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 |
| aroF | ilvA | FLB_03210 | FLB_27520 | Phospho-2-dehydro-3-deoxyheptonate aldolase. | L-threonine dehydratase biosynthetic IlvA; 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. | 0.417 |
| aroF | metX | FLB_03210 | FLB_17930 | Phospho-2-dehydro-3-deoxyheptonate aldolase. | Homoserine O-acetyltransferase; Belongs to the AB hydrolase superfamily. MetX family. | 0.640 |
| aroF | pabB | FLB_03210 | FLB_11420 | Phospho-2-dehydro-3-deoxyheptonate aldolase. | Aminodeoxychorismate synthase component 1. | 0.942 |
| aroF | pabC | FLB_03210 | FLB_05640 | Phospho-2-dehydro-3-deoxyheptonate aldolase. | Aminodeoxychorismate lyase. | 0.778 |
| aroF | thrA_1 | FLB_03210 | FLB_09230 | Phospho-2-dehydro-3-deoxyheptonate aldolase. | Bifunctional aspartokinase/homoserine dehydrogenase 1. | 0.625 |
| aroF | thrA_2 | FLB_03210 | FLB_17940 | Phospho-2-dehydro-3-deoxyheptonate aldolase. | Bifunctional aspartokinase/homoserine dehydrogenase 1. | 0.640 |
| bkdA2 | ilvA | FLB_09300 | FLB_27520 | 2-oxoisovalerate dehydrogenase subunit beta. | L-threonine dehydratase biosynthetic IlvA; 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. | 0.845 |
| bkdA2 | ldh | FLB_09300 | FLB_01560 | 2-oxoisovalerate dehydrogenase subunit beta. | Leucine dehydrogenase; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | 0.939 |
| bkdA2 | pabC | FLB_09300 | FLB_05640 | 2-oxoisovalerate dehydrogenase subunit beta. | Aminodeoxychorismate lyase. | 0.856 |
| ilvA | aroF | FLB_27520 | FLB_03210 | L-threonine dehydratase biosynthetic IlvA; 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. | Phospho-2-dehydro-3-deoxyheptonate aldolase. | 0.417 |
| ilvA | bkdA2 | FLB_27520 | FLB_09300 | L-threonine dehydratase biosynthetic IlvA; 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. | 2-oxoisovalerate dehydrogenase subunit beta. | 0.845 |
| ilvA | metX | FLB_27520 | FLB_17930 | L-threonine dehydratase biosynthetic IlvA; 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. | Homoserine O-acetyltransferase; Belongs to the AB hydrolase superfamily. MetX family. | 0.949 |
| ilvA | pabC | FLB_27520 | FLB_05640 | L-threonine dehydratase biosynthetic IlvA; 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. | Aminodeoxychorismate lyase. | 0.871 |
| ilvA | thrA_1 | FLB_27520 | FLB_09230 | L-threonine dehydratase biosynthetic IlvA; 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. | Bifunctional aspartokinase/homoserine dehydrogenase 1. | 0.907 |
| ilvA | thrA_2 | FLB_27520 | FLB_17940 | L-threonine dehydratase biosynthetic IlvA; 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. | Bifunctional aspartokinase/homoserine dehydrogenase 1. | 0.949 |
| ilvA | thrB | FLB_27520 | FLB_09220 | L-threonine dehydratase biosynthetic IlvA; 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. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.720 |
| ldh | bkdA2 | FLB_01560 | FLB_09300 | Leucine dehydrogenase; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | 2-oxoisovalerate dehydrogenase subunit beta. | 0.939 |
| ldh | metX | FLB_01560 | FLB_17930 | Leucine dehydrogenase; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | Homoserine O-acetyltransferase; Belongs to the AB hydrolase superfamily. MetX family. | 0.408 |
| ldh | pabC | FLB_01560 | FLB_05640 | Leucine dehydrogenase; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | Aminodeoxychorismate lyase. | 0.894 |
| ldh | thrA_2 | FLB_01560 | FLB_17940 | Leucine dehydrogenase; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. | Bifunctional aspartokinase/homoserine dehydrogenase 1. | 0.408 |
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