GenePage for the ilvA gene of Escherichia coli K-12

Primary Gene Name: ilvA
EcoGene Accession Number: EG10493
K-12 Gene Accession Number: ECK3764
MG1655 Gene Identifier: b3772
Gene Name Mnemonic: Isoleucine-valine (requirement)
Alternate Gene Symbols: None
Description: L-threonine dehydratase, biosynthetic, PLP-dependent; also known as threonine deaminase; tetrameric
  # bp Upstream # bp Downstream
MW: 56195.25 ---------514 aa Pre-Run BlastP UniProt
Pre-Run BlastP NR+Env
Left End: 3955331
Left Intergenic Region

Name: ilvD_ilvA

Length: 2 bp gap

Orientation: Codirectional+

Left_end: 3955329

Right_end: 3955330

Centisome: 85.21

Genomic Address
Clockwise
Minute or Centisome (%) = 85.21
Right End: 3956875
Right Intergenic Region

Name: ilvA_ilvY

Length: 51 bp gap

Orientation: Convergent

Left_end: 3956876

Right_end: 3956926

Centisome: 85.25

Isoleucine allosterically inhibits and valine allosterically activates IlvA, the first demonstration of end product inhibition for any enzyme (Umbarger, 1956). The activity and allosteric regulation of IlvA have been studied using purified enzymes in vitro (Grimminger, 1973; Calhoun, 1973; Koerner, 1975; Eisenstein, 1991; Eisenstein, 1994; Eisenstein, 1995; Chen, 2013). The Salmonella RidA(YjgF) is an enamine and imine deaminase required for the removal of the two unstable, toxic, tautomeric reactive intermediates, aminocrotonate and iminobutyrate, which are produced during the IlvA-mediated, PLP-dependent threonine dehydratase reaction; producing 2-ketobutyrate and releasing ammonia in a hydrolysis reaction that may require catalysis, due either to the low water environment or immediate toxicity in the cell; IlvA also dehydrates serine to yield pyruvate via analogous enamine/imine intermediates, also removed by RidA (Lambrecht, 2012). The N-terminal sequence of cloned and overproduced IlvA shows that the fMet is clipped, but the natural ilvA RBS was not used so it is not Verified, but the ATG start is reliable based on comparisons to Salmonella; 95% of the purified enzyme had its N-terminus blocked (Eisenstein, 1991). IlvA has two tandem C-terminal ACT-like regulatory domains (PF00585) required for maximal activity (Grant, 2006; Yu, 2014).

Go to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePage

BamHI EcoRI HindIII