| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaA | avtA | DR95_193 | DR95_2695 | Hypothetical protein. | Aminotransferase class I and II family protein. | 0.906 |
| alaA | ilvD | DR95_193 | DR95_3372 | Hypothetical protein. | ilvD: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.924 |
| alaA | ilvE | DR95_193 | DR95_3373 | Hypothetical protein. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.919 |
| alaA | leuA | DR95_193 | DR95_2885 | 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. | 0.920 |
| alaA | metL | DR95_193 | DR95_3042 | Hypothetical protein. | Bifunctional aspartokinase/homoserine dehydrogenase 2; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.710 |
| alaA | thrA | DR95_193 | DR95_1906 | Hypothetical protein. | Bifunctional aspartokinase/homoserine dehydrogenase 1; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.710 |
| avtA | alaA | DR95_2695 | DR95_193 | Aminotransferase class I and II family protein. | Hypothetical protein. | 0.906 |
| avtA | ilvD | DR95_2695 | DR95_3372 | Aminotransferase class I and II family protein. | ilvD: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.911 |
| avtA | ilvE | DR95_2695 | DR95_3373 | 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. | 0.915 |
| avtA | leuA | DR95_2695 | DR95_2885 | 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. | 0.902 |
| ilvA | ilvD | DR95_3370 | DR95_3372 | Threonine ammonia-lyase, biosynthetic; 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. | 0.924 |
| ilvA | ilvE | DR95_3370 | DR95_3373 | Threonine ammonia-lyase, biosynthetic; 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 | ilvM | DR95_3370 | DR95_3374 | Threonine ammonia-lyase, biosynthetic; 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. | 0.819 |
| ilvA | metB | DR95_3370 | DR95_3043 | Threonine ammonia-lyase, biosynthetic; 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_succ_thio_ly: O-succinylhomoserine (thiol)-lyase. | 0.812 |
| ilvA | metL | DR95_3370 | DR95_3042 | Threonine ammonia-lyase, biosynthetic; 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/homoserine dehydrogenase 2; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.665 |
| ilvA | thrA | DR95_3370 | DR95_1906 | Threonine ammonia-lyase, biosynthetic; 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/homoserine dehydrogenase 1; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.665 |
| ilvD | alaA | DR95_3372 | DR95_193 | ilvD: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Hypothetical protein. | 0.924 |
| ilvD | avtA | DR95_3372 | DR95_2695 | ilvD: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Aminotransferase class I and II family protein. | 0.911 |
| ilvD | ilvA | DR95_3372 | DR95_3370 | ilvD: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Threonine ammonia-lyase, biosynthetic; 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. | 0.924 |
| ilvD | ilvE | DR95_3372 | DR95_3373 | ilvD: 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 |