node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Rfer_0344 | Rfer_0818 | Rfer_0344 | Rfer_0818 | L-threonine ammonia-lyase; 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:homoserine phosphotransferase / homoserine kinase / phosphoserine phosphatase. | 0.908 |
Rfer_0344 | Rfer_1084 | Rfer_0344 | Rfer_1084 | L-threonine ammonia-lyase; 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; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.926 |
Rfer_0344 | Rfer_2496 | Rfer_0344 | Rfer_2496 | L-threonine ammonia-lyase; 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. | CDP-diacylglycerol--serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | 0.903 |
Rfer_0344 | Rfer_3325 | Rfer_0344 | Rfer_3325 | L-threonine ammonia-lyase; 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. | CDP-diacylglycerol--serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | 0.903 |
Rfer_0344 | glyA | Rfer_0344 | Rfer_2658 | L-threonine ammonia-lyase; 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 hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.913 |
Rfer_0344 | ilvA | Rfer_0344 | Rfer_0733 | L-threonine ammonia-lyase; 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 ammonia-lyase; 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. | 0.915 |
Rfer_0344 | serB | Rfer_0344 | Rfer_1329 | L-threonine ammonia-lyase; 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 dephosphorylation of phosphoserine (P-Ser) in vitro. Also catalyzes the dephosphorylation of phosphothreonine (P-Thr) in vitro. | 0.908 |
Rfer_0344 | trpA | Rfer_0344 | Rfer_1787 | L-threonine ammonia-lyase; 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. | 0.925 |
Rfer_0344 | trpB-2 | Rfer_0344 | Rfer_1788 | L-threonine ammonia-lyase; 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. | 0.935 |
Rfer_0818 | Rfer_0344 | Rfer_0818 | Rfer_0344 | Phosphoserine:homoserine phosphotransferase / homoserine kinase / phosphoserine phosphatase. | L-threonine ammonia-lyase; 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. | 0.908 |
Rfer_0818 | Rfer_1084 | Rfer_0818 | Rfer_1084 | Phosphoserine:homoserine phosphotransferase / homoserine kinase / phosphoserine phosphatase. | L-serine ammonia-lyase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.915 |
Rfer_0818 | Rfer_2496 | Rfer_0818 | Rfer_2496 | Phosphoserine:homoserine phosphotransferase / homoserine kinase / phosphoserine phosphatase. | CDP-diacylglycerol--serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | 0.903 |
Rfer_0818 | Rfer_3325 | Rfer_0818 | Rfer_3325 | Phosphoserine:homoserine phosphotransferase / homoserine kinase / phosphoserine phosphatase. | CDP-diacylglycerol--serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | 0.903 |
Rfer_0818 | glyA | Rfer_0818 | Rfer_2658 | Phosphoserine:homoserine phosphotransferase / homoserine kinase / phosphoserine phosphatase. | Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.927 |
Rfer_0818 | ilvA | Rfer_0818 | Rfer_0733 | Phosphoserine:homoserine phosphotransferase / homoserine kinase / phosphoserine phosphatase. | L-threonine ammonia-lyase; 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. | 0.908 |
Rfer_0818 | serB | Rfer_0818 | Rfer_1329 | Phosphoserine:homoserine phosphotransferase / homoserine kinase / phosphoserine phosphatase. | Phosphoserine phosphatase; Catalyzes the dephosphorylation of phosphoserine (P-Ser) in vitro. Also catalyzes the dephosphorylation of phosphothreonine (P-Thr) in vitro. | 0.907 |
Rfer_0818 | serC | Rfer_0818 | Rfer_1570 | Phosphoserine:homoserine phosphotransferase / homoserine kinase / phosphoserine phosphatase. | Phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. | 0.943 |
Rfer_0818 | trpA | Rfer_0818 | Rfer_1787 | Phosphoserine:homoserine phosphotransferase / homoserine kinase / phosphoserine phosphatase. | 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. | 0.906 |
Rfer_0818 | trpB-2 | Rfer_0818 | Rfer_1788 | Phosphoserine:homoserine phosphotransferase / homoserine kinase / phosphoserine phosphatase. | Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.924 |
Rfer_1084 | Rfer_0344 | Rfer_1084 | Rfer_0344 | L-serine ammonia-lyase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | L-threonine ammonia-lyase; 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. | 0.926 |