node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
KLR56687.1 | KLR58268.1 | OX89_15860 | OX89_07440 | Acetolactate 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. | 0.965 |
KLR56687.1 | KLR58271.1 | OX89_15860 | OX89_07455 | Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 5-methyltetrahydrofolate--homocysteine methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.465 |
KLR56687.1 | KLR58281.1 | OX89_15860 | OX89_07505 | Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.644 |
KLR56687.1 | KLR59207.1 | OX89_15860 | OX89_02670 | Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Threonine synthase; Catalyzes the formation of L-threonine from O-phospho-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.686 |
KLR56687.1 | KLR59632.1 | OX89_15860 | OX89_00750 | Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.888 |
KLR56687.1 | ilvA | OX89_15860 | OX89_00355 | Acetolactate 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. | 0.955 |
KLR56687.1 | ilvE | OX89_15860 | OX89_07950 | Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.687 |
KLR58268.1 | KLR56687.1 | OX89_07440 | OX89_15860 | 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.965 |
KLR58268.1 | KLR58271.1 | OX89_07440 | OX89_07455 | 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. | 5-methyltetrahydrofolate--homocysteine methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.935 |
KLR58268.1 | KLR58281.1 | OX89_07440 | OX89_07505 | 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 dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.913 |
KLR58268.1 | KLR58413.1 | OX89_07440 | OX89_06885 | 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. | Alanine racemase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.894 |
KLR58268.1 | KLR59207.1 | OX89_07440 | OX89_02670 | 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; Catalyzes the formation of L-threonine from O-phospho-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.946 |
KLR58268.1 | KLR59632.1 | OX89_07440 | OX89_00750 | 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. | 0.819 |
KLR58268.1 | ilvA | OX89_07440 | OX89_00355 | 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 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. | 0.910 |
KLR58268.1 | ilvE | OX89_07440 | OX89_07950 | 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. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.921 |
KLR58268.1 | trpA | OX89_07440 | OX89_11860 | 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 alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.907 |
KLR58271.1 | KLR56687.1 | OX89_07455 | OX89_15860 | 5-methyltetrahydrofolate--homocysteine methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.465 |
KLR58271.1 | KLR58268.1 | OX89_07455 | OX89_07440 | 5-methyltetrahydrofolate--homocysteine methyltransferase; 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. | 0.935 |
KLR58271.1 | KLR59632.1 | OX89_07455 | OX89_00750 | 5-methyltetrahydrofolate--homocysteine methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.805 |
KLR58271.1 | ilvA | OX89_07455 | OX89_00355 | 5-methyltetrahydrofolate--homocysteine methyltransferase; 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. | 0.911 |