PROSITE documentation PDOC00941N-acetyl-gamma-glutamyl-phosphate reductase active site
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.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Ludovice M. Martin J.F. Carrachas P. Liras P. |
| Title | Characterization of the Streptomyces clavuligerus argC gene encoding N-acetylglutamyl-phosphate reductase: expression in Streptomyces lividans and effect on clavulanic acid production. | |
| Source | J. Bacteriol. 174:4606-4613(1992). | |
| PubMed ID | 1339424 |
| 2 | Authors | Gessert S.F. Kim J.H. Nargang F.E. Weiss R.L. |
| Title | A polyprotein precursor of two mitochondrial enzymes in Neurospora crassa. Gene structure and precursor processing. | |
| Source | J. Biol. Chem. 269:8189-8203(1994). | |
| PubMed ID | 7907589 |
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