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 | 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 | ilvC | DIP1579 | DIP1100 | 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. | Ketol-acid reductoisomerase; 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. | 0.880 |
| ilvA | ilvD | DIP1579 | DIP1096 | 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 Streptomyces coelicolor dihydroxy-acid dehydratase IlvD or SCE7.12c SW:ILVD_STRCO (O69198) (617 aa) fasta scores: E(): 1.7e-161, 67.9% id in 617 aa, and to Escherichia coli dihydroxy-acid dehydratase IlvD or B3771 SW:ILVD_ECOLI (P05791) (616 aa) fasta scores: E(): 1.4e-155, 67.37% id in 613 aa; Belongs to the IlvD/Edd family. | 0.906 |
| 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 | leuA | DIP1579 | DIP0266 | 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. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily. | 0.614 |
| 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 | leuC | DIP1579 | DIP1127 | 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 dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.469 |
| ilvA | leuD | DIP1579 | DIP1128 | 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 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. | 0.558 |
| ilvA | metE | DIP1579 | DIP2167 | 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 fragment of Mycobacterium tuberculosis 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase MetE or Rv1133c or MT1165 or MTC22G8.22 SW:METE_MYCTU (O06584) (759 aa) fasta scores: E(): 2.5e-06, 70.732% id in 41 aa, and to Streptomyces griseus subspgriseus. 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferase- like protein TR:Q9KHC5 (EMBL:AF263012) (774 aa) fasta scores: E(): 4.1e-06, 77.778% id in 36 aa, and to Saccharomyces cerevisiae 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase Met6 or YER091c SW:METE_YEAST (P05694) ( [...] | 0.814 |
| 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 | ilvC | DIP1098 | DIP1100 | 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. | Ketol-acid reductoisomerase; 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. | 0.999 |
| ilvB | ilvD | DIP1098 | DIP1096 | 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 Streptomyces coelicolor dihydroxy-acid dehydratase IlvD or SCE7.12c SW:ILVD_STRCO (O69198) (617 aa) fasta scores: E(): 1.7e-161, 67.9% id in 617 aa, and to Escherichia coli dihydroxy-acid dehydratase IlvD or B3771 SW:ILVD_ECOLI (P05791) (616 aa) fasta scores: E(): 1.4e-155, 67.37% id in 613 aa; Belongs to the IlvD/Edd family. | 0.986 |
| 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 | leuA | DIP1098 | DIP0266 | 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. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily. | 0.965 |
| 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 | leuC | DIP1098 | DIP1127 | 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 dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.612 |
| ilvB | leuD | DIP1098 | DIP1128 | 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 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. | 0.614 |
| ilvC | ilvA | DIP1100 | DIP1579 | Ketol-acid reductoisomerase; 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. | 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. | 0.880 |
page 1 of 5