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 |
| DR97_3297 | DR97_3298 | DR97_3297 | DR97_3298 | Hypothetical protein; Uncharacterized protein | annotation not available | 0.811 |
| DR97_3297 | DR97_3300 | DR97_3297 | DR97_3300 | Hypothetical protein; Uncharacterized protein | Putative integral membrane protein; Uncharacterized protein | 0.735 |
| DR97_3297 | ilvA1 | DR97_3297 | DR97_3296 | Hypothetical protein; Uncharacterized protein | Threonine ammonia-lyase, 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 | 0.560 |
| DR97_3298 | DR97_3297 | DR97_3298 | DR97_3297 | annotation not available | Hypothetical protein; Uncharacterized protein | 0.811 |
| DR97_3298 | DR97_3300 | DR97_3298 | DR97_3300 | annotation not available | Putative integral membrane protein; Uncharacterized protein | 0.956 |
| DR97_3298 | ilvA1 | DR97_3298 | DR97_3296 | annotation not available | Threonine ammonia-lyase, 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 | 0.464 |
| DR97_3300 | DR97_3297 | DR97_3300 | DR97_3297 | Putative integral membrane protein; Uncharacterized protein | Hypothetical protein; Uncharacterized protein | 0.735 |
| DR97_3300 | DR97_3298 | DR97_3300 | DR97_3298 | Putative integral membrane protein; Uncharacterized protein | annotation not available | 0.956 |
| DR97_3300 | ilvA1 | DR97_3300 | DR97_3296 | Putative integral membrane protein; Uncharacterized protein | Threonine ammonia-lyase, 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 | 0.492 |
| DR97_3300 | rpiA | DR97_3300 | DR97_3295 | Putative integral membrane protein; Uncharacterized protein | Ribose 5-phosphate isomerase a; Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate | 0.471 |
| ilvA1 | DR97_3297 | DR97_3296 | DR97_3297 | Threonine ammonia-lyase, 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 | Hypothetical protein; Uncharacterized protein | 0.560 |
| ilvA1 | DR97_3298 | DR97_3296 | DR97_3298 | Threonine ammonia-lyase, 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 | annotation not available | 0.464 |
| ilvA1 | DR97_3300 | DR97_3296 | DR97_3300 | Threonine ammonia-lyase, 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 | Putative integral membrane protein; Uncharacterized protein | 0.492 |
| ilvA1 | rpiA | DR97_3296 | DR97_3295 | Threonine ammonia-lyase, 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 | Ribose 5-phosphate isomerase a; Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate | 0.506 |
| rpiA | DR97_3300 | DR97_3295 | DR97_3300 | Ribose 5-phosphate isomerase a; Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate | Putative integral membrane protein; Uncharacterized protein | 0.471 |
| rpiA | ilvA1 | DR97_3295 | DR97_3296 | Ribose 5-phosphate isomerase a; Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate | Threonine ammonia-lyase, 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 | 0.506 |
