| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KNB69851.1 | KNB69853.1 | ADS79_28860 | ADS79_28870 | Cytochrome B oxidoreductase; 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 |
| KNB69851.1 | KNB70045.1 | ADS79_28860 | ADS79_29970 | Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.941 |
| KNB69851.1 | KNB71056.1 | ADS79_28860 | ADS79_19725 | Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.967 |
| KNB69851.1 | KNB71057.1 | ADS79_28860 | ADS79_19730 | Cytochrome B oxidoreductase; 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. | 0.982 |
| KNB69851.1 | KNB71058.1 | ADS79_28860 | ADS79_19735 | Cytochrome B oxidoreductase; 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. | 0.993 |
| KNB69851.1 | KNB71920.1 | ADS79_28860 | ADS79_24570 | Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.942 |
| KNB69851.1 | KNB73021.1 | ADS79_28860 | ADS79_12205 | Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C551; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.941 |
| KNB69851.1 | nuoC | ADS79_28860 | ADS79_24135 | Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.943 |
| KNB69851.1 | nuoD | ADS79_28860 | ADS79_24140 | Cytochrome B oxidoreductase; 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. | 0.960 |
| KNB69851.1 | sdhB | ADS79_28860 | ADS79_07280 | Cytochrome B oxidoreductase; 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. | 0.956 |
| KNB69853.1 | KNB69851.1 | ADS79_28870 | ADS79_28860 | 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 |
| KNB69853.1 | KNB70045.1 | ADS79_28870 | ADS79_29970 | 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). | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.993 |
| KNB69853.1 | KNB71056.1 | ADS79_28870 | ADS79_19725 | 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KNB69853.1 | KNB71057.1 | ADS79_28870 | ADS79_19730 | 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 |
| KNB69853.1 | KNB71058.1 | ADS79_28870 | ADS79_19735 | 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 |
| KNB69853.1 | KNB71920.1 | ADS79_28870 | ADS79_24570 | 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). | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.993 |
| KNB69853.1 | KNB73021.1 | ADS79_28870 | ADS79_12205 | 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. | 0.993 |
| KNB69853.1 | nuoC | ADS79_28870 | ADS79_24135 | 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; 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 |
| KNB69853.1 | nuoD | ADS79_28870 | ADS79_24140 | 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. | 0.999 |
| KNB69853.1 | sdhB | ADS79_28870 | ADS79_07280 | 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. | 0.997 |
