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 |
| Ajs_0080 | Ajs_0095 | Ajs_0080 | Ajs_0095 | 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. | KEGG: pol:Bpro_4369 L-serine dehydratase 1; TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.922 |
| Ajs_0080 | Ajs_2044 | Ajs_0080 | Ajs_2044 | 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. | KEGG: pol:Bpro_2168 lactoylglutathione lyase. | 0.820 |
| Ajs_0080 | Ajs_2047 | Ajs_0080 | Ajs_2047 | 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. | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | 0.821 |
| Ajs_0080 | Ajs_2490 | Ajs_0080 | Ajs_2490 | 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. | PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, catalytic region; D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; KEGG: pol:Bpro_3078 D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding. | 0.815 |
| Ajs_0080 | Ajs_3758 | Ajs_0080 | Ajs_3758 | 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. | PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; KEGG: pol:Bpro_4156 D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding. | 0.840 |
| Ajs_0080 | Ajs_3847 | Ajs_0080 | Ajs_3847 | 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. | PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: pol:Bpro_4245 pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | 0.923 |
| Ajs_0080 | dsdA | Ajs_0080 | Ajs_2250 | 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: D-serine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: bur:Bcep18194_B1364 D-serine dehydratase; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | 0.904 |
| Ajs_0080 | ilvA | Ajs_0080 | Ajs_0679 | 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; 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. | 0.917 |
| Ajs_0095 | Ajs_0080 | Ajs_0095 | Ajs_0080 | KEGG: pol:Bpro_4369 L-serine dehydratase 1; TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 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. | 0.922 |
| Ajs_0095 | Ajs_2044 | Ajs_0095 | Ajs_2044 | KEGG: pol:Bpro_4369 L-serine dehydratase 1; TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | KEGG: pol:Bpro_2168 lactoylglutathione lyase. | 0.800 |
| Ajs_0095 | Ajs_2047 | Ajs_0095 | Ajs_2047 | KEGG: pol:Bpro_4369 L-serine dehydratase 1; TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | 0.800 |
| Ajs_0095 | Ajs_2490 | Ajs_0095 | Ajs_2490 | KEGG: pol:Bpro_4369 L-serine dehydratase 1; TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, catalytic region; D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; KEGG: pol:Bpro_3078 D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding. | 0.817 |
| Ajs_0095 | Ajs_3758 | Ajs_0095 | Ajs_3758 | KEGG: pol:Bpro_4369 L-serine dehydratase 1; TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; KEGG: pol:Bpro_4156 D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding. | 0.804 |
| Ajs_0095 | Ajs_3847 | Ajs_0095 | Ajs_3847 | KEGG: pol:Bpro_4369 L-serine dehydratase 1; TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: pol:Bpro_4245 pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | 0.918 |
| Ajs_0095 | dsdA | Ajs_0095 | Ajs_2250 | KEGG: pol:Bpro_4369 L-serine dehydratase 1; TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | TIGRFAM: D-serine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: bur:Bcep18194_B1364 D-serine dehydratase; Belongs to the serine/threonine dehydratase family. DsdA subfamily. | 0.916 |
| Ajs_0095 | ilvA | Ajs_0095 | Ajs_0679 | KEGG: pol:Bpro_4369 L-serine dehydratase 1; TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 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. | 0.918 |
| Ajs_2044 | Ajs_0080 | Ajs_2044 | Ajs_0080 | KEGG: pol:Bpro_2168 lactoylglutathione lyase. | 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. | 0.820 |
| Ajs_2044 | Ajs_0095 | Ajs_2044 | Ajs_0095 | KEGG: pol:Bpro_2168 lactoylglutathione lyase. | KEGG: pol:Bpro_4369 L-serine dehydratase 1; TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.800 |
| Ajs_2044 | Ajs_2047 | Ajs_2044 | Ajs_2047 | KEGG: pol:Bpro_2168 lactoylglutathione lyase. | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | 0.918 |
| Ajs_2044 | Ajs_2490 | Ajs_2044 | Ajs_2490 | KEGG: pol:Bpro_2168 lactoylglutathione lyase. | PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, catalytic region; D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; KEGG: pol:Bpro_3078 D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding. | 0.911 |
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