ID   ARGC_BACST              Reviewed;         345 AA.
AC   Q07906;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   16-JUN-2009, entry version 69.
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;
OS   Bacillus stearothermophilus (Geobacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-84, AND TRANSCRIPTIONAL
RP   REGULATION.
RC   STRAIN=NCIB 8224 / CCM 2186;
RX   PubMed=8804405; DOI=10.1007/s004389670008;
RA   Savchenko A., Charlier D.R.M., Dion M., Weigel P., Hallet J.-N.,
RA   Holtham C., Baumberg S., Glansdorff N., Sakanyan V.;
RT   "The arginine operon of Bacillus stearothermophilus: characterization
RT   of the control region and its interaction with the heterologous B.
RT   subtilis arginine repressor.";
RL   Mol. Gen. Genet. 252:69-78(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-345.
RC   STRAIN=NCIB 8224 / CCM 2186;
RX   MEDLINE=93232760; PubMed=8473852;
RA   Sakanyan V., Charlier D.R.M., Legrain C., Kochikyan A., Mett I.,
RA   Pierard P., Glansdorff N.;
RT   "Primary structure, partial purification and regulation of key enzymes
RT   of the acetyl cycle of arginine biosynthesis in Bacillus
RT   stearothermophilus: dual function of ornithine acetyltransferase.";
RL   J. Gen. Microbiol. 139:393-402(1993).
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   -!- INDUCTION: Expression of the argCJBD operon is regulated by argR.
CC       This binding is arginine dependent.
CC   -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC       subfamily.
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DR   EMBL; L06036; AAA22196.1; -; Genomic_DNA.
DR   PIR; S72490; S72490.
DR   BRENDA; 1.2.1.38; 266715.
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   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    345       N-acetyl-gamma-glutamyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_0000112384.
FT   ACT_SITE    149    149       By similarity.
SQ   SEQUENCE   345 AA;  37455 MW;  F488A7108E602FDD CRC64;
     MMNVAIIGAT GYSGAELFRL LYGHPHVSQC DVFSSSQDGI HLSESFPHVG AVDGAVLHKL
     EIEALAKYDA VFFATPPGVS GEWAPALVDR GVKVIDLSGD FRLKDGAVYA QWYGREAAPS
     AYLERAVYGL TEWNREAVRG AVLLSNPGCY PTATLLGLAP LVKEGLIKED SIIVDAKSGV
     SGAGRKAGLG THFSEVNENV KIYKVNAHQH IPEIEQALQT WNEAVAPITF STHLIPMTRG
     IMATIYAKAK QSISPNDLVD LYKTSYEGSP FVRIRQLGQF PATKDVYGSN YCDIGLAYDE
     RTERVTVVSV IDNLMKGAAG QAVQNFNLMM GWDEAEGLRS LPIYP
//