| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| acpP | ctaC | RMONA_00595 | RMONA_05015 | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | Cytochrome c oxidase subunit 2 precursor; 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). | 0.758 |
| acpP | ctaE | RMONA_00595 | RMONA_00660 | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | Cytochrome c oxidase subunit 3. | 0.759 |
| acpP | nqo2 | RMONA_00595 | RMONA_05430 | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | NADH-quinone oxidoreductase chain 2. | 0.999 |
| acpP | nqo3 | RMONA_00595 | RMONA_01030 | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | NADH-quinone oxidoreductase chain 3; 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. | 0.999 |
| acpP | nuoF | RMONA_00595 | RMONA_02860 | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | NADH-quinone oxidoreductase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | 0.999 |
| acpP | nuoI | RMONA_00595 | RMONA_01020 | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 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. | 0.999 |
| acpP | petA | RMONA_00595 | RMONA_04230 | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 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. | 0.996 |
| acpP | petB | RMONA_00595 | RMONA_04235 | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 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. | 0.919 |
| acpP | petC | RMONA_00595 | RMONA_04245 | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | Cytochrome c1 precursor. | 0.996 |
| acpP | ptrA | RMONA_00595 | RMONA_00260 | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | Protease 3 precursor; Belongs to the peptidase M16 family. | 0.971 |
| ctaC | acpP | RMONA_05015 | RMONA_00595 | Cytochrome c oxidase subunit 2 precursor; 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). | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.758 |
| ctaC | ctaE | RMONA_05015 | RMONA_00660 | Cytochrome c oxidase subunit 2 precursor; 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 c oxidase subunit 3. | 0.999 |
| ctaC | nqo2 | RMONA_05015 | RMONA_05430 | Cytochrome c oxidase subunit 2 precursor; 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 chain 2. | 0.837 |
| ctaC | nqo3 | RMONA_05015 | RMONA_01030 | Cytochrome c oxidase subunit 2 precursor; 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 chain 3; 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. | 0.821 |
| ctaC | nuoF | RMONA_05015 | RMONA_02860 | Cytochrome c oxidase subunit 2 precursor; 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 F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | 0.823 |
| ctaC | nuoI | RMONA_05015 | RMONA_01020 | Cytochrome c oxidase subunit 2 precursor; 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. | 0.796 |
| ctaC | petA | RMONA_05015 | RMONA_04230 | Cytochrome c oxidase subunit 2 precursor; 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 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. | 0.999 |
| ctaC | petB | RMONA_05015 | RMONA_04235 | Cytochrome c oxidase subunit 2 precursor; 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. | 0.999 |
| ctaC | petC | RMONA_05015 | RMONA_04245 | Cytochrome c oxidase subunit 2 precursor; 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 c1 precursor. | 0.999 |
| ctaC | ptrA | RMONA_05015 | RMONA_00260 | Cytochrome c oxidase subunit 2 precursor; 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). | Protease 3 precursor; Belongs to the peptidase M16 family. | 0.986 |