| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEB82526.1 | AEB82543.1 | Alide2_0086 | Alide2_0105 | Manually curated; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; KEGG: dia:Dtpsy_0083 CDP-diacylglycerol/serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I 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. | 0.903 |
| AEB82526.1 | AEB82560.1 | Alide2_0086 | Alide2_0122 | Manually curated; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; KEGG: dia:Dtpsy_0083 CDP-diacylglycerol/serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | L-serine dehydratase 1; TIGRFAM: Iron-sulphur-dependent L-serine dehydratase single chain form; KEGG: dia:Dtpsy_0112 L-serine dehydratase 1; PFAM: Serine dehydratase-like, alpha subunit; Serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.915 |
| AEB82526.1 | AEB85950.1 | Alide2_0086 | Alide2_3625 | Manually curated; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; KEGG: dia:Dtpsy_0083 CDP-diacylglycerol/serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | TIGRFAM: Phosphoserine phosphatase SerB; HAD-superfamily hydrolase, subfamily IB, PSPase-like; KEGG: dia:Dtpsy_2506 phosphoserine phosphatase SerB; PFAM: Haloacid dehalogenase-like hydrolase. | 0.905 |
| AEB82526.1 | AEB86557.1 | Alide2_0086 | Alide2_4242 | Manually curated; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; KEGG: dia:Dtpsy_0083 CDP-diacylglycerol/serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | Threonine ammonia-lyase; KEGG: dia:Dtpsy_3120 hypothetical protein; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | 0.903 |
| AEB82526.1 | glyA | Alide2_0086 | Alide2_2128 | Manually curated; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; KEGG: dia:Dtpsy_0083 CDP-diacylglycerol/serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | Glycine 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. | 0.904 |
| AEB82526.1 | ilvA | Alide2_0086 | Alide2_0760 | Manually curated; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; KEGG: dia:Dtpsy_0083 CDP-diacylglycerol/serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | Threonine dehydratase, biosynthetic; 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. | 0.903 |
| AEB82526.1 | trpA | Alide2_0086 | Alide2_1299 | Manually curated; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; KEGG: dia:Dtpsy_0083 CDP-diacylglycerol/serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | Tryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.900 |
| AEB82526.1 | trpB | Alide2_0086 | Alide2_1300 | Manually curated; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; KEGG: dia:Dtpsy_0083 CDP-diacylglycerol/serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.900 |
| AEB82526.1 | trpB-2 | Alide2_0086 | Alide2_2879 | Manually curated; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; KEGG: dia:Dtpsy_0083 CDP-diacylglycerol/serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.900 |
| AEB82543.1 | AEB82526.1 | Alide2_0105 | Alide2_0086 | 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. | Manually curated; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; KEGG: dia:Dtpsy_0083 CDP-diacylglycerol/serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | 0.903 |
| AEB82543.1 | AEB82560.1 | Alide2_0105 | Alide2_0122 | 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 1; TIGRFAM: Iron-sulphur-dependent L-serine dehydratase single chain form; KEGG: dia:Dtpsy_0112 L-serine dehydratase 1; PFAM: Serine dehydratase-like, alpha subunit; Serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.924 |
| AEB82543.1 | AEB85950.1 | Alide2_0105 | Alide2_3625 | 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. | TIGRFAM: Phosphoserine phosphatase SerB; HAD-superfamily hydrolase, subfamily IB, PSPase-like; KEGG: dia:Dtpsy_2506 phosphoserine phosphatase SerB; PFAM: Haloacid dehalogenase-like hydrolase. | 0.908 |
| AEB82543.1 | AEB86557.1 | Alide2_0105 | Alide2_4242 | 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 ammonia-lyase; KEGG: dia:Dtpsy_3120 hypothetical protein; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | 0.924 |
| AEB82543.1 | glyA | Alide2_0105 | Alide2_2128 | 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. | Glycine 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 |
| AEB82543.1 | ilvA | Alide2_0105 | Alide2_0760 | 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 dehydratase, biosynthetic; 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 |
| AEB82543.1 | trpA | Alide2_0105 | Alide2_1299 | 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, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.922 |
| AEB82543.1 | trpB | Alide2_0105 | Alide2_1300 | 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 subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.929 |
| AEB82543.1 | trpB-2 | Alide2_0105 | Alide2_2879 | 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 subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.929 |
| AEB82560.1 | AEB82526.1 | Alide2_0122 | Alide2_0086 | L-serine dehydratase 1; TIGRFAM: Iron-sulphur-dependent L-serine dehydratase single chain form; KEGG: dia:Dtpsy_0112 L-serine dehydratase 1; PFAM: Serine dehydratase-like, alpha subunit; Serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Manually curated; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; KEGG: dia:Dtpsy_0083 CDP-diacylglycerol/serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | 0.915 |
| AEB82560.1 | AEB82543.1 | Alide2_0122 | Alide2_0105 | L-serine dehydratase 1; TIGRFAM: Iron-sulphur-dependent L-serine dehydratase single chain form; KEGG: dia:Dtpsy_0112 L-serine dehydratase 1; PFAM: Serine dehydratase-like, alpha subunit; Serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase 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. | 0.924 |