| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADO46307.1 | ADO46308.1 | Entcl_0028 | Entcl_0029 | KEGG: enc:ECL_00034 acetolactate synthase catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | PFAM: amino acid-binding ACT domain protein; KEGG: enc:ECL_00035 acetolactate synthase 1 regulatory subunit. | 0.999 |
| ADO46307.1 | ADO46858.1 | Entcl_0028 | Entcl_0581 | KEGG: enc:ECL_00034 acetolactate synthase catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central 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 |
| ADO46307.1 | ADO46863.1 | Entcl_0028 | Entcl_0586 | KEGG: enc:ECL_00034 acetolactate synthase catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central 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. | 0.509 |
| ADO46307.1 | ADO49888.1 | Entcl_0028 | Entcl_3647 | KEGG: enc:ECL_00034 acetolactate synthase catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | TIGRFAM: acetolactate synthase, small subunit; KEGG: kva:Kvar_4299 acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. | 0.994 |
| ADO46307.1 | ADO49889.1 | Entcl_0028 | Entcl_3648 | KEGG: enc:ECL_00034 acetolactate synthase catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | KEGG: kpe:KPK_4659 acetolactate synthase 3 catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | 0.910 |
| ADO46307.1 | ADO50502.1 | Entcl_0028 | Entcl_4269 | KEGG: enc:ECL_00034 acetolactate synthase catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | Manually curated; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; KEGG: enc:ECL_05014 acetolactate synthase 2 catalytic subunit; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | 0.906 |
| ADO46307.1 | leuB | Entcl_0028 | Entcl_3651 | KEGG: enc:ECL_00034 acetolactate synthase catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | 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. | 0.983 |
| ADO46308.1 | ADO46307.1 | Entcl_0029 | Entcl_0028 | PFAM: amino acid-binding ACT domain protein; KEGG: enc:ECL_00035 acetolactate synthase 1 regulatory subunit. | KEGG: enc:ECL_00034 acetolactate synthase catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | 0.999 |
| ADO46308.1 | ADO46858.1 | Entcl_0029 | Entcl_0581 | PFAM: amino acid-binding ACT domain protein; KEGG: enc:ECL_00035 acetolactate synthase 1 regulatory subunit. | 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. | 0.943 |
| ADO46308.1 | ADO49888.1 | Entcl_0029 | Entcl_3647 | PFAM: amino acid-binding ACT domain protein; KEGG: enc:ECL_00035 acetolactate synthase 1 regulatory subunit. | TIGRFAM: acetolactate synthase, small subunit; KEGG: kva:Kvar_4299 acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. | 0.928 |
| ADO46308.1 | ADO49889.1 | Entcl_0029 | Entcl_3648 | PFAM: amino acid-binding ACT domain protein; KEGG: enc:ECL_00035 acetolactate synthase 1 regulatory subunit. | KEGG: kpe:KPK_4659 acetolactate synthase 3 catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | 0.980 |
| ADO46308.1 | ADO49955.1 | Entcl_0029 | Entcl_3714 | PFAM: amino acid-binding ACT domain protein; KEGG: enc:ECL_00035 acetolactate synthase 1 regulatory subunit. | TIGRFAM: threonine synthase; KEGG: cko:CKO_03383 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | 0.567 |
| ADO46308.1 | ADO50502.1 | Entcl_0029 | Entcl_4269 | PFAM: amino acid-binding ACT domain protein; KEGG: enc:ECL_00035 acetolactate synthase 1 regulatory subunit. | Manually curated; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; KEGG: enc:ECL_05014 acetolactate synthase 2 catalytic subunit; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | 0.980 |
| ADO46308.1 | leuB | Entcl_0029 | Entcl_3651 | PFAM: amino acid-binding ACT domain protein; KEGG: enc:ECL_00035 acetolactate synthase 1 regulatory subunit. | 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. | 0.958 |
| ADO46858.1 | ADO46307.1 | Entcl_0581 | Entcl_0028 | 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_00034 acetolactate synthase catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | 0.929 |
| ADO46858.1 | ADO46308.1 | Entcl_0581 | Entcl_0029 | 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. | PFAM: amino acid-binding ACT domain protein; KEGG: enc:ECL_00035 acetolactate synthase 1 regulatory subunit. | 0.943 |
| 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 | ADO49888.1 | Entcl_0581 | Entcl_3647 | 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: acetolactate synthase, small subunit; KEGG: kva:Kvar_4299 acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. | 0.946 |
| ADO46858.1 | ADO49889.1 | Entcl_0581 | Entcl_3648 | 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: kpe:KPK_4659 acetolactate synthase 3 catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | 0.931 |