| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AQS84675.1 | AQS85081.1 | A0U92_07680 | A0U92_10155 | Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.511 |
| AQS84675.1 | AQS86278.1 | A0U92_07680 | A0U92_05280 | Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Aspartate kinase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aspartokinase family. | 0.973 |
| AQS84675.1 | metX | A0U92_07680 | A0U92_16770 | Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Homoserine O-acetyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. | 0.985 |
| AQS84675.1 | metZ | A0U92_07680 | A0U92_09260 | Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide. | 0.882 |
| AQS85081.1 | AQS84675.1 | A0U92_10155 | A0U92_07680 | 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. | Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.511 |
| AQS85081.1 | AQS86179.1 | A0U92_10155 | A0U92_01360 | 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.917 |
| AQS85081.1 | AQS86278.1 | A0U92_10155 | A0U92_05280 | 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. | Aspartate kinase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aspartokinase family. | 0.418 |
| AQS85081.1 | glyA | A0U92_10155 | A0U92_04580 | 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. | 0.914 |
| AQS85081.1 | glyA-2 | A0U92_10155 | A0U92_13705 | 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. | 0.914 |
| AQS85081.1 | metX | A0U92_10155 | A0U92_16770 | 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. | Homoserine O-acetyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. | 0.833 |
| AQS85081.1 | metZ | A0U92_10155 | A0U92_09260 | 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. | O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide. | 0.871 |
| AQS85081.1 | trpA | A0U92_10155 | A0U92_01005 | 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 subunit alpha; 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 |
| AQS85081.1 | trpB | A0U92_10155 | A0U92_01010 | 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 subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.940 |
| AQS86135.1 | metX | A0U92_16775 | A0U92_16770 | Methionine biosynthesis protein MetW; Derived by automated computational analysis using gene prediction method: Protein Homology. | Homoserine O-acetyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. | 0.997 |
| AQS86179.1 | AQS85081.1 | A0U92_01360 | A0U92_10155 | Phosphoserine phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.917 |
| AQS86179.1 | glyA | A0U92_01360 | A0U92_04580 | Phosphoserine phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.923 |
| AQS86179.1 | glyA-2 | A0U92_01360 | A0U92_13705 | Phosphoserine phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.923 |
| AQS86179.1 | metX | A0U92_01360 | A0U92_16770 | Phosphoserine phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Homoserine O-acetyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. | 0.804 |
| AQS86179.1 | trpA | A0U92_01360 | A0U92_01005 | Phosphoserine phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Tryptophan synthase subunit alpha; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.902 |
| AQS86179.1 | trpB | A0U92_01360 | A0U92_01010 | Phosphoserine phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Tryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.917 |