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 protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ilvA | ilvB | gene:17575040 | gene:17575541 | 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 (By similarity). | Highly similar to many acetolactate synthases, large subunit, (EC 4.1.3.18) involved in valine and isoleucine biosynthesis, including: Mycobacterium avium SW:ILVB_MYCAV (Q59498) (621 aa); Fasta score E(): 0, 82.7% identity in 624 aa overlap and Mycobacterium tuberculosis RV3003C SW:ILVB_MYCTU (O53250) (618 aa); Fasta score E(): 0, 87.1% identity in 627 aa overlap. Contains Pfam match to entry PF00205 TPP_enzymes, Thiamine pyrophosphate enzymes. Contains PS00187 Thiamine pyrophosphate enzymes signature. | 0.941 |
| ilvA | ilvC | gene:17575040 | gene:17575539 | 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 (By similarity). | 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. | 0.751 |
| ilvA | ilvG | gene:17575040 | gene:17575935 | 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 (By similarity). | Acetolactate synthase II; Similar to Mycobacterium tuberculosis probable acetolactate synthase SW:ILVG_MYCTU (Q50613) fasta scores: E(): 0, 86.1% in 548 aa, and to Bacillus subtilis acetolactate synthase large subunit SW:ILVB_BACSU (P37251; P94564) fasta scores: E(): 1.2e-32, 28.5% in 543 aa. Contains Pfam match to entry PF00205 TPP_enzymes, Thiamine pyrophosphate enzymes. Contains PS00187 Thiamine pyrophosphate enzymes signature; Similar to ML1696, ML2167 and ML0354. | 0.939 |
| ilvA | ilvN | gene:17575040 | gene:17575540 | 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 (By similarity). | Highly similar to many acetolactate synthases, small subunit, (EC 4.1.3.18) involved in valine and isoleucine biosynthesis, including: Mycobacterium avium SW:ILVH_MYCAV (Q59499) (167 aa); Fasta score E(): 0, 78.9% identity in 166 aa overlap and Mycobacterium tuberculosis RV3002C SW:ILVH_MYCTU (O53249) (168 aa); Fasta score E(): 0, 83.5% identity in 164 aa overlap. Contains Pfam match to entry PF01842 ACT, ACT domain. | 0.980 |
| ilvA | ilvX | gene:17575040 | gene:17574173 | 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 (By similarity). | Similar to M. tuberculosis ilvX, putative acetohydroxyacid synthase I large subunit, TR:O53554 (EMBL:AL123456) (515 aa); Fasta score E(): 0, 82.9% identity in 515 aa overlap. Similar to Escherichia coli ilvI, acetolactate synthase isozyme III large subunit, SW:ILVI_ECOLI (P00893) (574 aa); Fasta score E(): 1.8e-07, 23.7% identity in 540 aa overlap. Also similar to Pseudomonas putida mdlC, benzoylformate decarboxylase, SW:MDLC_PSEPU (P20906) (528 aa); Fasta score E(): 6.6e-13, 29.3% identity in 529 aa overlap. Previously sequenced as TR:Q49865 (EMBL:U00020) (515 aa); Fasta score E(): 0, [...] | 0.941 |
| ilvA | leuA | gene:17575040 | gene:17576185 | 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 (By similarity). | 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. | 0.519 |
| ilvA | leuB | gene:17575040 | gene:17575536 | 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 (By similarity). | 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 (By similarity); Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.944 |
| ilvA | leuD | gene:17575040 | gene:17575527 | 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 (By similarity). | 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. | 0.430 |
| ilvB | ilvA | gene:17575541 | gene:17575040 | Highly similar to many acetolactate synthases, large subunit, (EC 4.1.3.18) involved in valine and isoleucine biosynthesis, including: Mycobacterium avium SW:ILVB_MYCAV (Q59498) (621 aa); Fasta score E(): 0, 82.7% identity in 624 aa overlap and Mycobacterium tuberculosis RV3003C SW:ILVB_MYCTU (O53250) (618 aa); Fasta score E(): 0, 87.1% identity in 627 aa overlap. Contains Pfam match to entry PF00205 TPP_enzymes, Thiamine pyrophosphate enzymes. Contains PS00187 Thiamine pyrophosphate enzymes signature. | 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 (By similarity). | 0.941 |
| ilvB | ilvC | gene:17575541 | gene:17575539 | Highly similar to many acetolactate synthases, large subunit, (EC 4.1.3.18) involved in valine and isoleucine biosynthesis, including: Mycobacterium avium SW:ILVB_MYCAV (Q59498) (621 aa); Fasta score E(): 0, 82.7% identity in 624 aa overlap and Mycobacterium tuberculosis RV3003C SW:ILVB_MYCTU (O53250) (618 aa); Fasta score E(): 0, 87.1% identity in 627 aa overlap. Contains Pfam match to entry PF00205 TPP_enzymes, Thiamine pyrophosphate enzymes. Contains PS00187 Thiamine pyrophosphate enzymes signature. | 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. | 0.995 |
| ilvB | ilvG | gene:17575541 | gene:17575935 | Highly similar to many acetolactate synthases, large subunit, (EC 4.1.3.18) involved in valine and isoleucine biosynthesis, including: Mycobacterium avium SW:ILVB_MYCAV (Q59498) (621 aa); Fasta score E(): 0, 82.7% identity in 624 aa overlap and Mycobacterium tuberculosis RV3003C SW:ILVB_MYCTU (O53250) (618 aa); Fasta score E(): 0, 87.1% identity in 627 aa overlap. Contains Pfam match to entry PF00205 TPP_enzymes, Thiamine pyrophosphate enzymes. Contains PS00187 Thiamine pyrophosphate enzymes signature. | Acetolactate synthase II; Similar to Mycobacterium tuberculosis probable acetolactate synthase SW:ILVG_MYCTU (Q50613) fasta scores: E(): 0, 86.1% in 548 aa, and to Bacillus subtilis acetolactate synthase large subunit SW:ILVB_BACSU (P37251; P94564) fasta scores: E(): 1.2e-32, 28.5% in 543 aa. Contains Pfam match to entry PF00205 TPP_enzymes, Thiamine pyrophosphate enzymes. Contains PS00187 Thiamine pyrophosphate enzymes signature; Similar to ML1696, ML2167 and ML0354. | 0.930 |
| ilvB | ilvN | gene:17575541 | gene:17575540 | Highly similar to many acetolactate synthases, large subunit, (EC 4.1.3.18) involved in valine and isoleucine biosynthesis, including: Mycobacterium avium SW:ILVB_MYCAV (Q59498) (621 aa); Fasta score E(): 0, 82.7% identity in 624 aa overlap and Mycobacterium tuberculosis RV3003C SW:ILVB_MYCTU (O53250) (618 aa); Fasta score E(): 0, 87.1% identity in 627 aa overlap. Contains Pfam match to entry PF00205 TPP_enzymes, Thiamine pyrophosphate enzymes. Contains PS00187 Thiamine pyrophosphate enzymes signature. | Highly similar to many acetolactate synthases, small subunit, (EC 4.1.3.18) involved in valine and isoleucine biosynthesis, including: Mycobacterium avium SW:ILVH_MYCAV (Q59499) (167 aa); Fasta score E(): 0, 78.9% identity in 166 aa overlap and Mycobacterium tuberculosis RV3002C SW:ILVH_MYCTU (O53249) (168 aa); Fasta score E(): 0, 83.5% identity in 164 aa overlap. Contains Pfam match to entry PF01842 ACT, ACT domain. | 0.999 |
| ilvB | ilvX | gene:17575541 | gene:17574173 | Highly similar to many acetolactate synthases, large subunit, (EC 4.1.3.18) involved in valine and isoleucine biosynthesis, including: Mycobacterium avium SW:ILVB_MYCAV (Q59498) (621 aa); Fasta score E(): 0, 82.7% identity in 624 aa overlap and Mycobacterium tuberculosis RV3003C SW:ILVB_MYCTU (O53250) (618 aa); Fasta score E(): 0, 87.1% identity in 627 aa overlap. Contains Pfam match to entry PF00205 TPP_enzymes, Thiamine pyrophosphate enzymes. Contains PS00187 Thiamine pyrophosphate enzymes signature. | Similar to M. tuberculosis ilvX, putative acetohydroxyacid synthase I large subunit, TR:O53554 (EMBL:AL123456) (515 aa); Fasta score E(): 0, 82.9% identity in 515 aa overlap. Similar to Escherichia coli ilvI, acetolactate synthase isozyme III large subunit, SW:ILVI_ECOLI (P00893) (574 aa); Fasta score E(): 1.8e-07, 23.7% identity in 540 aa overlap. Also similar to Pseudomonas putida mdlC, benzoylformate decarboxylase, SW:MDLC_PSEPU (P20906) (528 aa); Fasta score E(): 6.6e-13, 29.3% identity in 529 aa overlap. Previously sequenced as TR:Q49865 (EMBL:U00020) (515 aa); Fasta score E(): 0, [...] | 0.914 |
| ilvB | leuA | gene:17575541 | gene:17576185 | Highly similar to many acetolactate synthases, large subunit, (EC 4.1.3.18) involved in valine and isoleucine biosynthesis, including: Mycobacterium avium SW:ILVB_MYCAV (Q59498) (621 aa); Fasta score E(): 0, 82.7% identity in 624 aa overlap and Mycobacterium tuberculosis RV3003C SW:ILVB_MYCTU (O53250) (618 aa); Fasta score E(): 0, 87.1% identity in 627 aa overlap. Contains Pfam match to entry PF00205 TPP_enzymes, Thiamine pyrophosphate enzymes. Contains PS00187 Thiamine pyrophosphate enzymes signature. | 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. | 0.979 |
| ilvB | leuB | gene:17575541 | gene:17575536 | Highly similar to many acetolactate synthases, large subunit, (EC 4.1.3.18) involved in valine and isoleucine biosynthesis, including: Mycobacterium avium SW:ILVB_MYCAV (Q59498) (621 aa); Fasta score E(): 0, 82.7% identity in 624 aa overlap and Mycobacterium tuberculosis RV3003C SW:ILVB_MYCTU (O53250) (618 aa); Fasta score E(): 0, 87.1% identity in 627 aa overlap. Contains Pfam match to entry PF00205 TPP_enzymes, Thiamine pyrophosphate enzymes. Contains PS00187 Thiamine pyrophosphate enzymes signature. | 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 (By similarity); Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.955 |
| ilvB | leuC | gene:17575541 | gene:17575528 | Highly similar to many acetolactate synthases, large subunit, (EC 4.1.3.18) involved in valine and isoleucine biosynthesis, including: Mycobacterium avium SW:ILVB_MYCAV (Q59498) (621 aa); Fasta score E(): 0, 82.7% identity in 624 aa overlap and Mycobacterium tuberculosis RV3003C SW:ILVB_MYCTU (O53250) (618 aa); Fasta score E(): 0, 87.1% identity in 627 aa overlap. Contains Pfam match to entry PF00205 TPP_enzymes, Thiamine pyrophosphate enzymes. Contains PS00187 Thiamine pyrophosphate enzymes signature. | 3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.426 |
| ilvB | leuD | gene:17575541 | gene:17575527 | Highly similar to many acetolactate synthases, large subunit, (EC 4.1.3.18) involved in valine and isoleucine biosynthesis, including: Mycobacterium avium SW:ILVB_MYCAV (Q59498) (621 aa); Fasta score E(): 0, 82.7% identity in 624 aa overlap and Mycobacterium tuberculosis RV3003C SW:ILVB_MYCTU (O53250) (618 aa); Fasta score E(): 0, 87.1% identity in 627 aa overlap. Contains Pfam match to entry PF00205 TPP_enzymes, Thiamine pyrophosphate enzymes. Contains PS00187 Thiamine pyrophosphate enzymes signature. | 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. | 0.485 |
| ilvC | ilvA | gene:17575539 | gene:17575040 | 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 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 (By similarity). | 0.751 |
| ilvC | ilvB | gene:17575539 | gene:17575541 | 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. | Highly similar to many acetolactate synthases, large subunit, (EC 4.1.3.18) involved in valine and isoleucine biosynthesis, including: Mycobacterium avium SW:ILVB_MYCAV (Q59498) (621 aa); Fasta score E(): 0, 82.7% identity in 624 aa overlap and Mycobacterium tuberculosis RV3003C SW:ILVB_MYCTU (O53250) (618 aa); Fasta score E(): 0, 87.1% identity in 627 aa overlap. Contains Pfam match to entry PF00205 TPP_enzymes, Thiamine pyrophosphate enzymes. Contains PS00187 Thiamine pyrophosphate enzymes signature. | 0.995 |
| ilvC | ilvG | gene:17575539 | gene:17575935 | 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. | Acetolactate synthase II; Similar to Mycobacterium tuberculosis probable acetolactate synthase SW:ILVG_MYCTU (Q50613) fasta scores: E(): 0, 86.1% in 548 aa, and to Bacillus subtilis acetolactate synthase large subunit SW:ILVB_BACSU (P37251; P94564) fasta scores: E(): 1.2e-32, 28.5% in 543 aa. Contains Pfam match to entry PF00205 TPP_enzymes, Thiamine pyrophosphate enzymes. Contains PS00187 Thiamine pyrophosphate enzymes signature; Similar to ML1696, ML2167 and ML0354. | 0.971 |
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