| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ilvA | trpB | BSU21770 | BSU22640 | 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 (By similarity). | Tryptophan synthase (beta subunit); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.940 |
| ilvA | ysfE | BSU21770 | BSU28700 | 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 (By similarity). | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.800 |
| ilvA | ytbE | BSU21770 | BSU29050 | 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 (By similarity). | Putative aldo/keto reductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the aldo/keto reductase family. | 0.847 |
| ilvA | yvcT | BSU21770 | BSU34680 | 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 (By similarity). | Putative 2-hydroxyacid dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.836 |
| ilvA | yvgN | BSU21770 | BSU33400 | 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 (By similarity). | Glyoxal/methylglyoxal reductase; Reduces glyoxal and methylglyoxal (2-oxopropanal). Is not involved in the vitamin B6 biosynthesis; Belongs to the aldo/keto reductase family. | 0.815 |
| ilvA | ywbC | BSU21770 | BSU38370 | 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 (By similarity). | Putative lyase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the glyoxalase I family. | 0.804 |
| ilvA | yyaH | BSU21770 | BSU40860 | 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 (By similarity). | Putative lyase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.803 |
| trpB | ilvA | BSU22640 | BSU21770 | Tryptophan synthase (beta subunit); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 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 (By similarity). | 0.940 |
| trpB | ysfE | BSU22640 | BSU28700 | Tryptophan synthase (beta subunit); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.800 |
| trpB | ytbE | BSU22640 | BSU29050 | Tryptophan synthase (beta subunit); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | Putative aldo/keto reductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the aldo/keto reductase family. | 0.800 |
| trpB | yvcT | BSU22640 | BSU34680 | Tryptophan synthase (beta subunit); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | Putative 2-hydroxyacid dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.814 |
| trpB | yvgN | BSU22640 | BSU33400 | Tryptophan synthase (beta subunit); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | Glyoxal/methylglyoxal reductase; Reduces glyoxal and methylglyoxal (2-oxopropanal). Is not involved in the vitamin B6 biosynthesis; Belongs to the aldo/keto reductase family. | 0.800 |
| trpB | ywbC | BSU22640 | BSU38370 | Tryptophan synthase (beta subunit); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | Putative lyase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the glyoxalase I family. | 0.814 |
| trpB | yyaH | BSU22640 | BSU40860 | Tryptophan synthase (beta subunit); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | Putative lyase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.814 |
| ydeA | yurT | BSU05110 | BSU32660 | Putative enzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the peptidase C56 family. | Putative methylglyoxalase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the glyoxalase I family. | 0.732 |
| ydeA | ywbC | BSU05110 | BSU38370 | Putative enzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the peptidase C56 family. | Putative lyase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the glyoxalase I family. | 0.845 |
| yqgX | ysfE | BSU24790 | BSU28700 | Putative metal-binding hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.900 |
| yqgX | ywbC | BSU24790 | BSU38370 | Putative metal-binding hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative lyase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the glyoxalase I family. | 0.907 |
| yqgX | yyaH | BSU24790 | BSU40860 | Putative metal-binding hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative lyase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.905 |
| ysfE | ilvA | BSU28700 | BSU21770 | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 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 (By similarity). | 0.800 |
