| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DJ90_284 | DJ90_3434 | DJ90_284 | DJ90_3434 | Serine dehydratase alpha chain family protein. | D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain protein. | 0.417 |
| DJ90_284 | DJ90_5815 | DJ90_284 | DJ90_5815 | Serine dehydratase alpha chain family protein. | ACT domain protein. | 0.795 |
| DJ90_284 | cysE | DJ90_284 | DJ90_5562 | Serine dehydratase alpha chain family protein. | cysE: serine O-acetyltransferase. | 0.864 |
| DJ90_284 | glyA | DJ90_284 | DJ90_5388 | Serine dehydratase alpha chain family protein. | Transferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.926 |
| DJ90_284 | ilvA | DJ90_284 | DJ90_310 | Serine dehydratase alpha chain family protein. | Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.887 |
| DJ90_284 | metA | DJ90_284 | DJ90_3324 | Serine dehydratase alpha chain family protein. | Homoserine O-succinyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine; Belongs to the MetA family. | 0.784 |
| DJ90_284 | sdaAA | DJ90_284 | DJ90_53 | Serine dehydratase alpha chain family protein. | Sda_alpha: L-serine dehydratase, iron-sulfur-dependent, alpha subunit. | 0.870 |
| DJ90_284 | sdaAB | DJ90_284 | DJ90_54 | Serine dehydratase alpha chain family protein. | Sda_beta: L-serine dehydratase, iron-sulfur-dependent, beta subunit. | 0.982 |
| DJ90_284 | thrB | DJ90_284 | DJ90_5817 | Serine dehydratase alpha chain family protein. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.805 |
| DJ90_284 | trpA | DJ90_284 | DJ90_3192 | Serine dehydratase alpha chain family protein. | Tryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.859 |
| DJ90_3434 | DJ90_284 | DJ90_3434 | DJ90_284 | D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain protein. | Serine dehydratase alpha chain family protein. | 0.417 |
| DJ90_3434 | glyA | DJ90_3434 | DJ90_5388 | D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain protein. | Transferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.530 |
| DJ90_3434 | ilvA | DJ90_3434 | DJ90_310 | D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain protein. | Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.882 |
| DJ90_3434 | sdaAA | DJ90_3434 | DJ90_53 | D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain protein. | Sda_alpha: L-serine dehydratase, iron-sulfur-dependent, alpha subunit. | 0.862 |
| DJ90_3434 | sdaAB | DJ90_3434 | DJ90_54 | D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain protein. | Sda_beta: L-serine dehydratase, iron-sulfur-dependent, beta subunit. | 0.862 |
| DJ90_3434 | trpA | DJ90_3434 | DJ90_3192 | D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain protein. | Tryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.861 |
| DJ90_5815 | DJ90_284 | DJ90_5815 | DJ90_284 | ACT domain protein. | Serine dehydratase alpha chain family protein. | 0.795 |
| DJ90_5815 | cysE | DJ90_5815 | DJ90_5562 | ACT domain protein. | cysE: serine O-acetyltransferase. | 0.902 |
| DJ90_5815 | glyA | DJ90_5815 | DJ90_5388 | ACT domain protein. | Transferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.631 |
| DJ90_5815 | ilvA | DJ90_5815 | DJ90_310 | ACT domain protein. | Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.759 |