| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PMM0539 | gcsH, | PMM0539 | PMM1669 | Biotin/lipoate A/B protein ligase family; Alternative locus ID: PMED4_05881. | Putative Glycine cleavage H-protein; 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. | 0.951 |
| PMM0539 | lipA | PMM0539 | PMM1514 | Biotin/lipoate A/B protein ligase family; Alternative locus ID: PMED4_05881. | Lipoic acid synthetase; 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. | 0.933 |
| PMM0539 | lipA,lip | PMM0539 | PMM1096 | Biotin/lipoate A/B protein ligase family; Alternative locus ID: PMED4_05881. | Lipoate 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. | 0.935 |
| PMM0539 | lipB | PMM0539 | PMM0401 | Biotin/lipoate A/B protein ligase family; Alternative locus ID: PMED4_05881. | Putative lipoate-protein ligase B; 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. | 0.989 |
| gcsH, | PMM0539 | PMM1669 | PMM0539 | Putative Glycine cleavage H-protein; 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. | Biotin/lipoate A/B protein ligase family; Alternative locus ID: PMED4_05881. | 0.951 |
| gcsH, | gcvP | PMM1669 | PMM1668 | Putative Glycine cleavage H-protein; 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. | Glycine cleavage system P-protein; Alternative locus ID: PMED4_18781; Belongs to the GcvP family. | 0.999 |
| gcsH, | lipA | PMM1669 | PMM1514 | Putative Glycine cleavage H-protein; 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. | Lipoic acid synthetase; 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. | 0.723 |
| gcsH, | lipA,lip | PMM1669 | PMM1096 | Putative Glycine cleavage H-protein; 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. | Lipoate 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. | 0.722 |
| gcsH, | lipB | PMM1669 | PMM0401 | Putative Glycine cleavage H-protein; 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. | Putative lipoate-protein ligase B; 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. | 0.916 |
| gcvP | gcsH, | PMM1668 | PMM1669 | Glycine cleavage system P-protein; Alternative locus ID: PMED4_18781; Belongs to the GcvP family. | Putative Glycine cleavage H-protein; 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. | 0.999 |
| gcvP | guaA | PMM1668 | PMM0037 | Glycine cleavage system P-protein; Alternative locus ID: PMED4_18781; Belongs to the GcvP family. | Glutamine amidotransferase class-I:GMP synthase; Catalyzes the synthesis of GMP from XMP. | 0.567 |
| gcvP | lipA | PMM1668 | PMM1514 | Glycine cleavage system P-protein; Alternative locus ID: PMED4_18781; Belongs to the GcvP family. | Lipoic acid synthetase; 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. | 0.521 |
| gcvP | lipA,lip | PMM1668 | PMM1096 | Glycine cleavage system P-protein; Alternative locus ID: PMED4_18781; Belongs to the GcvP family. | Lipoate 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. | 0.522 |
| gcvP | lipB | PMM1668 | PMM0401 | Glycine cleavage system P-protein; Alternative locus ID: PMED4_18781; Belongs to the GcvP family. | Putative lipoate-protein ligase B; 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. | 0.572 |
| guaA | gcvP | PMM0037 | PMM1668 | Glutamine amidotransferase class-I:GMP synthase; Catalyzes the synthesis of GMP from XMP. | Glycine cleavage system P-protein; Alternative locus ID: PMED4_18781; Belongs to the GcvP family. | 0.567 |
| guaA | lipA | PMM0037 | PMM1514 | Glutamine amidotransferase class-I:GMP synthase; Catalyzes the synthesis of GMP from XMP. | Lipoic acid synthetase; 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. | 0.415 |
| guaA | lipA,lip | PMM0037 | PMM1096 | Glutamine amidotransferase class-I:GMP synthase; Catalyzes the synthesis of GMP from XMP. | Lipoate 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. | 0.415 |
| lipA | PMM0539 | PMM1514 | PMM0539 | Lipoic acid synthetase; 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. | Biotin/lipoate A/B protein ligase family; Alternative locus ID: PMED4_05881. | 0.933 |
| lipA | gcsH, | PMM1514 | PMM1669 | Lipoic acid synthetase; 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. | Putative Glycine cleavage H-protein; 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. | 0.723 |
| lipA | gcvP | PMM1514 | PMM1668 | Lipoic acid synthetase; 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. | Glycine cleavage system P-protein; Alternative locus ID: PMED4_18781; Belongs to the GcvP family. | 0.521 |