node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Chro_1312 | Chro_2041 | Chro_1312 | Chro_2041 | L-threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase; COGs: COG0498 Threonine synthase; InterPro IPR001926:IPR004450; KEGG: ava:Ava_4952 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; SPTR: L-threonine synthase; TIGRFAM: threonine synthase. | L-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.920 |
Chro_1312 | Chro_4020 | Chro_1312 | Chro_4020 | L-threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase; COGs: COG0498 Threonine synthase; InterPro IPR001926:IPR004450; KEGG: ava:Ava_4952 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; SPTR: L-threonine synthase; TIGRFAM: threonine synthase. | Pyridoxal-5'-phosphate-dependent protein beta subunit; PFAM: Pyridoxal-phosphate dependent enzyme; COGs: COG1171 Threonine dehydratase; InterPro IPR001926; KEGG: npu:Npun_R1256 serine/threonine dehydratase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; SPTR: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | 0.523 |
Chro_1312 | ilvA | Chro_1312 | Chro_1364 | L-threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase; COGs: COG0498 Threonine synthase; InterPro IPR001926:IPR004450; KEGG: ava:Ava_4952 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; SPTR: L-threonine synthase; TIGRFAM: threonine synthase. | L-threonine ammonia-lyase; 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. | 0.950 |
Chro_2041 | Chro_1312 | Chro_2041 | Chro_1312 | L-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | L-threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase; COGs: COG0498 Threonine synthase; InterPro IPR001926:IPR004450; KEGG: ava:Ava_4952 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; SPTR: L-threonine synthase; TIGRFAM: threonine synthase. | 0.920 |
Chro_2041 | Chro_4020 | Chro_2041 | Chro_4020 | L-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | Pyridoxal-5'-phosphate-dependent protein beta subunit; PFAM: Pyridoxal-phosphate dependent enzyme; COGs: COG1171 Threonine dehydratase; InterPro IPR001926; KEGG: npu:Npun_R1256 serine/threonine dehydratase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; SPTR: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | 0.523 |
Chro_2041 | ilvA | Chro_2041 | Chro_1364 | L-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | L-threonine ammonia-lyase; 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. | 0.950 |
Chro_4020 | Chro_1312 | Chro_4020 | Chro_1312 | Pyridoxal-5'-phosphate-dependent protein beta subunit; PFAM: Pyridoxal-phosphate dependent enzyme; COGs: COG1171 Threonine dehydratase; InterPro IPR001926; KEGG: npu:Npun_R1256 serine/threonine dehydratase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; SPTR: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | L-threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase; COGs: COG0498 Threonine synthase; InterPro IPR001926:IPR004450; KEGG: ava:Ava_4952 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; SPTR: L-threonine synthase; TIGRFAM: threonine synthase. | 0.523 |
Chro_4020 | Chro_2041 | Chro_4020 | Chro_2041 | Pyridoxal-5'-phosphate-dependent protein beta subunit; PFAM: Pyridoxal-phosphate dependent enzyme; COGs: COG1171 Threonine dehydratase; InterPro IPR001926; KEGG: npu:Npun_R1256 serine/threonine dehydratase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; SPTR: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | L-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.523 |
Chro_4093 | Chro_5595 | Chro_4093 | Chro_5595 | Pyridoxal-5'-phosphate-dependent protein beta subunit; PFAM: Pyridoxal-phosphate dependent enzyme; COGs: COG0031 Cysteine synthase; InterPro IPR001216:IPR001926; KEGG: amr:AM1_5090 cysteine synthase A; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; SPTR: Cysteine synthase. | Cysteine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: cysteine synthase A; cysteine synthases; COGs: COG0031 Cysteine synthase; InterPro IPR001216:IPR005856:IPR005859:IPR001926; KEGG: ava:Ava_2508 cysteine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; SPTR: Cysteine synthase; TIGRFAM: cysteine synthase A; cysteine synthase; Belongs to the cysteine synthase/cystathionine beta- synthase family. | 0.915 |
Chro_5595 | Chro_4093 | Chro_5595 | Chro_4093 | Cysteine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: cysteine synthase A; cysteine synthases; COGs: COG0031 Cysteine synthase; InterPro IPR001216:IPR005856:IPR005859:IPR001926; KEGG: ava:Ava_2508 cysteine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; SPTR: Cysteine synthase; TIGRFAM: cysteine synthase A; cysteine synthase; Belongs to the cysteine synthase/cystathionine beta- synthase family. | Pyridoxal-5'-phosphate-dependent protein beta subunit; PFAM: Pyridoxal-phosphate dependent enzyme; COGs: COG0031 Cysteine synthase; InterPro IPR001216:IPR001926; KEGG: amr:AM1_5090 cysteine synthase A; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; SPTR: Cysteine synthase. | 0.915 |
ilvA | Chro_1312 | Chro_1364 | Chro_1312 | L-threonine ammonia-lyase; 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-threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase; COGs: COG0498 Threonine synthase; InterPro IPR001926:IPR004450; KEGG: ava:Ava_4952 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; SPTR: L-threonine synthase; TIGRFAM: threonine synthase. | 0.950 |
ilvA | Chro_2041 | Chro_1364 | Chro_2041 | L-threonine ammonia-lyase; 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-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.950 |
ilvA | trpB | Chro_1364 | Chro_1239 | L-threonine ammonia-lyase; 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 chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.927 |
ilvA | trpB-2 | Chro_1364 | Chro_3143 | L-threonine ammonia-lyase; 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 chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.927 |
trpB | ilvA | Chro_1239 | Chro_1364 | Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | L-threonine ammonia-lyase; 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. | 0.927 |
trpB | trpB-2 | Chro_1239 | Chro_3143 | Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.900 |
trpB-2 | ilvA | Chro_3143 | Chro_1364 | Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | L-threonine ammonia-lyase; 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. | 0.927 |
trpB-2 | trpB | Chro_3143 | Chro_1239 | Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.900 |