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 |
| aspC | ilvA | llmg_0171 | llmg_1276 | Aspartate aminotransferase, Transaminase A (ASPAT), Aminotransferase, class I and II; High confidence in function and specificity. | IlvA protein; 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. | 0.421 |
| aspC | ilvD | llmg_0171 | llmg_1280 | Aspartate aminotransferase, Transaminase A (ASPAT), Aminotransferase, class I and II; High confidence in function and specificity. | PF00920: Dehydratase family, TIGR00110: dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.915 |
| aspC | ilvE | llmg_0171 | llmg_1181 | Aspartate aminotransferase, Transaminase A (ASPAT), Aminotransferase, class I and II; High confidence in function and specificity. | PF01063: Aminotransferase class IV, TIGR01123: branched-chain amino acid aminotransferase; High confidence in function and specificity. | 0.910 |
| ilvA | aspC | llmg_1276 | llmg_0171 | IlvA protein; 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. | Aspartate aminotransferase, Transaminase A (ASPAT), Aminotransferase, class I and II; High confidence in function and specificity. | 0.421 |
| ilvA | ilvB | llmg_1276 | llmg_1279 | IlvA protein; 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. | Acetolactate synthase large subunit; PF02776: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain, TIGR00118: acetolactate synthase, large subunit, biosynthetic type; High confidence in function and specificity. | 0.992 |
| ilvA | ilvC | llmg_1276 | llmg_1277 | IlvA protein; 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. | IlvC protein; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.986 |
| ilvA | ilvD | llmg_1276 | llmg_1280 | IlvA protein; 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. | PF00920: Dehydratase family, TIGR00110: dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.996 |
| ilvA | ilvE | llmg_1276 | llmg_1181 | IlvA protein; 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. | PF01063: Aminotransferase class IV, TIGR01123: branched-chain amino acid aminotransferase; High confidence in function and specificity. | 0.989 |
| ilvA | ilvN | llmg_1276 | llmg_1278 | IlvA protein; 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. | IPR004789: Acetolactate synthase, small subunit, TIGR00119: acetolactate synthase, small subunit; High confidence in function and specificity. | 0.991 |
| ilvA | leuC | llmg_1276 | llmg_1284 | IlvA protein; 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. | LeuC protein; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.795 |
| ilvA | leuD | llmg_1276 | llmg_1282 | IlvA protein; 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. | 3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.925 |
| ilvA | llmg_1281 | llmg_1276 | llmg_1281 | IlvA protein; 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. | PF00005: ABC transporter; Conserved hypothetical protein. | 0.700 |
| ilvB | ilvA | llmg_1279 | llmg_1276 | Acetolactate synthase large subunit; PF02776: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain, TIGR00118: acetolactate synthase, large subunit, biosynthetic type; High confidence in function and specificity. | IlvA protein; 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. | 0.992 |
| ilvB | ilvC | llmg_1279 | llmg_1277 | Acetolactate synthase large subunit; PF02776: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain, TIGR00118: acetolactate synthase, large subunit, biosynthetic type; High confidence in function and specificity. | IlvC protein; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.998 |
| ilvB | ilvD | llmg_1279 | llmg_1280 | Acetolactate synthase large subunit; PF02776: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain, TIGR00118: acetolactate synthase, large subunit, biosynthetic type; High confidence in function and specificity. | PF00920: Dehydratase family, TIGR00110: dihydroxy-acid dehydratase; High confidence in function and specificity; Belongs to the IlvD/Edd family. | 0.997 |
| ilvB | ilvE | llmg_1279 | llmg_1181 | Acetolactate synthase large subunit; PF02776: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain, TIGR00118: acetolactate synthase, large subunit, biosynthetic type; High confidence in function and specificity. | PF01063: Aminotransferase class IV, TIGR01123: branched-chain amino acid aminotransferase; High confidence in function and specificity. | 0.695 |
| ilvB | ilvN | llmg_1279 | llmg_1278 | Acetolactate synthase large subunit; PF02776: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain, TIGR00118: acetolactate synthase, large subunit, biosynthetic type; High confidence in function and specificity. | IPR004789: Acetolactate synthase, small subunit, TIGR00119: acetolactate synthase, small subunit; High confidence in function and specificity. | 0.999 |
| ilvB | leuC | llmg_1279 | llmg_1284 | Acetolactate synthase large subunit; PF02776: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain, TIGR00118: acetolactate synthase, large subunit, biosynthetic type; High confidence in function and specificity. | LeuC protein; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.832 |
| ilvB | leuD | llmg_1279 | llmg_1282 | Acetolactate synthase large subunit; PF02776: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain, TIGR00118: acetolactate synthase, large subunit, biosynthetic type; High confidence in function and specificity. | 3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.904 |
| ilvB | llmg_1281 | llmg_1279 | llmg_1281 | Acetolactate synthase large subunit; PF02776: Thiamine pyrophosphate enzyme, N-terminal TPP binding domain, TIGR00118: acetolactate synthase, large subunit, biosynthetic type; High confidence in function and specificity. | PF00005: ABC transporter; Conserved hypothetical protein. | 0.517 |
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