| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ANP65251.1 | ANP66631.1 | BAU10_09690 | BAU10_16735 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.800 |
| ANP65251.1 | ANP67055.1 | BAU10_09690 | BAU10_19015 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | Lactoylglutathione lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.902 |
| ANP65251.1 | ANP67810.1 | BAU10_09690 | BAU10_23020 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.800 |
| ANP65251.1 | dsdA | BAU10_09690 | BAU10_05535 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | D-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | 0.800 |
| ANP65251.1 | gloA_2 | BAU10_09690 | BAU10_09905 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | Lactoylglutathione lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.918 |
| ANP65251.1 | ilvA | BAU10_09690 | BAU10_15045 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | PLP-dependent 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. | 0.814 |
| ANP65251.1 | sdaA | BAU10_09690 | BAU10_08615 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.800 |
| ANP66631.1 | ANP65251.1 | BAU10_16735 | BAU10_09690 | L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | 0.800 |
| ANP66631.1 | ANP67055.1 | BAU10_16735 | BAU10_19015 | L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Lactoylglutathione lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.800 |
| ANP66631.1 | ANP67810.1 | BAU10_16735 | BAU10_23020 | L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.900 |
| ANP66631.1 | dsdA | BAU10_16735 | BAU10_05535 | L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | D-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | 0.915 |
| ANP66631.1 | gloA_2 | BAU10_16735 | BAU10_09905 | L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Lactoylglutathione lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.800 |
| ANP66631.1 | ilvA | BAU10_16735 | BAU10_15045 | L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | PLP-dependent 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. | 0.926 |
| ANP66631.1 | sdaA | BAU10_16735 | BAU10_08615 | L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.903 |
| ANP67055.1 | ANP65251.1 | BAU10_19015 | BAU10_09690 | Lactoylglutathione lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | 0.902 |
| ANP67055.1 | ANP66631.1 | BAU10_19015 | BAU10_16735 | Lactoylglutathione lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.800 |
| ANP67055.1 | ANP67810.1 | BAU10_19015 | BAU10_23020 | Lactoylglutathione lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.800 |
| ANP67055.1 | dsdA | BAU10_19015 | BAU10_05535 | Lactoylglutathione lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | D-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | 0.800 |
| ANP67055.1 | gloA_2 | BAU10_19015 | BAU10_09905 | Lactoylglutathione lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lactoylglutathione lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.913 |
| ANP67055.1 | ilvA | BAU10_19015 | BAU10_15045 | Lactoylglutathione lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | PLP-dependent 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. | 0.814 |