node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ilvA | ilvB1 | MCHLDSM_01885 | MCHLDSM_02514 | 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 large subunit IlvB1. | 0.974 |
ilvA | ilvE_1 | MCHLDSM_01885 | MCHLDSM_03229 | 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. | 0.947 |
ilvA | ilvG_1 | MCHLDSM_01885 | MCHLDSM_04248 | 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 large subunit. | 0.960 |
ilvA | ilvG_2 | MCHLDSM_01885 | MCHLDSM_05561 | 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 large subunit; Belongs to the TPP enzyme family. | 0.961 |
ilvA | ilvH | MCHLDSM_01885 | MCHLDSM_02513 | 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 small subunit. | 0.989 |
ilvA | ilvX | MCHLDSM_01885 | MCHLDSM_07231 | 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. | Putative acetolactate synthase large subunit IlvX. | 0.954 |
ilvA | leuB | MCHLDSM_01885 | MCHLDSM_02508 | 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-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. | 0.942 |
ilvA | metH | MCHLDSM_01885 | MCHLDSM_03324 | 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. | Methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 0.925 |
ilvA | oxc | MCHLDSM_01885 | MCHLDSM_06951 | 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. | Oxalyl-CoA decarboxylase; Belongs to the TPP enzyme family. | 0.960 |
ilvA | thrC | MCHLDSM_01885 | MCHLDSM_06349 | 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. | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.972 |
ilvB1 | ilvA | MCHLDSM_02514 | MCHLDSM_01885 | Acetolactate synthase large subunit IlvB1. | 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. | 0.974 |
ilvB1 | ilvE_1 | MCHLDSM_02514 | MCHLDSM_03229 | Acetolactate synthase large subunit IlvB1. | Branched-chain-amino-acid aminotransferase. | 0.619 |
ilvB1 | ilvG_1 | MCHLDSM_02514 | MCHLDSM_04248 | Acetolactate synthase large subunit IlvB1. | Acetolactate synthase isozyme 2 large subunit. | 0.905 |
ilvB1 | ilvG_2 | MCHLDSM_02514 | MCHLDSM_05561 | Acetolactate synthase large subunit IlvB1. | Acetolactate synthase isozyme 2 large subunit; Belongs to the TPP enzyme family. | 0.855 |
ilvB1 | ilvH | MCHLDSM_02514 | MCHLDSM_02513 | Acetolactate synthase large subunit IlvB1. | Acetolactate synthase small subunit. | 0.999 |
ilvB1 | ilvX | MCHLDSM_02514 | MCHLDSM_07231 | Acetolactate synthase large subunit IlvB1. | Putative acetolactate synthase large subunit IlvX. | 0.886 |
ilvB1 | leuB | MCHLDSM_02514 | MCHLDSM_02508 | Acetolactate synthase large subunit IlvB1. | 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. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.964 |
ilvB1 | oxc | MCHLDSM_02514 | MCHLDSM_06951 | Acetolactate synthase large subunit IlvB1. | Oxalyl-CoA decarboxylase; Belongs to the TPP enzyme family. | 0.851 |
ilvB1 | thrC | MCHLDSM_02514 | MCHLDSM_06349 | Acetolactate synthase large subunit IlvB1. | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.400 |
ilvE_1 | ilvA | MCHLDSM_03229 | MCHLDSM_01885 | Branched-chain-amino-acid aminotransferase. | 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. | 0.947 |