| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KZE44613.1 | KZE48147.1 | AV540_23550 | AV540_00880 | 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 C551; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KZE44613.1 | KZE53054.1 | AV540_23550 | AV540_08325 | 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). | Zinc protease; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KZE44613.1 | KZE53055.1 | AV540_23550 | AV540_08330 | 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). | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KZE44613.1 | KZE55489.1 | AV540_23550 | AV540_05395 | 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 |
| KZE44613.1 | cyoC_2 | AV540_23550 | AV540_00865 | 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. | 0.999 |
| KZE44613.1 | qcrA | AV540_23550 | AV540_05390 | 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. | 0.999 |
| KZE44613.1 | qcrC | AV540_23550 | AV540_05400 | 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 Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KZE44613.1 | qoxB_2 | AV540_23550 | AV540_00860 | 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 ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KZE44613.1 | sdhB | AV540_23550 | AV540_06475 | 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). | Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KZE44613.1 | sdhC | AV540_23550 | AV540_06485 | 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). | Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KZE48147.1 | KZE44613.1 | AV540_00880 | AV540_23550 | Cytochrome C551; 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). | 0.999 |
| KZE48147.1 | KZE55489.1 | AV540_00880 | AV540_05395 | Cytochrome C551; 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. | 0.986 |
| KZE48147.1 | cyoC_2 | AV540_00880 | AV540_00865 | Cytochrome C551; 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. | 0.981 |
| KZE48147.1 | qcrA | AV540_00880 | AV540_05390 | Cytochrome C551; 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. | 0.991 |
| KZE48147.1 | qcrC | AV540_00880 | AV540_05400 | Cytochrome C551; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C oxidase Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.980 |
| KZE48147.1 | qoxB_2 | AV540_00880 | AV540_00860 | Cytochrome C551; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.957 |
| KZE48147.1 | sdhB | AV540_00880 | AV540_06475 | Cytochrome C551; Derived by automated computational analysis using gene prediction method: Protein Homology. | Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.879 |
| KZE48147.1 | sdhC | AV540_00880 | AV540_06485 | Cytochrome C551; Derived by automated computational analysis using gene prediction method: Protein Homology. | Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.655 |
| KZE53054.1 | KZE44613.1 | AV540_08325 | AV540_23550 | Zinc protease; 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). | 0.999 |
| KZE53054.1 | KZE53055.1 | AV540_08325 | AV540_08330 | Zinc protease; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.994 |
STRING v12.5 is now available!
