Export your current network:
... as a bitmap image:
file format is 'PNG': portable network graphic
... as a high-resolution bitmap:
same PNG format, but at higher resolution
... 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_1041 | DR97_1093 | DR97_1041 | DR97_1093 | annotation not available | annotation not available | 0.913 |
DR97_1041 | ilvA1 | DR97_1041 | 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 | 0.921 |
DR97_1041 | ilvA2 | DR97_1041 | 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 | 0.913 |
DR97_1041 | ltaE | DR97_1041 | DR97_2790 | annotation not available | Low specificity l-threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde | 0.800 |
DR97_1041 | lysC | DR97_1041 | DR97_1039 | annotation not available | Aspartate kinase, monofunctional class; Belongs to the aspartokinase family | 0.478 |
DR97_1041 | thrC | DR97_1041 | DR97_4142 | annotation not available | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine | 0.921 |
DR97_1093 | DR97_1041 | DR97_1093 | DR97_1041 | annotation not available | annotation not available | 0.913 |
DR97_1093 | hom | DR97_1093 | DR97_4141 | annotation not available | annotation not available | 0.451 |
DR97_1093 | ilvA1 | DR97_1093 | 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 | 0.876 |
DR97_1093 | ilvA2 | DR97_1093 | 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 | 0.873 |
DR97_1093 | ltaE | DR97_1093 | DR97_2790 | annotation not available | Low specificity l-threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde | 0.913 |
DR97_1093 | thrC | DR97_1093 | DR97_4142 | annotation not available | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine | 0.927 |
hom | DR97_1093 | DR97_4141 | DR97_1093 | annotation not available | annotation not available | 0.451 |
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 | lysC | DR97_4141 | DR97_1039 | annotation not available | Aspartate kinase, monofunctional class; Belongs to the aspartokinase family | 0.992 |
hom | serC | DR97_4141 | DR97_4769 | annotation not available | Phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine | 0.424 |
hom | srr | DR97_4141 | DR97_5277 | annotation not available | annotation not available | 0.451 |
hom | thrB | DR97_4141 | DR97_2873 | annotation not available | Homoserine kinase type ii; thrB_alt: homoserine kinase; Belongs to the pseudomonas-type ThrB family | 0.960 |
hom | thrC | DR97_4141 | DR97_4142 | annotation not available | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine | 0.999 |
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