| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SCA91080.1 | gloA | LP2241_10217 | LP2241_20168 | Putative NAD(P)H nitroreductase YdgI; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Lactoylglutathione lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.557 |
| SCA91399.1 | SCA91492.1 | LP2241_20169 | LP2241_20262 | Putative metallo-hydrolase/oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative metallo-hydrolase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.905 |
| SCA91399.1 | gloA | LP2241_20169 | LP2241_20168 | Putative metallo-hydrolase/oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Lactoylglutathione lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.955 |
| SCA91492.1 | SCA91399.1 | LP2241_20262 | LP2241_20169 | Putative metallo-hydrolase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative metallo-hydrolase/oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.905 |
| SCA91492.1 | gloA | LP2241_20262 | LP2241_20168 | Putative metallo-hydrolase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Lactoylglutathione lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.906 |
| SCA92773.1 | gloA | LP2241_50350 | LP2241_20168 | Putative nitroreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the flavin oxidoreductase frp family. | Lactoylglutathione lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.522 |
| gloA | SCA91080.1 | LP2241_20168 | LP2241_10217 | Lactoylglutathione lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Putative NAD(P)H nitroreductase YdgI; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.557 |
| gloA | SCA91399.1 | LP2241_20168 | LP2241_20169 | Lactoylglutathione lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Putative metallo-hydrolase/oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.955 |
| gloA | SCA91492.1 | LP2241_20168 | LP2241_20262 | Lactoylglutathione lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Putative metallo-hydrolase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.906 |
| gloA | SCA92773.1 | LP2241_20168 | LP2241_50350 | Lactoylglutathione lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Putative nitroreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the flavin oxidoreductase frp family. | 0.522 |
| gloA | ilvA | LP2241_20168 | LP2241_10260 | Lactoylglutathione lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | L-threonine dehydratase biosynthetic 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. | 0.817 |
| gloA | sdaAA | LP2241_20168 | LP2241_20435 | Lactoylglutathione lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | L-serine dehydratase, alpha chain; Function of strongly homologous gene; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.807 |
| gloA | sdaAB | LP2241_20168 | LP2241_20436 | Lactoylglutathione lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | L-serine dehydratase, beta chain; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.804 |
| gloA | spy0809 | LP2241_20168 | LP2241_10180 | Lactoylglutathione lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Probable NAD(P)H nitroreductase Spy0809; Function of strongly homologous gene; enzyme. | 0.593 |
| gloA | trpA | LP2241_20168 | LP2241_20475 | Lactoylglutathione lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 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. | 0.800 |
| gloA | trpB | LP2241_20168 | LP2241_20474 | Lactoylglutathione lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.822 |
| ilvA | gloA | LP2241_10260 | LP2241_20168 | L-threonine dehydratase biosynthetic 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. | Lactoylglutathione lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.817 |
| ilvA | sdaAA | LP2241_10260 | LP2241_20435 | L-threonine dehydratase biosynthetic 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. | L-serine dehydratase, alpha chain; Function of strongly homologous gene; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.924 |
| ilvA | sdaAB | LP2241_10260 | LP2241_20436 | L-threonine dehydratase biosynthetic 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. | L-serine dehydratase, beta chain; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.925 |
| ilvA | trpA | LP2241_10260 | LP2241_20475 | L-threonine dehydratase biosynthetic 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. | 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. | 0.926 |