ID   ARGC_CLONN              Reviewed;         345 AA.
AC   A0Q1F0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-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=NT01CX_2379;
OS   Clostridium novyi (strain NT).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A.,
RA   Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W.,
RA   Vogelstein B., Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium
RT   novyi-NT.";
RL   Nat. Biotechnol. 24:1573-1580(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; CP000382; ABK61967.1; -; Genomic_DNA.
DR   RefSeq; YP_878452.1; -.
DR   GeneID; 4540066; -.
DR   GenomeReviews; CP000382_GR; NT01CX_2379.
DR   KEGG; cno:NT01CX_2379; -.
DR   OMA; A0Q1F0; 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; FALSE_NEG.
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_1000010989.
FT   ACT_SITE    151    151       By similarity.
SQ   SEQUENCE   345 AA;  39158 MW;  C342029CEDF443DD CRC64;
     MIKVGIIGST GYIGQQLVWL LKIHPNVEIV FLSSYNYAGY SFNSVYNNYK GFVETTCINI
     KEVKTRLKDV DIVFMALPHG KSFEMVKYSL NLGIKVIDLS GDFRLKDSKE YEKWYKIEHP
     LKEVLKYSVY GLPELFRKDI KKASLICNPG CYATASILAL APLIKLDLVE KGSIIVDAKS
     GVSGAGRALK TQSLYCECNE TMKAYGIGNH RHTPEIEQEL SRFCKEDIKL TFTPHLVPIN
     RGIFATCYAT LKKDLNKVQL EEAYEKFYEN DYFIKVMKEL VEVKWIKNSN FCNMNVNIDE
     RTNKVIVSSV IDNLMKGAAS QAVQNMNILF GIDEKTGLNI PSMMI
//