| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AJC20850.1 | ilvE | RO07_10875 | RO07_11570 | Glutamate--cysteine ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Catalyzes the transamination of the branched-chain amino acids to their respective alpha-keto acids; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.900 |
| AJC23490.1 | ilvD_1 | RO07_19580 | RO07_14985 | Aminotransferase; 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. | 0.907 |
| AJC23490.1 | ilvD_2 | RO07_19580 | RO07_14980 | Aminotransferase; 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. | 0.907 |
| AJC23490.1 | ilvD_6 | RO07_19580 | RO07_01105 | Aminotransferase; 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. | 0.907 |
| AJC23490.1 | ilvD_7 | RO07_19580 | RO07_24340 | Aminotransferase; 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. | 0.907 |
| AJC23490.1 | ilvE | RO07_19580 | RO07_11570 | Aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Catalyzes the transamination of the branched-chain amino acids to their respective alpha-keto acids; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.916 |
| AJC23490.1 | leuA_1 | RO07_19580 | RO07_11970 | Aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.903 |
| AJC23490.1 | leuA_2 | RO07_19580 | RO07_23635 | Aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.903 |
| ilvA | ilvD_1 | RO07_12530 | RO07_14985 | 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. | 0.676 |
| ilvA | ilvD_2 | RO07_12530 | RO07_14980 | 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. | 0.686 |
| ilvA | ilvD_6 | RO07_12530 | RO07_01105 | 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. | 0.621 |
| ilvA | ilvD_7 | RO07_12530 | RO07_24340 | 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. | 0.642 |
| ilvA | ilvE | RO07_12530 | RO07_11570 | 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. | Catalyzes the transamination of the branched-chain amino acids to their respective alpha-keto acids; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.911 |
| ilvD_1 | AJC23490.1 | RO07_14985 | RO07_19580 | Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | Aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.907 |
| ilvD_1 | ilvA | RO07_14985 | RO07_12530 | 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. | 0.676 |
| ilvD_1 | ilvD_2 | RO07_14985 | RO07_14980 | Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | 0.469 |
| ilvD_1 | ilvE | RO07_14985 | RO07_11570 | Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | Catalyzes the transamination of the branched-chain amino acids to their respective alpha-keto acids; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.965 |
| ilvD_1 | leuA_1 | RO07_14985 | RO07_11970 | Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd 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. | 0.941 |
| ilvD_1 | leuA_2 | RO07_14985 | RO07_23635 | Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd 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. | 0.951 |
| ilvD_1 | panB | RO07_14985 | RO07_03465 | Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | 3-methyl-2-oxobutanoate hydroxymethyltransferase; Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate; Belongs to the PanB family. | 0.915 |