| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEB82543.1 | AEB84844.1 | Alide2_0105 | Alide2_2485 | 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. | KEGG: dia:Dtpsy_1854 lactoylglutathione lyase. | 0.829 |
| AEB82543.1 | AEB85306.1 | Alide2_0105 | Alide2_2959 | 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. | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | 0.840 |
| AEB82543.1 | AEB85613.1 | Alide2_0105 | Alide2_3272 | 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. | Glyoxylate reductase; KEGG: dia:Dtpsy_1370 D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain. | 0.824 |
| AEB82543.1 | AEB86459.1 | Alide2_0105 | Alide2_4142 | 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. | Hydroxypyruvate reductase; KEGG: dia:Dtpsy_3039 D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding. | 0.853 |
| AEB82543.1 | AEB86557.1 | Alide2_0105 | Alide2_4242 | 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. | Threonine ammonia-lyase; KEGG: dia:Dtpsy_3120 hypothetical protein; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | 0.924 |
| AEB82543.1 | ilvA | Alide2_0105 | Alide2_0760 | 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. | 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. | 0.917 |
| AEB82543.1 | trpB | Alide2_0105 | Alide2_1300 | 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. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.929 |
| AEB82543.1 | trpB-2 | Alide2_0105 | Alide2_2879 | 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. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.929 |
| AEB82716.1 | AEB84844.1 | Alide2_0288 | Alide2_2485 | KEGG: ajs:Ajs_0228 beta-lactamase domain-containing protein; PFAM: Beta-lactamase-like; SMART: Beta-lactamase-like. | KEGG: dia:Dtpsy_1854 lactoylglutathione lyase. | 0.907 |
| AEB82716.1 | AEB85306.1 | Alide2_0288 | Alide2_2959 | KEGG: ajs:Ajs_0228 beta-lactamase domain-containing protein; PFAM: Beta-lactamase-like; SMART: Beta-lactamase-like. | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | 0.924 |
| AEB82716.1 | gloB | Alide2_0288 | Alide2_3164 | KEGG: ajs:Ajs_0228 beta-lactamase domain-containing protein; PFAM: Beta-lactamase-like; SMART: Beta-lactamase-like. | Hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | 0.911 |
| AEB84844.1 | AEB82543.1 | Alide2_2485 | Alide2_0105 | KEGG: dia:Dtpsy_1854 lactoylglutathione lyase. | 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. | 0.829 |
| AEB84844.1 | AEB82716.1 | Alide2_2485 | Alide2_0288 | KEGG: dia:Dtpsy_1854 lactoylglutathione lyase. | KEGG: ajs:Ajs_0228 beta-lactamase domain-containing protein; PFAM: Beta-lactamase-like; SMART: Beta-lactamase-like. | 0.907 |
| AEB84844.1 | AEB85306.1 | Alide2_2485 | Alide2_2959 | KEGG: dia:Dtpsy_1854 lactoylglutathione lyase. | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | 0.900 |
| AEB84844.1 | AEB85613.1 | Alide2_2485 | Alide2_3272 | KEGG: dia:Dtpsy_1854 lactoylglutathione lyase. | Glyoxylate reductase; KEGG: dia:Dtpsy_1370 D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain. | 0.915 |
| AEB84844.1 | AEB86459.1 | Alide2_2485 | Alide2_4142 | KEGG: dia:Dtpsy_1854 lactoylglutathione lyase. | Hydroxypyruvate reductase; KEGG: dia:Dtpsy_3039 D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding. | 0.906 |
| AEB84844.1 | AEB86557.1 | Alide2_2485 | Alide2_4242 | KEGG: dia:Dtpsy_1854 lactoylglutathione lyase. | Threonine ammonia-lyase; KEGG: dia:Dtpsy_3120 hypothetical protein; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. | 0.829 |
| AEB84844.1 | gloB | Alide2_2485 | Alide2_3164 | KEGG: dia:Dtpsy_1854 lactoylglutathione lyase. | Hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | 0.907 |
| AEB84844.1 | ilvA | Alide2_2485 | Alide2_0760 | KEGG: dia:Dtpsy_1854 lactoylglutathione 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. | 0.829 |
| AEB84844.1 | trpB | Alide2_2485 | Alide2_1300 | KEGG: dia:Dtpsy_1854 lactoylglutathione lyase. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.831 |