| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| XM1_3581 | birA | XM1_3581 | XM1_3583 | Putative hydrolase of the metallo-beta-lactamase superfamily; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Biotin--[acetyl-CoA-carboxylase] ligase; Function of strongly homologous gene; enzyme. | 0.906 |
| XM1_3581 | coaX | XM1_3581 | XM1_3582 | Putative hydrolase of the metallo-beta-lactamase superfamily; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Pantothenate kinase; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. | 0.828 |
| XM1_3581 | nuoG | XM1_3581 | XM1_3591 | Putative hydrolase of the metallo-beta-lactamase superfamily; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase 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. | 0.732 |
| XM1_3581 | nuoH | XM1_3581 | XM1_3590 | Putative hydrolase of the metallo-beta-lactamase superfamily; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH:ubiquinone oxidoreductase, membrane 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. | 0.732 |
| XM1_3581 | nuoI | XM1_3581 | XM1_3589 | Putative hydrolase of the metallo-beta-lactamase superfamily; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 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. | 0.749 |
| XM1_3581 | nuoJ | XM1_3581 | XM1_3588 | Putative hydrolase of the metallo-beta-lactamase superfamily; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase, subunit J; 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. | 0.763 |
| XM1_3581 | nuoK | XM1_3581 | XM1_3587 | Putative hydrolase of the metallo-beta-lactamase superfamily; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase subunit K; 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 subunit 4L family. | 0.763 |
| XM1_3581 | nuoL | XM1_3581 | XM1_3586 | Putative hydrolase of the metallo-beta-lactamase superfamily; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase subunit L; Function of strongly homologous gene; enzyme. | 0.767 |
| XM1_3581 | nuoM | XM1_3581 | XM1_3585 | Putative hydrolase of the metallo-beta-lactamase superfamily; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase subunit M; Function of strongly homologous gene; enzyme. | 0.796 |
| XM1_3581 | nuoN | XM1_3581 | XM1_3584 | Putative hydrolase of the metallo-beta-lactamase superfamily; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase subunit N; 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 subunit 2 family. | 0.821 |
| birA | XM1_3581 | XM1_3583 | XM1_3581 | Biotin--[acetyl-CoA-carboxylase] ligase; Function of strongly homologous gene; enzyme. | Putative hydrolase of the metallo-beta-lactamase superfamily; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.906 |
| birA | coaX | XM1_3583 | XM1_3582 | Biotin--[acetyl-CoA-carboxylase] ligase; Function of strongly homologous gene; enzyme. | Pantothenate kinase; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. | 0.893 |
| birA | nuoG | XM1_3583 | XM1_3591 | Biotin--[acetyl-CoA-carboxylase] ligase; Function of strongly homologous gene; enzyme. | NADH-quinone oxidoreductase 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. | 0.799 |
| birA | nuoH | XM1_3583 | XM1_3590 | Biotin--[acetyl-CoA-carboxylase] ligase; Function of strongly homologous gene; enzyme. | NADH:ubiquinone oxidoreductase, membrane 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. | 0.844 |
| birA | nuoI | XM1_3583 | XM1_3589 | Biotin--[acetyl-CoA-carboxylase] ligase; Function of strongly homologous gene; enzyme. | 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. | 0.782 |
| birA | nuoJ | XM1_3583 | XM1_3588 | Biotin--[acetyl-CoA-carboxylase] ligase; Function of strongly homologous gene; enzyme. | NADH-quinone oxidoreductase, subunit J; 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. | 0.837 |
| birA | nuoK | XM1_3583 | XM1_3587 | Biotin--[acetyl-CoA-carboxylase] ligase; Function of strongly homologous gene; enzyme. | NADH-quinone oxidoreductase subunit K; 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 subunit 4L family. | 0.774 |
| birA | nuoL | XM1_3583 | XM1_3586 | Biotin--[acetyl-CoA-carboxylase] ligase; Function of strongly homologous gene; enzyme. | NADH-quinone oxidoreductase subunit L; Function of strongly homologous gene; enzyme. | 0.844 |
| birA | nuoM | XM1_3583 | XM1_3585 | Biotin--[acetyl-CoA-carboxylase] ligase; Function of strongly homologous gene; enzyme. | NADH-quinone oxidoreductase subunit M; Function of strongly homologous gene; enzyme. | 0.903 |
| birA | nuoN | XM1_3583 | XM1_3584 | Biotin--[acetyl-CoA-carboxylase] ligase; Function of strongly homologous gene; enzyme. | NADH-quinone oxidoreductase subunit N; 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 subunit 2 family. | 0.874 |