| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RPA0135 | RPA1193 | RPA0135 | RPA1193 | Possible oxidoreductase. | Cytochrome b/c1 precursor; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.918 |
| RPA0135 | RPA2985 | RPA0135 | RPA2985 | Possible oxidoreductase. | Conserved unknownl protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.726 |
| RPA0135 | fdsB | RPA0135 | RPA0733 | Possible oxidoreductase. | NAD-dependent formate dehydrogenase beta subunit. | 0.939 |
| RPA0135 | nuoB1 | RPA0135 | RPA2951 | Possible oxidoreductase. | NADH-ubiquinone dehydrogenase chain 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. | 0.937 |
| RPA0135 | nuoB2 | RPA0135 | RPA4263 | Possible oxidoreductase. | NADH-ubiquinone dehydrogenase chain 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. | 0.937 |
| RPA0135 | nuoC | RPA0135 | RPA2950 | Possible oxidoreductase. | NADH-ubiquinone dehydrogenase chain 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. | 0.946 |
| RPA0135 | nuoCD | RPA0135 | RPA4262 | Possible oxidoreductase. | NADH-ubiquinone dehydrogenase chain 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. | 0.998 |
| RPA0135 | nuoD | RPA0135 | RPA2949 | Possible oxidoreductase. | NADH-ubiquinone dehydrogenase chain 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. | 0.945 |
| RPA0135 | nuoG1 | RPA0135 | RPA2944 | Possible oxidoreductase. | NADH-ubiquinone dehydrogenase chain 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. | 0.953 |
| RPA0135 | nuoG2 | RPA0135 | RPA4259 | Possible oxidoreductase. | NADH-ubiquinone dehydrogenase chain G; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.942 |
| RPA1193 | RPA0135 | RPA1193 | RPA0135 | Cytochrome b/c1 precursor; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | Possible oxidoreductase. | 0.918 |
| RPA1193 | RPA2985 | RPA1193 | RPA2985 | Cytochrome b/c1 precursor; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | Conserved unknownl protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.853 |
| RPA1193 | fdsB | RPA1193 | RPA0733 | Cytochrome b/c1 precursor; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | NAD-dependent formate dehydrogenase beta subunit. | 0.912 |
| RPA1193 | nuoB1 | RPA1193 | RPA2951 | Cytochrome b/c1 precursor; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | NADH-ubiquinone dehydrogenase chain 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. | 0.931 |
| RPA1193 | nuoB2 | RPA1193 | RPA4263 | Cytochrome b/c1 precursor; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | NADH-ubiquinone dehydrogenase chain 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. | 0.931 |
| RPA1193 | nuoC | RPA1193 | RPA2950 | Cytochrome b/c1 precursor; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | NADH-ubiquinone dehydrogenase chain 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. | 0.950 |
| RPA1193 | nuoCD | RPA1193 | RPA4262 | Cytochrome b/c1 precursor; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | NADH-ubiquinone dehydrogenase chain 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. | 0.996 |
| RPA1193 | nuoD | RPA1193 | RPA2949 | Cytochrome b/c1 precursor; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | NADH-ubiquinone dehydrogenase chain 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. | 0.955 |
| RPA1193 | nuoG1 | RPA1193 | RPA2944 | Cytochrome b/c1 precursor; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | NADH-ubiquinone dehydrogenase chain 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. | 0.953 |
| RPA1193 | nuoG2 | RPA1193 | RPA4259 | Cytochrome b/c1 precursor; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | NADH-ubiquinone dehydrogenase chain G; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.953 |
