| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PP_0662 | PP_2930 | PP_0662 | PP_2930 | Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.949 |
| PP_0662 | PP_3191 | PP_0662 | PP_3191 | Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Putative threonine ammonia-lyase / dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Energymetabolism : Amino acids and amines. | 0.938 |
| PP_0662 | PP_4430 | PP_0662 | PP_4430 | Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Putative threonine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.938 |
| PP_0662 | ilvA-II | PP_0662 | PP_5149 | Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Threonine deaminase; 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. | 0.938 |
| PP_0662 | ilvD | PP_0662 | PP_5128 | Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.407 |
| PP_0662 | leuB | PP_0662 | PP_1988 | Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily. | 0.551 |
| PP_0662 | ltaE | PP_0662 | PP_0321 | Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Low specificity L-threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | 0.926 |
| PP_0662 | thrC | PP_0662 | PP_1471 | Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Threonine synthase. | 0.907 |
| PP_2930 | PP_0662 | PP_2930 | PP_0662 | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.949 |
| PP_2930 | PP_3191 | PP_2930 | PP_3191 | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Putative threonine ammonia-lyase / dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Energymetabolism : Amino acids and amines. | 0.928 |
| PP_2930 | PP_4430 | PP_2930 | PP_4430 | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Putative threonine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.927 |
| PP_2930 | ilvA-II | PP_2930 | PP_5149 | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Threonine deaminase; 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. | 0.923 |
| PP_2930 | ilvD | PP_2930 | PP_5128 | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.576 |
| PP_2930 | leuB | PP_2930 | PP_1988 | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily. | 0.925 |
| PP_2930 | ltaE | PP_2930 | PP_0321 | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Low specificity L-threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | 0.912 |
| PP_2930 | thrC | PP_2930 | PP_1471 | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Threonine synthase. | 0.948 |
| PP_2930 | trpA | PP_2930 | PP_0082 | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 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. | 0.920 |
| PP_2930 | trpB | PP_2930 | PP_0083 | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.927 |
| PP_3191 | PP_0662 | PP_3191 | PP_0662 | Putative threonine ammonia-lyase / dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Energymetabolism : Amino acids and amines. | Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.938 |
| PP_3191 | PP_2930 | PP_3191 | PP_2930 | Putative threonine ammonia-lyase / dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Energymetabolism : Amino acids and amines. | Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.928 |