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ilvA protein (Escherichia coli K12 MG1655) - STRING interaction network
"ilvA" - L-threonine dehydratase biosynthetic IlvA in Escherichia coli K12 MG1655
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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ilvAL-threonine dehydratase biosynthetic IlvA; 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 (514 aa)    
Predicted Functional Partners:
ilvD
Dihydroxy-acid dehydratase; Enzyme; Amino acid biosynthesis- Isoleucine, Valine (616 aa)
   
  0.998
ilvE
Branched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine (309 aa)
   
 
  0.997
ilvH
Acetolactate synthase III, valine sensitive, small subunit (163 aa)
 
 
  0.985
ilvB
Acetolactate synthase I,valine-sensitive, large subunit; Belongs to the TPP enzyme family (562 aa)
 
  0.984
ilvI
Acetolactate synthase III, valine sensitive, large subunit (574 aa)
 
  0.983
ilvM
Pseudogene, acetolactate synthase 2 large subunit, valine-insensitive; acetolactate synthase II, large subunit, cryptic, interrupted (87 aa)
   
 
  0.978
ilvC
Ketol-acid reductoisomerase (NADP(+)); 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. Also able to use 2- ketopantoate, 2-ketoisovalerate, 2-ketovalerate, 2-ketobutyrate, [...] (491 aa)
 
 
  0.967
thrC
Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. To a lesser extent, is able to slowly catalyze the deamination of L-threonine into alpha-ketobutyrate and that of L- serine and 3-chloroalanine into pyruvate. Is also able to rapidly convert vinylglycine to threonine, which proves that the pyridoxal p-quinonoid of vinylglycine is an intermediate in the TS reaction (428 aa)
   
 
  0.959
leuB
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 1 subfamily (363 aa)
 
 
  0.956
ltaE
Low specificity L-threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L- threonine to glycine and acetaldehyde. L-threo-phenylserine and L- erythro-phenylserine are also good substrates (333 aa)
     
 
  0.954
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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