| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaA | avtA | RB151_026740 | RB151_003240 | Glutamate-pyruvate aminotransferase AlaA. | Valine--pyruvate aminotransferase. | 0.907 |
| alaA | ilvD | RB151_026740 | RB151_042290 | Glutamate-pyruvate aminotransferase AlaA. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.923 |
| alaA | ilvE | RB151_026740 | RB151_042300 | Glutamate-pyruvate aminotransferase AlaA. | Branched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.923 |
| alaA | leuA | RB151_026740 | RB151_030600 | Glutamate-pyruvate aminotransferase AlaA. | 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. | 0.924 |
| alaA | metL | RB151_026740 | RB151_043190 | Glutamate-pyruvate aminotransferase AlaA. | Bifunctional aspartokinase/homoserine dehydrogenase 2; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.696 |
| alaA | thrA | RB151_026740 | RB151_006570 | Glutamate-pyruvate aminotransferase AlaA. | Bifunctional aspartokinase/homoserine dehydrogenase 1; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.696 |
| avtA | alaA | RB151_003240 | RB151_026740 | Valine--pyruvate aminotransferase. | Glutamate-pyruvate aminotransferase AlaA. | 0.907 |
| avtA | ilvD | RB151_003240 | RB151_042290 | Valine--pyruvate aminotransferase. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.912 |
| avtA | ilvE | RB151_003240 | RB151_042300 | Valine--pyruvate aminotransferase. | Branched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.920 |
| avtA | leuA | RB151_003240 | RB151_030600 | Valine--pyruvate aminotransferase. | 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 | RB151_042280 | RB151_042290 | L-threonine dehydratase biosynthetic IlvA; 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. | 0.942 |
| ilvA | ilvE | RB151_042280 | RB151_042300 | L-threonine dehydratase biosynthetic IlvA; 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. | 0.945 |
| ilvA | ilvM | RB151_042280 | RB151_042310 | L-threonine dehydratase biosynthetic IlvA; 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. | 0.966 |
| ilvA | metC_3 | RB151_042280 | RB151_031470 | L-threonine dehydratase biosynthetic IlvA; 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. | Cystathionine beta-lyase. | 0.815 |
| ilvA | metL | RB151_042280 | RB151_043190 | L-threonine dehydratase biosynthetic IlvA; 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. | 0.709 |
| ilvA | thrA | RB151_042280 | RB151_006570 | L-threonine dehydratase biosynthetic IlvA; 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. | 0.709 |
| ilvD | alaA | RB151_042290 | RB151_026740 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Glutamate-pyruvate aminotransferase AlaA. | 0.923 |
| ilvD | avtA | RB151_042290 | RB151_003240 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Valine--pyruvate aminotransferase. | 0.912 |
| ilvD | ilvA | RB151_042290 | RB151_042280 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | L-threonine dehydratase biosynthetic IlvA; 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. | 0.942 |
| ilvD | ilvE | RB151_042290 | RB151_042300 | 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. | 0.992 |