| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KML35736.1 | KML35994.1 | VL14_22625 | VL14_22155 | Quinol oxidase subunit 2; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. | 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). | 0.811 |
| KML35736.1 | KML38858.1 | VL14_22625 | VL14_16885 | Quinol oxidase subunit 2; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.616 |
| KML35736.1 | KML39208.1 | VL14_22625 | VL14_16410 | Quinol oxidase subunit 2; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.616 |
| KML35736.1 | KML42422.1 | VL14_22625 | VL14_08720 | Quinol oxidase subunit 2; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. | Photosynthetic protein synthase I; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.762 |
| KML35736.1 | KML43348.1 | VL14_22625 | VL14_07175 | Quinol oxidase subunit 2; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.652 |
| KML35736.1 | KML45672.1 | VL14_22625 | VL14_02735 | Quinol oxidase subunit 2; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. | Cytochrome Cbb3; Component of the menaquinol-cytochrome c reductase complex. | 0.975 |
| KML35736.1 | ctaA | VL14_22625 | VL14_22145 | Quinol oxidase subunit 2; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. | Heme A synthase; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group; Belongs to the COX15/CtaA family. Type 1 subfamily. | 0.711 |
| KML35994.1 | KML35736.1 | VL14_22155 | VL14_22625 | 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 2; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. | 0.811 |
| KML35994.1 | KML35998.1 | VL14_22155 | VL14_22175 | 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 assembly protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.979 |
| KML35994.1 | KML38858.1 | VL14_22155 | VL14_16885 | 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). | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.807 |
| KML35994.1 | KML39208.1 | VL14_22155 | VL14_16410 | 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). | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.807 |
| KML35994.1 | KML39825.1 | VL14_22155 | VL14_14945 | 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 II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.979 |
| KML35994.1 | KML42422.1 | VL14_22155 | VL14_08720 | 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). | Photosynthetic protein synthase I; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.915 |
| KML35994.1 | KML43348.1 | VL14_22155 | VL14_07175 | 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). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.945 |
| 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 | KML46675.1 | VL14_22155 | VL14_00375 | 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 B5; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.988 |
| KML35994.1 | ctaA | VL14_22155 | VL14_22145 | 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). | Heme A synthase; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group; Belongs to the COX15/CtaA family. Type 1 subfamily. | 0.969 |
| KML35998.1 | KML35994.1 | VL14_22175 | VL14_22155 | Cytochrome C oxidase assembly protein; 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). | 0.979 |
| KML35998.1 | KML39825.1 | VL14_22175 | VL14_14945 | Cytochrome C oxidase assembly protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.478 |
| KML35998.1 | KML42422.1 | VL14_22175 | VL14_08720 | Cytochrome C oxidase assembly protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Photosynthetic protein synthase I; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.831 |
