node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
glyA | ilvA | cg1133 | cg2334 | 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. | 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). | 0.949 |
glyA | tdcB | cg1133 | cg1116 | 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. | THREONINE DEHYDRATASE. | 0.935 |
glyA | thrC | cg1133 | cg2437 | 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. | THREONINE SYNTHASE; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.457 |
hom | ilvA | cg1337 | cg2334 | Homoserine Dehydrogenase; Belongs to the homoserine dehydrogenase family. | 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). | 0.973 |
hom | ilvB | cg1337 | cg1435 | Homoserine Dehydrogenase; Belongs to the homoserine dehydrogenase family. | ACETOLACTATE SYNTHASE. | 0.738 |
hom | ilvD | cg1337 | cg1432 | Homoserine Dehydrogenase; Belongs to the homoserine dehydrogenase family. | DIHYDROXY-ACID DEHYDRATASE; Belongs to the IlvD/Edd family. | 0.488 |
hom | ilvE | cg1337 | cg2418 | Homoserine Dehydrogenase; Belongs to the homoserine dehydrogenase family. | BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE. | 0.903 |
hom | ilvN | cg1337 | cg1436 | Homoserine Dehydrogenase; Belongs to the homoserine dehydrogenase family. | ACETOHYDROXYACID SYNTHASE SMALL SUBUNIT. | 0.885 |
hom | leuB | cg1337 | cg1453 | Homoserine Dehydrogenase; Belongs to the homoserine dehydrogenase family. | 3-ISOPROPYLMALATE DEHYDROGENASE; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate (By similarity); Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.501 |
hom | tdcB | cg1337 | cg1116 | Homoserine Dehydrogenase; Belongs to the homoserine dehydrogenase family. | THREONINE DEHYDRATASE. | 0.790 |
hom | thrB | cg1337 | cg1338 | Homoserine Dehydrogenase; Belongs to the homoserine dehydrogenase family. | Homoserine Kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.999 |
hom | thrC | cg1337 | cg2437 | Homoserine Dehydrogenase; Belongs to the homoserine dehydrogenase family. | THREONINE SYNTHASE; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.997 |
ilvA | glyA | cg2334 | cg1133 | 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). | 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. | 0.949 |
ilvA | hom | cg2334 | cg1337 | 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). | Homoserine Dehydrogenase; Belongs to the homoserine dehydrogenase family. | 0.973 |
ilvA | ilvB | cg2334 | cg1435 | 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). | ACETOLACTATE SYNTHASE. | 0.997 |
ilvA | ilvD | cg2334 | cg1432 | 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). | DIHYDROXY-ACID DEHYDRATASE; Belongs to the IlvD/Edd family. | 0.972 |
ilvA | ilvE | cg2334 | cg2418 | 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). | BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE. | 0.995 |
ilvA | ilvN | cg2334 | cg1436 | 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). | ACETOHYDROXYACID SYNTHASE SMALL SUBUNIT. | 0.984 |
ilvA | leuB | cg2334 | cg1453 | 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). | 3-ISOPROPYLMALATE DEHYDROGENASE; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate (By similarity); Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.982 |
ilvA | tdcB | cg2334 | cg1116 | 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). | THREONINE DEHYDRATASE. | 0.934 |