| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ANQ24353.1 | ANQ24354.1 | BA893_22370 | BA893_22375 | Cytochrome o ubiquinol oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| ANQ24353.1 | ANQ24355.1 | BA893_22370 | BA893_22380 | Cytochrome o ubiquinol oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome o ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | 0.997 |
| ANQ24353.1 | ANQ24525.1 | BA893_22370 | BA893_23300 | Cytochrome o ubiquinol oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c oxidase subunit I; 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. | 0.960 |
| ANQ24353.1 | ANQ24526.1 | BA893_22370 | BA893_23305 | Cytochrome o ubiquinol oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c 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). | 0.970 |
| ANQ24353.1 | ANQ24913.1 | BA893_22370 | BA893_22385 | Cytochrome o ubiquinol oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology. | Ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| ANQ24353.1 | cyoE | BA893_22370 | BA893_22365 | Cytochrome o ubiquinol oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology. | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.983 |
| ANQ24353.1 | cyoE-2 | BA893_22370 | BA893_23265 | Cytochrome o ubiquinol oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology. | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.844 |
| ANQ24354.1 | ANQ24353.1 | BA893_22375 | BA893_22370 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome o ubiquinol oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| ANQ24354.1 | ANQ24355.1 | BA893_22375 | BA893_22380 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome o ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | 0.998 |
| ANQ24354.1 | ANQ24525.1 | BA893_22375 | BA893_23300 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c oxidase subunit I; 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. | 0.989 |
| ANQ24354.1 | ANQ24526.1 | BA893_22375 | BA893_23305 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c 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). | 0.999 |
| ANQ24354.1 | ANQ24913.1 | BA893_22375 | BA893_22385 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |
| ANQ24354.1 | ANQ24921.1 | BA893_22375 | BA893_23295 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c oxidase assembly protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.636 |
| ANQ24354.1 | cyoE | BA893_22375 | BA893_22365 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.984 |
| ANQ24354.1 | cyoE-2 | BA893_22375 | BA893_23265 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.908 |
| ANQ24355.1 | ANQ24353.1 | BA893_22380 | BA893_22370 | Cytochrome o ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | Cytochrome o ubiquinol oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| ANQ24355.1 | ANQ24354.1 | BA893_22380 | BA893_22375 | Cytochrome o ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |
| ANQ24355.1 | ANQ24520.1 | BA893_22380 | BA893_23270 | Cytochrome o ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.455 |
| ANQ24355.1 | ANQ24526.1 | BA893_22380 | BA893_23305 | Cytochrome o ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | Cytochrome c 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). | 0.998 |
| ANQ24355.1 | ANQ24913.1 | BA893_22380 | BA893_22385 | Cytochrome o ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | Ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |