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 |
| DSJ_01810 | ilvA | DSJ_01810 | DSJ_01795 | Acetolactate synthase 2 small subunit; 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. | 0.975 |
| DSJ_01810 | ilvD | DSJ_01810 | DSJ_01800 | Acetolactate synthase 2 small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | 0.908 |
| DSJ_01810 | ilvE | DSJ_01810 | DSJ_01805 | Acetolactate synthase 2 small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Branched chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.922 |
| DSJ_01810 | leuA | DSJ_01810 | DSJ_06160 | Acetolactate synthase 2 small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.821 |
| DSJ_17085 | avtA | DSJ_17085 | DSJ_00055 | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Valine--pyruvate transaminase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.903 |
| DSJ_17085 | ilvD | DSJ_17085 | DSJ_01800 | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | 0.919 |
| DSJ_17085 | ilvE | DSJ_17085 | DSJ_01805 | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Branched chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.910 |
| DSJ_17085 | leuA | DSJ_17085 | DSJ_06160 | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.910 |
| DSJ_17085 | metL | DSJ_17085 | DSJ_02735 | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional aspartate kinase/homoserine dehydrogenase II; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.609 |
| DSJ_17085 | thrA | DSJ_17085 | DSJ_05960 | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional aspartate kinase/homoserine dehydrogenase I; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.609 |
| avtA | DSJ_17085 | DSJ_00055 | DSJ_17085 | Valine--pyruvate transaminase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Aminotransferase; Broad specificity; family IV; in Corynebacterium glutamicum this protein can use glutamate, 2-aminobutyrate, and aspartate as amino donors and pyruvate as the acceptor; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.903 |
| avtA | ilvD | DSJ_00055 | DSJ_01800 | Valine--pyruvate transaminase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | 0.908 |
| avtA | ilvE | DSJ_00055 | DSJ_01805 | Valine--pyruvate transaminase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Branched chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.915 |
| avtA | leuA | DSJ_00055 | DSJ_06160 | Valine--pyruvate transaminase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.902 |
| ilvA | DSJ_01810 | DSJ_01795 | DSJ_01810 | 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 2 small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.975 |
| ilvA | ilvD | DSJ_01795 | DSJ_01800 | 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. | Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. | 0.918 |
| ilvA | ilvE | DSJ_01795 | DSJ_01805 | 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. | Branched chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.957 |
| ilvA | leuA | DSJ_01795 | DSJ_06160 | 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. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.493 |
| ilvA | metB | DSJ_01795 | DSJ_02730 | 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. | Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.817 |
| ilvA | metL | DSJ_01795 | DSJ_02735 | 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. | Bifunctional aspartate kinase/homoserine dehydrogenase II; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.635 |
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