node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ilvA | sdaB_1 | LuPra_04592 | LuPra_02220 | L-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 dehydratase 2. | 0.914 |
ilvA | sdaB_2 | LuPra_04592 | LuPra_03332 | L-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 dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.914 |
ilvA | tdcB_1 | LuPra_04592 | LuPra_05890 | L-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-threonine dehydratase catabolic TdcB. | 0.920 |
ilvA | tdcB_2 | LuPra_04592 | LuPra_06028 | L-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-threonine dehydratase catabolic TdcB. | 0.924 |
ilvA | thrC_2 | LuPra_04592 | LuPra_04610 | L-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 gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.937 |
ilvA | trpB_1 | LuPra_04592 | LuPra_01049 | L-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 beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.901 |
sdaB_1 | ilvA | LuPra_02220 | LuPra_04592 | L-serine dehydratase 2. | L-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. | 0.914 |
sdaB_1 | sdaB_2 | LuPra_02220 | LuPra_03332 | L-serine dehydratase 2. | L-serine dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.915 |
sdaB_1 | tdcB_1 | LuPra_02220 | LuPra_05890 | L-serine dehydratase 2. | L-threonine dehydratase catabolic TdcB. | 0.914 |
sdaB_1 | tdcB_2 | LuPra_02220 | LuPra_06028 | L-serine dehydratase 2. | L-threonine dehydratase catabolic TdcB. | 0.914 |
sdaB_1 | trpB_1 | LuPra_02220 | LuPra_01049 | L-serine dehydratase 2. | Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.900 |
sdaB_2 | ilvA | LuPra_03332 | LuPra_04592 | L-serine dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | L-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. | 0.914 |
sdaB_2 | sdaB_1 | LuPra_03332 | LuPra_02220 | L-serine dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | L-serine dehydratase 2. | 0.915 |
sdaB_2 | tdcB_1 | LuPra_03332 | LuPra_05890 | L-serine dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | L-threonine dehydratase catabolic TdcB. | 0.914 |
sdaB_2 | tdcB_2 | LuPra_03332 | LuPra_06028 | L-serine dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | L-threonine dehydratase catabolic TdcB. | 0.914 |
sdaB_2 | trpB_1 | LuPra_03332 | LuPra_01049 | L-serine dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.900 |
tdcB_1 | ilvA | LuPra_05890 | LuPra_04592 | L-threonine dehydratase catabolic TdcB. | L-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. | 0.920 |
tdcB_1 | sdaB_1 | LuPra_05890 | LuPra_02220 | L-threonine dehydratase catabolic TdcB. | L-serine dehydratase 2. | 0.914 |
tdcB_1 | sdaB_2 | LuPra_05890 | LuPra_03332 | L-threonine dehydratase catabolic TdcB. | L-serine dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.914 |
tdcB_1 | tdcB_2 | LuPra_05890 | LuPra_06028 | L-threonine dehydratase catabolic TdcB. | L-threonine dehydratase catabolic TdcB. | 0.923 |