| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADO46858.1 | ADO46863.1 | Entcl_0581 | Entcl_0586 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.935 |
| ADO46858.1 | ADO46919.1 | Entcl_0581 | Entcl_0642 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. | KEGG: enc:ECL_02360 cystathionine beta-synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; CBS domain containing protein; SMART: CBS domain containing protein. | 0.929 |
| ADO46858.1 | ADO47194.1 | Entcl_0581 | Entcl_0922 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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: L-serine dehydratase 1; KEGG: ent:Ent638_3250 L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.912 |
| ADO46858.1 | ADO49957.1 | Entcl_0581 | Entcl_3716 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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; KEGG: kpu:KP1_0820 bifunctional aspartokinase I/homeserine dehydrogenase I; TIGRFAM: aspartate kinase; PFAM: homoserine dehydrogenase; aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; homoserine dehydrogenase NAD-binding; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.601 |
| ADO46858.1 | ADO50564.1 | Entcl_0581 | Entcl_4334 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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; KEGG: cko:CKO_03054 bifunctional aspartate kinase II/homoserine dehydrogenase II; TIGRFAM: aspartate kinase; PFAM: homoserine dehydrogenase; aspartate/glutamate/uridylate kinase; homoserine dehydrogenase NAD-binding; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.601 |
| ADO46858.1 | ADO50565.1 | Entcl_0581 | Entcl_4335 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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 (thiol)-lyase; KEGG: cro:ROD_38041 cystathionine gamma-synthase; TIGRFAM: O-succinylhomoserine (thiol)-lyase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein. | 0.814 |
| ADO46858.1 | ilvA | Entcl_0581 | Entcl_4265 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. | 0.916 |
| ADO46858.1 | metAS | Entcl_0581 | Entcl_4152 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | 0.816 |
| ADO46858.1 | trpB | Entcl_0581 | Entcl_2526 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. | 0.924 |
| ADO46863.1 | ADO46858.1 | Entcl_0586 | Entcl_0581 | TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. | 0.935 |
| ADO46863.1 | ADO46919.1 | Entcl_0586 | Entcl_0642 | TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | KEGG: enc:ECL_02360 cystathionine beta-synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; CBS domain containing protein; SMART: CBS domain containing protein. | 0.910 |
| ADO46863.1 | ADO47194.1 | Entcl_0586 | Entcl_0922 | TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | TIGRFAM: L-serine dehydratase 1; KEGG: ent:Ent638_3250 L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.901 |
| ADO46863.1 | ADO49957.1 | Entcl_0586 | Entcl_3716 | TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Aspartate kinase; KEGG: kpu:KP1_0820 bifunctional aspartokinase I/homeserine dehydrogenase I; TIGRFAM: aspartate kinase; PFAM: homoserine dehydrogenase; aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; homoserine dehydrogenase NAD-binding; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.834 |
| ADO46863.1 | ADO50564.1 | Entcl_0586 | Entcl_4334 | TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Aspartate kinase; KEGG: cko:CKO_03054 bifunctional aspartate kinase II/homoserine dehydrogenase II; TIGRFAM: aspartate kinase; PFAM: homoserine dehydrogenase; aspartate/glutamate/uridylate kinase; homoserine dehydrogenase NAD-binding; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.834 |
| ADO46863.1 | ilvA | Entcl_0586 | Entcl_4265 | TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase 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. | 0.912 |
| ADO46863.1 | metAS | Entcl_0586 | Entcl_4152 | TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Homoserine O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | 0.812 |
| ADO46863.1 | trpB | Entcl_0586 | Entcl_2526 | TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.900 |
| ADO46919.1 | ADO46858.1 | Entcl_0642 | Entcl_0581 | KEGG: enc:ECL_02360 cystathionine beta-synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; CBS domain containing protein; SMART: CBS domain containing protein. | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. | 0.929 |
| ADO46919.1 | ADO46863.1 | Entcl_0642 | Entcl_0586 | KEGG: enc:ECL_02360 cystathionine beta-synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; CBS domain containing protein; SMART: CBS domain containing protein. | TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.910 |
| ADO46919.1 | ADO47194.1 | Entcl_0642 | Entcl_0922 | KEGG: enc:ECL_02360 cystathionine beta-synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; CBS domain containing protein; SMART: CBS domain containing protein. | TIGRFAM: L-serine dehydratase 1; KEGG: ent:Ent638_3250 L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.910 |