ID   ARGC_CALS8              Reviewed;         343 AA.
AC   A4XJN9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 17.
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=Csac_1531;
OS   Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis;
OC   Caldicellulosiruptor.
OX   NCBI_TaxID=351627;
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., Kiss H., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L.,
RA   Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M.,
RA   Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W.,
RA   Richardson P.;
RT   "Genome sequence of the thermophilic hydrogen-producing bacterium
RT   Caldicellulosiruptor saccharolyticus DSM 8903.";
RL   Submitted (APR-2007) 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; CP000679; ABP67124.1; -; Genomic_DNA.
DR   RefSeq; YP_001180315.1; -.
DR   GeneID; 5088113; -.
DR   GenomeReviews; CP000679_GR; Csac_1531.
DR   KEGG; csc:Csac_1531; -.
DR   OMA; A4XJN9; 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; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_C.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
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    343       N-acetyl-gamma-glutamyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_1000010983.
FT   ACT_SITE    148    148       By similarity.
SQ   SEQUENCE   343 AA;  38574 MW;  1AA8E0A4DE8975F5 CRC64;
     MIKASIIGAS GYVGIELIRL LLKHPEVEIS SIISSSNKDI SIENTNPQFK KILNLTFKEF
     DIDLVKEADV VFCALPHGVS QEYVKVAYDL GKVVIDLSSD FRYKDLTRYS KDYGNHKYPE
     LLNESSYGLC EIFREEIKSS KIVGNPGCYP TSAILGLAPL LKNKLIQKDS IIIDSKSGVS
     GAGKKADFAY SFCEVDENFK AYGVAKHRHT SEIEEKCSFL FGEDLNLSFT PHLLPVKRGI
     LSTIYATFTK SLNKNELIEI YKEFYRDEFF IRIYEDSLPE LKYVTGTNFV DIGLEVDKKT
     NRVIVISCID NLIKGAAGQA IQNMNIKFSL NEKTGLVIVG EYF
//