node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AFY75768.1 | AFY77742.1 | Ple7327_0303 | Ple7327_2444 | PFAM: Amino acid kinase family; ACT domain; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase. | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | 0.879 |
AFY75768.1 | AFY78498.1 | Ple7327_0303 | Ple7327_3277 | PFAM: Amino acid kinase family; ACT domain; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase. | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. | 0.765 |
AFY75768.1 | AFY79082.1 | Ple7327_0303 | Ple7327_3933 | PFAM: Amino acid kinase family; ACT domain; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase. | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.765 |
AFY75768.1 | ilvA | Ple7327_0303 | Ple7327_2262 | PFAM: Amino acid kinase family; ACT domain; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase. | Threonine ammonia-lyase, biosynthetic, long form; 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. | 0.480 |
AFY75768.1 | thrB | Ple7327_0303 | Ple7327_3229 | PFAM: Amino acid kinase family; ACT domain; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.769 |
AFY77742.1 | AFY75768.1 | Ple7327_2444 | Ple7327_0303 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | PFAM: Amino acid kinase family; ACT domain; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase. | 0.879 |
AFY77742.1 | AFY78498.1 | Ple7327_2444 | Ple7327_3277 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. | 0.862 |
AFY77742.1 | AFY79082.1 | Ple7327_2444 | Ple7327_3933 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.871 |
AFY77742.1 | ilvA | Ple7327_2444 | Ple7327_2262 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | Threonine ammonia-lyase, biosynthetic, long form; 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. | 0.543 |
AFY77742.1 | thrB | Ple7327_2444 | Ple7327_3229 | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.992 |
AFY78498.1 | AFY75768.1 | Ple7327_3277 | Ple7327_0303 | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. | PFAM: Amino acid kinase family; ACT domain; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase. | 0.765 |
AFY78498.1 | AFY77742.1 | Ple7327_3277 | Ple7327_2444 | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. | PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain. | 0.862 |
AFY78498.1 | AFY78919.1 | Ple7327_3277 | Ple7327_3743 | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. | Threonine aldolase; PFAM: Beta-eliminating lyase. | 0.923 |
AFY78498.1 | AFY79082.1 | Ple7327_3277 | Ple7327_3933 | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.921 |
AFY78498.1 | ilvA | Ple7327_3277 | Ple7327_2262 | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. | Threonine ammonia-lyase, biosynthetic, long form; 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. | 0.952 |
AFY78498.1 | thrB | Ple7327_3277 | Ple7327_3229 | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.982 |
AFY78919.1 | AFY78498.1 | Ple7327_3743 | Ple7327_3277 | Threonine aldolase; PFAM: Beta-eliminating lyase. | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. | 0.923 |
AFY78919.1 | AFY79082.1 | Ple7327_3743 | Ple7327_3933 | Threonine aldolase; PFAM: Beta-eliminating lyase. | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.923 |
AFY78919.1 | ilvA | Ple7327_3743 | Ple7327_2262 | Threonine aldolase; PFAM: Beta-eliminating lyase. | Threonine ammonia-lyase, biosynthetic, long form; 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. | 0.929 |
AFY79082.1 | AFY75768.1 | Ple7327_3933 | Ple7327_0303 | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | PFAM: Amino acid kinase family; ACT domain; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase. | 0.765 |