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 |
| glyA | ilvA | DIP0932 | DIP1579 | Serine 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. | 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. | 0.959 |
| glyA | sdaA | DIP0932 | DIP0490 | Serine 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. | L-serine dehydratase 1; Similar to Escherichia coli L-serine dehydratase 1 SdaA or B1814 SW:SDHL_ECOLI (P16095) (454 aa) fasta scores: E(): 4.8e-113, 63.08% id in 447 aa; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.959 |
| glyA | sdaB | DIP0932 | DIP1359 | Serine 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. | L-serine dehydratase; Similar to Pseudomonas aeruginosa L-serine dehydratase SdaB or PA5379 SWALL:Q9HTI5 (EMBL:AE004950) (458 aa) fasta scores: E(): 3.5e-84, 53.99% id in 463 aa, and to Escherichia coli L-serine dehydratase 1 SdaA or B1814 SWALL:SDHL_ECOLI (SWALL:P16095) (454 aa) fasta scores: E(): 3e-70, 49.24% id in 461 aa; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.956 |
| glyA | trpB1 | DIP0932 | DIP2351 | Serine 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. | Tryptophan synthase beta chain TrpB1; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.907 |
| glyA | trpB2 | DIP0932 | DIP2360 | Serine 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. | Tryptophan synthase beta chain TrpB2; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.907 |
| ilvA | glyA | DIP1579 | DIP0932 | 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. | Serine 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. | 0.959 |
| ilvA | ilvB | DIP1579 | DIP1098 | 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. | Similar to Corynebacterium glutamicum acetolactate synthase large subunit IlvB SW:ILVB_CORGL (P42463) (626 aa) fasta scores: E(): 4.3e-181, 75.32% id in 620 aa, and to Mycobacterium tuberculosis acetolactate synthase IlvB or Rv3003c or MT3083 or MTV012.17c SW:ILVB_MYCTU (O53250) (618 aa) fasta scores: E(): 1.6e-152, 64.94% id in 599 aa. | 0.991 |
| ilvA | ilvE | DIP1579 | DIP1636 | 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. | Similar to Mycobacterium tuberculosis probable branched-chain amino acid aminotransferase IlvE or Rv2210c or MT2266 or MTCY190.21c SW:ILVE_MYCTU (Q10399) (368 aa) fasta scores: E(): 4.3e-93, 62.53% id in 363 aa, and to Bacillus subtilis putative branched-chain amino acid aminotransferase YwaA or Ipa-0R SW:ILVE_BACSU (P39576) (362 aa) fasta scores: E(): 1.1e-60, 44.62% id in 363 aa. | 0.975 |
| ilvA | ilvH | DIP1579 | DIP1099 | 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. | Similar to Mycobacterium tuberculosis acetolactate synthase small subunit IlvH or IlvN or Rv3002c or MT3082 or MTV012.16c SW:ILVH_MYCTU (O53249) (168 aa) fasta scores: E(): 1.3e-28, 54.77% id in 157 aa, and to Corynebacterium glutamicum (Brevibacterium flavum) acetohydroxy acid synthase, small subunit IlvN or LivS TR:Q57091 (EMBL:L09232) (172 aa) fasta scores: E(): 5.4e-47, 81.06% id in 169 aa. | 0.985 |
| ilvA | leuB | DIP1579 | DIP1105 | 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. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.955 |
| ilvA | sdaA | DIP1579 | DIP0490 | 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-serine dehydratase 1; Similar to Escherichia coli L-serine dehydratase 1 SdaA or B1814 SW:SDHL_ECOLI (P16095) (454 aa) fasta scores: E(): 4.8e-113, 63.08% id in 447 aa; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.952 |
| ilvA | sdaB | DIP1579 | DIP1359 | 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-serine dehydratase; Similar to Pseudomonas aeruginosa L-serine dehydratase SdaB or PA5379 SWALL:Q9HTI5 (EMBL:AE004950) (458 aa) fasta scores: E(): 3.5e-84, 53.99% id in 463 aa, and to Escherichia coli L-serine dehydratase 1 SdaA or B1814 SWALL:SDHL_ECOLI (SWALL:P16095) (454 aa) fasta scores: E(): 3e-70, 49.24% id in 461 aa; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.928 |
| ilvA | thrC | DIP1579 | DIP1666 | 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. | Threonine synthase; Similar to Corynebacterium glutamicum threonine synthase ThrC SW:THRC_CORGL (P23669) (481 aa) fasta scores: E(): 7.1e-155, 79.07% id in 478 aa. | 0.980 |
| ilvA | trpB1 | DIP1579 | DIP2351 | 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. | Tryptophan synthase beta chain TrpB1; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.935 |
| ilvA | trpB2 | DIP1579 | DIP2360 | 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. | Tryptophan synthase beta chain TrpB2; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.947 |
| ilvB | ilvA | DIP1098 | DIP1579 | Similar to Corynebacterium glutamicum acetolactate synthase large subunit IlvB SW:ILVB_CORGL (P42463) (626 aa) fasta scores: E(): 4.3e-181, 75.32% id in 620 aa, and to Mycobacterium tuberculosis acetolactate synthase IlvB or Rv3003c or MT3083 or MTV012.17c SW:ILVB_MYCTU (O53250) (618 aa) fasta scores: E(): 1.6e-152, 64.94% id in 599 aa. | 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. | 0.991 |
| ilvB | ilvE | DIP1098 | DIP1636 | Similar to Corynebacterium glutamicum acetolactate synthase large subunit IlvB SW:ILVB_CORGL (P42463) (626 aa) fasta scores: E(): 4.3e-181, 75.32% id in 620 aa, and to Mycobacterium tuberculosis acetolactate synthase IlvB or Rv3003c or MT3083 or MTV012.17c SW:ILVB_MYCTU (O53250) (618 aa) fasta scores: E(): 1.6e-152, 64.94% id in 599 aa. | Similar to Mycobacterium tuberculosis probable branched-chain amino acid aminotransferase IlvE or Rv2210c or MT2266 or MTCY190.21c SW:ILVE_MYCTU (Q10399) (368 aa) fasta scores: E(): 4.3e-93, 62.53% id in 363 aa, and to Bacillus subtilis putative branched-chain amino acid aminotransferase YwaA or Ipa-0R SW:ILVE_BACSU (P39576) (362 aa) fasta scores: E(): 1.1e-60, 44.62% id in 363 aa. | 0.663 |
| ilvB | ilvH | DIP1098 | DIP1099 | Similar to Corynebacterium glutamicum acetolactate synthase large subunit IlvB SW:ILVB_CORGL (P42463) (626 aa) fasta scores: E(): 4.3e-181, 75.32% id in 620 aa, and to Mycobacterium tuberculosis acetolactate synthase IlvB or Rv3003c or MT3083 or MTV012.17c SW:ILVB_MYCTU (O53250) (618 aa) fasta scores: E(): 1.6e-152, 64.94% id in 599 aa. | Similar to Mycobacterium tuberculosis acetolactate synthase small subunit IlvH or IlvN or Rv3002c or MT3082 or MTV012.16c SW:ILVH_MYCTU (O53249) (168 aa) fasta scores: E(): 1.3e-28, 54.77% id in 157 aa, and to Corynebacterium glutamicum (Brevibacterium flavum) acetohydroxy acid synthase, small subunit IlvN or LivS TR:Q57091 (EMBL:L09232) (172 aa) fasta scores: E(): 5.4e-47, 81.06% id in 169 aa. | 0.999 |
| ilvB | leuB | DIP1098 | DIP1105 | Similar to Corynebacterium glutamicum acetolactate synthase large subunit IlvB SW:ILVB_CORGL (P42463) (626 aa) fasta scores: E(): 4.3e-181, 75.32% id in 620 aa, and to Mycobacterium tuberculosis acetolactate synthase IlvB or Rv3003c or MT3083 or MTV012.17c SW:ILVB_MYCTU (O53250) (618 aa) fasta scores: E(): 1.6e-152, 64.94% id in 599 aa. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.979 |
| ilvB | trpB1 | DIP1098 | DIP2351 | Similar to Corynebacterium glutamicum acetolactate synthase large subunit IlvB SW:ILVB_CORGL (P42463) (626 aa) fasta scores: E(): 4.3e-181, 75.32% id in 620 aa, and to Mycobacterium tuberculosis acetolactate synthase IlvB or Rv3003c or MT3083 or MTV012.17c SW:ILVB_MYCTU (O53250) (618 aa) fasta scores: E(): 1.6e-152, 64.94% id in 599 aa. | Tryptophan synthase beta chain TrpB1; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.434 |
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