| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| dsdA | ilvA | BSU23770 | BSU21770 | D-serine ammonia-lyase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | 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 (By similarity). | 0.946 |
| dsdA | pth | BSU23770 | BSU00530 | D-serine ammonia-lyase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | peptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Belongs to the PTH family. | 0.862 |
| dsdA | racX | BSU23770 | BSU34430 | D-serine ammonia-lyase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | Amino acid racemase; Amino-acid racemase able to utilize a broad range of substrates. Preferentially catalyzes the epimerization of LL- diaminopimelate, as well as the racemization of D-lysine, L-arginine, L-ornithine, L-lysine and D-arginine. Has lower activity against D- ornithine, L-histidine, L-alanine, L-tyrosine, L-phenylalanine, L- serine, L-glutamine, L-methionine, L-asparagine and L-homoserine. Has weak activity against L-norleucine, L-aminobutyric acid and L- norvaline. Has no activity toward nine L-amino acids (Thr, Glu, Asp, Val, Leu, Ile, Trp, Cit and Aad). D-amino acids m [...] | 0.900 |
| dsdA | sdaAA | BSU23770 | BSU15860 | D-serine ammonia-lyase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | L-serine dehydratase (alpha chain); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.916 |
| dsdA | sdaAB | BSU23770 | BSU15850 | D-serine ammonia-lyase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | L-serine dehydratase (beta chain); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.916 |
| dsdA | yqjP | BSU23770 | BSU23790 | D-serine ammonia-lyase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | Putative metal-dependent hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.895 |
| dsdA | yqjQ | BSU23770 | BSU23780 | D-serine ammonia-lyase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | Putative metabolite dehydrogenase, NAD-binding; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | 0.900 |
| dsdA | yqjT | BSU23770 | BSU23750 | D-serine ammonia-lyase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | Putative lyase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.892 |
| dsdA | ysfE | BSU23770 | BSU28700 | D-serine ammonia-lyase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.800 |
| dsdA | yvgN | BSU23770 | BSU33400 | D-serine ammonia-lyase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | Glyoxal/methylglyoxal reductase; Reduces glyoxal and methylglyoxal (2-oxopropanal). Is not involved in the vitamin B6 biosynthesis; Belongs to the aldo/keto reductase family. | 0.801 |
| ilvA | dsdA | BSU21770 | BSU23770 | 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 (By similarity). | D-serine ammonia-lyase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | 0.946 |
| ilvA | racX | BSU21770 | BSU34430 | 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 (By similarity). | Amino acid racemase; Amino-acid racemase able to utilize a broad range of substrates. Preferentially catalyzes the epimerization of LL- diaminopimelate, as well as the racemization of D-lysine, L-arginine, L-ornithine, L-lysine and D-arginine. Has lower activity against D- ornithine, L-histidine, L-alanine, L-tyrosine, L-phenylalanine, L- serine, L-glutamine, L-methionine, L-asparagine and L-homoserine. Has weak activity against L-norleucine, L-aminobutyric acid and L- norvaline. Has no activity toward nine L-amino acids (Thr, Glu, Asp, Val, Leu, Ile, Trp, Cit and Aad). D-amino acids m [...] | 0.901 |
| ilvA | sdaAA | BSU21770 | BSU15860 | 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 (By similarity). | L-serine dehydratase (alpha chain); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.931 |
| ilvA | sdaAB | BSU21770 | BSU15850 | 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 (By similarity). | L-serine dehydratase (beta chain); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.958 |
| ilvA | ysfE | BSU21770 | BSU28700 | 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 (By similarity). | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.800 |
| ilvA | yvgN | BSU21770 | BSU33400 | 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 (By similarity). | Glyoxal/methylglyoxal reductase; Reduces glyoxal and methylglyoxal (2-oxopropanal). Is not involved in the vitamin B6 biosynthesis; Belongs to the aldo/keto reductase family. | 0.815 |
| pth | dsdA | BSU00530 | BSU23770 | peptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Belongs to the PTH family. | D-serine ammonia-lyase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | 0.862 |
| racX | dsdA | BSU34430 | BSU23770 | Amino acid racemase; Amino-acid racemase able to utilize a broad range of substrates. Preferentially catalyzes the epimerization of LL- diaminopimelate, as well as the racemization of D-lysine, L-arginine, L-ornithine, L-lysine and D-arginine. Has lower activity against D- ornithine, L-histidine, L-alanine, L-tyrosine, L-phenylalanine, L- serine, L-glutamine, L-methionine, L-asparagine and L-homoserine. Has weak activity against L-norleucine, L-aminobutyric acid and L- norvaline. Has no activity toward nine L-amino acids (Thr, Glu, Asp, Val, Leu, Ile, Trp, Cit and Aad). D-amino acids m [...] | D-serine ammonia-lyase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | 0.900 |
| racX | ilvA | BSU34430 | BSU21770 | Amino acid racemase; Amino-acid racemase able to utilize a broad range of substrates. Preferentially catalyzes the epimerization of LL- diaminopimelate, as well as the racemization of D-lysine, L-arginine, L-ornithine, L-lysine and D-arginine. Has lower activity against D- ornithine, L-histidine, L-alanine, L-tyrosine, L-phenylalanine, L- serine, L-glutamine, L-methionine, L-asparagine and L-homoserine. Has weak activity against L-norleucine, L-aminobutyric acid and L- norvaline. Has no activity toward nine L-amino acids (Thr, Glu, Asp, Val, Leu, Ile, Trp, Cit and Aad). D-amino acids m [...] | 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 (By similarity). | 0.901 |
| racX | sdaAA | BSU34430 | BSU15860 | Amino acid racemase; Amino-acid racemase able to utilize a broad range of substrates. Preferentially catalyzes the epimerization of LL- diaminopimelate, as well as the racemization of D-lysine, L-arginine, L-ornithine, L-lysine and D-arginine. Has lower activity against D- ornithine, L-histidine, L-alanine, L-tyrosine, L-phenylalanine, L- serine, L-glutamine, L-methionine, L-asparagine and L-homoserine. Has weak activity against L-norleucine, L-aminobutyric acid and L- norvaline. Has no activity toward nine L-amino acids (Thr, Glu, Asp, Val, Leu, Ile, Trp, Cit and Aad). D-amino acids m [...] | L-serine dehydratase (alpha chain); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.900 |
