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 |
| SBG_0794 | ybjU | SBG_0794 | SBG_0795 | Conserved hypothetical protein. | L-allo-threonine aldolase. | 0.825 |
| engD | ybjU | SBG_1644 | SBG_0795 | Putative ATP/GTP-binding protein; ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner. | L-allo-threonine aldolase. | 0.717 |
| gcvP | glyA | SBG_2646 | SBG_2329 | Glycine dehydrogenase (decarboxylating); Belongs to the GcvP family. | Serine hydroxymethyltransferase. | 0.996 |
| gcvP | ilvA | SBG_2646 | SBG_3449 | Glycine dehydrogenase (decarboxylating); Belongs to the GcvP family. | Threonine deaminase; 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. | 0.424 |
| gcvP | kbl | SBG_2646 | SBG_3291 | Glycine dehydrogenase (decarboxylating); Belongs to the GcvP family. | 2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. | 0.939 |
| gcvP | tdcB | SBG_2646 | SBG_2881 | Glycine dehydrogenase (decarboxylating); Belongs to the GcvP family. | Catabolic threonine dehydratase; 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. | 0.424 |
| gcvP | thrC | SBG_2646 | SBG_0003 | Glycine dehydrogenase (decarboxylating); Belongs to the GcvP family. | Threonine synthase. | 0.491 |
| gcvP | ybjU | SBG_2646 | SBG_0795 | Glycine dehydrogenase (decarboxylating); Belongs to the GcvP family. | L-allo-threonine aldolase. | 0.959 |
| gcvP | ydfG_2 | SBG_2646 | SBG_1338 | Glycine dehydrogenase (decarboxylating); Belongs to the GcvP family. | Putative oxidoreductase. | 0.713 |
| glyA | gcvP | SBG_2329 | SBG_2646 | Serine hydroxymethyltransferase. | Glycine dehydrogenase (decarboxylating); Belongs to the GcvP family. | 0.996 |
| glyA | ilvA | SBG_2329 | SBG_3449 | Serine hydroxymethyltransferase. | Threonine deaminase; 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. | 0.926 |
| glyA | kbl | SBG_2329 | SBG_3291 | Serine hydroxymethyltransferase. | 2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. | 0.929 |
| glyA | tdcB | SBG_2329 | SBG_2881 | Serine hydroxymethyltransferase. | Catabolic threonine dehydratase; 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. | 0.912 |
| glyA | ybjU | SBG_2329 | SBG_0795 | Serine hydroxymethyltransferase. | L-allo-threonine aldolase. | 0.932 |
| ilvA | gcvP | SBG_3449 | SBG_2646 | Threonine deaminase; 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. | Glycine dehydrogenase (decarboxylating); Belongs to the GcvP family. | 0.424 |
| ilvA | glyA | SBG_3449 | SBG_2329 | Threonine deaminase; 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. | Serine hydroxymethyltransferase. | 0.926 |
| ilvA | tdcB | SBG_3449 | SBG_2881 | Threonine deaminase; 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. | Catabolic threonine dehydratase; 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. | 0.942 |
| ilvA | tdh | SBG_3449 | SBG_3290 | Threonine deaminase; 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 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.901 |
| ilvA | thrC | SBG_3449 | SBG_0003 | Threonine deaminase; 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. | 0.954 |
| ilvA | ybjU | SBG_3449 | SBG_0795 | Threonine deaminase; 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-allo-threonine aldolase. | 0.915 |
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