| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| gloA | ilvA | HI_0323 | HI_0738.1 | Lactoylglutathione lyase (gloA); Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | Threonine deaminase (ilvA); 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). | 0.922 |
| gloA | sdaA | HI_0323 | HI_0288 | Lactoylglutathione lyase (gloA); Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | L-serine deaminase (sdaA); Similar to GB:M28695 SP:P16095 PID:290464 GB:U00096 PID:1736451 percent identity: 68.79; identified by sequence similarity; putative. | 0.920 |
| gloA | trpA | HI_0323 | HI_1432 | Lactoylglutathione lyase (gloA); Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | Tryptophan synthase alpha subunit (trpA); The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.920 |
| gloA | trpB | HI_0323 | HI_1431 | Lactoylglutathione lyase (gloA); Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | Tryptophan synthase beta subunit (trpB); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.929 |
| gloA | trpC | HI_0323 | HI_1389.1 | Lactoylglutathione lyase (gloA); Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | Indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase (trpC); Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain (By similarity). | 0.810 |
| glyA | ilvA | HI_0889 | HI_0738.1 | Serine hydroxymethyltransferase (serine methylase) (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | Threonine deaminase (ilvA); 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). | 0.937 |
| glyA | pssA | HI_0889 | HI_0425 | Serine hydroxymethyltransferase (serine methylase) (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | Phosphatidylserine synthase (pssA); Similar to GB:M58699 SP:P23830 PID:147389 GB:U00096 PID:1788940 percent identity: 50.33; identified by sequence similarity; putative. | 0.935 |
| glyA | sdaA | HI_0889 | HI_0288 | Serine hydroxymethyltransferase (serine methylase) (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | L-serine deaminase (sdaA); Similar to GB:M28695 SP:P16095 PID:290464 GB:U00096 PID:1736451 percent identity: 68.79; identified by sequence similarity; putative. | 0.967 |
| glyA | serB | HI_0889 | HI_1033 | Serine hydroxymethyltransferase (serine methylase) (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | Phosphoserine phosphatase (serB); Catalyzes the dephosphorylation of phosphoserine (P-Ser). | 0.975 |
| glyA | trpA | HI_0889 | HI_1432 | Serine hydroxymethyltransferase (serine methylase) (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | Tryptophan synthase alpha subunit (trpA); The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.943 |
| glyA | trpB | HI_0889 | HI_1431 | Serine hydroxymethyltransferase (serine methylase) (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | Tryptophan synthase beta subunit (trpB); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.933 |
| glyA | trpC | HI_0889 | HI_1389.1 | Serine hydroxymethyltransferase (serine methylase) (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | Indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase (trpC); Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain (By similarity). | 0.862 |
| ilvA | gloA | HI_0738.1 | HI_0323 | Threonine deaminase (ilvA); 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). | Lactoylglutathione lyase (gloA); Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | 0.922 |
| ilvA | glyA | HI_0738.1 | HI_0889 | Threonine deaminase (ilvA); 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). | Serine hydroxymethyltransferase (serine methylase) (glyA); Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.937 |
| ilvA | pssA | HI_0738.1 | HI_0425 | Threonine deaminase (ilvA); 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). | Phosphatidylserine synthase (pssA); Similar to GB:M58699 SP:P23830 PID:147389 GB:U00096 PID:1788940 percent identity: 50.33; identified by sequence similarity; putative. | 0.920 |
| ilvA | sdaA | HI_0738.1 | HI_0288 | Threonine deaminase (ilvA); 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 deaminase (sdaA); Similar to GB:M28695 SP:P16095 PID:290464 GB:U00096 PID:1736451 percent identity: 68.79; identified by sequence similarity; putative. | 0.938 |
| ilvA | serB | HI_0738.1 | HI_1033 | Threonine deaminase (ilvA); 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). | Phosphoserine phosphatase (serB); Catalyzes the dephosphorylation of phosphoserine (P-Ser). | 0.923 |
| ilvA | trpA | HI_0738.1 | HI_1432 | Threonine deaminase (ilvA); 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). | Tryptophan synthase alpha subunit (trpA); The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.925 |
| ilvA | trpB | HI_0738.1 | HI_1431 | Threonine deaminase (ilvA); 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). | Tryptophan synthase beta subunit (trpB); The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.949 |
| ilvA | trpC | HI_0738.1 | HI_1389.1 | Threonine deaminase (ilvA); 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). | Indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase (trpC); Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain (By similarity). | 0.929 |
