| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| gsh1 | ilvE-2 | AGA_2131 | AGA_2431 | Glutamate-cysteine ligase; Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC). Belongs to the glutamate--cysteine ligase type 2 family. EgtA subfamily. | Branched-chain amino acid aminotransferase. | 0.868 |
| gsh1 | putA | AGA_2131 | AGA_1201 | Glutamate-cysteine ligase; Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC). Belongs to the glutamate--cysteine ligase type 2 family. EgtA subfamily. | K00318 proline dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | 0.871 |
| hom | ilvA | AGA_2396 | AGA_1448 | Homoserine dehydrogenase. | 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. | 0.593 |
| hom | ilvE-2 | AGA_2396 | AGA_2431 | Homoserine dehydrogenase. | Branched-chain amino acid aminotransferase. | 0.904 |
| hom | thrB | AGA_2396 | AGA_2340 | Homoserine dehydrogenase. | Homoserine kinase type II; Belongs to the pseudomonas-type ThrB family. | 0.948 |
| ilvA | hom | AGA_1448 | AGA_2396 | 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. | Homoserine dehydrogenase. | 0.593 |
| ilvA | ilvD | AGA_1448 | AGA_1043 | 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; Belongs to the IlvD/Edd family. | 0.540 |
| ilvA | ilvD-2 | AGA_1448 | AGA_1044 | 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. | 0.540 |
| ilvA | ilvD-3 | AGA_1448 | AGA_241 | 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; Belongs to the IlvD/Edd family. | 0.540 |
| ilvA | ilvE-2 | AGA_1448 | AGA_2431 | 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. | 0.917 |
| ilvA | thrB | AGA_1448 | AGA_2340 | 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. | Homoserine kinase type II; Belongs to the pseudomonas-type ThrB family. | 0.466 |
| ilvD | ilvA | AGA_1043 | AGA_1448 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd 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. | 0.540 |
| ilvD | ilvD-2 | AGA_1043 | AGA_1044 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Dihydroxy-acid dehydratase. | 0.994 |
| ilvD | ilvE-2 | AGA_1043 | AGA_2431 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Branched-chain amino acid aminotransferase. | 0.795 |
| ilvD | leuA | AGA_1043 | AGA_569 | Dihydroxy-acid dehydratase; 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. | 0.669 |
| ilvD | panB | AGA_1043 | AGA_1313 | Dihydroxy-acid dehydratase; 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. | 0.556 |
| ilvD-2 | ilvA | AGA_1044 | AGA_1448 | Dihydroxy-acid dehydratase. | 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. | 0.540 |
| ilvD-2 | ilvD | AGA_1044 | AGA_1043 | Dihydroxy-acid dehydratase. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.994 |
| ilvD-2 | ilvE-2 | AGA_1044 | AGA_2431 | Dihydroxy-acid dehydratase. | Branched-chain amino acid aminotransferase. | 0.795 |
| ilvD-2 | leuA | AGA_1044 | AGA_569 | Dihydroxy-acid dehydratase. | 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. | 0.711 |