| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RMCC_0584 | RMCC_2520 | RMCC_0584 | RMCC_2520 | NADH-quinone oxidoreductase subunit F. | Fatty acyl-CoA synthetase. | 0.799 |
| RMCC_0584 | RMCC_2601 | RMCC_0584 | RMCC_2601 | NADH-quinone oxidoreductase subunit F. | Alpha/beta hydrolase fold protein. | 0.771 |
| RMCC_0584 | RMCC_3174 | RMCC_0584 | RMCC_3174 | NADH-quinone oxidoreductase subunit F. | NADH dehydrogenase subunit E. | 0.999 |
| RMCC_0584 | RMCC_3176 | RMCC_0584 | RMCC_3176 | NADH-quinone oxidoreductase subunit F. | NADH dehydrogenase 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. | 0.998 |
| RMCC_0584 | RMCC_6601 | RMCC_0584 | RMCC_6601 | NADH-quinone oxidoreductase subunit F. | Beta-ketoacyl synthase. | 0.837 |
| RMCC_0584 | nuoB | RMCC_0584 | RMCC_3171 | NADH-quinone oxidoreductase subunit F. | NADH dehydrogenase subunit B; 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. | 0.994 |
| RMCC_0584 | nuoD | RMCC_0584 | RMCC_3173 | NADH-quinone oxidoreductase subunit F. | NADH dehydrogenase 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. | 0.995 |
| RMCC_0584 | nuoI | RMCC_0584 | RMCC_3178 | NADH-quinone oxidoreductase subunit F. | NADH dehydrogenase 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. | 0.996 |
| RMCC_0584 | pks5-2 | RMCC_0584 | RMCC_1121 | NADH-quinone oxidoreductase subunit F. | Polyketide synthase pks5. | 0.837 |
| RMCC_2520 | RMCC_0584 | RMCC_2520 | RMCC_0584 | Fatty acyl-CoA synthetase. | NADH-quinone oxidoreductase subunit F. | 0.799 |
| RMCC_2520 | RMCC_2601 | RMCC_2520 | RMCC_2601 | Fatty acyl-CoA synthetase. | Alpha/beta hydrolase fold protein. | 0.847 |
| RMCC_2520 | RMCC_3174 | RMCC_2520 | RMCC_3174 | Fatty acyl-CoA synthetase. | NADH dehydrogenase subunit E. | 0.899 |
| RMCC_2520 | RMCC_3175 | RMCC_2520 | RMCC_3175 | Fatty acyl-CoA synthetase. | NADH dehydrogenase I chain F nuoF; 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. | 0.799 |
| RMCC_2520 | RMCC_3176 | RMCC_2520 | RMCC_3176 | Fatty acyl-CoA synthetase. | NADH dehydrogenase 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. | 0.918 |
| RMCC_2520 | RMCC_6601 | RMCC_2520 | RMCC_6601 | Fatty acyl-CoA synthetase. | Beta-ketoacyl synthase. | 0.997 |
| RMCC_2520 | nuoB | RMCC_2520 | RMCC_3171 | Fatty acyl-CoA synthetase. | NADH dehydrogenase subunit B; 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. | 0.923 |
| RMCC_2520 | nuoD | RMCC_2520 | RMCC_3173 | Fatty acyl-CoA synthetase. | NADH dehydrogenase 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. | 0.899 |
| RMCC_2520 | nuoI | RMCC_2520 | RMCC_3178 | Fatty acyl-CoA synthetase. | NADH dehydrogenase 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. | 0.922 |
| RMCC_2520 | pks5-2 | RMCC_2520 | RMCC_1121 | Fatty acyl-CoA synthetase. | Polyketide synthase pks5. | 0.997 |
| RMCC_2601 | RMCC_0584 | RMCC_2601 | RMCC_0584 | Alpha/beta hydrolase fold protein. | NADH-quinone oxidoreductase subunit F. | 0.771 |