ID   ARGC_BACA2              Reviewed;         345 AA.
AC   A7Z3A7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 14.
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=RBAM_011190;
OS   Bacillus amyloliquefaciens (strain FZB42).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant
RT   growth-promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS73483.1; -; Genomic_DNA.
DR   RefSeq; YP_001420714.1; -.
DR   GeneID; 5462905; -.
DR   GenomeReviews; CP000560_GR; RBAM_011190.
DR   KEGG; bay:RBAM_011190; -.
DR   OMA; A7Z3A7; 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    345       N-acetyl-gamma-glutamyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_1000010976.
FT   ACT_SITE    149    149       By similarity.
SQ   SEQUENCE   345 AA;  37681 MW;  CEC3AD5125DCBF5C CRC64;
     MKIGIIGATG YGGAELVRIL NHHPYAEDCI LYSSSDEGKE YAASYPHLRN IASQSLQPLH
     IETIRNEIDV MFIAAPPGVS GEWSPKLAEA GIPVIDLSGD LRIQNPAVYE KWYKRKAAPK
     GTIQSAVYGL AELQKEEIQT AKLIANPGCF PTAVLLGLAP LAKNGLLQDS FLIVDAKTGV
     SGAGRKASMG THYSELNDNF KIYKVNEHQH TPEIEQQLAA WQPGTGPITF SAHLAPMTRG
     IMATMYTEAP PGMSAAQVRE LYSEFYKDSY FVRIRPEGEF PATKEVYGSN FCDISVTVDE
     RTNRATIVSV IDNLMKGAAG QAVQNLNIMN GWQEETGLTM TPVYP
//