ID   ARGC_ARTS2              Reviewed;         343 AA.
AC   A0JV20;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=Arth_1496;
OS   Arthrobacter sp. (strain FB24).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=290399;
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., Chertkov O., Thompson S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K.,
RA   Nakatsu C.H., Richardson P.;
RT   "Complete sequence of chromosome 1 of Arthrobacter sp. FB24.";
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; CP000454; ABK02890.1; -; Genomic_DNA.
DR   RefSeq; YP_830990.1; -.
DR   GeneID; 4445992; -.
DR   GenomeReviews; CP000454_GR; Arth_1496.
DR   KEGG; art:Arth_1496; -.
DR   TIGR; Arth_1496; -.
DR   OMA; A0JV20; 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_1000010975.
FT   ACT_SITE    146    146       By similarity.
SQ   SEQUENCE   343 AA;  34930 MW;  E7CCF8508BE698BF CRC64;
     MTISVAVSGA SGYAGGEVLR LLAGHPDVTI GAITAHSNAG SRLGELQPHL HGLASRILED
     TTVENLSGHD VVFLALPHGA SADIAAQLPE GTVVIDAGAD HRLEDPAAWE KFYGSAHAGT
     WPYGLPELPG QREKLKGANR IAVPGCYPTS ALLALTPGFA GSLLQPDDVV IVAASGTSGA
     GKAAKVNLIG SEVMGSMSPY GVGGGHRHTP EIEQGLGNAA GEAVTVSFTP TLAPMSRGIL
     TTATAKVKPG VTAAELRSAW EEAYDDEPFV HLLPEGQWPS TKSVQGSNHA VMQVAFDAHT
     GRVIVTCAID NLTKGTAGGA VQSMNIALGL AETAGLNLQG VAP
//