| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PMM1714 | PMM1715 | PMM1714 | PMM1715 | Possible protein kinase:ABC1 family; Alternative locus ID: PMED4_19261. | Conserved hypothetical protein; Alternative locus ID: PMED4_19271. | 0.819 |
| PMM1714 | thrC | PMM1714 | PMM1716 | Possible protein kinase:ABC1 family; Alternative locus ID: PMED4_19261. | Threonine synthase: Pyridoxal-5'-phosphate-dependent enzymes, beta family; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.820 |
| PMM1715 | PMM1714 | PMM1715 | PMM1714 | Conserved hypothetical protein; Alternative locus ID: PMED4_19271. | Possible protein kinase:ABC1 family; Alternative locus ID: PMED4_19261. | 0.819 |
| PMM1715 | thrC | PMM1715 | PMM1716 | Conserved hypothetical protein; Alternative locus ID: PMED4_19271. | Threonine synthase: Pyridoxal-5'-phosphate-dependent enzymes, beta family; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.824 |
| 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, | leuD | PMM1512 | PMM0255 | Ferredoxin-dependent glutamate synthase, Fd-GOGAT; Alternative locus ID: PMED4_17221. | 3-isopropylmalate dehydratase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.673 |
| glsF, | lysC | PMM1512 | PMM1648 | Ferredoxin-dependent glutamate synthase, Fd-GOGAT; Alternative locus ID: PMED4_17221. | Aspartate kinase; Putative assignment; alpha and beta subunits, and additional region with similarity to beta subunit (BY SIMILARITY); Alternative locus ID: PMED4_18581. | 0.601 |
| glsF, | thrA,hom | PMM1512 | PMM1051 | Ferredoxin-dependent glutamate synthase, Fd-GOGAT; Alternative locus ID: PMED4_17221. | Homoserine dehydrogenase:ACT domain; Putative assignment; Alternative locus ID: PMED4_11971. | 0.662 |
| glsF, | thrB | PMM1512 | PMM0595 | Ferredoxin-dependent glutamate synthase, Fd-GOGAT; Alternative locus ID: PMED4_17221. | Homoserine kinase:GHMP kinases putative ATP-binding domain; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.540 |
| glsF, | thrC | PMM1512 | PMM1716 | Ferredoxin-dependent glutamate synthase, Fd-GOGAT; Alternative locus ID: PMED4_17221. | Threonine synthase: Pyridoxal-5'-phosphate-dependent enzymes, beta family; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.720 |
| 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 | lysC | PMM0908 | PMM1648 | 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. | Aspartate kinase; Putative assignment; alpha and beta subunits, and additional region with similarity to beta subunit (BY SIMILARITY); Alternative locus ID: PMED4_18581. | 0.430 |
| ilvA | thrA,hom | PMM0908 | PMM1051 | 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:ACT domain; Putative assignment; Alternative locus ID: PMED4_11971. | 0.431 |
| ilvA | thrC | PMM0908 | PMM1716 | 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. | Threonine synthase: Pyridoxal-5'-phosphate-dependent enzymes, beta family; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.983 |
| ilvC | glsF, | PMM1315 | PMM1512 | 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. | Ferredoxin-dependent glutamate synthase, Fd-GOGAT; Alternative locus ID: PMED4_17221. | 0.772 |
| ilvC | ilvA | PMM1315 | PMM0908 | 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. | 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. | 0.832 |
| ilvC | leuD | PMM1315 | PMM0255 | 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. | 3-isopropylmalate dehydratase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.760 |
| ilvC | thrB | PMM1315 | PMM0595 | 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. | Homoserine kinase:GHMP kinases putative ATP-binding domain; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.456 |
