| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| badB | nuoCD | RPA0662 | RPA4262 | Ferredoxin. | 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. | 0.997 |
| badB | phaA | RPA0662 | RPA2789 | Ferredoxin. | pH adaptation potassium efflux system components phaA and phaB; Citation: Putkorny et al. (1998) Mol. Microbiol. 28:1091-1101. | 0.980 |
| badB | phaD | RPA0662 | RPA2791 | Ferredoxin. | Putative component of pH adaptation K-efflux system phaD; Citation: Putkorny et al. (1998) Mol. Microbiol. 28:1091-1101. | 0.433 |
| fdxB | nuoCD | RPA4612 | RPA4262 | Ferredoxin 2[4Fe-4S] III, fdxB; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 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. | 0.997 |
| fdxB | phaA | RPA4612 | RPA2789 | Ferredoxin 2[4Fe-4S] III, fdxB; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | pH adaptation potassium efflux system components phaA and phaB; Citation: Putkorny et al. (1998) Mol. Microbiol. 28:1091-1101. | 0.980 |
| fdxB | phaD | RPA4612 | RPA2791 | Ferredoxin 2[4Fe-4S] III, fdxB; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative component of pH adaptation K-efflux system phaD; Citation: Putkorny et al. (1998) Mol. Microbiol. 28:1091-1101. | 0.433 |
| nuoCD | badB | RPA4262 | RPA0662 | 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. | Ferredoxin. | 0.997 |
| nuoCD | fdxB | RPA4262 | RPA4612 | 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. | Ferredoxin 2[4Fe-4S] III, fdxB; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.997 |
| nuoCD | nuoI1 | RPA4262 | RPA2942 | 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. | NADH-ubiquinone dehydrogenase chain 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. | 0.998 |
| nuoCD | nuoI2 | RPA4262 | RPA4257 | 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. | NADH-ubiquinone dehydrogenase chain 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 |
| nuoCD | phaA | RPA4262 | RPA2789 | 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. | pH adaptation potassium efflux system components phaA and phaB; Citation: Putkorny et al. (1998) Mol. Microbiol. 28:1091-1101. | 0.997 |
| nuoCD | phaC | RPA4262 | RPA2790 | 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. | pH adaptation K efflux system component; Citation: Putkorny et al. (1998) Mol. Microbiol. 28:1091-1101. | 0.865 |
| nuoCD | phaD | RPA4262 | RPA2791 | 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. | Putative component of pH adaptation K-efflux system phaD; Citation: Putkorny et al. (1998) Mol. Microbiol. 28:1091-1101. | 0.895 |
| nuoCD | phaE | RPA4262 | RPA2792 | 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. | Putative component of pH adaptation K-efflux system phaE; Citation: Putkorny et al. (1998) Mol. Microbiol. 28:1091-1101. | 0.873 |
| nuoCD | phaF | RPA4262 | RPA2793 | 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. | pH adaptation potassium efflux system phaF; Citation: Putkorny et al. (1998) Mol. Microbiol. 28:1091-1101. | 0.865 |
| nuoCD | phaG | RPA4262 | RPA2794 | 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. | Putative pH adaptation potassium efflux system component phaG; Citation: Putkorny et al. (1998) Mol. Microbiol. 28:1091-1101. | 0.865 |
| nuoI1 | nuoCD | RPA2942 | RPA4262 | NADH-ubiquinone dehydrogenase chain 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. | 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 |
| nuoI1 | nuoI2 | RPA2942 | RPA4257 | NADH-ubiquinone dehydrogenase chain 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. | NADH-ubiquinone dehydrogenase chain 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. | 0.915 |
| nuoI1 | phaA | RPA2942 | RPA2789 | NADH-ubiquinone dehydrogenase chain 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. | pH adaptation potassium efflux system components phaA and phaB; Citation: Putkorny et al. (1998) Mol. Microbiol. 28:1091-1101. | 0.980 |
| nuoI1 | phaD | RPA2942 | RPA2791 | NADH-ubiquinone dehydrogenase chain 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. | Putative component of pH adaptation K-efflux system phaD; Citation: Putkorny et al. (1998) Mol. Microbiol. 28:1091-1101. | 0.466 |
