ID   ARGC_CAMJR              Reviewed;         342 AA.
AC   Q5HWN8;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-NOV-2008, entry version 30.
DE   RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase;
DE            Short=AGPR;
DE            EC=1.2.1.38;
DE   AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase;
DE            Short=NAGSA dehydrogenase;
GN   Name=argC; OrderedLocusNames=CJE0275;
OS   Campylobacter jejuni (strain RM1221).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA   Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA   Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA   Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA   Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA   Nelson K.E.;
RT   "Major structural differences and novel potential virulence mechanisms
RT   from the genomes of multiple Campylobacter species.";
RL   PLoS Biol. 3:72-85(2005).
CC   -!- CATALYTIC ACTIVITY: N-acetyl-L-glutamate 5-semialdehyde + NADP(+)
CC       + phosphate = N-acetyl-5-glutamyl phosphate + NADPH.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 3/4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC       subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000025; AAW34867.1; -; Genomic_DNA.
DR   RefSeq; YP_178297.1; -.
DR   GeneID; 3231037; -.
DR   GenomeReviews; CP000025_GR; CJE0275.
DR   KEGG; cjr:CJE0275; -.
DR   TIGR; CJE0275; -.
DR   HOGENOM; Q5HWN8; -.
DR   BioCyc; CJEJ195099:CJE_0275-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase...; IEA:HAMAP.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_00150; -; 1.
DR   InterPro; IPR000706; AGPR_act_site.
DR   InterPro; IPR000534; Semialdehyde_DHase_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DHase_C.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   ProDom; PD003765; AGPR_act_site; 1.
DR   TIGRFAMs; TIGR01850; argC; 1.
DR   PROSITE; PS01224; ARGC; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome;
KW   Cytoplasm; NADP; Oxidoreductase.
FT   CHAIN         1    342       N-acetyl-gamma-glutamyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_0000112394.
FT   ACT_SITE    147    147       By similarity.
SQ   SEQUENCE   342 AA;  38886 MW;  80584471E19322D9 CRC64;
     MKIKVGILGA SGYAGNELVR ILLNHPKVEI SYLGSSSSVG QNYQDLYPNT PLNLCFENKN
     LDELELDLLF LATPHEFSAK LLNENLLKKM KIIDLSADFR LKNPKDYELW YKFTHPNQEL
     LQNAVYGLCE LYKEEIKKAS LVANPGCYTT CSILSLYPLF KEKIIDFSSV IIDAKSGVSG
     AGRSAKVENL FCEVNENIKA YNLALHRHTP EIEEHLSYAA KKKITLQFTP HLVSMQRGIL
     ISAYANLKED LQEQDIRDIY TKYYQNNKFI RLLPPQSLPQ TRWVKSSNFA DINFSVDQRT
     KRVIVLGAID NLIKGAAGQA VQNMNLMFDF DEDEGLKFFA NL
//