| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BVIR_331 | mhqO | BVIR_331 | BVIR_1411 | 2'-N-acetylparomamine deacetylase. | Putative ring-cleaving dioxygenase MhqO. | 0.572 |
| lgrD_1 | mhqO | BVIR_2860 | BVIR_1411 | Carboxylic acid reductase. | Putative ring-cleaving dioxygenase MhqO. | 0.556 |
| lgrD_1 | nuoD | BVIR_2860 | BVIR_1320 | Carboxylic acid reductase. | 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 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; Belongs to the complex I 49 kDa subunit family. | 0.789 |
| lgrD_1 | nuoI | BVIR_2860 | BVIR_1328 | Carboxylic acid reductase. | 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. | 0.829 |
| lgrD_1 | polA_1 | BVIR_2860 | BVIR_2749 | Carboxylic acid reductase. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.714 |
| mhpD | mhqO | BVIR_1068 | BVIR_1411 | 2-keto-4-pentenoate hydratase. | Putative ring-cleaving dioxygenase MhqO. | 0.545 |
| mhqO | BVIR_331 | BVIR_1411 | BVIR_331 | Putative ring-cleaving dioxygenase MhqO. | 2'-N-acetylparomamine deacetylase. | 0.572 |
| mhqO | lgrD_1 | BVIR_1411 | BVIR_2860 | Putative ring-cleaving dioxygenase MhqO. | Carboxylic acid reductase. | 0.556 |
| mhqO | mhpD | BVIR_1411 | BVIR_1068 | Putative ring-cleaving dioxygenase MhqO. | 2-keto-4-pentenoate hydratase. | 0.545 |
| mhqO | nox | BVIR_1411 | BVIR_899 | Putative ring-cleaving dioxygenase MhqO. | 5,6-dimethylbenzimidazole synthase. | 0.597 |
| mhqO | nuoD | BVIR_1411 | BVIR_1320 | Putative ring-cleaving dioxygenase MhqO. | 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 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; Belongs to the complex I 49 kDa subunit family. | 0.637 |
| mhqO | nuoI | BVIR_1411 | BVIR_1328 | Putative ring-cleaving dioxygenase MhqO. | 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. | 0.718 |
| mhqO | polA_1 | BVIR_1411 | BVIR_2749 | Putative ring-cleaving dioxygenase MhqO. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.558 |
| mhqO | proA_1 | BVIR_1411 | BVIR_644 | Putative ring-cleaving dioxygenase MhqO. | 4-hydroxy-4-methyl-2-oxoglutarate aldolase. | 0.630 |
| mhqO | sdhC | BVIR_1411 | BVIR_2658 | Putative ring-cleaving dioxygenase MhqO. | Succinate dehydrogenase cytochrome b556 subunit. | 0.638 |
| mhqO | ydjA | BVIR_1411 | BVIR_1771 | Putative ring-cleaving dioxygenase MhqO. | Putative NAD(P)H nitroreductase YdjA. | 0.597 |
| nox | mhqO | BVIR_899 | BVIR_1411 | 5,6-dimethylbenzimidazole synthase. | Putative ring-cleaving dioxygenase MhqO. | 0.597 |
| nuoD | lgrD_1 | BVIR_1320 | BVIR_2860 | 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 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; Belongs to the complex I 49 kDa subunit family. | Carboxylic acid reductase. | 0.789 |
| nuoD | mhqO | BVIR_1320 | BVIR_1411 | 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 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; Belongs to the complex I 49 kDa subunit family. | Putative ring-cleaving dioxygenase MhqO. | 0.637 |
| nuoD | nuoI | BVIR_1320 | BVIR_1328 | 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 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; Belongs to the complex I 49 kDa subunit 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. | 0.999 |