| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PP_0550 | nuoA | PP_0550 | PP_4119 | Homologs of previously reported genes of unknown function. | NADH-quinone oxidoreductase subunit A; 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 3 family. | 0.938 |
| PP_0550 | nuoB | PP_0550 | PP_4120 | Homologs of previously reported genes of unknown function. | 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. | 0.981 |
| PP_0550 | nuoC | PP_0550 | PP_4121 | Homologs of previously reported genes of unknown function. | NADH-quinone oxidoreductase subunit C/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; In the N-terminal section; belongs to the complex I 30 kDa subunit family. | 0.999 |
| PP_0550 | nuoG | PP_0550 | PP_4124 | Homologs of previously reported genes of unknown function. | 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. 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 (By similarity). | 0.922 |
| PP_0550 | nuoH | PP_0550 | PP_4125 | Homologs of previously reported genes of unknown function. | NADH-quinone oxidoreductase 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. | 0.936 |
| PP_0550 | nuoM | PP_0550 | PP_4130 | Homologs of previously reported genes of unknown function. | NADH:ubiquinone oxidoreductase, membrane subunit M; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Energymetabolism : Aerobic. | 0.937 |
| PP_0550 | nuoN | PP_0550 | PP_4131 | Homologs of previously reported genes of unknown function. | 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. | 0.929 |
| PP_0550 | yfhL | PP_0550 | PP_5124 | Homologs of previously reported genes of unknown function. | Putative 4Fe-4S cluster-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; carrier; Energymetabolism : Electron transport. | 0.940 |
| mrpAB | nuoA | PP_2230 | PP_4119 | Putative K(+)/H(+) antiporter subunit A/B; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. | NADH-quinone oxidoreductase subunit A; 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 3 family. | 0.945 |
| mrpAB | nuoB | PP_2230 | PP_4120 | Putative K(+)/H(+) antiporter subunit A/B; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. | 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. | 0.977 |
| mrpAB | nuoC | PP_2230 | PP_4121 | Putative K(+)/H(+) antiporter subunit A/B; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. | NADH-quinone oxidoreductase subunit C/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; In the N-terminal section; belongs to the complex I 30 kDa subunit family. | 0.997 |
| mrpAB | nuoG | PP_2230 | PP_4124 | Putative K(+)/H(+) antiporter subunit A/B; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. | 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. 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 (By similarity). | 0.938 |
| mrpAB | nuoH | PP_2230 | PP_4125 | Putative K(+)/H(+) antiporter subunit A/B; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. | NADH-quinone oxidoreductase 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. | 0.963 |
| mrpAB | nuoJ | PP_2230 | PP_4127 | Putative K(+)/H(+) antiporter subunit A/B; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. | 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. | 0.954 |
| mrpAB | nuoM | PP_2230 | PP_4130 | Putative K(+)/H(+) antiporter subunit A/B; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. | NADH:ubiquinone oxidoreductase, membrane subunit M; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Energymetabolism : Aerobic. | 0.960 |
| mrpAB | nuoN | PP_2230 | PP_4131 | Putative K(+)/H(+) antiporter subunit A/B; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. | 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. | 0.960 |
| mrpAB | yfhL | PP_2230 | PP_5124 | Putative K(+)/H(+) antiporter subunit A/B; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. | Putative 4Fe-4S cluster-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; carrier; Energymetabolism : Electron transport. | 0.993 |
| nuoA | PP_0550 | PP_4119 | PP_0550 | NADH-quinone oxidoreductase subunit A; 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 3 family. | Homologs of previously reported genes of unknown function. | 0.938 |
| nuoA | mrpAB | PP_4119 | PP_2230 | NADH-quinone oxidoreductase subunit A; 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 3 family. | Putative K(+)/H(+) antiporter subunit A/B; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. | 0.945 |
| nuoA | nuoB | PP_4119 | PP_4120 | NADH-quinone oxidoreductase subunit A; 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 3 family. | 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. | 0.999 |