| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Lgor_2191 | Lgor_2244 | Lgor_2191 | Lgor_2244 | Poly(3-hydroxybutyrate) depolymerase. | PHB/PHA accumulation regulator DNA-binding domain protein. | 0.733 |
| Lgor_2191 | coxB | Lgor_2191 | Lgor_2088 | Poly(3-hydroxybutyrate) depolymerase. | 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). | 0.727 |
| Lgor_2191 | nqo1 | Lgor_2191 | Lgor_0922 | Poly(3-hydroxybutyrate) depolymerase. | 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. | 0.735 |
| Lgor_2191 | nuoG | Lgor_2191 | Lgor_0921 | Poly(3-hydroxybutyrate) depolymerase. | NADH dehydrogenase I 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. | 0.738 |
| Lgor_2191 | nuoI | Lgor_2191 | Lgor_0919 | Poly(3-hydroxybutyrate) depolymerase. | NADH-quinone oxidoreductase 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. | 0.724 |
| Lgor_2191 | nuoN | Lgor_2191 | Lgor_0914 | Poly(3-hydroxybutyrate) depolymerase. | NADH dehydrogenase I chain 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. | 0.712 |
| Lgor_2191 | phbC_1 | Lgor_2191 | Lgor_0393 | Poly(3-hydroxybutyrate) depolymerase. | PHA synthase. | 0.928 |
| Lgor_2191 | phbC_2 | Lgor_2191 | Lgor_1481 | Poly(3-hydroxybutyrate) depolymerase. | PHA synthase. | 0.924 |
| Lgor_2191 | phbC_3 | Lgor_2191 | Lgor_2144 | Poly(3-hydroxybutyrate) depolymerase. | PHA synthase. | 0.927 |
| Lgor_2191 | phbC_4 | Lgor_2191 | Lgor_0067 | Poly(3-hydroxybutyrate) depolymerase. | Poly-beta-hydroxybutyrate synthase. | 0.933 |
| Lgor_2244 | Lgor_2191 | Lgor_2244 | Lgor_2191 | PHB/PHA accumulation regulator DNA-binding domain protein. | Poly(3-hydroxybutyrate) depolymerase. | 0.733 |
| Lgor_2244 | phbC_1 | Lgor_2244 | Lgor_0393 | PHB/PHA accumulation regulator DNA-binding domain protein. | PHA synthase. | 0.766 |
| Lgor_2244 | phbC_2 | Lgor_2244 | Lgor_1481 | PHB/PHA accumulation regulator DNA-binding domain protein. | PHA synthase. | 0.761 |
| Lgor_2244 | phbC_3 | Lgor_2244 | Lgor_2144 | PHB/PHA accumulation regulator DNA-binding domain protein. | PHA synthase. | 0.766 |
| Lgor_2244 | phbC_4 | Lgor_2244 | Lgor_0067 | PHB/PHA accumulation regulator DNA-binding domain protein. | Poly-beta-hydroxybutyrate synthase. | 0.771 |
| coxB | Lgor_2191 | Lgor_2088 | Lgor_2191 | 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). | Poly(3-hydroxybutyrate) depolymerase. | 0.727 |
| coxB | nqo1 | Lgor_2088 | Lgor_0922 | 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. | 0.986 |
| coxB | nuoG | Lgor_2088 | Lgor_0921 | 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 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. | 0.983 |
| coxB | nuoI | Lgor_2088 | Lgor_0919 | 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 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. | 0.984 |
| coxB | nuoN | Lgor_2088 | Lgor_0914 | 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 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. | 0.997 |