| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ilvA | ilvB | CV_3093 | CV_3889 | 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; Identified by sequence similarity; putative; ORF located using Blastx/COG0028; Belongs to the TPP enzyme family. | 0.938 |
| ilvA | ilvC | CV_3093 | CV_0588 | 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. | 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. | 0.691 |
| ilvA | ilvD | CV_3093 | CV_1277 | 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; Identified by sequence similarity; putative; ORF located using Blastx/COG0129; Belongs to the IlvD/Edd family. | 0.912 |
| ilvA | ilvH | CV_3093 | CV_0587 | 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 isozyme III, small subunit; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0440. | 0.967 |
| ilvA | ilvI | CV_3093 | CV_0586 | 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 isozyme III, large subunit; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG0028. | 0.946 |
| ilvA | leuB | CV_3093 | CV_2778 | 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; 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. | 0.952 |
| ilvA | maeB | CV_3093 | CV_0916 | 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. | NADP-dependent malate dehydrogenase; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0281. | 0.415 |
| ilvA | pflB | CV_3093 | CV_1412 | 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. | Formate C-acetyltransferase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1882. | 0.817 |
| ilvA | tdcB | CV_3093 | CV_3250 | 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 dehydratase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1171. | 0.915 |
| ilvB | ilvA | CV_3889 | CV_3093 | Acetolactate synthase; Identified by sequence similarity; putative; ORF located using Blastx/COG0028; Belongs to the TPP enzyme family. | 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. | 0.938 |
| ilvB | ilvC | CV_3889 | CV_0588 | Acetolactate synthase; Identified by sequence similarity; putative; ORF located using Blastx/COG0028; 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. | 0.995 |
| ilvB | ilvD | CV_3889 | CV_1277 | Acetolactate synthase; Identified by sequence similarity; putative; ORF located using Blastx/COG0028; Belongs to the TPP enzyme family. | Dihydroxy-acid dehydratase; Identified by sequence similarity; putative; ORF located using Blastx/COG0129; Belongs to the IlvD/Edd family. | 0.886 |
| ilvB | ilvH | CV_3889 | CV_0587 | Acetolactate synthase; Identified by sequence similarity; putative; ORF located using Blastx/COG0028; Belongs to the TPP enzyme family. | Acetolactate synthase isozyme III, small subunit; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0440. | 0.998 |
| ilvB | ilvI | CV_3889 | CV_0586 | Acetolactate synthase; Identified by sequence similarity; putative; ORF located using Blastx/COG0028; Belongs to the TPP enzyme family. | Acetolactate synthase isozyme III, large subunit; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG0028. | 0.923 |
| ilvB | leuA | CV_3889 | CV_0595 | Acetolactate synthase; Identified by sequence similarity; putative; ORF located using Blastx/COG0028; Belongs to the TPP enzyme 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. | 0.949 |
| ilvB | leuB | CV_3889 | CV_2778 | Acetolactate synthase; Identified by sequence similarity; putative; ORF located using Blastx/COG0028; 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. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily. | 0.980 |
| ilvB | maeB | CV_3889 | CV_0916 | Acetolactate synthase; Identified by sequence similarity; putative; ORF located using Blastx/COG0028; Belongs to the TPP enzyme family. | NADP-dependent malate dehydrogenase; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0281. | 0.927 |
| ilvB | pflB | CV_3889 | CV_1412 | Acetolactate synthase; Identified by sequence similarity; putative; ORF located using Blastx/COG0028; Belongs to the TPP enzyme family. | Formate C-acetyltransferase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1882. | 0.915 |
| ilvB | tdcB | CV_3889 | CV_3250 | Acetolactate synthase; Identified by sequence similarity; putative; ORF located using Blastx/COG0028; Belongs to the TPP enzyme family. | Threonine dehydratase; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1171. | 0.945 |
| ilvC | ilvA | CV_0588 | CV_3093 | 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. | 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. | 0.691 |
