL14_22615 | VL14_14950 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.947 |
| KML35734.1 | KML45670.1 | VL14_22615 | VL14_02725 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.926 |
| KML35734.1 | KML45671.1 | VL14_22615 | VL14_02730 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.887 |
| KML35734.1 | KML45672.1 | VL14_22615 | VL14_02735 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome Cbb3; Component of the menaquinol-cytochrome c reductase complex. | 0.993 |
| KML35734.1 | KML46450.1 | VL14_22615 | VL14_00805 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH-quinone oxidoreductase subunit C; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.801 |
| KML35734.1 | nuoD | VL14_22615 | VL14_00810 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; 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. | 0.807 |
| KML35994.1 | KML35734.1 | VL14_22155 | VL14_22615 | Cytochrome B; 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). | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |
| KML35994.1 | KML35995.1 | VL14_22155 | VL14_22160 | Cytochrome B; 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). | Quinol oxidase subunit 1; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | 0.999 |
| KML35994.1 | KML35996.1 | VL14_22155 | VL14_22165 | Cytochrome B; 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). | Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KML35994.1 | KML35997.1 | VL14_22155 | VL14_22170 | Cytochrome B; 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). | Cytochrome B6; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KML35994.1 | KML39826.1 | VL14_22155 | VL14_14950 | Cytochrome B; 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). | Cytochrome C oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |
| KML35994.1 | KML45670.1 | VL14_22155 | VL14_02725 | Cytochrome B; 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). | Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |
| KML35994.1 | KML45671.1 | VL14_22155 | VL14_02730 | Cytochrome B; 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). | Cytochrome b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KML35994.1 | KML45672.1 | VL14_22155 | VL14_02735 | Cytochrome B; 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). | Cytochrome Cbb3; Component of the menaquinol-cytochrome c reductase complex. | 0.999 |
| KML35994.1 | KML46450.1 | VL14_22155 | VL14_00805 | Cytochrome B; 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| KML35994.1 | nuoD | VL14_22155 | VL14_00810 | Cytochrome B; 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; 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 |
| KML35995.1 | KML35734.1 | VL14_22160 | VL14_22615 | Quinol oxidase subunit 1; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.994 |
