| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| aat_1 | avtA | CH53_384 | CH53_1706 | Hypothetical protein. | Aminotransferase class I and II family protein. | 0.909 |
| aat_1 | ilvD | CH53_384 | CH53_1953 | Hypothetical protein. | ilvD: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.914 |
| aat_1 | ilvE | CH53_384 | CH53_1952 | Hypothetical protein. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.917 |
| aat_1 | leuA | CH53_384 | CH53_1035 | Hypothetical protein. | 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. | 0.912 |
| aat_1 | metL | CH53_384 | CH53_1908 | Hypothetical protein. | Homoserine dehydrogenase, NAD binding domain protein; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.545 |
| aat_1 | thrA | CH53_384 | CH53_1086 | Hypothetical protein. | Asp_kinase: aspartate kinase domain protein; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.542 |
| avtA | aat_1 | CH53_1706 | CH53_384 | Aminotransferase class I and II family protein. | Hypothetical protein. | 0.909 |
| avtA | ilvD | CH53_1706 | CH53_1953 | Aminotransferase class I and II family protein. | ilvD: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.901 |
| avtA | ilvE | CH53_1706 | CH53_1952 | Aminotransferase class I and II family protein. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.931 |
| avtA | leuA | CH53_1706 | CH53_1035 | Aminotransferase class I and II family protein. | 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. | 0.922 |
| ilvA-2 | ilvD | CH53_1954 | CH53_1953 | Threonine ammonia-lyase; 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. | ilvD: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.956 |
| ilvA-2 | ilvE | CH53_1954 | CH53_1952 | Threonine ammonia-lyase; 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. | 0.967 |
| ilvA-2 | ilvM | CH53_1954 | CH53_1951 | Threonine ammonia-lyase; 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 isozyme 2 small subunit. | 0.854 |
| ilvA-2 | leuA | CH53_1954 | CH53_1035 | Threonine ammonia-lyase; 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. | 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. | 0.643 |
| ilvA-2 | metB | CH53_1954 | CH53_1907 | Threonine ammonia-lyase; 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. | O-succinylhomoserine (thiol)-lyase; Cystathionine gamma-lyase-like protein; O_succ_thio_ly: O-succinylhomoserine (thiol)-lyase. | 0.822 |
| ilvA-2 | metL | CH53_1954 | CH53_1908 | Threonine ammonia-lyase; 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. | Homoserine dehydrogenase, NAD binding domain protein; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.642 |
| ilvA-2 | thrA | CH53_1954 | CH53_1086 | Threonine ammonia-lyase; 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. | Asp_kinase: aspartate kinase domain protein; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.607 |
| ilvD | aat_1 | CH53_1953 | CH53_384 | ilvD: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Hypothetical protein. | 0.914 |
| ilvD | avtA | CH53_1953 | CH53_1706 | ilvD: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Aminotransferase class I and II family protein. | 0.901 |
| ilvD | ilvA-2 | CH53_1953 | CH53_1954 | ilvD: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Threonine ammonia-lyase; 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. | 0.956 |