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 |
| DR97_3367 | hom | DR97_3367 | DR97_4141 | annotation not available | annotation not available | 0.942 |
| DR97_3367 | ilvA1 | DR97_3367 | DR97_3296 | annotation not available | 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 | 0.914 |
| DR97_3367 | ilvA2 | DR97_3367 | DR97_468 | annotation not available | 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 | 0.914 |
| DR97_3367 | metH | DR97_3367 | DR97_34 | annotation not available | 5-methyltetrahydrofolate--homocysteine methyltransferase; 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 (By similarity) | 0.965 |
| DR97_3367 | metX | DR97_3367 | DR97_3357 | annotation not available | Homoserine o-acetyltransferase/o-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine | 0.858 |
| DR97_3367 | metY | DR97_3367 | DR97_2380 | annotation not available | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein | 0.950 |
| DR97_3367 | metZ | DR97_3367 | DR97_4826 | annotation not available | O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide. Cannot use the other activated form of L-homoserine, O-acetyl-L-homoserine, as a substrate | 0.962 |
| DR97_3367 | pssA | DR97_3367 | DR97_2035 | annotation not available | Cdp-diacylglycerol---serine o-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family | 0.906 |
| DR97_3367 | serB | DR97_3367 | DR97_2313 | annotation not available | serB: phosphoserine phosphatase SerB | 0.914 |
| hom | DR97_3367 | DR97_4141 | DR97_3367 | annotation not available | annotation not available | 0.942 |
| hom | ilvA1 | DR97_4141 | DR97_3296 | annotation not available | 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 | 0.677 |
| hom | ilvA2 | DR97_4141 | DR97_468 | annotation not available | 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 | 0.631 |
| hom | metH | DR97_4141 | DR97_34 | annotation not available | 5-methyltetrahydrofolate--homocysteine methyltransferase; 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 (By similarity) | 0.966 |
| hom | metW | DR97_4141 | DR97_3356 | annotation not available | Putative methionine biosynthesis protein; metW: methionine biosynthesis protein MetW | 0.758 |
| hom | metX | DR97_4141 | DR97_3357 | annotation not available | Homoserine o-acetyltransferase/o-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine | 0.985 |
| hom | metY | DR97_4141 | DR97_2380 | annotation not available | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein | 0.887 |
| hom | metZ | DR97_4141 | DR97_4826 | annotation not available | O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide. Cannot use the other activated form of L-homoserine, O-acetyl-L-homoserine, as a substrate | 0.937 |
| hom | serB | DR97_4141 | DR97_2313 | annotation not available | serB: phosphoserine phosphatase SerB | 0.585 |
| ilvA1 | DR97_3367 | DR97_3296 | DR97_3367 | 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 | annotation not available | 0.914 |
| ilvA1 | hom | DR97_3296 | DR97_4141 | 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 | annotation not available | 0.677 |
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