| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BirA | PMM0539 | PMM0433 | PMM0539 | Putative Biotin--acetyl-CoA-carboxylase ligase; Citation: Howard et al. (1985) Gene 35:321-331; Alternative locus ID: PMED4_04801. | Biotin/lipoate A/B protein ligase family; Alternative locus ID: PMED4_05881. | 0.815 |
| BirA | lipB | PMM0433 | PMM0401 | Putative Biotin--acetyl-CoA-carboxylase ligase; Citation: Howard et al. (1985) Gene 35:321-331; Alternative locus ID: PMED4_04801. | 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. | 0.806 |
| PMM0539 | BirA | PMM0539 | PMM0433 | Biotin/lipoate A/B protein ligase family; Alternative locus ID: PMED4_05881. | Putative Biotin--acetyl-CoA-carboxylase ligase; Citation: Howard et al. (1985) Gene 35:321-331; Alternative locus ID: PMED4_04801. | 0.815 |
| 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 |
| acpP,acp | fabF | PMM1608 | PMM1609 | Acyl carrier protein (ACP); Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. | 3-oxoacyl-[acyl-carrier-protein] synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 0.997 |
| acpP,acp | fabI | PMM1608 | PMM0282 | Acyl carrier protein (ACP); Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. | Enoyl-[acyl-carrier-protein] reductase; Alternative locus ID: PMED4_02871. | 0.856 |
| acpP,acp | gcsH, | PMM1608 | PMM1669 | Acyl carrier protein (ACP); Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) 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. | 0.885 |
| acpP,acp | leuC | PMM1608 | PMM0256 | Acyl carrier protein (ACP); Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. | 3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.566 |
| acpP,acp | lipB | PMM1608 | PMM0401 | Acyl carrier protein (ACP); Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) 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. | 0.966 |
| fabF | acpP,acp | PMM1609 | PMM1608 | 3-oxoacyl-[acyl-carrier-protein] synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | Acyl carrier protein (ACP); Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. | 0.997 |
| fabF | fabI | PMM1609 | PMM0282 | 3-oxoacyl-[acyl-carrier-protein] synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | Enoyl-[acyl-carrier-protein] reductase; Alternative locus ID: PMED4_02871. | 0.996 |
| fabF | lipB | PMM1609 | PMM0401 | 3-oxoacyl-[acyl-carrier-protein] synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 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. | 0.818 |
| fabI | acpP,acp | PMM0282 | PMM1608 | Enoyl-[acyl-carrier-protein] reductase; Alternative locus ID: PMED4_02871. | Acyl carrier protein (ACP); Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. | 0.856 |
| fabI | fabF | PMM0282 | PMM1609 | Enoyl-[acyl-carrier-protein] reductase; Alternative locus ID: PMED4_02871. | 3-oxoacyl-[acyl-carrier-protein] synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 0.996 |
| fabI | lipB | PMM0282 | PMM0401 | Enoyl-[acyl-carrier-protein] reductase; Alternative locus ID: PMED4_02871. | 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. | 0.800 |
| fadD | lipB | PMM0402 | PMM0401 | Putative long-chain-fatty-acid--CoA ligase; Alternative locus ID: PMED4_04431. | 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. | 0.762 |
| 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 |