| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaA | avtA | WL1483_1007 | WL1483_1194 | Aminotransferase AlaT. | Valine--pyruvate transaminase. | 0.908 |
| alaA | ilvD | WL1483_1007 | WL1483_2083 | Aminotransferase AlaT. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.929 |
| alaA | ilvE | WL1483_1007 | WL1483_2300 | Aminotransferase AlaT. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.930 |
| alaA | leuA | WL1483_1007 | WL1483_3739 | Aminotransferase AlaT. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.921 |
| alaA | metL | WL1483_1007 | WL1483_482 | Aminotransferase AlaT. | Aspartate kinase; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.687 |
| alaA | thrA | WL1483_1007 | WL1483_3647 | Aminotransferase AlaT. | Bifunctional aspartokinase I/homoserine dehydrogenase I; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.687 |
| avtA | alaA | WL1483_1194 | WL1483_1007 | Valine--pyruvate transaminase. | Aminotransferase AlaT. | 0.908 |
| avtA | ilvD | WL1483_1194 | WL1483_2083 | Valine--pyruvate transaminase. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.917 |
| avtA | ilvE | WL1483_1194 | WL1483_2300 | Valine--pyruvate transaminase. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.924 |
| avtA | leuA | WL1483_1194 | WL1483_3739 | Valine--pyruvate transaminase. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.903 |
| ilvA | ilvD | WL1483_1569 | WL1483_2083 | 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. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.953 |
| ilvA | ilvE | WL1483_1569 | WL1483_2300 | 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. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.951 |
| ilvA | ilvG | WL1483_1569 | WL1483_1907 | 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. | Acetolactate synthase 2 catalytic subunit. | 0.968 |
| ilvA | ilvM | WL1483_1569 | WL1483_3006 | 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. | Acetolactate synthase II small subunit. | 0.963 |
| ilvA | metL | WL1483_1569 | WL1483_482 | 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. | Aspartate kinase; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.746 |
| ilvA | thrA | WL1483_1569 | WL1483_3647 | 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. | Bifunctional aspartokinase I/homoserine dehydrogenase I; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.746 |
| ilvD | alaA | WL1483_2083 | WL1483_1007 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Aminotransferase AlaT. | 0.929 |
| ilvD | avtA | WL1483_2083 | WL1483_1194 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Valine--pyruvate transaminase. | 0.917 |
| ilvD | ilvA | WL1483_2083 | WL1483_1569 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 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. | 0.953 |
| ilvD | ilvE | WL1483_2083 | WL1483_2300 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.993 |