| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| gly | ilvA | MVIS_0815 | MVIS_4367 | L-allo-threonine aldolase. | 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. | 0.934 |
| gly | thrC | MVIS_0815 | MVIS_0831 | L-allo-threonine aldolase. | Threonine synthase. | 0.936 |
| ilvA | gly | MVIS_4367 | MVIS_0815 | 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. | L-allo-threonine aldolase. | 0.934 |
| ilvA | ilvD | MVIS_4367 | MVIS_4371 | 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. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.968 |
| ilvA | ilvE | MVIS_4367 | MVIS_4372 | 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. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.950 |
| ilvA | ilvG | MVIS_4367 | MVIS_4374 | 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 isozyme II large subunit. | 0.965 |
| ilvA | ilvH | MVIS_4367 | MVIS_0563 | 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 isozyme III small subunit. | 0.974 |
| ilvA | ilvI | MVIS_4367 | MVIS_0562 | 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 isozyme III large subunit. | 0.959 |
| ilvA | ilvM | MVIS_4367 | MVIS_4373 | 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 regulatory subunit. | 0.951 |
| ilvA | leuB | MVIS_4367 | MVIS_0557 | 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; 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. | 0.961 |
| ilvA | thrC | MVIS_4367 | MVIS_0831 | 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. | 0.969 |
| ilvA | trpB | MVIS_4367 | MVIS_1056 | 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 1; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.949 |
| ilvD | ilvA | MVIS_4371 | MVIS_4367 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd 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. | 0.968 |
| ilvD | ilvE | MVIS_4371 | MVIS_4372 | 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 | ilvG | MVIS_4371 | MVIS_4374 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Acetolactate synthase isozyme II large subunit. | 0.967 |
| ilvD | ilvH | MVIS_4371 | MVIS_0563 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Acetolactate synthase isozyme III small subunit. | 0.974 |
| ilvD | ilvI | MVIS_4371 | MVIS_0562 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Acetolactate synthase isozyme III large subunit. | 0.952 |
| ilvD | ilvM | MVIS_4371 | MVIS_4373 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Acetolactate synthase small regulatory subunit. | 0.938 |
| ilvD | leuB | MVIS_4371 | MVIS_0557 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd 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. | 0.863 |
| ilvD | thrC | MVIS_4371 | MVIS_0831 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Threonine synthase. | 0.698 |
