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
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DR97_2674 | DR97_4810 | DR97_2674 | DR97_4810 | annotation not available | annotation not available | 0.502 |
| DR97_367 | DR97_4810 | DR97_367 | DR97_4810 | annotation not available | annotation not available | 0.590 |
| DR97_367 | srr | DR97_367 | DR97_5277 | annotation not available | annotation not available | 0.428 |
| DR97_4808 | DR97_4809 | DR97_4808 | DR97_4809 | annotation not available | Bacterial regulatory helix-turn-helix , lysr family protein; Belongs to the LysR transcriptional regulatory family | 0.699 |
| DR97_4808 | DR97_4810 | DR97_4808 | DR97_4810 | annotation not available | annotation not available | 0.461 |
| DR97_4809 | DR97_4808 | DR97_4809 | DR97_4808 | Bacterial regulatory helix-turn-helix , lysr family protein; Belongs to the LysR transcriptional regulatory family | annotation not available | 0.699 |
| DR97_4809 | DR97_4810 | DR97_4809 | DR97_4810 | Bacterial regulatory helix-turn-helix , lysr family protein; Belongs to the LysR transcriptional regulatory family | annotation not available | 0.643 |
| DR97_4810 | DR97_2674 | DR97_4810 | DR97_2674 | annotation not available | annotation not available | 0.502 |
| DR97_4810 | DR97_367 | DR97_4810 | DR97_367 | annotation not available | annotation not available | 0.590 |
| DR97_4810 | DR97_4808 | DR97_4810 | DR97_4808 | annotation not available | annotation not available | 0.461 |
| DR97_4810 | DR97_4809 | DR97_4810 | DR97_4809 | annotation not available | Bacterial regulatory helix-turn-helix , lysr family protein; Belongs to the LysR transcriptional regulatory family | 0.643 |
| DR97_4810 | ilvA1 | DR97_4810 | 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 | 0.433 |
| DR97_4810 | ilvA2 | DR97_4810 | DR97_468 | 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 | 0.428 |
| DR97_4810 | srr | DR97_4810 | DR97_5277 | annotation not available | annotation not available | 0.458 |
| DR97_4810 | tkt | DR97_4810 | DR97_3517 | annotation not available | Transketolase; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate | 0.406 |
| ilvA1 | DR97_4810 | DR97_3296 | DR97_4810 | 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 | 0.433 |
| ilvA1 | ilvA2 | DR97_3296 | DR97_468 | 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 | 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 | 0.802 |
| ilvA2 | DR97_4810 | DR97_468 | DR97_4810 | 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 | 0.428 |
| ilvA2 | ilvA1 | DR97_468 | DR97_3296 | 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 | 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 | 0.802 |
| srr | DR97_367 | DR97_5277 | DR97_367 | annotation not available | annotation not available | 0.428 |
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