| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EAR49614.1 | EAR49631.1 | OG2516_04828 | OG2516_15119 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | Cytochrome c oxidase polypeptide II precursor (Cytochrome AA3 subunit 2); 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). | 0.991 |
| EAR49614.1 | EAR49635.1 | OG2516_04828 | OG2516_15139 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.999 |
| EAR49614.1 | EAR50022.1 | OG2516_04828 | OG2516_07465 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | Formate dehydrogenase, beta subunit; COG1905 NADH:ubiquinone oxidoreductase 24 kD subunit. | 0.999 |
| EAR49614.1 | EAR50420.1 | OG2516_04828 | OG2516_02853 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). | 0.998 |
| EAR49614.1 | EAR52050.1 | OG2516_04828 | OG2516_18335 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | 0.999 |
| EAR49614.1 | EAR52051.1 | OG2516_04828 | OG2516_18340 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | 0.961 |
| EAR49614.1 | EAR52299.1 | OG2516_04828 | OG2516_07477 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | Formate dehydrogenase, beta subunit; COG1894 NADH:ubiquinone oxidoreductase, NADH-binding (51 kD) subunit. | 0.999 |
| EAR49614.1 | EAR52909.1 | OG2516_04828 | OG2516_10616 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | Ubiquinol--cytochrome c reductase, 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. | 0.999 |
| EAR49614.1 | ctaB | OG2516_04828 | OG2516_15124 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. | 0.997 |
| EAR49614.1 | nuoH | OG2516_04828 | OG2516_02888 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | NADH dehydrogenase subunit H; 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. This subunit may bind ubiquinone. | 0.998 |
| EAR49631.1 | EAR49614.1 | OG2516_15119 | OG2516_04828 | Cytochrome c oxidase polypeptide II precursor (Cytochrome AA3 subunit 2); 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). | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | 0.991 |
| EAR49631.1 | EAR49635.1 | OG2516_15119 | OG2516_15139 | Cytochrome c oxidase polypeptide II precursor (Cytochrome AA3 subunit 2); 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). | COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.999 |
| EAR49631.1 | EAR50022.1 | OG2516_15119 | OG2516_07465 | Cytochrome c oxidase polypeptide II precursor (Cytochrome AA3 subunit 2); 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). | Formate dehydrogenase, beta subunit; COG1905 NADH:ubiquinone oxidoreductase 24 kD subunit. | 0.977 |
| EAR49631.1 | EAR50420.1 | OG2516_15119 | OG2516_02853 | Cytochrome c oxidase polypeptide II precursor (Cytochrome AA3 subunit 2); 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). | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). | 0.977 |
| EAR49631.1 | EAR52050.1 | OG2516_15119 | OG2516_18335 | Cytochrome c oxidase polypeptide II precursor (Cytochrome AA3 subunit 2); 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). | COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. | 0.999 |
| EAR49631.1 | EAR52051.1 | OG2516_15119 | OG2516_18340 | Cytochrome c oxidase polypeptide II precursor (Cytochrome AA3 subunit 2); 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). | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | 0.885 |
| EAR49631.1 | EAR52299.1 | OG2516_15119 | OG2516_07477 | Cytochrome c oxidase polypeptide II precursor (Cytochrome AA3 subunit 2); 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). | Formate dehydrogenase, beta subunit; COG1894 NADH:ubiquinone oxidoreductase, NADH-binding (51 kD) subunit. | 0.977 |
| EAR49631.1 | EAR52909.1 | OG2516_15119 | OG2516_10616 | Cytochrome c oxidase polypeptide II precursor (Cytochrome AA3 subunit 2); 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). | Ubiquinol--cytochrome c reductase, 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 |
| EAR49631.1 | ctaB | OG2516_15119 | OG2516_15124 | Cytochrome c oxidase polypeptide II precursor (Cytochrome AA3 subunit 2); 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). | 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; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. | 0.999 |
| EAR49631.1 | nuoH | OG2516_15119 | OG2516_02888 | Cytochrome c oxidase polypeptide II precursor (Cytochrome AA3 subunit 2); 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 subunit H; 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. This subunit may bind ubiquinone. | 0.977 |