| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| APD13348.1 | ilvA | RO07_13770 | RO07_12530 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | PLP-dependent 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. | 0.941 |
| APD13348.1 | ilvH | RO07_13770 | RO07_23660 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Acetolactate synthase small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.584 |
| APD13348.1 | thrC_1 | RO07_13770 | RO07_19590 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.900 |
| APD13348.1 | thrC_2 | RO07_13770 | RO07_10985 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.928 |
| ilvA | APD13348.1 | RO07_12530 | RO07_13770 | PLP-dependent 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.941 |
| ilvA | ilvB1 | RO07_12530 | RO07_15650 | PLP-dependent 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 catalytic subunit; Catalyzes the formation of 2-acetolactate from pyruvate, leucine sensitive; catalytic; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | 0.924 |
| ilvA | ilvB_1 | RO07_12530 | RO07_14805 | PLP-dependent 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | 0.928 |
| ilvA | ilvB_2 | RO07_12530 | RO07_22155 | PLP-dependent 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, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.924 |
| ilvA | ilvH | RO07_12530 | RO07_23660 | PLP-dependent 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 subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.961 |
| ilvA | leuB | RO07_12530 | RO07_18230 | PLP-dependent 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. | 0.943 |
| ilvA | sdaA | RO07_12530 | RO07_07670 | PLP-dependent 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-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.925 |
| ilvA | thrC_1 | RO07_12530 | RO07_19590 | PLP-dependent 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.942 |
| ilvA | thrC_2 | RO07_12530 | RO07_10985 | PLP-dependent 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.941 |
| ilvA | trpB | RO07_12530 | RO07_18255 | PLP-dependent 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. | 0.934 |
| ilvB1 | ilvA | RO07_15650 | RO07_12530 | Acetolactate synthase catalytic subunit; Catalyzes the formation of 2-acetolactate from pyruvate, leucine sensitive; catalytic; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | PLP-dependent 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. | 0.924 |
| ilvB1 | ilvB_1 | RO07_15650 | RO07_14805 | Acetolactate synthase catalytic subunit; Catalyzes the formation of 2-acetolactate from pyruvate, leucine sensitive; catalytic; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | 0.662 |
| ilvB1 | ilvB_2 | RO07_15650 | RO07_22155 | Acetolactate synthase catalytic subunit; Catalyzes the formation of 2-acetolactate from pyruvate, leucine sensitive; catalytic; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.663 |
| ilvB1 | ilvH | RO07_15650 | RO07_23660 | Acetolactate synthase catalytic subunit; Catalyzes the formation of 2-acetolactate from pyruvate, leucine sensitive; catalytic; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | Acetolactate synthase small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.964 |
| ilvB1 | leuB | RO07_15650 | RO07_18230 | Acetolactate synthase catalytic subunit; Catalyzes the formation of 2-acetolactate from pyruvate, leucine sensitive; catalytic; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme 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. | 0.969 |
| ilvB_1 | ilvA | RO07_14805 | RO07_12530 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | PLP-dependent 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. | 0.928 |
