| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ilvA-2 | ilvB | SACE_4356 | SACE_0604 | Threonine dehydratase; 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 large subunit; Belongs to the TPP enzyme family. | 0.974 |
| ilvA-2 | ilvB-2 | SACE_4356 | SACE_6159 | Threonine dehydratase; 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 acetolactate synthase large subunit. | 0.976 |
| ilvA-2 | ilvB1 | SACE_4356 | SACE_3465 | Threonine dehydratase; 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; Belongs to the TPP enzyme family. | 0.937 |
| ilvA-2 | ilvB1-2 | SACE_4356 | SACE_4565 | Threonine dehydratase; 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; Belongs to the TPP enzyme family. | 0.937 |
| ilvA-2 | ilvB4 | SACE_4356 | SACE_5632 | Threonine dehydratase; 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 acetolactate synthase; Belongs to the TPP enzyme family. | 0.936 |
| ilvA-2 | ilvN | SACE_4356 | SACE_6158 | Threonine dehydratase; 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 small subunit. | 0.975 |
| ilvA-2 | leuB | SACE_4356 | SACE_3196 | Threonine dehydratase; 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. | 0.980 |
| ilvA-2 | leuB-2 | SACE_4356 | SACE_6154 | Threonine dehydratase; 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. | Beta-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. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.979 |
| ilvA-2 | thrC | SACE_4356 | SACE_6297 | Threonine dehydratase; 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 synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.935 |
| ilvA-2 | trpB | SACE_4356 | SACE_5749 | Threonine dehydratase; 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 chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.933 |
| ilvB | ilvA-2 | SACE_0604 | SACE_4356 | Acetolactate synthase large subunit; Belongs to the TPP enzyme family. | Threonine dehydratase; 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. | 0.974 |
| ilvB | ilvB-2 | SACE_0604 | SACE_6159 | Acetolactate synthase large subunit; Belongs to the TPP enzyme family. | Putative acetolactate synthase large subunit. | 0.667 |
| ilvB | ilvB1 | SACE_0604 | SACE_3465 | Acetolactate synthase large subunit; Belongs to the TPP enzyme family. | Acetolactate synthase; Belongs to the TPP enzyme family. | 0.675 |
| ilvB | ilvB1-2 | SACE_0604 | SACE_4565 | Acetolactate synthase large subunit; Belongs to the TPP enzyme family. | Acetolactate synthase; Belongs to the TPP enzyme family. | 0.708 |
| ilvB | ilvB4 | SACE_0604 | SACE_5632 | Acetolactate synthase large subunit; Belongs to the TPP enzyme family. | Putative acetolactate synthase; Belongs to the TPP enzyme family. | 0.656 |
| ilvB | ilvN | SACE_0604 | SACE_6158 | Acetolactate synthase large subunit; Belongs to the TPP enzyme family. | Acetolactate synthase small subunit. | 0.953 |
| ilvB | leuB | SACE_0604 | SACE_3196 | Acetolactate synthase large subunit; Belongs to the TPP enzyme family. | 3-isopropylmalate dehydrogenase. | 0.986 |
| ilvB | leuB-2 | SACE_0604 | SACE_6154 | Acetolactate synthase large subunit; Belongs to the TPP enzyme family. | Beta-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. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.983 |
| ilvB-2 | ilvA-2 | SACE_6159 | SACE_4356 | Putative acetolactate synthase large subunit. | Threonine dehydratase; 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. | 0.976 |
| ilvB-2 | ilvB | SACE_6159 | SACE_0604 | Putative acetolactate synthase large subunit. | Acetolactate synthase large subunit; Belongs to the TPP enzyme family. | 0.667 |
