ID   ARGC_BACHK              Reviewed;         345 AA.
AC   Q6HE28;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 40.
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=BT9727_3879;
OS   Bacillus thuringiensis subsp. konkukian.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=180856;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G.,
RA   Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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.
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DR   EMBL; AE017355; AAT60755.1; -; Genomic_DNA.
DR   RefSeq; YP_038198.1; -.
DR   GeneID; 2854844; -.
DR   GenomeReviews; AE017355_GR; BT9727_3879.
DR   KEGG; btk:BT9727_3879; -.
DR   NMPDR; fig|281309.1.peg.3838; -.
DR   HOGENOM; Q6HE28; -.
DR   OMA; Q6HE28; VCRIAVH.
DR   BioCyc; BTHU281309:BT9727_3879-MON; -.
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    345       N-acetyl-gamma-glutamyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_0000112381.
FT   ACT_SITE    149    149       By similarity.
SQ   SEQUENCE   345 AA;  38681 MW;  C33972A0CCD4E510 CRC64;
     MKVAIIGATG YGGIELIRLL EQHPYFSIAS LHSFSQVGEC ITNVYPHFQN VLVHTLQEID
     VEEIEKEAEI VFLATPAGVS AELTPKLLAV GLKVIDLSGD FRMKDPFIYE KWYKRVAAKE
     GVLREAVYGL SEWKRYEIQK ANLIANPGCF ATAALLAVLP LVRSGIIEED SIIIDAKSGV
     SGAGKTPTTM THFPELYDNL RIYKVNEHQH VPEIEQMLTE WNRETKPITF STHLIPISRG
     IMVTLYAKVK REMEIEQLQQ LYEKAYEQSA FVRIRMQGEF PSPKEVRGSN YCDMGIAYDE
     RTGRVTVVSV IDNMMKGAAG QAIQNANIVA GLEETTGLQH MPLYL
//