| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Q91_0519 | Q91_1355 | Q91_0519 | Q91_1355 | 3-oxoacyl-[acyl-carrier-protein] synthase I; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | AMP-dependent synthetase and ligase. | 0.982 |
| Q91_0519 | Q91_1368 | Q91_0519 | Q91_1368 | 3-oxoacyl-[acyl-carrier-protein] synthase I; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases 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. | 0.910 |
| Q91_0519 | acpP | Q91_0519 | Q91_1369 | 3-oxoacyl-[acyl-carrier-protein] synthase I; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.868 |
| Q91_0519 | fabV | Q91_0519 | Q91_0539 | 3-oxoacyl-[acyl-carrier-protein] synthase I; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | Short-chain alcohol dehydrogenase family; Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon- carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP); Belongs to the TER reductase family. | 0.922 |
| Q91_0519 | lipB | Q91_0519 | Q91_1754 | 3-oxoacyl-[acyl-carrier-protein] synthase I; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 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. | 0.813 |
| Q91_1355 | Q91_0519 | Q91_1355 | Q91_0519 | AMP-dependent synthetase and ligase. | 3-oxoacyl-[acyl-carrier-protein] synthase I; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.982 |
| Q91_1355 | Q91_1368 | Q91_1355 | Q91_1368 | AMP-dependent synthetase and ligase. | 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 |
| Q91_1355 | Q91_1752 | Q91_1355 | Q91_1752 | AMP-dependent synthetase and ligase. | Aminotransferase, class IV superfamily. | 0.587 |
| Q91_1355 | acpP | Q91_1355 | Q91_1369 | AMP-dependent synthetase and ligase. | Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.996 |
| Q91_1355 | gcvH | Q91_1355 | Q91_1955 | AMP-dependent synthetase and ligase. | Glycine cleavage complex 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. | 0.730 |
| Q91_1355 | lipA | Q91_1355 | Q91_1755 | AMP-dependent synthetase and ligase. | 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. | 0.437 |
| Q91_1355 | lipB | Q91_1355 | Q91_1754 | AMP-dependent synthetase and ligase. | 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. | 0.801 |
| Q91_1368 | Q91_0519 | Q91_1368 | Q91_0519 | 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. | 3-oxoacyl-[acyl-carrier-protein] synthase I; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.910 |
| Q91_1368 | Q91_1355 | Q91_1368 | Q91_1355 | 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. | AMP-dependent synthetase and ligase. | 0.996 |
| Q91_1368 | acpP | Q91_1368 | Q91_1369 | 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; Carrier of the growing fatty acid chain in fatty acid biosynthesis. | 0.969 |
| Q91_1368 | fabV | Q91_1368 | Q91_0539 | 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. | Short-chain alcohol dehydrogenase family; Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon- carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP); Belongs to the TER reductase family. | 0.922 |
| Q91_1368 | lipB | Q91_1368 | Q91_1754 | 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. | 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. | 0.813 |
| Q91_1751 | Q91_1752 | Q91_1751 | Q91_1752 | Beta-lactamase; Belongs to the peptidase S11 family. | Aminotransferase, class IV superfamily. | 0.806 |
| Q91_1751 | Q91_1753 | Q91_1751 | Q91_1753 | Beta-lactamase; Belongs to the peptidase S11 family. | Cytoplasmic protein; Belongs to the UPF0250 family. | 0.818 |
| Q91_1751 | lipA | Q91_1751 | Q91_1755 | Beta-lactamase; Belongs to the peptidase S11 family. | 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. | 0.821 |