node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
KQW91072.1 | ilvD | ASC79_17110 | ASC79_15015 | Amino acid dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | Dihydroxy-acid dehydratase; Catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate to 3-methyl-2-oxobutanoate in valine and isoleucine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | 0.862 |
KQW91072.1 | ilvE | ASC79_17110 | ASC79_12050 | Amino acid dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.875 |
KQW91072.1 | leuA | ASC79_17110 | ASC79_04995 | Amino acid dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | 2-isopropylmalate synthase; 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 1 subfamily. | 0.694 |
KQW91072.1 | leuA-2 | ASC79_17110 | ASC79_16505 | Amino acid dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | 2-isopropylmalate synthase; 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. | 0.694 |
KQW92567.1 | KQW94581.1 | ASC79_13810 | ASC79_02200 | Pyridoxal-5'-phosphate-dependent protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.667 |
KQW92567.1 | KQW95324.1 | ASC79_13810 | ASC79_06305 | Pyridoxal-5'-phosphate-dependent protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.864 |
KQW92567.1 | KQW95753.1 | ASC79_13810 | ASC79_08720 | Pyridoxal-5'-phosphate-dependent protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cystathionine beta-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.858 |
KQW92567.1 | ilvD | ASC79_13810 | ASC79_15015 | Pyridoxal-5'-phosphate-dependent protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dihydroxy-acid dehydratase; Catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate to 3-methyl-2-oxobutanoate in valine and isoleucine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | 0.753 |
KQW92567.1 | ilvE | ASC79_13810 | ASC79_12050 | Pyridoxal-5'-phosphate-dependent protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.913 |
KQW94581.1 | KQW92567.1 | ASC79_02200 | ASC79_13810 | Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Pyridoxal-5'-phosphate-dependent protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.667 |
KQW94581.1 | KQW95324.1 | ASC79_02200 | ASC79_06305 | Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.792 |
KQW94581.1 | KQW95753.1 | ASC79_02200 | ASC79_08720 | Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cystathionine beta-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.767 |
KQW94581.1 | ilvE | ASC79_02200 | ASC79_12050 | Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.845 |
KQW94581.1 | thrB | ASC79_02200 | ASC79_12480 | Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Homoserine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the pseudomonas-type ThrB family. | 0.942 |
KQW95324.1 | KQW92567.1 | ASC79_06305 | ASC79_13810 | 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. | Pyridoxal-5'-phosphate-dependent protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.864 |
KQW95324.1 | KQW94581.1 | ASC79_06305 | ASC79_02200 | 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. | Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.792 |
KQW95324.1 | KQW95753.1 | ASC79_06305 | ASC79_08720 | 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. | Cystathionine beta-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.870 |
KQW95324.1 | ilvD | ASC79_06305 | ASC79_15015 | 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. | Dihydroxy-acid dehydratase; Catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate to 3-methyl-2-oxobutanoate in valine and isoleucine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | 0.806 |
KQW95324.1 | ilvE | ASC79_06305 | ASC79_12050 | 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. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.885 |
KQW95324.1 | leuA | ASC79_06305 | ASC79_04995 | 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. | 2-isopropylmalate synthase; 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 1 subfamily. | 0.428 |