| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PMM0408 | ilvA | PMM0408 | PMM0908 | Possible Cystathionine gamma-synthase; Alternative locus ID: PMED4_04511. | 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. | 0.830 |
| PMM0408 | ilvE | PMM0408 | PMM0878 | Possible Cystathionine gamma-synthase; Alternative locus ID: PMED4_04511. | Putative Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.909 |
| PMM0408 | metH | PMM0408 | PMM0877 | Possible Cystathionine gamma-synthase; Alternative locus ID: PMED4_04511. | Putative 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. | 0.970 |
| PMM0408 | thrA,hom | PMM0408 | PMM1051 | Possible Cystathionine gamma-synthase; Alternative locus ID: PMED4_04511. | Homoserine dehydrogenase:ACT domain; Putative assignment; Alternative locus ID: PMED4_11971. | 0.864 |
| PMM0408 | thrB | PMM0408 | PMM0595 | Possible Cystathionine gamma-synthase; Alternative locus ID: PMED4_04511. | Homoserine kinase:GHMP kinases putative ATP-binding domain; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.826 |
| PMM1012 | ilvA | PMM1012 | PMM0908 | 4-hydroxybenzoyl-CoA thioesterase family active site; Alternative locus ID: PMED4_11421. | 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. | 0.683 |
| PMM1012 | ilvD | PMM1012 | PMM0774 | 4-hydroxybenzoyl-CoA thioesterase family active site; Alternative locus ID: PMED4_11421. | Dihydroxy-acid dehydratase; Alternative locus ID: PMED4_08591; Belongs to the IlvD/Edd family. | 0.871 |
| PMM1012 | ilvE | PMM1012 | PMM0878 | 4-hydroxybenzoyl-CoA thioesterase family active site; Alternative locus ID: PMED4_11421. | Putative Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.838 |
| ilvA | PMM0408 | PMM0908 | PMM0408 | 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. | Possible Cystathionine gamma-synthase; Alternative locus ID: PMED4_04511. | 0.830 |
| ilvA | PMM1012 | PMM0908 | PMM1012 | 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. | 4-hydroxybenzoyl-CoA thioesterase family active site; Alternative locus ID: PMED4_11421. | 0.683 |
| ilvA | ilvD | PMM0908 | PMM0774 | 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; Alternative locus ID: PMED4_08591; Belongs to the IlvD/Edd family. | 0.951 |
| ilvA | ilvE | PMM0908 | PMM0878 | 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 Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.956 |
| ilvA | leuA | PMM0908 | PMM1066 | 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. | 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 1 subfamily. | 0.759 |
| ilvA | metH | PMM0908 | PMM0877 | 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 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. | 0.903 |
| ilvA | thrA,hom | PMM0908 | PMM1051 | 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. | Homoserine dehydrogenase:ACT domain; Putative assignment; Alternative locus ID: PMED4_11971. | 0.431 |
| ilvD | PMM1012 | PMM0774 | PMM1012 | Dihydroxy-acid dehydratase; Alternative locus ID: PMED4_08591; Belongs to the IlvD/Edd family. | 4-hydroxybenzoyl-CoA thioesterase family active site; Alternative locus ID: PMED4_11421. | 0.871 |
| ilvD | ilvA | PMM0774 | PMM0908 | Dihydroxy-acid dehydratase; Alternative locus ID: PMED4_08591; 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. | 0.951 |
| ilvD | ilvE | PMM0774 | PMM0878 | Dihydroxy-acid dehydratase; Alternative locus ID: PMED4_08591; Belongs to the IlvD/Edd family. | Putative Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.988 |
| ilvD | leuA | PMM0774 | PMM1066 | Dihydroxy-acid dehydratase; Alternative locus ID: PMED4_08591; 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 1 subfamily. | 0.971 |
| ilvD | metH | PMM0774 | PMM0877 | Dihydroxy-acid dehydratase; Alternative locus ID: PMED4_08591; Belongs to the IlvD/Edd family. | Putative 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. | 0.712 |
