| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ACPL_1643 | ctaB | ACPL_1643 | ACPL_1866 | Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. | 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. | 0.947 |
| ACPL_1643 | ctaC | ACPL_1643 | ACPL_1642 | Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF 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). | 0.999 |
| ACPL_1643 | ctaD-3 | ACPL_1643 | ACPL_2710 | Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. | 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. | 0.990 |
| ACPL_1643 | ctaE | ACPL_1643 | ACPL_1648 | Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. | Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.998 |
| ACPL_1643 | qcrA | ACPL_1643 | ACPL_1650 | Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. | Putative menaquinol-cytochrome c reductase iron-sulfur subunit; Rieske Fe-S protein. | 0.992 |
| ACPL_1643 | qcrB | ACPL_1643 | ACPL_1651 | Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. | Cytochrome b subunit of the bc complex. | 0.996 |
| ACPL_1643 | qcrC | ACPL_1643 | ACPL_1649 | Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. | Cytochrome c, mono- and diheme variants. | 0.991 |
| ACPL_746 | ACPL_7851 | ACPL_746 | ACPL_7851 | NADH:ubiquinone oxidoreductase subunit 4 (chain M). | NADH dehydrogenase I subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. | 0.994 |
| ACPL_746 | ctaC | ACPL_746 | ACPL_1642 | NADH:ubiquinone oxidoreductase subunit 4 (chain M). | 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). | 0.966 |
| ACPL_746 | ctaD-3 | ACPL_746 | ACPL_2710 | NADH:ubiquinone oxidoreductase subunit 4 (chain M). | 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. | 0.924 |
| ACPL_746 | ctaE | ACPL_746 | ACPL_1648 | NADH:ubiquinone oxidoreductase subunit 4 (chain M). | Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.971 |
| ACPL_746 | nuoA | ACPL_746 | ACPL_445 | NADH:ubiquinone oxidoreductase subunit 4 (chain M). | NADH dehydrogenase I subunit A; 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 subunit 3 family. | 0.995 |
| ACPL_746 | qcrA | ACPL_746 | ACPL_1650 | NADH:ubiquinone oxidoreductase subunit 4 (chain M). | Putative menaquinol-cytochrome c reductase iron-sulfur subunit; Rieske Fe-S protein. | 0.781 |
| ACPL_746 | qcrB | ACPL_746 | ACPL_1651 | NADH:ubiquinone oxidoreductase subunit 4 (chain M). | Cytochrome b subunit of the bc complex. | 0.986 |
| ACPL_746 | qcrC | ACPL_746 | ACPL_1649 | NADH:ubiquinone oxidoreductase subunit 4 (chain M). | Cytochrome c, mono- and diheme variants. | 0.739 |
| ACPL_7851 | ACPL_746 | ACPL_7851 | ACPL_746 | NADH dehydrogenase I subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. | NADH:ubiquinone oxidoreductase subunit 4 (chain M). | 0.994 |
| ACPL_7851 | ctaC | ACPL_7851 | ACPL_1642 | NADH dehydrogenase I subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. | 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). | 0.965 |
| ACPL_7851 | ctaD-3 | ACPL_7851 | ACPL_2710 | NADH dehydrogenase I subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. | 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. | 0.935 |
| ACPL_7851 | ctaE | ACPL_7851 | ACPL_1648 | NADH dehydrogenase I subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. | Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.962 |
| ACPL_7851 | nuoA | ACPL_7851 | ACPL_445 | NADH dehydrogenase I subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. | NADH dehydrogenase I subunit A; 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 subunit 3 family. | 0.983 |