{PDOC00941}
{PS01224; ARGC}
{BEGIN}
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* N-acetyl-gamma-glutamyl-phosphate reductase active site *
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N-acetyl-gamma-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.

-Consensus pattern: [LIVMA]-[GSA]-x-[PA]-G-C-[FYN]-[AVPST]-T-[GSACVT]-x(3)-
                    [GTACLPS]-[LIVMCAF]-x-[PL]
                    [C is the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2006 / Pattern revised.

[ 1] Ludovice M., Martin J.F., Carrachas P., Liras P.
     "Characterization of the Streptomyces clavuligerus argC gene encoding
     N-acetylglutamyl-phosphate reductase: expression in Streptomyces
     lividans and effect on clavulanic acid production."
     J. Bacteriol. 174:4606-4613(1992).
     PubMed=1339424
[ 2] Gessert S.F., Kim J.H., Nargang F.E., Weiss R.L.
     "A polyprotein precursor of two mitochondrial enzymes in Neurospora
     crassa. Gene structure and precursor processing."
     J. Biol. Chem. 269:8189-8203(1994).
     PubMed=7907589

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