node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AFZ33650.1 | AFZ36849.1 | Sta7437_0024 | Sta7437_3343 | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase; COGs: COG0498 Threonine synthase; InterPro IPR004450:IPR001926; KEGG: mar:MAE_17060 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; PRIAM: Threonine synthase; SPTR: 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 |
AFZ33650.1 | AFZ37582.1 | Sta7437_0024 | Sta7437_4105 | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase; COGs: COG0498 Threonine synthase; InterPro IPR004450:IPR001926; KEGG: mar:MAE_17060 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; PRIAM: Threonine synthase; SPTR: Threonine synthase; TIGRFAM: Threonine synthase. | PFAM: Small subunit of acetolactate synthase; ACT domain; TIGRFAM: acetolactate synthase, small subunit; COGs: COG0440 Acetolactate synthase small (regulatory) subunit; InterPro IPR004789:IPR002912:IPR019455; KEGG: mar:MAE_48120 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase small subunit; TIGRFAM: Acetolactate synthase, small subunit. | 0.528 |
AFZ33650.1 | AFZ37729.1 | Sta7437_0024 | Sta7437_4256 | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase; COGs: COG0498 Threonine synthase; InterPro IPR004450:IPR001926; KEGG: mar:MAE_17060 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; PRIAM: Threonine synthase; SPTR: Threonine synthase; TIGRFAM: Threonine synthase. | Threonine dehydratase; PFAM: ACT domain; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine dehydratase, medium form; COGs: COG1171 Threonine dehydratase; InterPro IPR005789:IPR001926:IPR002912; KEGG: nhl:Nhal_3584 threonine dehydratase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; Amino acid-binding ACT; SPTR: Threonine dehydratase; TIGRFAM: Threonine dehydratase II. | 0.951 |
AFZ33650.1 | ilvA | Sta7437_0024 | Sta7437_3390 | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase; COGs: COG0498 Threonine synthase; InterPro IPR004450:IPR001926; KEGG: mar:MAE_17060 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; PRIAM: Threonine synthase; SPTR: 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. | 0.946 |
AFZ34254.1 | AFZ37582.1 | Sta7437_0659 | Sta7437_4105 | Acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterPro IPR012001:IPR012000:IPR011766; KEGG: cyt:cce_4227 acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase large subunit. | PFAM: Small subunit of acetolactate synthase; ACT domain; TIGRFAM: acetolactate synthase, small subunit; COGs: COG0440 Acetolactate synthase small (regulatory) subunit; InterPro IPR004789:IPR002912:IPR019455; KEGG: mar:MAE_48120 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase small subunit; TIGRFAM: Acetolactate synthase, small subunit. | 0.998 |
AFZ34254.1 | AFZ37729.1 | Sta7437_0659 | Sta7437_4256 | Acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterPro IPR012001:IPR012000:IPR011766; KEGG: cyt:cce_4227 acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase large subunit. | Threonine dehydratase; PFAM: ACT domain; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine dehydratase, medium form; COGs: COG1171 Threonine dehydratase; InterPro IPR005789:IPR001926:IPR002912; KEGG: nhl:Nhal_3584 threonine dehydratase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; Amino acid-binding ACT; SPTR: Threonine dehydratase; TIGRFAM: Threonine dehydratase II. | 0.948 |
AFZ34254.1 | AFZ37759.1 | Sta7437_0659 | Sta7437_4288 | Acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterPro IPR012001:IPR012000:IPR011766; KEGG: cyt:cce_4227 acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase large subunit. | Acetolactate synthase, large subunit; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterPro IPR012846:IPR012001:IPR012000:IPR011766; KEGG: cyh:Cyan8802_0929 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate [...] | 0.919 |
AFZ34254.1 | ilvA | Sta7437_0659 | Sta7437_3390 | Acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterPro IPR012001:IPR012000:IPR011766; KEGG: cyt:cce_4227 acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase large subunit. | 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. | 0.926 |
AFZ34254.1 | leuB | Sta7437_0659 | Sta7437_2590 | Acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterPro IPR012001:IPR012000:IPR011766; KEGG: cyt:cce_4227 acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase large subunit. | 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. | 0.950 |
AFZ36548.1 | AFZ37729.1 | Sta7437_3030 | Sta7437_4256 | Alanine-glyoxylate aminotransferase apoenzyme; PFAM: Aminotransferase class-V; COGs: COG0075 Serine-pyruvate aminotransferase/ aspartate aminotransferase; InterPro IPR000192; KEGG: cyc:PCC7424_5094 aminotransferase class V; PFAM: Aminotransferase, class V/Cysteine desulfurase; PRIAM: Serine--pyruvate transaminase; SPTR: Aminotransferase class V. | Threonine dehydratase; PFAM: ACT domain; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine dehydratase, medium form; COGs: COG1171 Threonine dehydratase; InterPro IPR005789:IPR001926:IPR002912; KEGG: nhl:Nhal_3584 threonine dehydratase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; Amino acid-binding ACT; SPTR: Threonine dehydratase; TIGRFAM: Threonine dehydratase II. | 0.923 |
AFZ36548.1 | ilvA | Sta7437_3030 | Sta7437_3390 | Alanine-glyoxylate aminotransferase apoenzyme; PFAM: Aminotransferase class-V; COGs: COG0075 Serine-pyruvate aminotransferase/ aspartate aminotransferase; InterPro IPR000192; KEGG: cyc:PCC7424_5094 aminotransferase class V; PFAM: Aminotransferase, class V/Cysteine desulfurase; PRIAM: Serine--pyruvate transaminase; SPTR: Aminotransferase class V. | 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. | 0.923 |
AFZ36548.1 | trpA | Sta7437_3030 | Sta7437_2033 | Alanine-glyoxylate aminotransferase apoenzyme; PFAM: Aminotransferase class-V; COGs: COG0075 Serine-pyruvate aminotransferase/ aspartate aminotransferase; InterPro IPR000192; KEGG: cyc:PCC7424_5094 aminotransferase class V; PFAM: Aminotransferase, class V/Cysteine desulfurase; PRIAM: Serine--pyruvate transaminase; SPTR: Aminotransferase class V. | 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. | 0.903 |
AFZ36548.1 | trpB | Sta7437_3030 | Sta7437_2968 | Alanine-glyoxylate aminotransferase apoenzyme; PFAM: Aminotransferase class-V; COGs: COG0075 Serine-pyruvate aminotransferase/ aspartate aminotransferase; InterPro IPR000192; KEGG: cyc:PCC7424_5094 aminotransferase class V; PFAM: Aminotransferase, class V/Cysteine desulfurase; PRIAM: Serine--pyruvate transaminase; SPTR: Aminotransferase class V. | Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.914 |
AFZ36849.1 | AFZ33650.1 | Sta7437_3343 | Sta7437_0024 | L-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase; COGs: COG0498 Threonine synthase; InterPro IPR004450:IPR001926; KEGG: mar:MAE_17060 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; PRIAM: Threonine synthase; SPTR: Threonine synthase; TIGRFAM: Threonine synthase. | 0.920 |
AFZ36849.1 | AFZ37582.1 | Sta7437_3343 | Sta7437_4105 | L-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | PFAM: Small subunit of acetolactate synthase; ACT domain; TIGRFAM: acetolactate synthase, small subunit; COGs: COG0440 Acetolactate synthase small (regulatory) subunit; InterPro IPR004789:IPR002912:IPR019455; KEGG: mar:MAE_48120 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase small subunit; TIGRFAM: Acetolactate synthase, small subunit. | 0.528 |
AFZ36849.1 | AFZ37729.1 | Sta7437_3343 | Sta7437_4256 | L-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | Threonine dehydratase; PFAM: ACT domain; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine dehydratase, medium form; COGs: COG1171 Threonine dehydratase; InterPro IPR005789:IPR001926:IPR002912; KEGG: nhl:Nhal_3584 threonine dehydratase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; Amino acid-binding ACT; SPTR: Threonine dehydratase; TIGRFAM: Threonine dehydratase II. | 0.954 |
AFZ36849.1 | ilvA | Sta7437_3343 | Sta7437_3390 | 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. | 0.946 |
AFZ37582.1 | AFZ33650.1 | Sta7437_4105 | Sta7437_0024 | PFAM: Small subunit of acetolactate synthase; ACT domain; TIGRFAM: acetolactate synthase, small subunit; COGs: COG0440 Acetolactate synthase small (regulatory) subunit; InterPro IPR004789:IPR002912:IPR019455; KEGG: mar:MAE_48120 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase small subunit; TIGRFAM: Acetolactate synthase, small subunit. | Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase; COGs: COG0498 Threonine synthase; InterPro IPR004450:IPR001926; KEGG: mar:MAE_17060 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; PRIAM: Threonine synthase; SPTR: Threonine synthase; TIGRFAM: Threonine synthase. | 0.528 |
AFZ37582.1 | AFZ34254.1 | Sta7437_4105 | Sta7437_0659 | PFAM: Small subunit of acetolactate synthase; ACT domain; TIGRFAM: acetolactate synthase, small subunit; COGs: COG0440 Acetolactate synthase small (regulatory) subunit; InterPro IPR004789:IPR002912:IPR019455; KEGG: mar:MAE_48120 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase small subunit; TIGRFAM: Acetolactate synthase, small subunit. | Acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; COGs: COG0028 Thiamine pyrophosphate-requiring protein; InterPro IPR012001:IPR012000:IPR011766; KEGG: cyt:cce_4227 acetolactate synthase; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase large subunit. | 0.998 |
AFZ37582.1 | AFZ36849.1 | Sta7437_4105 | Sta7437_3343 | PFAM: Small subunit of acetolactate synthase; ACT domain; TIGRFAM: acetolactate synthase, small subunit; COGs: COG0440 Acetolactate synthase small (regulatory) subunit; InterPro IPR004789:IPR002912:IPR019455; KEGG: mar:MAE_48120 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT; PRIAM: Acetolactate synthase; SPTR: Acetolactate synthase small subunit; TIGRFAM: Acetolactate synthase, small subunit. | L-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.528 |