ID   ARGC_ACAM1              Reviewed;         352 AA.
AC   B0CD68;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-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=AM1_0609;
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M.,
RA   Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J.,
RA   Mimuro M., Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(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; CP000828; ABW25659.1; -; Genomic_DNA.
DR   RefSeq; YP_001514973.1; -.
DR   GeneID; 5679437; -.
DR   GenomeReviews; CP000828_GR; AM1_0609.
DR   KEGG; amr:AM1_0609; -.
DR   OMA; B0CD68; TAEDCTT.
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   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    352       N-acetyl-gamma-glutamyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_1000076725.
FT   ACT_SITE    155    155       By similarity.
SQ   SEQUENCE   352 AA;  38109 MW;  179DFEF39CA1DE3E CRC64;
     MGSQEDIPVG IIGASGYGGV QLTRLLLEHP HVHLAYLGGD SSAGRPFADL YPHLGFKQDL
     KVEAIDLDKV VERTQVVFLA LPNGLAAEMA PTLVECGCKV LDLSADYRFT NLDTYEDWYG
     TKRQDRDLAS TAVYGLPELY RQGISTASLV GCPGCFPTAS LLALAPLLKQ GLIDPNSAII
     DAKTGTSGGG RQAKTHLLLA EANGSIGPYG VAHHRHTPEI EQVSSDLAGR EVVVQFTPHL
     APMTRGILAT VYATMRDPGL VREDLITIFS AFYRNSPWVK VLPGSTYPFT KWAYGTNLCY
     LGIEVDQRTG RVIVISAIDN LMKGQAGQAV QCLNLMMGWP ETMGLPELTF YP
//