node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AHN28407.1 | AHN28569.1 | SALWKB2_1025 | SALWKB2_1187 | Homoserine dehydrogenase. | Acetolactate synthase small subunit. | 0.798 |
AHN28407.1 | ilvA | SALWKB2_1025 | SALWKB2_0822 | Homoserine dehydrogenase. | Threonine dehydratase biosynthetic; 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. | 0.503 |
AHN28407.1 | ilvE | SALWKB2_1025 | SALWKB2_1248 | Homoserine dehydrogenase. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.884 |
AHN28407.1 | thrB | SALWKB2_1025 | SALWKB2_0065 | Homoserine dehydrogenase. | Homoserine kinase; Belongs to the pseudomonas-type ThrB family. | 0.928 |
AHN28569.1 | AHN28407.1 | SALWKB2_1187 | SALWKB2_1025 | Acetolactate synthase small subunit. | Homoserine dehydrogenase. | 0.798 |
AHN28569.1 | ilvA | SALWKB2_1187 | SALWKB2_0822 | Acetolactate synthase small subunit. | Threonine dehydratase biosynthetic; 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. | 0.975 |
AHN28569.1 | ilvD | SALWKB2_1187 | SALWKB2_0765 | Acetolactate synthase small subunit. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.732 |
AHN28569.1 | ilvE | SALWKB2_1187 | SALWKB2_1248 | Acetolactate synthase small subunit. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.593 |
AHN28569.1 | ldh | SALWKB2_1187 | SALWKB2_2218 | Acetolactate synthase small subunit. | L-lactate dehydrogenase; Catalyzes the conversion of lactate to pyruvate. | 0.830 |
AHN28569.1 | leuA | SALWKB2_1187 | SALWKB2_0444 | Acetolactate synthase small subunit. | 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. | 0.958 |
AHN28631.1 | ilvE | SALWKB2_1249 | SALWKB2_1248 | Hypothetical protein. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.608 |
AHN28769.1 | ilvE | SALWKB2_1387 | SALWKB2_1248 | Glutamate--cysteine ligase, divergent, of Alpha- and Beta-proteobacteria type. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.900 |
ilvA | AHN28407.1 | SALWKB2_0822 | SALWKB2_1025 | Threonine dehydratase biosynthetic; 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. | 0.503 |
ilvA | AHN28569.1 | SALWKB2_0822 | SALWKB2_1187 | Threonine dehydratase biosynthetic; 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. | 0.975 |
ilvA | ilvD | SALWKB2_0822 | SALWKB2_0765 | Threonine dehydratase biosynthetic; 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. | 0.934 |
ilvA | ilvE | SALWKB2_0822 | SALWKB2_1248 | Threonine dehydratase biosynthetic; 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. | 0.910 |
ilvA | ldh | SALWKB2_0822 | SALWKB2_2218 | Threonine dehydratase biosynthetic; 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-lactate dehydrogenase; Catalyzes the conversion of lactate to pyruvate. | 0.823 |
ilvD | AHN28569.1 | SALWKB2_0765 | SALWKB2_1187 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Acetolactate synthase small subunit. | 0.732 |
ilvD | ilvA | SALWKB2_0765 | SALWKB2_0822 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Threonine dehydratase biosynthetic; 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. | 0.934 |
ilvD | ilvE | SALWKB2_0765 | SALWKB2_1248 | Dihydroxy-acid dehydratase; 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. | 0.985 |