| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| budB | ilvA | DM82_6168 | DM82_5441 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme 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. | 0.923 |
| budB | ilvB | DM82_6168 | DM82_609 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type. | 0.640 |
| budB | ilvB_1 | DM82_6168 | DM82_5075 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | 0.635 |
| budB | ilvB_2 | DM82_6168 | DM82_4491 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | Thiamine pyrophosphate enzyme, central domain protein. | 0.668 |
| budB | ilvG | DM82_6168 | DM82_3092 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | 0.639 |
| budB | ilvN | DM82_6168 | DM82_610 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | Acolac_sm: acetolactate synthase, small subunit. | 0.940 |
| budB | leuB | DM82_6168 | DM82_5953 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | 0.967 |
| budB | psdht | DM82_6168 | DM82_1653 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | Phenylserine dehydratase. | 0.932 |
| ilvA | budB | DM82_5441 | DM82_6168 | 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. | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | 0.923 |
| ilvA | ilvB | DM82_5441 | DM82_609 | 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. | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type. | 0.940 |
| ilvA | ilvB_1 | DM82_5441 | DM82_5075 | 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. | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | 0.925 |
| ilvA | ilvB_2 | DM82_5441 | DM82_4491 | 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. | Thiamine pyrophosphate enzyme, central domain protein. | 0.933 |
| ilvA | ilvG | DM82_5441 | DM82_3092 | 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. | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | 0.923 |
| ilvA | ilvN | DM82_5441 | DM82_610 | 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. | Acolac_sm: acetolactate synthase, small subunit. | 0.957 |
| ilvA | leuB | DM82_5441 | DM82_5953 | 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. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | 0.946 |
| ilvA | psdht | DM82_5441 | DM82_1653 | 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. | Phenylserine dehydratase. | 0.925 |
| ilvA | thrC | DM82_5441 | DM82_1534 | 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. | thrC: threonine synthase. | 0.952 |
| ilvA | trpB | DM82_5441 | DM82_5948 | 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. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.930 |
| ilvB | budB | DM82_609 | DM82_6168 | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type. | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | 0.640 |
| ilvB | ilvA | DM82_609 | DM82_5441 | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type. | 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. | 0.940 |
