| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BAV3241 | ilvA | BAV3241 | BAV3102 | Putative dihydroxy-acid/6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | Threonine dehydratase 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. | 0.584 |
| BAV3241 | ilvD | BAV3241 | BAV0317 | Putative dihydroxy-acid/6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.913 |
| BAV3241 | ilvE | BAV3241 | BAV0746 | Putative dihydroxy-acid/6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | Branched-chain amino acid aminotransferase. | 0.961 |
| BAV3241 | ilvE-2 | BAV3241 | BAV1085 | Putative dihydroxy-acid/6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | Putative branched-chain amino-acid aminotransferase. | 0.961 |
| BAV3241 | leuA1 | BAV3241 | BAV1174 | Putative dihydroxy-acid/6-phosphogluconate 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. | 0.954 |
| BAV3241 | leuA2 | BAV3241 | BAV3351 | Putative dihydroxy-acid/6-phosphogluconate 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. | 0.954 |
| BAV3241 | tdcB-2 | BAV3241 | BAV2664 | Putative dihydroxy-acid/6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | Threonine dehydratase catabolic. | 0.670 |
| gshA | ilvE | BAV3188 | BAV0746 | Glutamate--cysteine ligase; Start codon not provided. | Branched-chain amino acid aminotransferase. | 0.900 |
| gshA | ilvE-2 | BAV3188 | BAV1085 | Glutamate--cysteine ligase; Start codon not provided. | Putative branched-chain amino-acid aminotransferase. | 0.900 |
| hom | ilvE | BAV2163 | BAV0746 | Homoserine dehydrogenase. | Branched-chain amino acid aminotransferase. | 0.860 |
| hom | ilvE-2 | BAV2163 | BAV1085 | Homoserine dehydrogenase. | Putative branched-chain amino-acid aminotransferase. | 0.860 |
| ilvA | BAV3241 | BAV3102 | BAV3241 | Threonine dehydratase 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. | Putative dihydroxy-acid/6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.584 |
| ilvA | ilvD | BAV3102 | BAV0317 | Threonine dehydratase 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. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.584 |
| ilvA | ilvE | BAV3102 | BAV0746 | Threonine dehydratase 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. | 0.902 |
| ilvA | ilvE-2 | BAV3102 | BAV1085 | Threonine dehydratase 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. | Putative branched-chain amino-acid aminotransferase. | 0.858 |
| ilvA | ldh | BAV3102 | BAV3171 | Threonine dehydratase 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. | L-lactate dehydrogenase; Belongs to the LDH2/MDH2 oxidoreductase family. | 0.800 |
| ilvA | tdcB-2 | BAV3102 | BAV2664 | Threonine dehydratase 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. | Threonine dehydratase catabolic. | 0.917 |
| ilvD | BAV3241 | BAV0317 | BAV3241 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Putative dihydroxy-acid/6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.913 |
| ilvD | ilvA | BAV0317 | BAV3102 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Threonine dehydratase 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. | 0.584 |
| ilvD | ilvE | BAV0317 | BAV0746 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Branched-chain amino acid aminotransferase. | 0.961 |