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 |
| KB13_975 | KB13_999 | KB13_975 | KB13_999 | Asparate kinase, monofunctional class; [E] COG0263 Glutamate 5-kinase; Belongs to the aspartokinase family. | [E] COG0460 Homoserine dehydrogenase. | 0.952 |
| KB13_975 | ilvA | KB13_975 | KB13_711 | Asparate kinase, monofunctional class; [E] COG0263 Glutamate 5-kinase; Belongs to the aspartokinase family. | Threonine ammonia-lyase, biosynthetic; 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. | 0.726 |
| KB13_975 | ilvE | KB13_975 | KB13_413 | Asparate kinase, monofunctional class; [E] COG0263 Glutamate 5-kinase; Belongs to the aspartokinase family. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.543 |
| KB13_975 | metH | KB13_975 | KB13_806 | Asparate kinase, monofunctional class; [E] COG0263 Glutamate 5-kinase; Belongs to the aspartokinase family. | Methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 0.809 |
| KB13_975 | metZ | KB13_975 | KB13_629 | Asparate kinase, monofunctional class; [E] COG0263 Glutamate 5-kinase; Belongs to the aspartokinase family. | O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide. | 0.756 |
| KB13_975 | thrC | KB13_975 | KB13_112 | Asparate kinase, monofunctional class; [E] COG0263 Glutamate 5-kinase; Belongs to the aspartokinase family. | [E] COG0498 Threonine synthase. | 0.843 |
| KB13_975 | trpB | KB13_975 | KB13_1270 | Asparate kinase, monofunctional class; [E] COG0263 Glutamate 5-kinase; Belongs to the aspartokinase family. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.647 |
| KB13_999 | KB13_975 | KB13_999 | KB13_975 | [E] COG0460 Homoserine dehydrogenase. | Asparate kinase, monofunctional class; [E] COG0263 Glutamate 5-kinase; Belongs to the aspartokinase family. | 0.952 |
| KB13_999 | ilvA | KB13_999 | KB13_711 | [E] COG0460 Homoserine dehydrogenase. | Threonine ammonia-lyase, biosynthetic; 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. | 0.761 |
| KB13_999 | ilvE | KB13_999 | KB13_413 | [E] COG0460 Homoserine dehydrogenase. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.656 |
| KB13_999 | ilvN | KB13_999 | KB13_289 | [E] COG0460 Homoserine dehydrogenase. | [E] COG0440 Acetolactate synthase, small (regulatory) subunit. | 0.915 |
| KB13_999 | metH | KB13_999 | KB13_806 | [E] COG0460 Homoserine dehydrogenase. | Methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 0.846 |
| KB13_999 | metZ | KB13_999 | KB13_629 | [E] COG0460 Homoserine dehydrogenase. | O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide. | 0.758 |
| KB13_999 | thrC | KB13_999 | KB13_112 | [E] COG0460 Homoserine dehydrogenase. | [E] COG0498 Threonine synthase. | 0.994 |
| KB13_999 | trpB | KB13_999 | KB13_1270 | [E] COG0460 Homoserine dehydrogenase. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.594 |
| ilvA | KB13_975 | KB13_711 | KB13_975 | Threonine ammonia-lyase, biosynthetic; 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. | Asparate kinase, monofunctional class; [E] COG0263 Glutamate 5-kinase; Belongs to the aspartokinase family. | 0.726 |
| ilvA | KB13_999 | KB13_711 | KB13_999 | Threonine ammonia-lyase, biosynthetic; 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. | [E] COG0460 Homoserine dehydrogenase. | 0.761 |
| ilvA | ilvB_2 | KB13_711 | KB13_33 | Threonine ammonia-lyase, biosynthetic; 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; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | 0.727 |
| ilvA | ilvD | KB13_711 | KB13_839 | Threonine ammonia-lyase, biosynthetic; 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. | [EG] COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.910 |
| ilvA | ilvE | KB13_711 | KB13_413 | Threonine ammonia-lyase, biosynthetic; 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. | 0.772 |
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