| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ilvA | mdeA_1 | RB151_042280 | RB151_004800 | 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 gamma-lyase. | 0.809 |
| ilvA | metA | RB151_042280 | RB151_004290 | 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. | Homoserine O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | 0.809 |
| ilvA | metB | RB151_042280 | RB151_043200 | 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. | Cystathionine gamma-synthase. | 0.820 |
| ilvA | metH | RB151_042280 | RB151_004390 | 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. | 0.881 |
| ilvA | metL | RB151_042280 | RB151_043190 | 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. | Bifunctional aspartokinase/homoserine dehydrogenase 2; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.580 |
| ilvA | serB | RB151_042280 | RB151_006460 | 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. | Phosphoserine phosphatase. | 0.902 |
| ilvA | thrA | RB151_042280 | RB151_006570 | 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. | Bifunctional aspartokinase/homoserine dehydrogenase 1; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.580 |
| ilvA | trpB | RB151_042280 | RB151_023440 | 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. | Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.933 |
| mdeA_1 | ilvA | RB151_004800 | RB151_042280 | Methionine gamma-lyase. | 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. | 0.809 |
| mdeA_1 | metA | RB151_004800 | RB151_004290 | Methionine gamma-lyase. | Homoserine O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | 0.963 |
| mdeA_1 | metB | RB151_004800 | RB151_043200 | Methionine gamma-lyase. | Cystathionine gamma-synthase. | 0.929 |
| mdeA_1 | metH | RB151_004800 | RB151_004390 | Methionine gamma-lyase. | 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 |
| mdeA_1 | metL | RB151_004800 | RB151_043190 | Methionine gamma-lyase. | Bifunctional aspartokinase/homoserine dehydrogenase 2; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.914 |
| mdeA_1 | thrA | RB151_004800 | RB151_006570 | Methionine gamma-lyase. | Bifunctional aspartokinase/homoserine dehydrogenase 1; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.914 |
| mdeA_1 | thrB | RB151_004800 | RB151_006580 | Methionine gamma-lyase. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.814 |
| metA | ilvA | RB151_004290 | RB151_042280 | Homoserine O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | 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. | 0.809 |
| metA | mdeA_1 | RB151_004290 | RB151_004800 | Homoserine O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | Methionine gamma-lyase. | 0.963 |
| metA | metB | RB151_004290 | RB151_043200 | Homoserine O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | Cystathionine gamma-synthase. | 0.973 |
| metA | metF | RB151_004290 | RB151_043140 | Homoserine O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | 5,10-methylenetetrahydrofolate reductase; Belongs to the methylenetetrahydrofolate reductase family. | 0.950 |
| metA | metH | RB151_004290 | RB151_004390 | Homoserine O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | 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. | 0.901 |
