| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AMY55899.1 | ctaD_1 | A3L23_04596 | A3L23_04774 | Putative zinc protease; Belongs to the peptidase M16 family. | Putative cytochrome c oxidase subunit 1; 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. | 0.829 |
| AMY55899.1 | ctaE | A3L23_04596 | A3L23_03908 | Putative zinc protease; Belongs to the peptidase M16 family. | Putative cytochrome c oxidase subunit 3. | 0.834 |
| AMY55899.1 | nuoC | A3L23_04596 | A3L23_04582 | Putative zinc protease; Belongs to the peptidase M16 family. | 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. | 0.919 |
| AMY55899.1 | nuoD | A3L23_04596 | A3L23_04581 | Putative zinc protease; Belongs to the peptidase M16 family. | NADH-quinone oxidoreductase subunit D; 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. | 0.925 |
| AMY55899.1 | nuoE | A3L23_04596 | A3L23_04580 | Putative zinc protease; Belongs to the peptidase M16 family. | NADH-quinone oxidoreductase subunit E. | 0.921 |
| AMY55899.1 | nuoI | A3L23_04596 | A3L23_04576 | Putative zinc protease; Belongs to the peptidase M16 family. | 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. | 0.931 |
| AMY55899.1 | petC1 | A3L23_04596 | A3L23_00439 | Putative zinc protease; Belongs to the peptidase M16 family. | Cytochrome b6-f complex iron-sulfur subunit 1. | 0.945 |
| AMY55899.1 | qcrB | A3L23_04596 | A3L23_03905 | Putative zinc protease; Belongs to the peptidase M16 family. | Ubiquinol-cytochrome c reductase cytochrome b subunit. | 0.944 |
| AMY55899.1 | sdhA | A3L23_04596 | A3L23_00132 | Putative zinc protease; Belongs to the peptidase M16 family. | Succinate dehydrogenase flavoprotein subunit. | 0.851 |
| ctaD_1 | AMY55899.1 | A3L23_04774 | A3L23_04596 | Putative cytochrome c oxidase subunit 1; 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. | Putative zinc protease; Belongs to the peptidase M16 family. | 0.829 |
| ctaD_1 | ctaE | A3L23_04774 | A3L23_03908 | Putative cytochrome c oxidase subunit 1; 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. | Putative cytochrome c oxidase subunit 3. | 0.999 |
| ctaD_1 | nuoC | A3L23_04774 | A3L23_04582 | Putative cytochrome c oxidase subunit 1; 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. | 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. | 0.889 |
| ctaD_1 | nuoD | A3L23_04774 | A3L23_04581 | Putative cytochrome c oxidase subunit 1; 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. | NADH-quinone oxidoreductase subunit D; 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. | 0.890 |
| ctaD_1 | nuoE | A3L23_04774 | A3L23_04580 | Putative cytochrome c oxidase subunit 1; 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. | NADH-quinone oxidoreductase subunit E. | 0.878 |
| ctaD_1 | nuoI | A3L23_04774 | A3L23_04576 | Putative cytochrome c oxidase subunit 1; 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. | 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. | 0.843 |
| ctaD_1 | petC1 | A3L23_04774 | A3L23_00439 | Putative cytochrome c oxidase subunit 1; 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. | Cytochrome b6-f complex iron-sulfur subunit 1. | 0.940 |
| ctaD_1 | qcrB | A3L23_04774 | A3L23_03905 | Putative cytochrome c oxidase subunit 1; 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. | Ubiquinol-cytochrome c reductase cytochrome b subunit. | 0.998 |
| ctaD_1 | qcrC | A3L23_04774 | A3L23_03907 | Putative cytochrome c oxidase subunit 1; 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. | Ubiquinol-cytochrome c reductase cytochrome c subunit. | 0.991 |
| ctaD_1 | sdhA | A3L23_04774 | A3L23_00132 | Putative cytochrome c oxidase subunit 1; 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. | Succinate dehydrogenase flavoprotein subunit. | 0.696 |
| ctaE | AMY55899.1 | A3L23_03908 | A3L23_04596 | Putative cytochrome c oxidase subunit 3. | Putative zinc protease; Belongs to the peptidase M16 family. | 0.834 |