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 |
| Sps_01097 | Sps_02405 | Sps_01097 | Sps_02405 | Threonine dehydratase; PFAM: Pyridoxal-phosphate dependent enzyme. | PFAM: Threonine synthase N terminus; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | 0.609 |
| Sps_01137 | Sps_03543 | Sps_01137 | Sps_03543 | Cysteine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. | Cysteine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: cysteine synthase A; cysteine synthase; Belongs to the cysteine synthase/cystathionine beta- synthase family. | 0.908 |
| Sps_01248 | Sps_02405 | Sps_01248 | Sps_02405 | L-threonine ammonia-lyase; PFAM: Pyridoxal-phosphate dependent enzyme. | PFAM: Threonine synthase N terminus; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | 0.656 |
| Sps_02405 | Sps_01097 | Sps_02405 | Sps_01097 | PFAM: Threonine synthase N terminus; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | Threonine dehydratase; PFAM: Pyridoxal-phosphate dependent enzyme. | 0.609 |
| Sps_02405 | Sps_01248 | Sps_02405 | Sps_01248 | PFAM: Threonine synthase N terminus; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | L-threonine ammonia-lyase; PFAM: Pyridoxal-phosphate dependent enzyme. | 0.656 |
| Sps_02405 | ilvA | Sps_02405 | Sps_03123 | PFAM: Threonine synthase N terminus; Pyridoxal-phosphate dependent enzyme; 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. | 0.959 |
| Sps_02405 | trpB | Sps_02405 | Sps_01695 | PFAM: Threonine synthase N terminus; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.426 |
| Sps_03543 | Sps_01137 | Sps_03543 | Sps_01137 | Cysteine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: cysteine synthase A; cysteine synthase; Belongs to the cysteine synthase/cystathionine beta- synthase family. | Cysteine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. | 0.908 |
| dsdA | ilvA | Sps_04143 | Sps_03123 | D-serine ammonia-lyase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: D-serine ammonia-lyase; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | 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. | 0.907 |
| ilvA | Sps_02405 | Sps_03123 | Sps_02405 | 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. | PFAM: Threonine synthase N terminus; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | 0.959 |
| ilvA | dsdA | Sps_03123 | Sps_04143 | 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. | D-serine ammonia-lyase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: D-serine ammonia-lyase; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | 0.907 |
| ilvA | trpB | Sps_03123 | Sps_01695 | 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. | 0.936 |
| trpB | Sps_02405 | Sps_01695 | Sps_02405 | Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | PFAM: Threonine synthase N terminus; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. | 0.426 |
| trpB | ilvA | Sps_01695 | Sps_03123 | 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. | 0.936 |