| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AJC20353.1 | AJC23033.1 | RO07_07500 | RO07_03675 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.910 |
| AJC20353.1 | AJC23366.1 | RO07_07500 | RO07_14975 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.910 |
| AJC23033.1 | AJC20353.1 | RO07_03675 | RO07_07500 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.910 |
| AJC23033.1 | AJC23366.1 | RO07_03675 | RO07_14975 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.910 |
| AJC23033.1 | ctaC_1 | RO07_03675 | RO07_11010 | 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). | 0.914 |
| AJC23033.1 | fbcH | RO07_03675 | RO07_06435 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.934 |
| AJC23033.1 | nqo2_2 | RO07_03675 | RO07_17995 | Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH-quinone oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.845 |
| AJC23033.1 | nqo3 | RO07_03675 | RO07_18005 | Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH-quinone oxidoreductase subunit G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family. | 0.833 |
| AJC23033.1 | nuoD | RO07_03675 | RO07_17990 | 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 ubiquinone. 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. | 0.881 |
| AJC23033.1 | nuoI | RO07_03675 | RO07_18015 | Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH-quinone oxidoreductase subunit I; 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 ubiquinone. 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. | 0.918 |
| AJC23033.1 | petA | RO07_03675 | RO07_06440 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Ubiquinol-cytochrome c reductase iron-sulfur subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.987 |
| AJC23033.1 | petC | RO07_03675 | RO07_06430 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.955 |
| AJC23366.1 | AJC20353.1 | RO07_14975 | RO07_07500 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.910 |
| AJC23366.1 | AJC23033.1 | RO07_14975 | RO07_03675 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.910 |
| ctaC_1 | AJC23033.1 | RO07_11010 | RO07_03675 | 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). | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.914 |
| ctaC_1 | fbcH | RO07_11010 | RO07_06435 | 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). | Cytochrome B; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.998 |
| ctaC_1 | nqo2_2 | RO07_11010 | RO07_17995 | 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). | NADH-quinone oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.849 |
| ctaC_1 | nqo3 | RO07_11010 | RO07_18005 | 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). | NADH-quinone oxidoreductase subunit G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family. | 0.819 |
| ctaC_1 | nuoD | RO07_11010 | RO07_17990 | 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). | 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 ubiquinone. 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. | 0.945 |
| ctaC_1 | nuoI | RO07_11010 | RO07_18015 | 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). | NADH-quinone oxidoreductase subunit I; 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 ubiquinone. 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. | 0.918 |
