node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AXG55_06330 | AXG55_12065 | AXG55_06330 | AXG55_12065 | Undecaprenyl-phosphate glucose phosphotransferase. | Polysacc_synt_2 domain-containing protein. | 0.873 |
AXG55_06330 | AXG55_12350 | AXG55_06330 | AXG55_12350 | Undecaprenyl-phosphate glucose phosphotransferase. | Iron-sulfur cluster carrier protein; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 0.973 |
AXG55_10830 | AXG55_10835 | AXG55_10830 | AXG55_10835 | Uncharacterized protein. | NADH-quinone oxidoreductase 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. | 0.999 |
AXG55_10830 | AXG55_10840 | AXG55_10830 | AXG55_10840 | Uncharacterized protein. | Uncharacterized protein. | 0.999 |
AXG55_10830 | AXG55_10845 | AXG55_10830 | AXG55_10845 | Uncharacterized protein. | NADH dehydrogenase (Quinone) subunit 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 C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.999 |
AXG55_10830 | AXG55_12350 | AXG55_10830 | AXG55_12350 | Uncharacterized protein. | Iron-sulfur cluster carrier protein; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 0.814 |
AXG55_10830 | nuoB | AXG55_10830 | AXG55_09645 | Uncharacterized protein. | NADH-quinone oxidoreductase subunit B; 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 |
AXG55_10830 | nuoI | AXG55_10830 | AXG55_10825 | Uncharacterized protein. | NADH-quinone oxidoreductase subunit 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 |
AXG55_10835 | AXG55_10830 | AXG55_10835 | AXG55_10830 | NADH-quinone oxidoreductase 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. | Uncharacterized protein. | 0.999 |
AXG55_10835 | AXG55_10840 | AXG55_10835 | AXG55_10840 | NADH-quinone oxidoreductase 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. | Uncharacterized protein. | 0.999 |
AXG55_10835 | AXG55_10845 | AXG55_10835 | AXG55_10845 | NADH-quinone oxidoreductase 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. | NADH dehydrogenase (Quinone) subunit 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 C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.999 |
AXG55_10835 | AXG55_12350 | AXG55_10835 | AXG55_12350 | NADH-quinone oxidoreductase 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. | Iron-sulfur cluster carrier protein; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 0.789 |
AXG55_10835 | nuoB | AXG55_10835 | AXG55_09645 | NADH-quinone oxidoreductase 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. | NADH-quinone oxidoreductase subunit B; 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 |
AXG55_10835 | nuoI | AXG55_10835 | AXG55_10825 | NADH-quinone oxidoreductase 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. | NADH-quinone oxidoreductase subunit 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 |
AXG55_10840 | AXG55_10830 | AXG55_10840 | AXG55_10830 | Uncharacterized protein. | Uncharacterized protein. | 0.999 |
AXG55_10840 | AXG55_10835 | AXG55_10840 | AXG55_10835 | Uncharacterized protein. | NADH-quinone oxidoreductase 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. | 0.999 |
AXG55_10840 | AXG55_10845 | AXG55_10840 | AXG55_10845 | Uncharacterized protein. | NADH dehydrogenase (Quinone) subunit 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 C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.999 |
AXG55_10840 | AXG55_12345 | AXG55_10840 | AXG55_12345 | Uncharacterized protein. | NifU domain-containing protein. | 0.436 |
AXG55_10840 | AXG55_12350 | AXG55_10840 | AXG55_12350 | Uncharacterized protein. | Iron-sulfur cluster carrier protein; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 0.795 |
AXG55_10840 | nuoB | AXG55_10840 | AXG55_09645 | Uncharacterized protein. | NADH-quinone oxidoreductase subunit B; 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 |