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 |
| ilvA | ilvE | b3772 | b3770 | L-threonine dehydratase, 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. | 0.995 |
| ilvA | ridA | b3772 | b4243 | L-threonine dehydratase, 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. | Enamine/imine deaminase, reaction intermediate detoxification; Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis (By similarity); Belongs to the RutC family. | 0.840 |
| ilvA | tdcB | b3772 | b3117 | L-threonine dehydratase, 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. | L-threonine dehydratase, catabolic; 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. TdcB also dehydrates serine t [...] | 0.927 |
| ilvE | ilvA | b3770 | b3772 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. | L-threonine dehydratase, 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. | 0.995 |
| ilvE | ridA | b3770 | b4243 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. | Enamine/imine deaminase, reaction intermediate detoxification; Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis (By similarity); Belongs to the RutC family. | 0.568 |
| ilvE | tdcB | b3770 | b3117 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. | L-threonine dehydratase, catabolic; 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. TdcB also dehydrates serine t [...] | 0.960 |
| pyrB | pyrI | b4245 | b4244 | Aspartate carbamoyltransferase, catalytic subunit; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. | Aspartate carbamoyltransferase, regulatory subunit; Involved in allosteric regulation of aspartate carbamoyltransferase; Belongs to the PyrI family. | 0.999 |
| pyrB | pyrL | b4245 | b4246 | Aspartate carbamoyltransferase, catalytic subunit; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. | pyrBI operon leader peptide; Protein involved in pyrimidine nucleotide biosynthetic process. | 0.841 |
| pyrB | ridA | b4245 | b4243 | Aspartate carbamoyltransferase, catalytic subunit; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. | Enamine/imine deaminase, reaction intermediate detoxification; Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis (By similarity); Belongs to the RutC family. | 0.950 |
| pyrB | yjgH | b4245 | b4248 | Aspartate carbamoyltransferase, catalytic subunit; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. | UPF0131 family protein; Protein involved in translation. | 0.432 |
| pyrI | pyrB | b4244 | b4245 | Aspartate carbamoyltransferase, regulatory subunit; Involved in allosteric regulation of aspartate carbamoyltransferase; Belongs to the PyrI family. | Aspartate carbamoyltransferase, catalytic subunit; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. | 0.999 |
| pyrI | pyrL | b4244 | b4246 | Aspartate carbamoyltransferase, regulatory subunit; Involved in allosteric regulation of aspartate carbamoyltransferase; Belongs to the PyrI family. | pyrBI operon leader peptide; Protein involved in pyrimidine nucleotide biosynthetic process. | 0.887 |
| pyrI | ridA | b4244 | b4243 | Aspartate carbamoyltransferase, regulatory subunit; Involved in allosteric regulation of aspartate carbamoyltransferase; Belongs to the PyrI family. | Enamine/imine deaminase, reaction intermediate detoxification; Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis (By similarity); Belongs to the RutC family. | 0.963 |
| pyrI | yjgH | b4244 | b4248 | Aspartate carbamoyltransferase, regulatory subunit; Involved in allosteric regulation of aspartate carbamoyltransferase; Belongs to the PyrI family. | UPF0131 family protein; Protein involved in translation. | 0.425 |
| pyrL | pyrB | b4246 | b4245 | pyrBI operon leader peptide; Protein involved in pyrimidine nucleotide biosynthetic process. | Aspartate carbamoyltransferase, catalytic subunit; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. | 0.841 |
| pyrL | pyrI | b4246 | b4244 | pyrBI operon leader peptide; Protein involved in pyrimidine nucleotide biosynthetic process. | Aspartate carbamoyltransferase, regulatory subunit; Involved in allosteric regulation of aspartate carbamoyltransferase; Belongs to the PyrI family. | 0.887 |
| pyrL | ridA | b4246 | b4243 | pyrBI operon leader peptide; Protein involved in pyrimidine nucleotide biosynthetic process. | Enamine/imine deaminase, reaction intermediate detoxification; Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis (By similarity); Belongs to the RutC family. | 0.566 |
| pyrL | yjgH | b4246 | b4248 | pyrBI operon leader peptide; Protein involved in pyrimidine nucleotide biosynthetic process. | UPF0131 family protein; Protein involved in translation. | 0.439 |
| ridA | ilvA | b4243 | b3772 | Enamine/imine deaminase, reaction intermediate detoxification; Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis (By similarity); Belongs to the RutC family. | L-threonine dehydratase, 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. | 0.840 |
| ridA | ilvE | b4243 | b3770 | Enamine/imine deaminase, reaction intermediate detoxification; Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis (By similarity); Belongs to the RutC family. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. | 0.568 |
page 1 of 2