ID   ARGC_CHLTE              Reviewed;         341 AA.
AC   Q8KDE3;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 47.
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=CT1109;
OS   Chlorobium tepidum.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=1097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(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; AE006470; AAM72342.1; -; Genomic_DNA.
DR   RefSeq; NP_662000.1; -.
DR   GeneID; 1006899; -.
DR   GenomeReviews; AE006470_GR; CT1109.
DR   KEGG; cte:CT1109; -.
DR   NMPDR; fig|194439.1.peg.1094; -.
DR   TIGR; CT1109; -.
DR   HOGENOM; Q8KDE3; -.
DR   OMA; Q8KDE3; VCRIAVH.
DR   BioCyc; CTEP194439:CT_1109-MON; -.
DR   BRENDA; 1.2.1.38; 189605.
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    341       N-acetyl-gamma-glutamyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_0000112395.
FT   ACT_SITE    151    151       By similarity.
SQ   SEQUENCE   341 AA;  36613 MW;  EF684FBDD4075F3D CRC64;
     MNHIPMQNKK VTVSVIGASG YSGAELVKLL MKHPGIVIEE LYAHTQAGKR FTELYPSIPC
     DKTFQTYAGQ TNSDVYLLAL PHGEALQLVP GIVAAGKKVI DLSGDFRLKN TAEHKRFYGG
     DKSAEDVLQY GMPELFRDEI AGSTAISNPG CYATSIILGL APLFLGGMAG LDVESVNVTA
     VSGISGAGRS AKLELSFSEM SGNMRAYKVG KHQHTPEIMQ TLGTSVTDPS FRFVFTPMIA
     PYVRGIYSVL NVRLASPVAM EPVRELYAGF YANAPFVRLR DGVTEVSHVA YTNFCDISLA
     FESDGSLVII TAIDNLVKGA AGQAVQNMNL MLGFGETTAL L
//