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 |
| ADU12399.1 | ADU13708.1 | Astex_0713 | Astex_2046 | KEGG: mmr:Mmar10_0289 acetolactate synthase 2 catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; KEGG: azc:AZC_4176 thiamine pyrophosphate protein; Belongs to the TPP enzyme family. | 0.921 |
| ADU12399.1 | ADU13961.1 | Astex_0713 | Astex_2307 | KEGG: mmr:Mmar10_0289 acetolactate synthase 2 catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | 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. | 0.928 |
| ADU12399.1 | leuB | Astex_0713 | Astex_0707 | KEGG: mmr:Mmar10_0289 acetolactate synthase 2 catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | 0.992 |
| ADU12484.1 | ADU13961.1 | Astex_0800 | Astex_2307 | KEGG: bxe:Bxe_A1314 L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase. | 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. | 0.907 |
| ADU12484.1 | ADU13979.1 | Astex_0800 | Astex_2325 | KEGG: bxe:Bxe_A1314 L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase. | TIGRFAM: threonine synthase; KEGG: hne:HNE_1045 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | 0.919 |
| ADU12484.1 | ADU14434.1 | Astex_0800 | Astex_2796 | KEGG: bxe:Bxe_A1314 L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase. | Threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | 0.910 |
| ADU12484.1 | glyA | Astex_0800 | Astex_2943 | KEGG: bxe:Bxe_A1314 L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase. | Glycine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.918 |
| ADU13641.1 | ADU13961.1 | Astex_1979 | Astex_2307 | KEGG: hba:Hbal_0580 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. | 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. | 0.923 |
| ADU13641.1 | glyA | Astex_1979 | Astex_2943 | KEGG: hba:Hbal_0580 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. | Glycine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.968 |
| ADU13641.1 | trpA | Astex_1979 | Astex_2359 | KEGG: hba:Hbal_0580 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. | Tryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.903 |
| ADU13641.1 | trpB | Astex_1979 | Astex_2360 | KEGG: hba:Hbal_0580 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. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.900 |
| ADU13708.1 | ADU12399.1 | Astex_2046 | Astex_0713 | PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; KEGG: azc:AZC_4176 thiamine pyrophosphate protein; Belongs to the TPP enzyme family. | KEGG: mmr:Mmar10_0289 acetolactate synthase 2 catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | 0.921 |
| ADU13708.1 | ADU13961.1 | Astex_2046 | Astex_2307 | PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; KEGG: azc:AZC_4176 thiamine pyrophosphate protein; Belongs to the TPP enzyme family. | 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. | 0.928 |
| ADU13708.1 | leuB | Astex_2046 | Astex_0707 | PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; KEGG: azc:AZC_4176 thiamine pyrophosphate protein; Belongs to the TPP enzyme family. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | 0.951 |
| ADU13961.1 | ADU12399.1 | Astex_2307 | Astex_0713 | 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. | KEGG: mmr:Mmar10_0289 acetolactate synthase 2 catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. | 0.928 |
| ADU13961.1 | ADU12484.1 | Astex_2307 | Astex_0800 | 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. | KEGG: bxe:Bxe_A1314 L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase. | 0.907 |
| ADU13961.1 | ADU13641.1 | Astex_2307 | Astex_1979 | 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. | KEGG: hba:Hbal_0580 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. | 0.923 |
| ADU13961.1 | ADU13708.1 | Astex_2307 | Astex_2046 | 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. | PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; KEGG: azc:AZC_4176 thiamine pyrophosphate protein; Belongs to the TPP enzyme family. | 0.928 |
| ADU13961.1 | ADU13979.1 | Astex_2307 | Astex_2325 | 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. | TIGRFAM: threonine synthase; KEGG: hne:HNE_1045 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | 0.951 |
| ADU13961.1 | ADU14434.1 | Astex_2307 | Astex_2796 | 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. | Threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | 0.907 |
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