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 |
| ADO46414.1 | ADO46858.1 | Entcl_0136 | Entcl_0581 | TIGRFAM: serine O-acetyltransferase; KEGG: enc:ECL_00157 serine acetyltransferase; Belongs to the transferase hexapeptide repeat family. | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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 |
| ADO46414.1 | ADO46863.1 | Entcl_0136 | Entcl_0586 | TIGRFAM: serine O-acetyltransferase; KEGG: enc:ECL_00157 serine acetyltransferase; Belongs to the transferase hexapeptide repeat family. | TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.906 |
| ADO46414.1 | ADO46919.1 | Entcl_0136 | Entcl_0642 | TIGRFAM: serine O-acetyltransferase; KEGG: enc:ECL_00157 serine acetyltransferase; Belongs to the transferase hexapeptide repeat family. | KEGG: enc:ECL_02360 cystathionine beta-synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; CBS domain containing protein; SMART: CBS domain containing protein. | 0.961 |
| ADO46414.1 | ADO47194.1 | Entcl_0136 | Entcl_0922 | TIGRFAM: serine O-acetyltransferase; KEGG: enc:ECL_00157 serine acetyltransferase; Belongs to the transferase hexapeptide repeat family. | TIGRFAM: L-serine dehydratase 1; KEGG: ent:Ent638_3250 L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.906 |
| ADO46414.1 | ADO48234.1 | Entcl_0136 | Entcl_1979 | TIGRFAM: serine O-acetyltransferase; KEGG: enc:ECL_00157 serine acetyltransferase; Belongs to the transferase hexapeptide repeat family. | TIGRFAM: L-serine dehydratase 1; KEGG: ent:Ent638_2383 L-serine ammonia-lyase; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.906 |
| ADO46414.1 | ADO49986.1 | Entcl_0136 | Entcl_3745 | TIGRFAM: serine O-acetyltransferase; KEGG: enc:ECL_00157 serine acetyltransferase; Belongs to the transferase hexapeptide repeat family. | TIGRFAM: phosphoserine phosphatase SerB; HAD-superfamily hydrolase, subfamily IB (PSPase-like); KEGG: ect:ECIAI39_4920 phosphoserine phosphatase; PFAM: Haloacid dehalogenase domain protein hydrolase. | 0.837 |
| ADO46414.1 | glyA | Entcl_0136 | Entcl_1200 | TIGRFAM: serine O-acetyltransferase; KEGG: enc:ECL_00157 serine acetyltransferase; Belongs to the transferase hexapeptide repeat family. | Glycine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.833 |
| ADO46414.1 | ilvA | Entcl_0136 | Entcl_4265 | TIGRFAM: serine O-acetyltransferase; KEGG: enc:ECL_00157 serine acetyltransferase; Belongs to the transferase hexapeptide repeat family. | 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. | 0.802 |
| ADO46414.1 | trpA | Entcl_0136 | Entcl_2527 | TIGRFAM: serine O-acetyltransferase; KEGG: enc:ECL_00157 serine acetyltransferase; Belongs to the transferase hexapeptide repeat family. | Tryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.813 |
| ADO46858.1 | ADO46414.1 | Entcl_0581 | Entcl_0136 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. | TIGRFAM: serine O-acetyltransferase; KEGG: enc:ECL_00157 serine acetyltransferase; Belongs to the transferase hexapeptide repeat family. | 0.802 |
| ADO46858.1 | ADO46863.1 | Entcl_0581 | Entcl_0586 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. | TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.935 |
| ADO46858.1 | ADO46919.1 | Entcl_0581 | Entcl_0642 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. | KEGG: enc:ECL_02360 cystathionine beta-synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; CBS domain containing protein; SMART: CBS domain containing protein. | 0.929 |
| ADO46858.1 | ADO47194.1 | Entcl_0581 | Entcl_0922 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. | TIGRFAM: L-serine dehydratase 1; KEGG: ent:Ent638_3250 L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.912 |
| ADO46858.1 | ADO48234.1 | Entcl_0581 | Entcl_1979 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. | TIGRFAM: L-serine dehydratase 1; KEGG: ent:Ent638_2383 L-serine ammonia-lyase; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.912 |
| ADO46858.1 | ADO49986.1 | Entcl_0581 | Entcl_3745 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. | TIGRFAM: phosphoserine phosphatase SerB; HAD-superfamily hydrolase, subfamily IB (PSPase-like); KEGG: ect:ECIAI39_4920 phosphoserine phosphatase; PFAM: Haloacid dehalogenase domain protein hydrolase. | 0.904 |
| ADO46858.1 | dsdA | Entcl_0581 | Entcl_0022 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. | TIGRFAM: D-serine ammonia-lyase; KEGG: enc:ECL_00023 D-serine deaminase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. | 0.906 |
| ADO46858.1 | glyA | Entcl_0581 | Entcl_1200 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. | Glycine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.910 |
| ADO46858.1 | ilvA | Entcl_0581 | Entcl_4265 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. | 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. | 0.916 |
| ADO46858.1 | trpA | Entcl_0581 | Entcl_2527 | Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. | Tryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.915 |
| ADO46863.1 | ADO46414.1 | Entcl_0586 | Entcl_0136 | TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | TIGRFAM: serine O-acetyltransferase; KEGG: enc:ECL_00157 serine acetyltransferase; Belongs to the transferase hexapeptide repeat family. | 0.906 |
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