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 |
| Spea_1068 | Spea_4080 | Spea_1068 | Spea_4080 | KEGG: slo:Shew_1081 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | TIGRFAM: diaminopropionate ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: pin:Ping_2030 diaminopropionate ammonia-lyase. | 0.656 |
| Spea_1068 | ilvA | Spea_1068 | Spea_0349 | KEGG: slo:Shew_1081 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | 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. | 0.964 |
| Spea_1682 | Spea_2347 | Spea_1682 | Spea_2347 | TIGRFAM: cysteine synthase; cysteine synthase A; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: slo:Shew_2382 cysteine synthase A; Belongs to the cysteine synthase/cystathionine beta- synthase family. | PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: sbm:Shew185_2117 pyridoxal-5'-phosphate-dependent protein beta subunit. | 0.910 |
| Spea_1682 | Spea_3653 | Spea_1682 | Spea_3653 | TIGRFAM: cysteine synthase; cysteine synthase A; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: slo:Shew_2382 cysteine synthase A; Belongs to the cysteine synthase/cystathionine beta- synthase family. | PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: ilo:IL2163 cysteine synthase. | 0.921 |
| Spea_2347 | Spea_1682 | Spea_2347 | Spea_1682 | PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: sbm:Shew185_2117 pyridoxal-5'-phosphate-dependent protein beta subunit. | TIGRFAM: cysteine synthase; cysteine synthase A; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: slo:Shew_2382 cysteine synthase A; Belongs to the cysteine synthase/cystathionine beta- synthase family. | 0.910 |
| Spea_2347 | Spea_3653 | Spea_2347 | Spea_3653 | PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: sbm:Shew185_2117 pyridoxal-5'-phosphate-dependent protein beta subunit. | PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: ilo:IL2163 cysteine synthase. | 0.915 |
| Spea_3653 | Spea_1682 | Spea_3653 | Spea_1682 | PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: ilo:IL2163 cysteine synthase. | TIGRFAM: cysteine synthase; cysteine synthase A; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: slo:Shew_2382 cysteine synthase A; Belongs to the cysteine synthase/cystathionine beta- synthase family. | 0.921 |
| Spea_3653 | Spea_2347 | Spea_3653 | Spea_2347 | PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: ilo:IL2163 cysteine synthase. | PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: sbm:Shew185_2117 pyridoxal-5'-phosphate-dependent protein beta subunit. | 0.915 |
| Spea_4080 | Spea_1068 | Spea_4080 | Spea_1068 | TIGRFAM: diaminopropionate ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: pin:Ping_2030 diaminopropionate ammonia-lyase. | KEGG: slo:Shew_1081 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | 0.656 |
| dsdA | ilvA | Spea_3449 | Spea_0349 | KEGG: asa:ASA_2940 D-serine dehydratase; TIGRFAM: D-serine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | 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. | 0.908 |
| ilvA | Spea_1068 | Spea_0349 | Spea_1068 | 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. | KEGG: slo:Shew_1081 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | 0.964 |
| ilvA | dsdA | Spea_0349 | Spea_3449 | 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. | KEGG: asa:ASA_2940 D-serine dehydratase; TIGRFAM: D-serine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | 0.908 |
| ilvA | trpB | Spea_0349 | Spea_1586 | 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 |
| trpB | ilvA | Spea_1586 | Spea_0349 | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 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. | 0.933 |