Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AAO53954.1 | AAO55360.1 | PSPTO_0410 | PSPTO_1841 | Threonine aldolase, low-specificity; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | Threonine aldolase, low-specificity; See PMID:20190049 for expression data; similar to SP:P75823; identified by sequence similarity; putative. | 0.900 |
| AAO53954.1 | ilvA-2 | PSPTO_0410 | PSPTO_5288 | Threonine aldolase, low-specificity; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | Threonine dehydratase, biosynthetic; 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. | 0.910 |
| AAO53954.1 | thrC | PSPTO_0410 | PSPTO_1481 | Threonine aldolase, low-specificity; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | Threonine synthase; See PMID:20190049 for expression data. | 0.922 |
| AAO55360.1 | AAO53954.1 | PSPTO_1841 | PSPTO_0410 | Threonine aldolase, low-specificity; See PMID:20190049 for expression data; similar to SP:P75823; identified by sequence similarity; putative. | Threonine aldolase, low-specificity; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | 0.900 |
| AAO55360.1 | ilvA-2 | PSPTO_1841 | PSPTO_5288 | Threonine aldolase, low-specificity; See PMID:20190049 for expression data; similar to SP:P75823; identified by sequence similarity; putative. | Threonine dehydratase, biosynthetic; 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. | 0.910 |
| AAO55360.1 | thrC | PSPTO_1841 | PSPTO_1481 | Threonine aldolase, low-specificity; See PMID:20190049 for expression data; similar to SP:P75823; identified by sequence similarity; putative. | Threonine synthase; See PMID:20190049 for expression data. | 0.922 |
| AAO58385.1 | ilvA-2 | PSPTO_4957 | PSPTO_5288 | ACT domain protein/phosphoserine phosphatase SerB; See PMID:20190049 for expression data. | Threonine dehydratase, biosynthetic; 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. | 0.909 |
| AAO58385.1 | sdaA | PSPTO_4957 | PSPTO_1886 | ACT domain protein/phosphoserine phosphatase SerB; See PMID:20190049 for expression data. | L-serine dehydratase 1; See PMID:20190049 for expression data; identified by match to PFAM protein family HMM PF03313; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.940 |
| AAO58385.1 | trpA | PSPTO_4957 | PSPTO_0159 | ACT domain protein/phosphoserine phosphatase SerB; See PMID:20190049 for expression data. | Tryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.906 |
| AAO58385.1 | trpB | PSPTO_4957 | PSPTO_0158 | ACT domain protein/phosphoserine phosphatase SerB; See PMID:20190049 for expression data. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.927 |
| ilvA-2 | AAO53954.1 | PSPTO_5288 | PSPTO_0410 | Threonine dehydratase, biosynthetic; 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. | Threonine aldolase, low-specificity; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | 0.910 |
| ilvA-2 | AAO55360.1 | PSPTO_5288 | PSPTO_1841 | Threonine dehydratase, biosynthetic; 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. | Threonine aldolase, low-specificity; See PMID:20190049 for expression data; similar to SP:P75823; identified by sequence similarity; putative. | 0.910 |
| ilvA-2 | AAO58385.1 | PSPTO_5288 | PSPTO_4957 | Threonine dehydratase, biosynthetic; 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. | ACT domain protein/phosphoserine phosphatase SerB; See PMID:20190049 for expression data. | 0.909 |
| ilvA-2 | ilvB | PSPTO_5288 | PSPTO_0981 | Threonine dehydratase, biosynthetic; 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. | Acetolactate synthase, large subunit, biosynthetic type; Similar to SP:P00893; identified by sequence similarity; putative; see PMID:20190049 for expression data; similar to SP:P00893, identified by sequence similarity, putative. | 0.946 |
| ilvA-2 | ilvN | PSPTO_5288 | PSPTO_0982 | Threonine dehydratase, biosynthetic; 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. | Acetolactate synthase, small subunit; Similar to SP:P00894; identified by sequence similarity; putative; see PMID:20190049 for expression data; similar to SP:P00894, identified by sequence similarity, putative. | 0.963 |
| ilvA-2 | leuB | PSPTO_5288 | PSPTO_2175 | Threonine dehydratase, biosynthetic; 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. | 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. | 0.942 |
| ilvA-2 | sdaA | PSPTO_5288 | PSPTO_1886 | Threonine dehydratase, biosynthetic; 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 1; See PMID:20190049 for expression data; identified by match to PFAM protein family HMM PF03313; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.926 |
| ilvA-2 | thrC | PSPTO_5288 | PSPTO_1481 | Threonine dehydratase, biosynthetic; 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. | Threonine synthase; See PMID:20190049 for expression data. | 0.956 |
| ilvA-2 | trpA | PSPTO_5288 | PSPTO_0159 | Threonine dehydratase, biosynthetic; 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 subunit; 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 |
| ilvA-2 | trpB | PSPTO_5288 | PSPTO_0158 | Threonine dehydratase, biosynthetic; 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 subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.933 |
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