node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
PSEEN1897 | trpA | PSEEN1897 | PSEEN0037 | Putative para-aminodeoxychorismate synthase subunit I PabB; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Tryptophan synthase alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.941 |
PSEEN1897 | trpB | PSEEN1897 | PSEEN0038 | Putative para-aminodeoxychorismate synthase subunit I PabB; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Tryptophan synthase beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.948 |
PSEEN1897 | trpC | PSEEN1897 | PSEEN0449 | Putative para-aminodeoxychorismate synthase subunit I PabB; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Indole-3-glycerol phosphate synthase (IGPS); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the TrpC family. | 0.981 |
PSEEN1897 | trpD | PSEEN1897 | PSEEN0448 | Putative para-aminodeoxychorismate synthase subunit I PabB; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). | 0.969 |
PSEEN1897 | trpE | PSEEN1897 | PSEEN0444 | Putative para-aminodeoxychorismate synthase subunit I PabB; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Anthranilate synthase component I; Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentr [...] | 0.836 |
PSEEN1897 | trpF | PSEEN1897 | PSEEN1690 | Putative para-aminodeoxychorismate synthase subunit I PabB; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | N-(5'-phosphoribosyl)anthranilate isomerase (PRAI); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the TrpF family. | 0.937 |
PSEEN1897 | trpG | PSEEN1897 | PSEEN0447 | Putative para-aminodeoxychorismate synthase subunit I PabB; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Anthranilate synthase component II (Glutamine amido-transferase); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.999 |
PSEEN2008 | ilvA-1 | PSEEN2008 | PSEEN2960 | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Threonine dehydratase biosynthetic (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. | 0.919 |
PSEEN2008 | serB | PSEEN2008 | PSEEN4962 | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Phosphoserine phosphatase; Function of strongly homologous gene; enzyme. | 0.908 |
PSEEN2008 | trpA | PSEEN2008 | PSEEN0037 | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Tryptophan synthase alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.918 |
PSEEN2008 | trpB | PSEEN2008 | PSEEN0038 | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Tryptophan synthase beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.925 |
ilvA-1 | PSEEN2008 | PSEEN2960 | PSEEN2008 | Threonine dehydratase biosynthetic (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. | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | 0.919 |
ilvA-1 | serB | PSEEN2960 | PSEEN4962 | Threonine dehydratase biosynthetic (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. | Phosphoserine phosphatase; Function of strongly homologous gene; enzyme. | 0.908 |
ilvA-1 | trpA | PSEEN2960 | PSEEN0037 | Threonine dehydratase biosynthetic (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. | Tryptophan synthase alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.918 |
ilvA-1 | trpB | PSEEN2960 | PSEEN0038 | Threonine dehydratase biosynthetic (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. | Tryptophan synthase beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.925 |
serB | PSEEN2008 | PSEEN4962 | PSEEN2008 | Phosphoserine phosphatase; Function of strongly homologous gene; enzyme. | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | 0.908 |
serB | ilvA-1 | PSEEN4962 | PSEEN2960 | Phosphoserine phosphatase; Function of strongly homologous gene; enzyme. | Threonine dehydratase biosynthetic (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. | 0.908 |
serB | trpA | PSEEN4962 | PSEEN0037 | Phosphoserine phosphatase; Function of strongly homologous gene; enzyme. | Tryptophan synthase alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.908 |
serB | trpB | PSEEN4962 | PSEEN0038 | Phosphoserine phosphatase; Function of strongly homologous gene; enzyme. | Tryptophan synthase beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.930 |
trpA | PSEEN1897 | PSEEN0037 | PSEEN1897 | Tryptophan synthase alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | Putative para-aminodeoxychorismate synthase subunit I PabB; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | 0.941 |