node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
alsS | ilvA | BSU36010 | BSU21770 | Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 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 (By similarity). | 0.961 |
alsS | ilvB | BSU36010 | BSU28310 | Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Acetolactate synthase (acetohydroxy-acid synthase) (large subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 0.938 |
alsS | ilvC | BSU36010 | BSU28290 | Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Acetohydroxy-acid isomeroreductase; 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. | 0.997 |
alsS | ilvD | BSU36010 | BSU21870 | Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Dihydroxy-acid dehydratase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the IlvD/Edd family. | 0.971 |
alsS | ilvE | BSU36010 | BSU02390 | Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Ketomethiobutyrate-branched-chain/aromatic amino acid aminotransferase; Transaminates branched-chain amino acids and ketoglutarate. Involved in the final step of the methionine regeneration pathway, where ketomethiobutyrate (KMTB) is converted to methionine via a transamination. The amino donor preference is isoleucine, leucine, valine, phenylalanine, and tyrosine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.810 |
alsS | ilvH | BSU36010 | BSU28300 | Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Acetolactate synthase (acetohydroxy-acid synthase) (small subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the acetolactate synthase small subunit family. | 0.998 |
alsS | leuA | BSU36010 | BSU28280 | Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 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. | 0.925 |
alsS | leuB | BSU36010 | BSU28270 | Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 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; Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily. | 0.950 |
alsS | leuC | BSU36010 | BSU28260 | Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 3-isopropylmalate dehydratase (large subunit); Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate; Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily. | 0.461 |
alsS | leuD | BSU36010 | BSU28250 | Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 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. | 0.477 |
ilvA | alsS | BSU21770 | BSU36010 | 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 (By similarity). | Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 0.961 |
ilvA | ilvB | BSU21770 | BSU28310 | 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 (By similarity). | Acetolactate synthase (acetohydroxy-acid synthase) (large subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 0.997 |
ilvA | ilvC | BSU21770 | BSU28290 | 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 (By similarity). | Acetohydroxy-acid isomeroreductase; 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. | 0.979 |
ilvA | ilvD | BSU21770 | BSU21870 | 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 (By similarity). | Dihydroxy-acid dehydratase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the IlvD/Edd family. | 0.997 |
ilvA | ilvE | BSU21770 | BSU02390 | 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 (By similarity). | Ketomethiobutyrate-branched-chain/aromatic amino acid aminotransferase; Transaminates branched-chain amino acids and ketoglutarate. Involved in the final step of the methionine regeneration pathway, where ketomethiobutyrate (KMTB) is converted to methionine via a transamination. The amino donor preference is isoleucine, leucine, valine, phenylalanine, and tyrosine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.989 |
ilvA | ilvH | BSU21770 | BSU28300 | 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 (By similarity). | Acetolactate synthase (acetohydroxy-acid synthase) (small subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the acetolactate synthase small subunit family. | 0.996 |
ilvA | leuA | BSU21770 | BSU28280 | 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 (By similarity). | 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. | 0.963 |
ilvA | leuB | BSU21770 | BSU28270 | 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 (By similarity). | 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; Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily. | 0.996 |
ilvA | leuC | BSU21770 | BSU28260 | 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 (By similarity). | 3-isopropylmalate dehydratase (large subunit); Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate; Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily. | 0.785 |
ilvA | leuD | BSU21770 | BSU28250 | 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 (By similarity). | 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. | 0.930 |