Putative acetolactate synthase large subunit (ilvG); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the TPP enzyme family.

Threonine deaminase; 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.

Putative acetolactate synthase large subunit (ilvG); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the TPP enzyme family.

Dihydroxyacid dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family.

Putative acetolactate synthase large subunit (ilvG); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the TPP enzyme family.

Acetolactate synthase III, small subunit; Function of strongly homologous gene; enzyme.

Putative acetolactate synthase large subunit (ilvG); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the TPP enzyme family.

Acetolactate synthase III, large subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme.

Putative acetolactate synthase large subunit (ilvG); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; 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.

Threonine deaminase; 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.

Putative acetolactate synthase large subunit (ilvG); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the TPP enzyme family.

Threonine deaminase; 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.

Dihydroxyacid dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family.

Threonine deaminase; 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 III, small subunit; Function of strongly homologous gene; enzyme.

Threonine deaminase; 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 III, large subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme.

Threonine deaminase; 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.

Threonine deaminase; 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 deaminase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family.

Threonine deaminase; 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.

Serine-glyoxylate aminotransferase (SGAT); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family.

Threonine deaminase; 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.

Serine-glyoxylate aminotransferase; Function of homologous gene experimentally demonstrated in an other organism; enzyme.

Threonine deaminase; 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; Function of homologous gene experimentally demonstrated in an other organism; enzyme.

Threonine deaminase; 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 protein; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.

Dihydroxyacid dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family.

Putative acetolactate synthase large subunit (ilvG); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the TPP enzyme family.

Dihydroxyacid dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family.

Threonine deaminase; 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.

Dihydroxyacid dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family.

Acetolactate synthase III, small subunit; Function of strongly homologous gene; enzyme.

Dihydroxyacid dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family.

Acetolactate synthase III, large subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme.

Dihydroxyacid dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd 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.