ID   ARGC_CLAMS              Reviewed;         349 AA.
AC   B0RHD0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   16-JUN-2009, entry version 12.
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=CMS1231;
OS   Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / JCM
OS   9667).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=31964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18192393; DOI=10.1128/JB.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis
RT   subsp. sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(2008).
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC       subfamily.
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DR   EMBL; AM849034; CAQ01347.1; -; Genomic_DNA.
DR   RefSeq; YP_001709969.1; -.
DR   GeneID; 6158866; -.
DR   GenomeReviews; AM849034_GR; CMS1231.
DR   KEGG; cms:CMS_1231; -.
DR   OMA; B0RHD0; VCRIAVH.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase...; IEA:HAMAP.
DR   GO; GO:0051287; F:NAD or NADH 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_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_C.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 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    349       N-acetyl-gamma-glutamyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_1000076728.
FT   ACT_SITE    152    152       By similarity.
SQ   SEQUENCE   349 AA;  36005 MW;  E6574AFB15A3DB36 CRC64;
     MSFSVAVAGA SGYAGGELLR LLADHPRLEV QTLTAFQNAG ERLREVHPHL TSYADRTFVE
     TTAEQLAGHD VVFLALPHGK SGAITAELDD QTLVVDCGAD HRLVDEAAWD AFYGGDFAGA
     WPYGLPELLH AEEGGTQRTR LSGVKRIAVP GCNVTAITLG LQPGIRAGVI EPEDVVAVLA
     VGPSGAGRSL RTNLLASEIL GSASAYAVGG THRHTPEIRQ NLETAGGGHV SVSFTPVLVP
     MARGILATAT ARLAPGFSAH DVRAAWELAY ADEPFVHLLP EGTFPNVSDV TGSNTALVGL
     AIDEAAGRVV TVTAIDNLVK GTAGAAIQSA NIALGLPEAM GLPVNGVAP
//