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 |
| AKS72627.1 | AKS73877.1 | RN70_01170 | RN70_08190 | 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. | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.909 |
| AKS72627.1 | AKS74678.1 | RN70_01170 | RN70_08185 | 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. | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.909 |
| AKS72627.1 | cysE | RN70_01170 | RN70_11320 | 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. | Serine acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.805 |
| AKS72627.1 | glyA | RN70_01170 | RN70_03815 | 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. | Serine 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. | 0.911 |
| AKS72627.1 | ilvA | RN70_01170 | RN70_04080 | 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 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. | 0.915 |
| AKS72627.1 | sdaAA | RN70_01170 | RN70_02430 | 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. | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.909 |
| AKS72627.1 | sdaAB | RN70_01170 | RN70_02435 | 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. | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.909 |
| AKS72627.1 | trpA | RN70_01170 | RN70_02310 | 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. | Tryptophan synthase subunit alpha; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.919 |
| AKS72627.1 | trpB | RN70_01170 | RN70_02305 | 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. | Tryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.932 |
| AKS73877.1 | AKS72627.1 | RN70_08190 | RN70_01170 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; 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. | 0.909 |
| AKS73877.1 | AKS74678.1 | RN70_08190 | RN70_08185 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.999 |
| AKS73877.1 | cysE | RN70_08190 | RN70_11320 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Serine acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.902 |
| AKS73877.1 | glyA | RN70_08190 | RN70_03815 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Serine 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. | 0.933 |
| AKS73877.1 | ilvA | RN70_08190 | RN70_04080 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; 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. | 0.909 |
| AKS73877.1 | sdaAA | RN70_08190 | RN70_02430 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.998 |
| AKS73877.1 | sdaAB | RN70_08190 | RN70_02435 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.913 |
| AKS73877.1 | thrB | RN70_08190 | RN70_07440 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Serine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.820 |
| AKS73877.1 | trpA | RN70_08190 | RN70_02310 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Tryptophan synthase subunit alpha; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.902 |
| AKS73877.1 | trpB | RN70_08190 | RN70_02305 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Tryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.900 |
| AKS74678.1 | AKS72627.1 | RN70_08185 | RN70_01170 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; 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. | 0.909 |
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