node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Moth_0064 | Moth_0234 | Moth_0064 | Moth_0234 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and carbon dioxide. The two electrons that are generated as a result of pyruvate decarboxylation are used in the reduction of low potential ferredoxins, which provide reducing equivalents for central metabolism. Also catalyzes the reverse reaction, i.e. the synthesis of pyruvate from acetyl-CoA and carbon dioxide. Appears to function physiologically in both directions. The oxidation of pyruvate by PFOR is required to connect glycolysis and the Wood- Ljungdahl pathway of re [...] | 4Fe-4S ferredoxin, iron-sulfur binding protein. | 0.995 |
Moth_0064 | Moth_0986 | Moth_0064 | Moth_0986 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and carbon dioxide. The two electrons that are generated as a result of pyruvate decarboxylation are used in the reduction of low potential ferredoxins, which provide reducing equivalents for central metabolism. Also catalyzes the reverse reaction, i.e. the synthesis of pyruvate from acetyl-CoA and carbon dioxide. Appears to function physiologically in both directions. The oxidation of pyruvate by PFOR is required to connect glycolysis and the Wood- Ljungdahl pathway of re [...] | NADH dehydrogenase subunit M. | 0.529 |
Moth_0064 | Moth_1888 | Moth_0064 | Moth_1888 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and carbon dioxide. The two electrons that are generated as a result of pyruvate decarboxylation are used in the reduction of low potential ferredoxins, which provide reducing equivalents for central metabolism. Also catalyzes the reverse reaction, i.e. the synthesis of pyruvate from acetyl-CoA and carbon dioxide. Appears to function physiologically in both directions. The oxidation of pyruvate by PFOR is required to connect glycolysis and the Wood- Ljungdahl pathway of re [...] | Ferredoxin. | 0.969 |
Moth_0064 | acpP | Moth_0064 | Moth_0949 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and carbon dioxide. The two electrons that are generated as a result of pyruvate decarboxylation are used in the reduction of low potential ferredoxins, which provide reducing equivalents for central metabolism. Also catalyzes the reverse reaction, i.e. the synthesis of pyruvate from acetyl-CoA and carbon dioxide. Appears to function physiologically in both directions. The oxidation of pyruvate by PFOR is required to connect glycolysis and the Wood- Ljungdahl pathway of re [...] | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.893 |
Moth_0064 | nuoA | Moth_0064 | Moth_0977 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and carbon dioxide. The two electrons that are generated as a result of pyruvate decarboxylation are used in the reduction of low potential ferredoxins, which provide reducing equivalents for central metabolism. Also catalyzes the reverse reaction, i.e. the synthesis of pyruvate from acetyl-CoA and carbon dioxide. Appears to function physiologically in both directions. The oxidation of pyruvate by PFOR is required to connect glycolysis and the Wood- Ljungdahl pathway of re [...] | NADH dehydrogenase subunit 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 a menaquinone. 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. | 0.679 |
Moth_0064 | nuoB | Moth_0064 | Moth_0978 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and carbon dioxide. The two electrons that are generated as a result of pyruvate decarboxylation are used in the reduction of low potential ferredoxins, which provide reducing equivalents for central metabolism. Also catalyzes the reverse reaction, i.e. the synthesis of pyruvate from acetyl-CoA and carbon dioxide. Appears to function physiologically in both directions. The oxidation of pyruvate by PFOR is required to connect glycolysis and the Wood- Ljungdahl pathway of re [...] | NADH dehydrogenase 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 a menaquinone. 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. | 0.652 |
Moth_0064 | nuoC | Moth_0064 | Moth_0979 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and carbon dioxide. The two electrons that are generated as a result of pyruvate decarboxylation are used in the reduction of low potential ferredoxins, which provide reducing equivalents for central metabolism. Also catalyzes the reverse reaction, i.e. the synthesis of pyruvate from acetyl-CoA and carbon dioxide. Appears to function physiologically in both directions. The oxidation of pyruvate by PFOR is required to connect glycolysis and the Wood- Ljungdahl pathway of re [...] | NADH dehydrogenase subunit C; 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 a menaquinone. 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. | 0.703 |
Moth_0064 | nuoD | Moth_0064 | Moth_0980 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and carbon dioxide. The two electrons that are generated as a result of pyruvate decarboxylation are used in the reduction of low potential ferredoxins, which provide reducing equivalents for central metabolism. Also catalyzes the reverse reaction, i.e. the synthesis of pyruvate from acetyl-CoA and carbon dioxide. Appears to function physiologically in both directions. The oxidation of pyruvate by PFOR is required to connect glycolysis and the Wood- Ljungdahl pathway of re [...] | NADH dehydrogenase 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 a menaquinone. 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. | 0.533 |
Moth_0064 | nuoH | Moth_0064 | Moth_0981 | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and carbon dioxide. The two electrons that are generated as a result of pyruvate decarboxylation are used in the reduction of low potential ferredoxins, which provide reducing equivalents for central metabolism. Also catalyzes the reverse reaction, i.e. the synthesis of pyruvate from acetyl-CoA and carbon dioxide. Appears to function physiologically in both directions. The oxidation of pyruvate by PFOR is required to connect glycolysis and the Wood- Ljungdahl pathway of re [...] | NADH dehydrogenase subunit H; 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. This subunit may bind ubiquinone. | 0.533 |
Moth_0234 | Moth_0064 | Moth_0234 | Moth_0064 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and carbon dioxide. The two electrons that are generated as a result of pyruvate decarboxylation are used in the reduction of low potential ferredoxins, which provide reducing equivalents for central metabolism. Also catalyzes the reverse reaction, i.e. the synthesis of pyruvate from acetyl-CoA and carbon dioxide. Appears to function physiologically in both directions. The oxidation of pyruvate by PFOR is required to connect glycolysis and the Wood- Ljungdahl pathway of re [...] | 0.995 |
Moth_0234 | Moth_0986 | Moth_0234 | Moth_0986 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | NADH dehydrogenase subunit M. | 0.985 |
Moth_0234 | Moth_1888 | Moth_0234 | Moth_1888 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | Ferredoxin. | 0.986 |
Moth_0234 | acpP | Moth_0234 | Moth_0949 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.972 |
Moth_0234 | nuoA | Moth_0234 | Moth_0977 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | NADH dehydrogenase subunit 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 a menaquinone. 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. | 0.985 |
Moth_0234 | nuoB | Moth_0234 | Moth_0978 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | NADH dehydrogenase 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 a menaquinone. 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. | 0.987 |
Moth_0234 | nuoC | Moth_0234 | Moth_0979 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | NADH dehydrogenase subunit C; 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 a menaquinone. 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. | 0.987 |
Moth_0234 | nuoD | Moth_0234 | Moth_0980 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | NADH dehydrogenase 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 a menaquinone. 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. | 0.987 |
Moth_0234 | nuoH | Moth_0234 | Moth_0981 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | NADH dehydrogenase subunit H; 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. This subunit may bind ubiquinone. | 0.985 |
Moth_0234 | nuoN | Moth_0234 | Moth_0987 | 4Fe-4S ferredoxin, iron-sulfur binding protein. | NADH dehydrogenase 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 a menaquinone. 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. | 0.984 |
Moth_0986 | Moth_0064 | Moth_0986 | Moth_0064 | NADH dehydrogenase subunit M. | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and carbon dioxide. The two electrons that are generated as a result of pyruvate decarboxylation are used in the reduction of low potential ferredoxins, which provide reducing equivalents for central metabolism. Also catalyzes the reverse reaction, i.e. the synthesis of pyruvate from acetyl-CoA and carbon dioxide. Appears to function physiologically in both directions. The oxidation of pyruvate by PFOR is required to connect glycolysis and the Wood- Ljungdahl pathway of re [...] | 0.529 |