| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AOI82038.1 | LpdA | WI67_06040 | WI67_11555 | Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.825 |
| AOI82038.1 | gcvH | WI67_06040 | WI67_00825 | Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glycine cleavage system protein H; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | 0.877 |
| AOI82038.1 | gcvP | WI67_06040 | WI67_00820 | Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glycine dehydrogenase (aminomethyl-transferring); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.778 |
| AOI82038.1 | lipA | WI67_06040 | WI67_09775 | Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.558 |
| AOI82038.1 | lipA-2 | WI67_06040 | WI67_15405 | Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.553 |
| AOI82038.1 | lipB | WI67_06040 | WI67_15410 | Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoate--protein ligase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.582 |
| AOI82038.1 | odhB | WI67_06040 | WI67_07485 | Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dihydrolipoamide succinyltransferase; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). | 0.963 |
| AOI84217.1 | lipA-2 | WI67_15415 | WI67_15405 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.575 |
| AOI84217.1 | lipB | WI67_15415 | WI67_15410 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoate--protein ligase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.576 |
| AOI84264.1 | LpdA | WI67_17005 | WI67_11555 | Mercuric reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.703 |
| AOI84264.1 | gcvH | WI67_17005 | WI67_00825 | Mercuric reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glycine cleavage system protein H; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | 0.821 |
| AOI84264.1 | gcvP | WI67_17005 | WI67_00820 | Mercuric reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glycine dehydrogenase (aminomethyl-transferring); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.570 |
| AOI84264.1 | lipA | WI67_17005 | WI67_09775 | Mercuric reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.555 |
| AOI84264.1 | lipA-2 | WI67_17005 | WI67_15405 | Mercuric reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.531 |
| AOI84264.1 | odhB | WI67_17005 | WI67_07485 | Mercuric reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dihydrolipoamide succinyltransferase; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). | 0.853 |
| LpdA | AOI82038.1 | WI67_11555 | WI67_06040 | Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.825 |
| LpdA | AOI84264.1 | WI67_11555 | WI67_17005 | Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Mercuric reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.703 |
| LpdA | gcvH | WI67_11555 | WI67_00825 | Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glycine cleavage system protein H; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | 0.984 |
| LpdA | gcvP | WI67_11555 | WI67_00820 | Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glycine dehydrogenase (aminomethyl-transferring); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.971 |
| LpdA | lipA | WI67_11555 | WI67_09775 | Dihydrolipoamide dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.593 |