| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PMM1012 | ilvA | PMM1012 | PMM0908 | 4-hydroxybenzoyl-CoA thioesterase family active site; Alternative locus ID: PMED4_11421. | 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. | 0.683 |
| PMM1012 | ilvC | PMM1012 | PMM1315 | 4-hydroxybenzoyl-CoA thioesterase family active site; Alternative locus ID: PMED4_11421. | 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. | 0.858 |
| PMM1012 | ilvD | PMM1012 | PMM0774 | 4-hydroxybenzoyl-CoA thioesterase family active site; Alternative locus ID: PMED4_11421. | Dihydroxy-acid dehydratase; Alternative locus ID: PMED4_08591; Belongs to the IlvD/Edd family. | 0.871 |
| PMM1012 | ilvE | PMM1012 | PMM0878 | 4-hydroxybenzoyl-CoA thioesterase family active site; Alternative locus ID: PMED4_11421. | Putative Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.838 |
| cobD | ilvC | PMM1316 | PMM1315 | Putative cobalamin biosynthetic protein; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. | 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. | 0.818 |
| glsF, | ilvA | PMM1512 | PMM0908 | Ferredoxin-dependent glutamate synthase, Fd-GOGAT; Alternative locus ID: PMED4_17221. | 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. | 0.692 |
| glsF, | ilvC | PMM1512 | PMM1315 | Ferredoxin-dependent glutamate synthase, Fd-GOGAT; Alternative locus ID: PMED4_17221. | 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. | 0.772 |
| glsF, | ilvD | PMM1512 | PMM0774 | Ferredoxin-dependent glutamate synthase, Fd-GOGAT; Alternative locus ID: PMED4_17221. | Dihydroxy-acid dehydratase; Alternative locus ID: PMED4_08591; Belongs to the IlvD/Edd family. | 0.761 |
| glsF, | ilvE | PMM1512 | PMM0878 | Ferredoxin-dependent glutamate synthase, Fd-GOGAT; Alternative locus ID: PMED4_17221. | Putative Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.588 |
| glsF, | ilvH | PMM1512 | PMM0526 | Ferredoxin-dependent glutamate synthase, Fd-GOGAT; Alternative locus ID: PMED4_17221. | Acetolactate synthase large subunit; Alternative locus ID: PMED4_05751. | 0.704 |
| glsF, | ilvH-2 | PMM1512 | PMM1154 | Ferredoxin-dependent glutamate synthase, Fd-GOGAT; Alternative locus ID: PMED4_17221. | Acetolactate synthase small subunit; Alternative locus ID: PMED4_13141. | 0.716 |
| glsF, | leuB | PMM1512 | PMM0786 | Ferredoxin-dependent glutamate synthase, Fd-GOGAT; Alternative locus ID: PMED4_17221. | 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. | 0.652 |
| glsF, | leuC | PMM1512 | PMM0256 | Ferredoxin-dependent glutamate synthase, Fd-GOGAT; Alternative locus ID: PMED4_17221. | 3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.701 |
| ilvA | PMM1012 | PMM0908 | PMM1012 | 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. | 4-hydroxybenzoyl-CoA thioesterase family active site; Alternative locus ID: PMED4_11421. | 0.683 |
| ilvA | glsF, | PMM0908 | PMM1512 | 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. | Ferredoxin-dependent glutamate synthase, Fd-GOGAT; Alternative locus ID: PMED4_17221. | 0.692 |
| ilvA | ilvC | PMM0908 | PMM1315 | 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. | 0.832 |
| ilvA | ilvD | PMM0908 | PMM0774 | 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: PMED4_08591; Belongs to the IlvD/Edd family. | 0.951 |
| ilvA | ilvE | PMM0908 | PMM0878 | 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. | Putative Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.956 |
| ilvA | ilvH | PMM0908 | PMM0526 | 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: PMED4_05751. | 0.953 |
| ilvA | ilvH-2 | PMM0908 | PMM1154 | 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 small subunit; Alternative locus ID: PMED4_13141. | 0.950 |
