ID   ARGC_ALHEH              Reviewed;         343 AA.
AC   Q0ABJ9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=Mlg_0434;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000453; ABI55788.1; -; Genomic_DNA.
DR   RefSeq; YP_741278.1; -.
DR   GeneID; 4268287; -.
DR   GenomeReviews; CP000453_GR; Mlg_0434.
DR   KEGG; aeh:Mlg_0434; -.
DR   NMPDR; fig|187272.6.peg.412; -.
DR   HOGENOM; Q0ABJ9; -.
DR   OMA; Q0ABJ9; TAEDCTT.
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    343       N-acetyl-gamma-glutamyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_1000010973.
FT   ACT_SITE    149    149       By similarity.
SQ   SEQUENCE   343 AA;  36618 MW;  37E8B83615D5E0F0 CRC64;
     MIEVGIVGGT GYTGVELLRL LARHPEARLR VITSRGNAGT RVDELFPSLR GEVELAFSEP
     DVDRLAACDL VFFATPNGTA MQMVPDLLAR DTRVVDLGAD FRLKDVETWS RWYGMTHACP
     ELVAEAAYGL PELNREAIRG ARLVANPGCY PTAVGLGWLP LLEAGLVETR GLVASCVSGA
     SGAGRAANVA TLLCEVNESF KAYGADGHRH LPEIRQSLAQ VAGGAVELTF VPHLVPMTRG
     MHASLYATLR GDAGDLQVLF EQRYADEPFV DVLPAGAHPE TRTVRGTNLC RLAVRRAPES
     DQVIVLSVID NLTKGAAGQA VQNMNLMFGL PETAGLDAPA VLP
//