| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| avtA | ilvD_3 | EAG7_04275 | EAG7_04044 | Valine--pyruvate aminotransferase. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.913 |
| avtA | ilvE | EAG7_04275 | EAG7_04045 | Valine--pyruvate aminotransferase. | Branched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.918 |
| avtA | leuA_1 | EAG7_04275 | EAG7_05204 | 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 2 subfamily. | 0.902 |
| avtA | leuA_2 | EAG7_04275 | EAG7_03258 | Valine--pyruvate aminotransferase. | 2-isopropylmalate synthase; Belongs to the alpha-IPM synthase/homocitrate synthase family. | 0.905 |
| ilvA | ilvD_3 | EAG7_04043 | EAG7_04044 | 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. | 0.983 |
| ilvA | ilvE | EAG7_04043 | EAG7_04045 | 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. | 0.982 |
| ilvA | ilvM | EAG7_04043 | EAG7_04046 | 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. | 0.965 |
| ilvA | leuA_1 | EAG7_04043 | EAG7_05204 | 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. | 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 2 subfamily. | 0.670 |
| ilvA | leuA_2 | EAG7_04043 | EAG7_03258 | 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. | 2-isopropylmalate synthase; Belongs to the alpha-IPM synthase/homocitrate synthase family. | 0.542 |
| ilvA | metB_3 | EAG7_04043 | EAG7_03910 | 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 gamma-synthase. | 0.822 |
| ilvA | metL_1 | EAG7_04043 | EAG7_03909 | 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. | 0.679 |
| ilvA | panB_3 | EAG7_04043 | EAG7_03193 | 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. | 3-methyl-2-oxobutanoate hydroxymethyltransferase. | 0.446 |
| ilvA | thrA | EAG7_04043 | EAG7_03362 | 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. | 0.679 |
| ilvD_3 | avtA | EAG7_04044 | EAG7_04275 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Valine--pyruvate aminotransferase. | 0.913 |
| ilvD_3 | ilvA | EAG7_04044 | EAG7_04043 | 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. | 0.983 |
| ilvD_3 | ilvE | EAG7_04044 | EAG7_04045 | 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. | 0.995 |
| ilvD_3 | ilvM | EAG7_04044 | EAG7_04046 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Acetolactate synthase isozyme 2 small subunit. | 0.916 |
| ilvD_3 | leuA_1 | EAG7_04044 | EAG7_05204 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 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 2 subfamily. | 0.981 |
| ilvD_3 | leuA_2 | EAG7_04044 | EAG7_03258 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 2-isopropylmalate synthase; Belongs to the alpha-IPM synthase/homocitrate synthase family. | 0.988 |
| ilvD_3 | metL_1 | EAG7_04044 | EAG7_03909 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Bifunctional aspartokinase/homoserine dehydrogenase 2. | 0.675 |