| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AKL34396.1 | ilvA | AB185_10995 | AB185_06310 | Cystathionine beta-synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.918 |
| AKL34396.1 | metAS | AB185_10995 | AB185_05555 | Cystathionine beta-synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Homoserine O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | 0.838 |
| AKL34396.1 | metB | AB185_10995 | AB185_06495 | Cystathionine beta-synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.993 |
| AKL34396.1 | metH | AB185_10995 | AB185_05525 | Cystathionine beta-synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | B12-dependent 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. | 0.954 |
| AKL34396.1 | metL | AB185_10995 | AB185_06490 | Cystathionine beta-synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Aspartate kinase; Multifunctional homodimeric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.852 |
| AKL34396.1 | serB | AB185_10995 | AB185_32125 | Cystathionine beta-synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Phosphoserine phosphatase; Catalyzes the formation of serine from O-phosphoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.916 |
| AKL34396.1 | thrA | AB185_10995 | AB185_32045 | Cystathionine beta-synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Aspartate kinase; Multifunctional homotetrameric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.852 |
| AKL34396.1 | thrB | AB185_10995 | AB185_32040 | Cystathionine beta-synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Serine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.828 |
| AKL34396.1 | trpB | AB185_10995 | AB185_23865 | Cystathionine beta-synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Tryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.915 |
| ilvA | AKL34396.1 | AB185_06310 | AB185_10995 | 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. | Cystathionine beta-synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.918 |
| ilvA | metAS | AB185_06310 | AB185_05555 | 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 O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | 0.818 |
| ilvA | metB | AB185_06310 | AB185_06495 | 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. | Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.840 |
| ilvA | metH | AB185_06310 | AB185_05525 | 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. | B12-dependent 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. | 0.889 |
| ilvA | metL | AB185_06310 | AB185_06490 | 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. | Aspartate kinase; Multifunctional homodimeric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.627 |
| ilvA | serB | AB185_06310 | AB185_32125 | 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. | Phosphoserine phosphatase; Catalyzes the formation of serine from O-phosphoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.905 |
| ilvA | thrA | AB185_06310 | AB185_32045 | 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. | Aspartate kinase; Multifunctional homotetrameric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.739 |
| ilvA | thrB | AB185_06310 | AB185_32040 | 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. | Serine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.443 |
| ilvA | trpB | AB185_06310 | AB185_23865 | 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 subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.938 |
| metAS | AKL34396.1 | AB185_05555 | AB185_10995 | Homoserine O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | Cystathionine beta-synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.838 |
| metAS | ilvA | AB185_05555 | AB185_06310 | Homoserine O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA 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. | 0.818 |
