| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| NIDE1742 | NIDE3598 | NIDE1742 | NIDE3598 | Putative Multi-domain non-ribosomal peptide synthetase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative Oxidoreductase, NmrA-like; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.937 |
| NIDE1742 | nuoB | NIDE1742 | NIDE0235 | Putative Multi-domain non-ribosomal peptide synthetase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase, 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 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. | 0.831 |
| NIDE1742 | nuoB-2 | NIDE1742 | NIDE0614 | Putative Multi-domain non-ribosomal peptide synthetase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase, 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 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. | 0.831 |
| NIDE1742 | nuoC | NIDE1742 | NIDE0234 | Putative Multi-domain non-ribosomal peptide synthetase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase, subunit C; 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 30 kDa subunit family. | 0.800 |
| NIDE1742 | nuoCD | NIDE1742 | NIDE0613 | Putative Multi-domain non-ribosomal peptide synthetase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase, subunits C and D; Function of homologous gene experimentally demonstrated in an other organism; enzyme; In the N-terminal section; belongs to the complex I 30 kDa subunit family. | 0.994 |
| NIDE1742 | nuoD | NIDE1742 | NIDE0233 | Putative Multi-domain non-ribosomal peptide synthetase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 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. | 0.689 |
| NIDE1742 | nuoH | NIDE1742 | NIDE0608 | Putative Multi-domain non-ribosomal peptide synthetase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone 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. | 0.893 |
| NIDE1742 | nuoI | NIDE1742 | NIDE0231 | Putative Multi-domain non-ribosomal peptide synthetase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase, subunit I (modular protein); 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. | 0.935 |
| NIDE1742 | nuoI-2 | NIDE1742 | NIDE0607 | Putative Multi-domain non-ribosomal peptide synthetase; 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. | 0.935 |
| NIDE1742 | yfhL | NIDE1742 | NIDE4140 | Putative Multi-domain non-ribosomal peptide synthetase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 4Fe-4S ferredoxin; Function of strongly homologous gene; carrier. | 0.935 |
| NIDE3598 | NIDE1742 | NIDE3598 | NIDE1742 | Putative Oxidoreductase, NmrA-like; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative Multi-domain non-ribosomal peptide synthetase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.937 |
| NIDE3598 | nuoB | NIDE3598 | NIDE0235 | Putative Oxidoreductase, NmrA-like; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase, 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 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. | 0.962 |
| NIDE3598 | nuoB-2 | NIDE3598 | NIDE0614 | Putative Oxidoreductase, NmrA-like; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase, 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 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. | 0.962 |
| NIDE3598 | nuoC | NIDE3598 | NIDE0234 | Putative Oxidoreductase, NmrA-like; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase, subunit C; 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 30 kDa subunit family. | 0.978 |
| NIDE3598 | nuoCD | NIDE3598 | NIDE0613 | Putative Oxidoreductase, NmrA-like; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase, subunits C and D; Function of homologous gene experimentally demonstrated in an other organism; enzyme; In the N-terminal section; belongs to the complex I 30 kDa subunit family. | 0.999 |
| NIDE3598 | nuoD | NIDE3598 | NIDE0233 | Putative Oxidoreductase, NmrA-like; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 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. | 0.968 |
| NIDE3598 | nuoH | NIDE3598 | NIDE0608 | Putative Oxidoreductase, NmrA-like; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone 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. | 0.947 |
| NIDE3598 | nuoI | NIDE3598 | NIDE0231 | Putative Oxidoreductase, NmrA-like; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | NADH-quinone oxidoreductase, subunit I (modular protein); 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. | 0.962 |
| NIDE3598 | nuoI-2 | NIDE3598 | NIDE0607 | Putative Oxidoreductase, NmrA-like; 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. | 0.962 |
| NIDE3598 | yfhL | NIDE3598 | NIDE4140 | Putative Oxidoreductase, NmrA-like; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 4Fe-4S ferredoxin; Function of strongly homologous gene; carrier. | 0.962 |