| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ilvA | ilvC | PSHAa2768 | PSHAa0849 | Threonine deaminase; 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 (NADP(+)); 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. | 0.736 |
| ilvA | ltaE | PSHAa2768 | PSHAb0295 | Threonine deaminase; 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. | Low-specificity L-threonine aldolase (Low-specificity L-TA); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.929 |
| ilvA | metL | PSHAa2768 | PSHAa2722 | Threonine deaminase; 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. | Bifunctional: aspartokinase II (N-terminal); Function of homologous gene experimentally demonstrated in an other organism; enzyme; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.644 |
| ilvA | tdh | PSHAa2768 | PSHAa2315 | Threonine deaminase; 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 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.914 |
| ilvA | thrA | PSHAa2768 | PSHAa2379 | Threonine deaminase; 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. | Bifunctional aspartokinase/homoserine dehydrogenase I; Function of homologous gene experimentally demonstrated in an other organism; enzyme; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.644 |
| ilvA | thrB | PSHAa2768 | PSHAa2378 | Threonine deaminase; 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; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.480 |
| ilvA | thrC | PSHAa2768 | PSHAa2377 | Threonine deaminase; 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; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.955 |
| ilvC | ilvA | PSHAa0849 | PSHAa2768 | Ketol-acid reductoisomerase (NADP(+)); 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 deaminase; 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. | 0.736 |
| ilvC | metL | PSHAa0849 | PSHAa2722 | Ketol-acid reductoisomerase (NADP(+)); 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. | Bifunctional: aspartokinase II (N-terminal); Function of homologous gene experimentally demonstrated in an other organism; enzyme; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.597 |
| ilvC | thrA | PSHAa0849 | PSHAa2379 | Ketol-acid reductoisomerase (NADP(+)); 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. | Bifunctional aspartokinase/homoserine dehydrogenase I; Function of homologous gene experimentally demonstrated in an other organism; enzyme; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.683 |
| ilvC | thrB | PSHAa0849 | PSHAa2378 | Ketol-acid reductoisomerase (NADP(+)); 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; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.676 |
| ilvC | thrC | PSHAa0849 | PSHAa2377 | Ketol-acid reductoisomerase (NADP(+)); 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 synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.916 |
| ltaE | ilvA | PSHAb0295 | PSHAa2768 | Low-specificity L-threonine aldolase (Low-specificity L-TA); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Threonine deaminase; 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. | 0.929 |
| ltaE | tdh | PSHAb0295 | PSHAa2315 | Low-specificity L-threonine aldolase (Low-specificity L-TA); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.907 |
| ltaE | thrC | PSHAb0295 | PSHAa2377 | Low-specificity L-threonine aldolase (Low-specificity L-TA); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Threonine synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.928 |
| lysC-2 | metL | PSHAa1250 | PSHAa2722 | Lysine-sensitive aspartokinase III; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the aspartokinase family. | Bifunctional: aspartokinase II (N-terminal); Function of homologous gene experimentally demonstrated in an other organism; enzyme; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.677 |
| lysC-2 | thrA | PSHAa1250 | PSHAa2379 | Lysine-sensitive aspartokinase III; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the aspartokinase family. | Bifunctional aspartokinase/homoserine dehydrogenase I; Function of homologous gene experimentally demonstrated in an other organism; enzyme; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.679 |
| lysC-2 | thrB | PSHAa1250 | PSHAa2378 | Lysine-sensitive aspartokinase III; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the aspartokinase family. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.909 |
| lysC-2 | thrC | PSHAa1250 | PSHAa2377 | Lysine-sensitive aspartokinase III; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the aspartokinase family. | Threonine synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.873 |
| metL | ilvA | PSHAa2722 | PSHAa2768 | Bifunctional: aspartokinase II (N-terminal); Function of homologous gene experimentally demonstrated in an other organism; enzyme; In the C-terminal section; belongs to the homoserine dehydrogenase family. | Threonine deaminase; 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. | 0.644 |
