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 |
| ilvA | ilvB_1 | NA29_08605 | NA29_14765 | PLP-dependent 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. | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.922 |
| ilvA | ilvB_2 | NA29_08605 | NA29_22335 | PLP-dependent 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | 0.922 |
| ilvA | ilvH | NA29_08605 | NA29_13295 | PLP-dependent 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. | Acetolactate synthase small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.956 |
| ilvA | ilvI | NA29_08605 | NA29_13290 | PLP-dependent 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. | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.922 |
| ilvA | leuB | NA29_08605 | NA29_18955 | PLP-dependent 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. | 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. | 0.932 |
| ilvA | psdht | NA29_08605 | NA29_14220 | PLP-dependent 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/threonine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.923 |
| ilvA | tdcB_2 | NA29_08605 | NA29_15830 | PLP-dependent 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.924 |
| ilvA | thrC_1 | NA29_08605 | NA29_06810 | PLP-dependent 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.945 |
| ilvA | thrC_2 | NA29_08605 | NA29_17630 | PLP-dependent 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 synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.937 |
| ilvA | trpB | NA29_08605 | NA29_18930 | PLP-dependent 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. | 0.927 |
| ilvB_1 | ilvA | NA29_14765 | NA29_08605 | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | PLP-dependent 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. | 0.922 |
| ilvB_1 | ilvB_2 | NA29_14765 | NA29_22335 | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | 0.926 |
| ilvB_1 | ilvH | NA29_14765 | NA29_13295 | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | Acetolactate synthase small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.994 |
| ilvB_1 | ilvI | NA29_14765 | NA29_13290 | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.910 |
| ilvB_1 | leuB | NA29_14765 | NA29_18955 | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.980 |
| ilvB_1 | psdht | NA29_14765 | NA29_14220 | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | Serine/threonine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.922 |
| ilvB_1 | tdcB_2 | NA29_14765 | NA29_15830 | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.922 |
| ilvB_2 | ilvA | NA29_22335 | NA29_08605 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | PLP-dependent 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. | 0.922 |
| ilvB_2 | ilvB_1 | NA29_22335 | NA29_14765 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.926 |
| ilvB_2 | ilvH | NA29_22335 | NA29_13295 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. | Acetolactate synthase small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.987 |
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