| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Acry_0909 | Acry_0996 | Acry_0909 | Acry_0996 | L-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. | TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.918 |
| Acry_0909 | Acry_1270 | Acry_0909 | Acry_1270 | L-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. | PFAM: isocitrate/isopropylmalate dehydrogenase. | 0.915 |
| Acry_0909 | Acry_1787 | Acry_0909 | Acry_1787 | L-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. | TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | 0.934 |
| Acry_0909 | Acry_1902 | Acry_0909 | Acry_1902 | L-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. | PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | 0.915 |
| Acry_0909 | Acry_2234 | Acry_0909 | Acry_2234 | L-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. | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | 0.920 |
| Acry_0909 | Acry_2832 | Acry_0909 | Acry_2832 | L-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. | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein. | 0.937 |
| Acry_0909 | Acry_2833 | Acry_0909 | Acry_2833 | L-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. | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein. | 0.927 |
| Acry_0909 | Acry_2860 | Acry_0909 | Acry_2860 | L-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. | PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme TPP binding domain protein. | 0.927 |
| Acry_0909 | leuB | Acry_0909 | Acry_2147 | L-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. | 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. | 0.926 |
| Acry_0909 | trpB | Acry_0909 | Acry_1328 | L-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, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.926 |
| Acry_0996 | Acry_0909 | Acry_0996 | Acry_0909 | TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | L-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. | 0.918 |
| Acry_0996 | Acry_1902 | Acry_0996 | Acry_1902 | TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | 0.918 |
| Acry_0996 | Acry_2234 | Acry_0996 | Acry_2234 | TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | 0.918 |
| Acry_0996 | trpB | Acry_0996 | Acry_1328 | TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.900 |
| Acry_1270 | Acry_0909 | Acry_1270 | Acry_0909 | PFAM: isocitrate/isopropylmalate dehydrogenase. | L-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. | 0.915 |
| Acry_1270 | Acry_1902 | Acry_1270 | Acry_1902 | PFAM: isocitrate/isopropylmalate dehydrogenase. | PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | 0.915 |
| Acry_1270 | Acry_2234 | Acry_1270 | Acry_2234 | PFAM: isocitrate/isopropylmalate dehydrogenase. | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | 0.915 |
| Acry_1270 | Acry_2832 | Acry_1270 | Acry_2832 | PFAM: isocitrate/isopropylmalate dehydrogenase. | TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein. | 0.968 |
| Acry_1270 | Acry_2833 | Acry_1270 | Acry_2833 | PFAM: isocitrate/isopropylmalate dehydrogenase. | TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein. | 0.946 |
| Acry_1270 | Acry_2860 | Acry_1270 | Acry_2860 | PFAM: isocitrate/isopropylmalate dehydrogenase. | PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme TPP binding domain protein. | 0.933 |
