PLP-dependent 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; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family.

PLP-dependent 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.

PLP-dependent 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 2 catalytic subunit; Catalyzes the formation of 2-acetolactate from pyruvate; also known as acetolactate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.

PLP-dependent 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 small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.

PLP-dependent 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 3 large subunit; Catalyzes the formation of 2-acetolactate from pyruvate, leucine sensitive; Derived by automated computational analysis using gene prediction method: Protein Homology.

PLP-dependent 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 2 regulatory subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.

PLP-dependent 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; Derived by automated computational analysis using gene prediction method: Protein Homology.

PLP-dependent 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 ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family.

PLP-dependent 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 synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.

PLP-dependent 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 subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.

Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family.

PLP-dependent 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; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family.

Branched chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.

Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family.

Acetolactate synthase 2 catalytic subunit; Catalyzes the formation of 2-acetolactate from pyruvate; also known as acetolactate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.

Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family.

Acetolactate synthase small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.

Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family.

Acetolactate synthase 3 large subunit; Catalyzes the formation of 2-acetolactate from pyruvate, leucine sensitive; Derived by automated computational analysis using gene prediction method: Protein Homology.

Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family.

Acetolactate synthase 2 regulatory subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.

Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family.

3-isopropylmalate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.

Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family.

Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.

Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family.

Tryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.

Branched chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.

PLP-dependent 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.