node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CFU_0328 | ilvA | CFU_0328 | CFU_0624 | Pyridoxal-phosphate-dependent enzyme, beta subunit. | Threonine dehydratase biosynthetic; 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. | 0.915 |
CFU_0328 | pabB | CFU_0328 | CFU_1180 | Pyridoxal-phosphate-dependent enzyme, beta subunit. | Aminodeoxychorismate lyase. | 0.555 |
CFU_0328 | sdsL | CFU_0328 | CFU_4268 | Pyridoxal-phosphate-dependent enzyme, beta subunit. | Putative L-serine dehydratase protein. | 0.928 |
CFU_0328 | trpA | CFU_0328 | CFU_1874 | Pyridoxal-phosphate-dependent enzyme, beta subunit. | Tryptophan synthase alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.914 |
CFU_0328 | trpB | CFU_0328 | CFU_1873 | Pyridoxal-phosphate-dependent enzyme, beta subunit. | Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.927 |
ilvA | CFU_0328 | CFU_0624 | CFU_0328 | Threonine dehydratase biosynthetic; 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. | Pyridoxal-phosphate-dependent enzyme, beta subunit. | 0.915 |
ilvA | pabB | CFU_0624 | CFU_1180 | Threonine dehydratase biosynthetic; 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. | Aminodeoxychorismate lyase. | 0.555 |
ilvA | sdsL | CFU_0624 | CFU_4268 | Threonine dehydratase biosynthetic; 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 protein. | 0.925 |
ilvA | trpA | CFU_0624 | CFU_1874 | Threonine dehydratase biosynthetic; 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 chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.914 |
ilvA | trpB | CFU_0624 | CFU_1873 | Threonine dehydratase biosynthetic; 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 chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.927 |
pabB | CFU_0328 | CFU_1180 | CFU_0328 | Aminodeoxychorismate lyase. | Pyridoxal-phosphate-dependent enzyme, beta subunit. | 0.555 |
pabB | ilvA | CFU_1180 | CFU_0624 | Aminodeoxychorismate lyase. | Threonine dehydratase biosynthetic; 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. | 0.555 |
pabB | sdsL | CFU_1180 | CFU_4268 | Aminodeoxychorismate lyase. | Putative L-serine dehydratase protein. | 0.555 |
pabB | trpA | CFU_1180 | CFU_1874 | Aminodeoxychorismate lyase. | Tryptophan synthase alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.970 |
pabB | trpB | CFU_1180 | CFU_1873 | Aminodeoxychorismate lyase. | Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.976 |
pabB | trpC | CFU_1180 | CFU_0699 | Aminodeoxychorismate lyase. | Indole-3-glycerol phosphate synthase; Belongs to the TrpC family. | 0.985 |
pabB | trpD | CFU_1180 | CFU_0700 | Aminodeoxychorismate lyase. | Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). | 0.987 |
pabB | trpE | CFU_1180 | CFU_0702 | Aminodeoxychorismate lyase. | Anthranilate synthase, aminase component; 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 c [...] | 0.874 |
pabB | trpF | CFU_1180 | CFU_1872 | Aminodeoxychorismate lyase. | Phosphoribosylanthranilate isomerase; Belongs to the TrpF family. | 0.918 |
pabB | trpG | CFU_1180 | CFU_0701 | Aminodeoxychorismate lyase. | Anthranilate synthase, amidotransferase component. | 0.999 |