ID   ARGC_BRUSI              Reviewed;         310 AA.
AC   B0CLB5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   16-JUN-2009, entry version 13.
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=BSUIS_A0825;
OS   Brucella suis (strain ATCC 23445 / NCTC 10510).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=470137;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J.,
RA   Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S.,
RA   Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K.,
RA   Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W.,
RA   Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C.,
RA   Munk C., Brettin T.S.;
RT   "Brucella suis ATCC 23445 whole genome shotgun sequencing project.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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 2
CC       subfamily.
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DR   EMBL; CP000911; ABY37895.1; -; Genomic_DNA.
DR   RefSeq; YP_001627465.1; -.
DR   GeneID; 5837575; -.
DR   GenomeReviews; CP000911_GR; BSUIS_A0825.
DR   KEGG; bmt:BSUIS_A0825; -.
DR   OMA; B0CLB5; FRQGMLV.
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:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01110; -; 1.
DR   InterPro; IPR000706; AGPR_act_site.
DR   InterPro; IPR010136; AGPR_subtype.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   ProDom; PD003765; AGPR_act_site; 1.
DR   TIGRFAMs; TIGR01851; argC_other; 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    310       N-acetyl-gamma-glutamyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_1000084869.
FT   ACT_SITE    117    117       By similarity.
SQ   SEQUENCE   310 AA;  33813 MW;  4188DB892BC32AF5 CRC64;
     MKPKIFIDGE HGTTGLQIRT RLAERDDLEV ISIPEAERRN KDLRADYLRA ADIAILCLPD
     DASKEAVSLL EGHNSTRIID TSTAHRVHPD WAYGFAELTK GQRERIAEAR LVANPGCYPT
     GAIALVRPLR DAGLLPADYP VSVNAVSGYT GGGKQLIAQM EDRNHPDYLA ANNFLYGLPL
     KHKHVPELQL HGRLDRRPIF SPSVGRFPQG MIVQVPLFLS ELEGSPSLAK VHAVLTEHYA
     GQDIVDVVPL EESAKLPRVD AEELAGKDGM KLFVFGTEDH GQVNLVALLD NLGKGASGAA
     VQNMNLMLGK
//