| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RSc0087 | coxB | RSc0087 | RSc0362 | Putative nadh-ubiquinone oxidoreductase oxidoreductase protein. | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.787 |
| RSc0087 | coxM | RSc0087 | RSp1564 | Putative nadh-ubiquinone oxidoreductase oxidoreductase protein. | Probable cytochrome c oxidase polypeptide II (cytochrome bb3 subunit 2) transmembrane protein. | 0.865 |
| RSc0087 | nuoA | RSc0087 | RSc2062 | Putative nadh-ubiquinone oxidoreductase oxidoreductase protein. | Probable transmembrane nadh dehydrogenaseI(chain a) oxidoreductase 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; Belongs to the complex I subunit 3 family. | 0.850 |
| RSc0087 | nuoC | RSc0087 | RSc2060 | Putative nadh-ubiquinone oxidoreductase oxidoreductase protein. | Probable nadh dehydrogenaseI(chain c) oxidoreductase 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; Belongs to the complex I 30 kDa subunit family. | 0.958 |
| RSc0087 | nuoD | RSc0087 | RSc2059 | Putative nadh-ubiquinone oxidoreductase oxidoreductase protein. | Probable nadh dehydrogenaseI(chain d) oxidoreductase 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; Belongs to the complex I 49 kDa subunit family. | 0.921 |
| RSc0087 | nuoG | RSc0087 | RSc2056 | Putative nadh-ubiquinone oxidoreductase oxidoreductase protein. | Probable nadh dehydrogenaseI(chain g) oxidoreductase protein; 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. | 0.894 |
| RSc0087 | nuoI | RSc0087 | RSc2054 | Putative nadh-ubiquinone oxidoreductase oxidoreductase protein. | Probable nadh dehydrogenaseI(chainI oxidoreductase 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. | 0.927 |
| RSc0087 | nuoN | RSc0087 | RSc2049 | Putative nadh-ubiquinone oxidoreductase oxidoreductase protein. | Probable transmembrane nadh dehydrogenaseI(chain n) oxidoreductase 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; Belongs to the complex I subunit 2 family. | 0.774 |
| RSc0087 | pcm | RSc0087 | RSc0697 | Putative nadh-ubiquinone oxidoreductase oxidoreductase protein. | Probable protein-l-isoaspartate o-methyltransferase. | 0.837 |
| RSc0696 | pcm | RSc0696 | RSc0697 | Putative rhodanese-related sulfurtransferase protein. | Probable protein-l-isoaspartate o-methyltransferase. | 0.792 |
| coxB | RSc0087 | RSc0362 | RSc0087 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Putative nadh-ubiquinone oxidoreductase oxidoreductase protein. | 0.787 |
| coxB | coxM | RSc0362 | RSp1564 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Probable cytochrome c oxidase polypeptide II (cytochrome bb3 subunit 2) transmembrane protein. | 0.998 |
| coxB | nuoA | RSc0362 | RSc2062 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Probable transmembrane nadh dehydrogenaseI(chain a) oxidoreductase 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; Belongs to the complex I subunit 3 family. | 0.971 |
| coxB | nuoC | RSc0362 | RSc2060 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Probable nadh dehydrogenaseI(chain c) oxidoreductase 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; Belongs to the complex I 30 kDa subunit family. | 0.935 |
| coxB | nuoD | RSc0362 | RSc2059 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Probable nadh dehydrogenaseI(chain d) oxidoreductase 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; Belongs to the complex I 49 kDa subunit family. | 0.913 |
| coxB | nuoG | RSc0362 | RSc2056 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Probable nadh dehydrogenaseI(chain g) oxidoreductase protein; 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. | 0.902 |
| coxB | nuoI | RSc0362 | RSc2054 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Probable nadh dehydrogenaseI(chainI oxidoreductase 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. | 0.880 |
| coxB | nuoN | RSc0362 | RSc2049 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Probable transmembrane nadh dehydrogenaseI(chain n) oxidoreductase 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; Belongs to the complex I subunit 2 family. | 0.970 |
| coxB | pcm | RSc0362 | RSc0697 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Probable protein-l-isoaspartate o-methyltransferase. | 0.774 |
| coxM | RSc0087 | RSp1564 | RSc0087 | Probable cytochrome c oxidase polypeptide II (cytochrome bb3 subunit 2) transmembrane protein. | Putative nadh-ubiquinone oxidoreductase oxidoreductase protein. | 0.865 |