| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ANL57943.1 | ANL57944.1 | AMC85_CH00512 | AMC85_CH00513 | GGDEF domain-containing protein; Protein involved in phosphorus-oxygen lyase activity, cyclic nucleotide biosynthetic process and intracellular signal transduction. | Glyoxalase/bleomycin resistance protein/dioxygenase family protein. | 0.442 |
| ANL57944.1 | ANL57943.1 | AMC85_CH00513 | AMC85_CH00512 | Glyoxalase/bleomycin resistance protein/dioxygenase family protein. | GGDEF domain-containing protein; Protein involved in phosphorus-oxygen lyase activity, cyclic nucleotide biosynthetic process and intracellular signal transduction. | 0.442 |
| ANL57944.1 | nuoI-1 | AMC85_CH00513 | AMC85_CH01679 | Glyoxalase/bleomycin resistance protein/dioxygenase family protein. | NADH dehydrogenase (quinone) subunit I 1; 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. | 0.424 |
| ANL57944.1 | nuoI-2 | AMC85_CH00513 | AMC85_CH03560 | Glyoxalase/bleomycin resistance protein/dioxygenase family protein. | NADH dehydrogenase (quinone) subunit I 2; 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. | 0.424 |
| ANL57944.1 | sdhC | AMC85_CH00513 | AMC85_CH04160 | Glyoxalase/bleomycin resistance protein/dioxygenase family protein. | Succinate dehydrogenase cytochrome b556 subunit; Protein involved in succinate dehydrogenase activity and tricarboxylic acid cycle. | 0.416 |
| nuoI-1 | ANL57944.1 | AMC85_CH01679 | AMC85_CH00513 | NADH dehydrogenase (quinone) subunit I 1; 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. | Glyoxalase/bleomycin resistance protein/dioxygenase family protein. | 0.424 |
| nuoI-1 | nuoI-2 | AMC85_CH01679 | AMC85_CH03560 | NADH dehydrogenase (quinone) subunit I 1; 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 dehydrogenase (quinone) subunit I 2; 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. | 0.916 |
| nuoI-1 | sdhC | AMC85_CH01679 | AMC85_CH04160 | NADH dehydrogenase (quinone) subunit I 1; 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. | Succinate dehydrogenase cytochrome b556 subunit; Protein involved in succinate dehydrogenase activity and tricarboxylic acid cycle. | 0.866 |
| nuoI-2 | ANL57944.1 | AMC85_CH03560 | AMC85_CH00513 | NADH dehydrogenase (quinone) subunit I 2; 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. | Glyoxalase/bleomycin resistance protein/dioxygenase family protein. | 0.424 |
| nuoI-2 | nuoI-1 | AMC85_CH03560 | AMC85_CH01679 | NADH dehydrogenase (quinone) subunit I 2; 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 dehydrogenase (quinone) subunit I 1; 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. | 0.916 |
| nuoI-2 | sdhC | AMC85_CH03560 | AMC85_CH04160 | NADH dehydrogenase (quinone) subunit I 2; 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. | Succinate dehydrogenase cytochrome b556 subunit; Protein involved in succinate dehydrogenase activity and tricarboxylic acid cycle. | 0.848 |
| sdhC | ANL57944.1 | AMC85_CH04160 | AMC85_CH00513 | Succinate dehydrogenase cytochrome b556 subunit; Protein involved in succinate dehydrogenase activity and tricarboxylic acid cycle. | Glyoxalase/bleomycin resistance protein/dioxygenase family protein. | 0.416 |
| sdhC | nuoI-1 | AMC85_CH04160 | AMC85_CH01679 | Succinate dehydrogenase cytochrome b556 subunit; Protein involved in succinate dehydrogenase activity and tricarboxylic acid cycle. | NADH dehydrogenase (quinone) subunit I 1; 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. | 0.866 |
| sdhC | nuoI-2 | AMC85_CH04160 | AMC85_CH03560 | Succinate dehydrogenase cytochrome b556 subunit; Protein involved in succinate dehydrogenase activity and tricarboxylic acid cycle. | NADH dehydrogenase (quinone) subunit I 2; 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. | 0.848 |