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 |
| ilvA-I | ilvA-II | PP_3446 | PP_5149 | Threonine deaminase; 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 deaminase; 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. | 0.901 |
| ilvA-I | serB | PP_3446 | PP_4909 | Threonine deaminase; 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. | Phosphoserine phosphatase; Function experimentally demonstrated in the studied genus; enzyme; Aminoacidbiosynthesis : Serine family. | 0.909 |
| ilvA-I | trpA | PP_3446 | PP_0082 | Threonine deaminase; 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 chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.920 |
| ilvA-I | trpB | PP_3446 | PP_0083 | Threonine deaminase; 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 beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.936 |
| ilvA-II | ilvA-I | PP_5149 | PP_3446 | Threonine deaminase; 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 deaminase; 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. | 0.901 |
| ilvA-II | serB | PP_5149 | PP_4909 | Threonine deaminase; 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. | Phosphoserine phosphatase; Function experimentally demonstrated in the studied genus; enzyme; Aminoacidbiosynthesis : Serine family. | 0.909 |
| ilvA-II | trpA | PP_5149 | PP_0082 | Threonine deaminase; 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 chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.920 |
| ilvA-II | trpB | PP_5149 | PP_0083 | Threonine deaminase; 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 beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.936 |
| pabA | pabB | PP_0420 | PP_2329 | Aminodeoxychorismate synthase / para-aminobenzoate synthase multi-enzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. | Aminodeoxychorismate synthase / para-aminobenzoate synthase multi-enzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. | 0.999 |
| pabA | trpA | PP_0420 | PP_0082 | Aminodeoxychorismate synthase / para-aminobenzoate synthase multi-enzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. | Tryptophan synthase alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.987 |
| pabA | trpB | PP_0420 | PP_0083 | Aminodeoxychorismate synthase / para-aminobenzoate synthase multi-enzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. | Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.987 |
| pabA | trpC | PP_0420 | PP_0422 | Aminodeoxychorismate synthase / para-aminobenzoate synthase multi-enzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. | Indole-3-glycerol phosphate synthase; Belongs to the TrpC family. | 0.999 |
| pabA | trpD | PP_0420 | PP_0421 | Aminodeoxychorismate synthase / para-aminobenzoate synthase multi-enzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. | Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). | 0.999 |
| pabA | trpE | PP_0420 | PP_0417 | Aminodeoxychorismate synthase / para-aminobenzoate synthase multi-enzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. | Anthranilate synthase component 1; Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentr [...] | 0.999 |
| pabA | trpF | PP_0420 | PP_1995 | Aminodeoxychorismate synthase / para-aminobenzoate synthase multi-enzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. | N-(5'-phosphoribosyl)anthranilate isomerase; Belongs to the TrpF family. | 0.998 |
| pabB | pabA | PP_2329 | PP_0420 | Aminodeoxychorismate synthase / para-aminobenzoate synthase multi-enzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. | Aminodeoxychorismate synthase / para-aminobenzoate synthase multi-enzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. | 0.999 |
| pabB | trpA | PP_2329 | PP_0082 | Aminodeoxychorismate synthase / para-aminobenzoate synthase multi-enzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. | Tryptophan synthase alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.939 |
| pabB | trpB | PP_2329 | PP_0083 | Aminodeoxychorismate synthase / para-aminobenzoate synthase multi-enzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. | Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.948 |
| pabB | trpC | PP_2329 | PP_0422 | Aminodeoxychorismate synthase / para-aminobenzoate synthase multi-enzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. | Indole-3-glycerol phosphate synthase; Belongs to the TrpC family. | 0.985 |
| pabB | trpD | PP_2329 | PP_0421 | Aminodeoxychorismate synthase / para-aminobenzoate synthase multi-enzyme complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Biosynthesisofcofactors,prostheticgroups,andcarriers : Folic acid. | Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). | 0.979 |
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