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PROSITE documentation PDOC00941

N-acetyl-gamma-glutamyl-phosphate reductase active site





Description

N-acetyl-γ-glutamyl-phosphate reductase (EC 1.2.1.38) (AGPR) [1,2] is the enzyme that catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde.

In bacteria it is a monofunctional protein of 35 to 38 Kd (gene argC) while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase (EC 2.7.2.8) domain and a C-terminal AGPR domain.

In the Escherichia coli enzyme, a cysteine has been shown to be implicated in the catalytic activity, the region around this residue is well conserved and can be used as a signature pattern.

Last update:

April 2006 / Pattern revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

ARGC, PS01224; N-acetyl-gamma-glutamyl-phosphate reductase active site  (PATTERN)


References

1AuthorsLudovice M. Martin J.F. Carrachas P. Liras P.
TitleCharacterization of the Streptomyces clavuligerus argC gene encoding N-acetylglutamyl-phosphate reductase: expression in Streptomyces lividans and effect on clavulanic acid production.
SourceJ. Bacteriol. 174:4606-4613(1992).
PubMed ID1339424

2AuthorsGessert S.F. Kim J.H. Nargang F.E. Weiss R.L.
TitleA polyprotein precursor of two mitochondrial enzymes in Neurospora crassa. Gene structure and precursor processing.
SourceJ. Biol. Chem. 269:8189-8203(1994).
PubMed ID7907589



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