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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Meso_0309 | Meso_0760 | Meso_0309 | Meso_0760 | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: ret:RHE_CH03537 probable threonine dehydratase protein. | TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: mlo:mll7517 threonine synthase. | 0.946 |
| Meso_0309 | ilvA | Meso_0309 | Meso_1421 | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: ret:RHE_CH03537 probable threonine dehydratase protein. | 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. | 0.924 |
| Meso_0309 | trpB | Meso_0309 | Meso_0666 | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: ret:RHE_CH03537 probable threonine dehydratase protein. | Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.929 |
| Meso_0760 | Meso_0309 | Meso_0760 | Meso_0309 | TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: mlo:mll7517 threonine synthase. | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: ret:RHE_CH03537 probable threonine dehydratase protein. | 0.946 |
| Meso_0760 | Meso_1424 | Meso_0760 | Meso_1424 | TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: mlo:mll7517 threonine synthase. | PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: mlo:mlr0353 O-acetylserine (thiol) lyase. | 0.479 |
| Meso_0760 | Meso_3309 | Meso_0760 | Meso_3309 | TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: mlo:mll7517 threonine synthase. | PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: cps:CPS_4888 putative threonine dehydratase, catabolic. | 0.731 |
| Meso_0760 | ilvA | Meso_0760 | Meso_1421 | TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: mlo:mll7517 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. | 0.952 |
| Meso_1424 | Meso_0760 | Meso_1424 | Meso_0760 | PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: mlo:mlr0353 O-acetylserine (thiol) lyase. | TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: mlo:mll7517 threonine synthase. | 0.479 |
| Meso_3309 | Meso_0760 | Meso_3309 | Meso_0760 | PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: cps:CPS_4888 putative threonine dehydratase, catabolic. | TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: mlo:mll7517 threonine synthase. | 0.731 |
| ilvA | Meso_0309 | Meso_1421 | Meso_0309 | 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. | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: ret:RHE_CH03537 probable threonine dehydratase protein. | 0.924 |
| ilvA | Meso_0760 | Meso_1421 | Meso_0760 | 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. | TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: mlo:mll7517 threonine synthase. | 0.952 |
| ilvA | trpB | Meso_1421 | Meso_0666 | 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. | 0.929 |
| trpB | Meso_0309 | Meso_0666 | Meso_0309 | Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: ret:RHE_CH03537 probable threonine dehydratase protein. | 0.929 |
| trpB | ilvA | Meso_0666 | Meso_1421 | 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. | 0.929 |