| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EU91_0396 | ilvD | EU91_0396 | EU91_0804 | 4-Hydroxy-2-oxoglutarate aldolase; Alternative locus ID: PGP2_0718; 2-dehydro-3-deoxyphosphogluconate aldolase. | Dihydroxy-acid dehydratase; Alternative locus ID: PGP2_1110; Belongs to the IlvD/Edd family. | 0.870 |
| EU91_1859 | EU91_1920 | EU91_1859 | EU91_1920 | Aminodeoxychorismate lyase; Alternative locus ID: PGP2_0461. | Acetolactate synthase large subunit; Alternative locus ID: PGP2_1871. | 0.735 |
| EU91_1859 | ilvA | EU91_1859 | EU91_0924 | Aminodeoxychorismate lyase; Alternative locus ID: PGP2_0461. | 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. | 0.941 |
| EU91_1859 | ilvD | EU91_1859 | EU91_0804 | Aminodeoxychorismate lyase; Alternative locus ID: PGP2_0461. | Dihydroxy-acid dehydratase; Alternative locus ID: PGP2_1110; Belongs to the IlvD/Edd family. | 0.965 |
| EU91_1859 | ilvE | EU91_1859 | EU91_0954 | Aminodeoxychorismate lyase; Alternative locus ID: PGP2_0461. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.918 |
| EU91_1859 | leuA | EU91_1859 | EU91_1122 | Aminodeoxychorismate lyase; Alternative locus ID: PGP2_0461. | 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. | 0.969 |
| EU91_1859 | panB | EU91_1859 | EU91_1476 | Aminodeoxychorismate lyase; Alternative locus ID: PGP2_0461. | 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. | 0.901 |
| EU91_1920 | EU91_1859 | EU91_1920 | EU91_1859 | Acetolactate synthase large subunit; Alternative locus ID: PGP2_1871. | Aminodeoxychorismate lyase; Alternative locus ID: PGP2_0461. | 0.735 |
| EU91_1920 | ilvA | EU91_1920 | EU91_0924 | Acetolactate synthase large subunit; Alternative locus ID: PGP2_1871. | 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. | 0.969 |
| EU91_1920 | ilvC | EU91_1920 | EU91_1481 | Acetolactate synthase large subunit; Alternative locus ID: PGP2_1871. | 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. | 0.996 |
| EU91_1920 | ilvD | EU91_1920 | EU91_0804 | Acetolactate synthase large subunit; Alternative locus ID: PGP2_1871. | Dihydroxy-acid dehydratase; Alternative locus ID: PGP2_1110; Belongs to the IlvD/Edd family. | 0.972 |
| EU91_1920 | ilvE | EU91_1920 | EU91_0954 | Acetolactate synthase large subunit; Alternative locus ID: PGP2_1871. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.735 |
| EU91_1920 | leuA | EU91_1920 | EU91_1122 | Acetolactate synthase large subunit; Alternative locus ID: PGP2_1871. | 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. | 0.956 |
| EU91_1920 | leuC | EU91_1920 | EU91_0426 | Acetolactate synthase large subunit; Alternative locus ID: PGP2_1871. | 3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.727 |
| ilvA | EU91_1859 | EU91_0924 | EU91_1859 | 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. | Aminodeoxychorismate lyase; Alternative locus ID: PGP2_0461. | 0.941 |
| ilvA | EU91_1920 | EU91_0924 | EU91_1920 | 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 large subunit; Alternative locus ID: PGP2_1871. | 0.969 |
| ilvA | ilvC | EU91_0924 | EU91_1481 | 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. | 0.724 |
| ilvA | ilvD | EU91_0924 | EU91_0804 | 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; Alternative locus ID: PGP2_1110; Belongs to the IlvD/Edd family. | 0.847 |
| ilvA | ilvE | EU91_0924 | EU91_0954 | 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; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.961 |
| ilvA | leuA | EU91_0924 | EU91_1122 | 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. | 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. | 0.576 |