ID   ARGC_BUCAP              Reviewed;         334 AA.
AC   Q8KA61;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 51.
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=BUsg_045;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67616.1; -; Genomic_DNA.
DR   RefSeq; NP_660405.1; -.
DR   GeneID; 1005861; -.
DR   GenomeReviews; AE013218_GR; BUsg_045.
DR   KEGG; bas:BUsg045; -.
DR   HOGENOM; Q8KA61; -.
DR   OMA; Q8KA61; VCRIAVH.
DR   BioCyc; BAPH198804:BUSG045-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    334       N-acetyl-gamma-glutamyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_0000112392.
FT   ACT_SITE    154    154       By similarity.
SQ   SEQUENCE   334 AA;  37835 MW;  9F7487A9B3816B77 CRC64;
     MLNVLIVGAS GYSGAELVNY INRHMFSKIK KIFVSENSSH IGKLFSELHQ EFKNIIDLPF
     EAINYDTLIE KDIDAVFLAT DHHVSYSLVP FFLSLNCVVF DLSGAYRVKN TDTYLKYYGF
     SHQHQDILKR SVYGLAEWNK QEIKKAELIA VPGCYATCIQ LALKPLIKEN FLNDEFIPII
     NAISGVSGAG RKANITNSFC EVSLHPYNVF THRHTPEIIE HLGIPVIFIP HLGSFSRGIL
     ASITCKLKCN FTFQDIYNLY NTVYKEKPLI RVYEKNFPSI KAVVKLPFCD IGFIIQDKYI
     VIIAAEDNLL KGAAAQAIQC FNIRFGFSEI ESII
//