| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 | AEB83199.1 | Alide2_0105 | Alide2_0783 | 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. | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | 0.929 |
| AEB82543.1 | AEB83428.1 | Alide2_0105 | Alide2_1021 | 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. | Acetolactate synthase; KEGG: ajs:Ajs_3488 hypothetical protein; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain. | 0.936 |
| AEB82543.1 | AEB83582.1 | Alide2_0105 | Alide2_1178 | 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: Threonine synthase; KEGG: dia:Dtpsy_2558 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | 0.944 |
| AEB82543.1 | AEB85394.1 | Alide2_0105 | Alide2_3047 | 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. | Acetolactate synthase; KEGG: ajs:Ajs_2520 thiamine pyrophosphate protein; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Belongs to the TPP enzyme family. | 0.936 |
| AEB82543.1 | AEB85472.1 | Alide2_0105 | Alide2_3130 | 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. | KEGG: ctt:CtCNB1_1659 acetolactate synthase, small subunit; TIGRFAM: Acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. | 0.957 |
| AEB82543.1 | AEB85473.1 | Alide2_0105 | Alide2_3131 | 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: Acetolactate synthase, large subunit, biosynthetic; KEGG: ajs:Ajs_1769 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, central domain. | 0.936 |
| AEB82543.1 | leuB | Alide2_0105 | Alide2_1305 | 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. | 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. | 0.932 |
| 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 | 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 |
| AEB82560.1 | trpB | Alide2_0122 | Alide2_1300 | 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. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.901 |
| AEB82560.1 | trpB-2 | Alide2_0122 | Alide2_2879 | 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. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.901 |
| AEB83199.1 | AEB82543.1 | Alide2_0783 | Alide2_0105 | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | 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. | 0.929 |
| AEB83199.1 | AEB83428.1 | Alide2_0783 | Alide2_1021 | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | Acetolactate synthase; KEGG: ajs:Ajs_3488 hypothetical protein; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain. | 0.944 |
| AEB83199.1 | AEB83582.1 | Alide2_0783 | Alide2_1178 | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | TIGRFAM: Threonine synthase; KEGG: dia:Dtpsy_2558 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | 0.435 |
| AEB83199.1 | AEB85394.1 | Alide2_0783 | Alide2_3047 | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | Acetolactate synthase; KEGG: ajs:Ajs_2520 thiamine pyrophosphate protein; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Belongs to the TPP enzyme family. | 0.944 |
| AEB83199.1 | AEB85472.1 | Alide2_0783 | Alide2_3130 | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | KEGG: ctt:CtCNB1_1659 acetolactate synthase, small subunit; TIGRFAM: Acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT. | 0.975 |
| AEB83199.1 | AEB85473.1 | Alide2_0783 | Alide2_3131 | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: ajs:Ajs_1769 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, central domain. | 0.958 |
| AEB83199.1 | leuB | Alide2_0783 | Alide2_1305 | KEGG: vei:Veis_1349 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. | 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. | 0.919 |
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