| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEB82543.1 | AEB83420.1 | Alide2_0105 | Alide2_1013 | 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: Para-aminobenzoate synthase, component I; KEGG: ajs:Ajs_3496 para-aminobenzoate synthase, subunit I; PFAM: Chorismate binding, C-terminal; Aminotransferase, class IV. | 0.584 |
| 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 | 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-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 |
| AEB83420.1 | AEB82543.1 | Alide2_1013 | Alide2_0105 | TIGRFAM: Para-aminobenzoate synthase, component I; KEGG: ajs:Ajs_3496 para-aminobenzoate synthase, subunit I; PFAM: Chorismate binding, C-terminal; Aminotransferase, class IV. | 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. | 0.584 |
| AEB83420.1 | AEB86557.1 | Alide2_1013 | Alide2_4242 | TIGRFAM: Para-aminobenzoate synthase, component I; KEGG: ajs:Ajs_3496 para-aminobenzoate synthase, subunit I; PFAM: Chorismate binding, C-terminal; Aminotransferase, class IV. | Threonine ammonia-lyase; KEGG: dia:Dtpsy_3120 hypothetical protein; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | 0.584 |
| AEB83420.1 | AEB86693.1 | Alide2_1013 | Alide2_4388 | TIGRFAM: Para-aminobenzoate synthase, component I; KEGG: ajs:Ajs_3496 para-aminobenzoate synthase, subunit I; PFAM: Chorismate binding, C-terminal; Aminotransferase, class IV. | TIGRFAM: Anthranilate synthase, glutamine amidotransferase domain; KEGG: dia:Dtpsy_0358 anthranilate synthase component II; PFAM: Glutamine amidotransferase class-I, C-terminal. | 0.999 |
| AEB83420.1 | ilvA | Alide2_1013 | Alide2_0760 | TIGRFAM: Para-aminobenzoate synthase, component I; KEGG: ajs:Ajs_3496 para-aminobenzoate synthase, subunit I; PFAM: Chorismate binding, C-terminal; Aminotransferase, class IV. | 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. | 0.584 |
| AEB83420.1 | trpA | Alide2_1013 | Alide2_1299 | TIGRFAM: Para-aminobenzoate synthase, component I; KEGG: ajs:Ajs_3496 para-aminobenzoate synthase, subunit I; PFAM: Chorismate binding, C-terminal; Aminotransferase, class IV. | 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. | 0.954 |
| AEB83420.1 | trpB-2 | Alide2_1013 | Alide2_2879 | TIGRFAM: Para-aminobenzoate synthase, component I; KEGG: ajs:Ajs_3496 para-aminobenzoate synthase, subunit I; PFAM: Chorismate binding, C-terminal; Aminotransferase, class IV. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.932 |
| AEB83420.1 | trpC | Alide2_1013 | Alide2_4385 | TIGRFAM: Para-aminobenzoate synthase, component I; KEGG: ajs:Ajs_3496 para-aminobenzoate synthase, subunit I; PFAM: Chorismate binding, C-terminal; Aminotransferase, class IV. | KEGG: dia:Dtpsy_0361 indole-3-glycerol-phosphate synthase; PFAM: Indole-3-glycerol phosphate synthase; Belongs to the TrpC family. | 0.985 |
| AEB83420.1 | trpD | Alide2_1013 | Alide2_4387 | TIGRFAM: Para-aminobenzoate synthase, component I; KEGG: ajs:Ajs_3496 para-aminobenzoate synthase, subunit I; PFAM: Chorismate binding, C-terminal; Aminotransferase, class IV. | Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). | 0.983 |
| AEB83420.1 | trpE | Alide2_1013 | Alide2_4395 | TIGRFAM: Para-aminobenzoate synthase, component I; KEGG: ajs:Ajs_3496 para-aminobenzoate synthase, subunit I; PFAM: Chorismate binding, C-terminal; Aminotransferase, class IV. | Anthranilate synthase component I; Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentr [...] | 0.888 |
| AEB83420.1 | trpF | Alide2_1013 | Alide2_1301 | TIGRFAM: Para-aminobenzoate synthase, component I; KEGG: ajs:Ajs_3496 para-aminobenzoate synthase, subunit I; PFAM: Chorismate binding, C-terminal; Aminotransferase, class IV. | KEGG: ajs:Ajs_3238 phosphoribosylanthranilate isomerase; PFAM: N-(5'phosphoribosyl)anthranilate isomerase (PRAI); Belongs to the TrpF family. | 0.941 |
| AEB86557.1 | AEB82543.1 | Alide2_4242 | Alide2_0105 | Threonine ammonia-lyase; KEGG: dia:Dtpsy_3120 hypothetical protein; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | 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 |
| AEB86557.1 | AEB83420.1 | Alide2_4242 | Alide2_1013 | Threonine ammonia-lyase; KEGG: dia:Dtpsy_3120 hypothetical protein; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | TIGRFAM: Para-aminobenzoate synthase, component I; KEGG: ajs:Ajs_3496 para-aminobenzoate synthase, subunit I; PFAM: Chorismate binding, C-terminal; Aminotransferase, class IV. | 0.584 |
| AEB86557.1 | ilvA | Alide2_4242 | Alide2_0760 | Threonine ammonia-lyase; KEGG: dia:Dtpsy_3120 hypothetical protein; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | 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. | 0.924 |
| AEB86557.1 | trpA | Alide2_4242 | Alide2_1299 | Threonine ammonia-lyase; KEGG: dia:Dtpsy_3120 hypothetical protein; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | 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 |
| AEB86557.1 | trpB-2 | Alide2_4242 | Alide2_2879 | Threonine ammonia-lyase; KEGG: dia:Dtpsy_3120 hypothetical protein; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.929 |