| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| coxB | ndh | Lfee_0287 | Lfee_0376 | Cytochrome c oxidase subunit II; 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). | Respiratory NADH dehydrogenase 2/cupric reductase. | 0.635 |
| coxB | nqo1 | Lfee_0287 | Lfee_1898 | Cytochrome c oxidase subunit II; 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). | NADH dehydrogenase I subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | 0.954 |
| coxB | nuoA | Lfee_0287 | Lfee_1893 | Cytochrome c oxidase subunit II; 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). | NADH dehydrogenase I chain 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. | 0.997 |
| coxB | nuoK | Lfee_0287 | Lfee_1903 | Cytochrome c oxidase subunit II; 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). | NADH-quinone oxidoreductase chain K; 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 4L family. | 0.928 |
| coxB | nuoL | Lfee_0287 | Lfee_1904 | Cytochrome c oxidase subunit II; 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). | NADH-quinone oxidoreductase chain L. | 0.916 |
| coxB | nuoL_1 | Lfee_0287 | Lfee_1637 | Cytochrome c oxidase subunit II; 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). | NADH-ubiquinone oxidoreductase chain 5. | 0.914 |
| coxB | nuoM | Lfee_0287 | Lfee_1905 | Cytochrome c oxidase subunit II; 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). | NADH-quinone oxidoreductase chain M. | 0.996 |
| coxB | nuoN | Lfee_0287 | Lfee_1906 | Cytochrome c oxidase subunit II; 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). | NADH dehydrogenase I 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. | 0.996 |
| glpD | ndh | Lfee_2993 | Lfee_0376 | Glycerol-3-phosphate dehydrogenase; Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family. | Respiratory NADH dehydrogenase 2/cupric reductase. | 0.670 |
| ndh | coxB | Lfee_0376 | Lfee_0287 | Respiratory NADH dehydrogenase 2/cupric reductase. | Cytochrome c oxidase subunit II; 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). | 0.635 |
| ndh | glpD | Lfee_0376 | Lfee_2993 | Respiratory NADH dehydrogenase 2/cupric reductase. | Glycerol-3-phosphate dehydrogenase; Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family. | 0.670 |
| ndh | nqo1 | Lfee_0376 | Lfee_1898 | Respiratory NADH dehydrogenase 2/cupric reductase. | NADH dehydrogenase I subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | 0.633 |
| ndh | nuoA | Lfee_0376 | Lfee_1893 | Respiratory NADH dehydrogenase 2/cupric reductase. | NADH dehydrogenase I chain 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. | 0.605 |
| ndh | nuoK | Lfee_0376 | Lfee_1903 | Respiratory NADH dehydrogenase 2/cupric reductase. | NADH-quinone oxidoreductase chain K; 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 4L family. | 0.616 |
| ndh | nuoL | Lfee_0376 | Lfee_1904 | Respiratory NADH dehydrogenase 2/cupric reductase. | NADH-quinone oxidoreductase chain L. | 0.652 |
| ndh | nuoL_1 | Lfee_0376 | Lfee_1637 | Respiratory NADH dehydrogenase 2/cupric reductase. | NADH-ubiquinone oxidoreductase chain 5. | 0.652 |
| ndh | nuoM | Lfee_0376 | Lfee_1905 | Respiratory NADH dehydrogenase 2/cupric reductase. | NADH-quinone oxidoreductase chain M. | 0.616 |
| ndh | nuoN | Lfee_0376 | Lfee_1906 | Respiratory NADH dehydrogenase 2/cupric reductase. | NADH dehydrogenase I 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. | 0.645 |
| ndh | vhtD | Lfee_0376 | Lfee_1338 | Respiratory NADH dehydrogenase 2/cupric reductase. | Hydrogenase expression/formation protein. | 0.769 |
| nqo1 | coxB | Lfee_1898 | Lfee_0287 | NADH dehydrogenase I subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | Cytochrome c oxidase subunit II; 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). | 0.954 |