ID   ARGC_ARTAT              Reviewed;         343 AA.
AC   A1R585;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=AAur_1631;
OS   Arthrobacter aurescens (strain TC1).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=290340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA   Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA   Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA   Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT   "Secrets of soil survival revealed by the genome sequence of
RT   Arthrobacter aurescens TC1.";
RL   PLoS Genet. 2:2094-2106(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; CP000474; ABM10170.1; -; Genomic_DNA.
DR   RefSeq; YP_947397.1; -.
DR   GeneID; 4641044; -.
DR   GenomeReviews; CP000474_GR; AAur_1631.
DR   KEGG; aau:AAur_1631; -.
DR   TIGR; AAur_1631; -.
DR   OMA; A1R585; 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   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    343       N-acetyl-gamma-glutamyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_1000010974.
FT   ACT_SITE    146    146       By similarity.
SQ   SEQUENCE   343 AA;  35120 MW;  9A5BA263C290E354 CRC64;
     MTISVAVSGA SGYAGGEVLR LLAGHPNVTI GAITAHSNAG SRLGELQPHL HGLASRILED
     TTVENLSGHD VVFLALPHGA SAEIAAQLPE GTVVIDAGAD HRLQDAAAWE RFYGSAHAGT
     WPYGLPELPG QREALKGATR IAVPGCYPTS ALLALTPGFA NNLLLTDDVV IVSASGTSGA
     GKAAKVNLIG AEVMGSMSPY GVGGGHRHTP EIEQGLSNAA GEPVTVSFTP TLVPMSRGIL
     TTATAKVGHG VSYAELRQAW ADAYDDEPFV HLLPEGQWPT TKSVQGSNHA VMQLAFDAHT
     GRVIVTCAID NLTKGTAGGA VQSMNIALGL DETAGLNLQG VAP
//