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 simple tabular text output:
TSV: tab separated values - can be opened in Excel
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... 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 annotated functions of the network proteins
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| gly1 | ilvA1 | DR97_1041 | DR97_3296 | annotation not available | L-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 | 0.923 |
| gly1 | ilvA3 | DR97_1041 | DR97_468 | annotation not available | L-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 | 0.916 |
| gly1 | ltaE | DR97_1041 | DR97_2790 | annotation not available | L-threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L- threonine to glycine and acetaldehyde | 0.800 |
| gly1 | lysC | DR97_1041 | DR97_1039 | annotation not available | Aspartokinase; Asp_kin_monofn: aspartate kinase, monofunctional class; Belongs to the aspartokinase family | 0.498 |
| gly1 | srr | DR97_1041 | DR97_5277 | annotation not available | annotation not available | 0.917 |
| gly1 | tdcB_1 | DR97_1041 | DR97_1093 | annotation not available | annotation not available | 0.916 |
| gly1 | thrC | DR97_1041 | DR97_4142 | annotation not available | thrC: threonine synthase | 0.916 |
| hom | ilvA1 | DR97_4141 | DR97_3296 | annotation not available | L-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 | 0.680 |
| hom | ilvA3 | DR97_4141 | DR97_468 | annotation not available | L-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 | 0.640 |
| hom | lysC | DR97_4141 | DR97_1039 | annotation not available | Aspartokinase; Asp_kin_monofn: aspartate kinase, monofunctional class; Belongs to the aspartokinase family | 0.993 |
| 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; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily | 0.407 |
| hom | srr | DR97_4141 | DR97_5277 | annotation not available | annotation not available | 0.445 |
| hom | tdcB_1 | DR97_4141 | DR97_1093 | annotation not available | annotation not available | 0.445 |
| hom | thrB | DR97_4141 | DR97_2873 | annotation not available | thrB_alt: homoserine kinase; Belongs to the pseudomonas-type ThrB family | 0.985 |
| hom | thrC | DR97_4141 | DR97_4142 | annotation not available | thrC: threonine synthase | 0.999 |
| ilvA1 | gly1 | DR97_3296 | DR97_1041 | L-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 | annotation not available | 0.923 |
| ilvA1 | hom | DR97_3296 | DR97_4141 | L-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 | annotation not available | 0.680 |
| ilvA1 | ilvA3 | DR97_3296 | DR97_468 | L-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 | L-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 | 0.802 |
| ilvA1 | ltaE | DR97_3296 | DR97_2790 | L-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 | L-threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L- threonine to glycine and acetaldehyde | 0.917 |
| ilvA1 | lysC | DR97_3296 | DR97_1039 | L-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 | Aspartokinase; Asp_kin_monofn: aspartate kinase, monofunctional class; Belongs to the aspartokinase family | 0.494 |
page 1 of 4
STRING Data Update
