| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| APR69898.1 | ilvA | AHTJS_05520 | AHTJS_08385 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | Threonine ammonia-lyase, 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. | 0.945 |
| APR69898.1 | ilvB_1 | AHTJS_05520 | AHTJS_13820 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.927 |
| APR69898.1 | ilvC | AHTJS_05520 | AHTJS_13810 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.984 |
| APR69898.1 | ilvD | AHTJS_05520 | AHTJS_00155 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | 0.715 |
| APR69898.1 | ilvN | AHTJS_05520 | AHTJS_13815 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | Acetolactate synthase small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.994 |
| APR69898.1 | leuA | AHTJS_05520 | AHTJS_02450 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | Homoserine O-acetyltransferase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily. | 0.892 |
| APR69898.1 | leuB | AHTJS_05520 | AHTJS_14320 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | 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. | 0.959 |
| APR69898.1 | leuC | AHTJS_05520 | AHTJS_14335 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | 3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.562 |
| APR69898.1 | leuD | AHTJS_05520 | AHTJS_14330 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | 3-isopropylmalate dehydratase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.531 |
| ilvA | APR69898.1 | AHTJS_08385 | AHTJS_05520 | Threonine ammonia-lyase, 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | 0.945 |
| ilvA | ilvB_1 | AHTJS_08385 | AHTJS_13820 | Threonine ammonia-lyase, 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. | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.954 |
| ilvA | ilvC | AHTJS_08385 | AHTJS_13810 | Threonine ammonia-lyase, 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. | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.698 |
| ilvA | ilvD | AHTJS_08385 | AHTJS_00155 | Threonine ammonia-lyase, 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. | Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | 0.827 |
| ilvA | ilvN | AHTJS_08385 | AHTJS_13815 | Threonine ammonia-lyase, 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. | Acetolactate synthase small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.969 |
| ilvA | leuA | AHTJS_08385 | AHTJS_02450 | Threonine ammonia-lyase, 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. | Homoserine O-acetyltransferase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily. | 0.469 |
| ilvA | leuB | AHTJS_08385 | AHTJS_14320 | Threonine ammonia-lyase, 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. | 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. | 0.966 |
| ilvA | leuC | AHTJS_08385 | AHTJS_14335 | Threonine ammonia-lyase, 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. | 3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.511 |
| ilvA | leuD | AHTJS_08385 | AHTJS_14330 | Threonine ammonia-lyase, 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. | 3-isopropylmalate dehydratase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.568 |
| ilvB_1 | APR69898.1 | AHTJS_13820 | AHTJS_05520 | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | 0.927 |
| ilvB_1 | ilvA | AHTJS_13820 | AHTJS_08385 | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | Threonine ammonia-lyase, 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. | 0.954 |
