ID   ARGC_CLAM3              Reviewed;         349 AA.
AC   A5CSI9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-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=CMM_2001;
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=443906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18192381; DOI=10.1128/JB.01595-07;
RA   Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M.,
RA   Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O.,
RA   Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S.,
RA   Rueckert C., Schneiker S., Zellermann E.-M., Puehler A.,
RA   Eichenlaub R., Kaiser O., Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island
RT   involved in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(2008).
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; AM711867; CAN02064.1; -; Genomic_DNA.
DR   RefSeq; YP_001222743.1; -.
DR   GeneID; 5175474; -.
DR   GenomeReviews; AM711867_GR; CMM_2001.
DR   KEGG; cmi:CMM_2001; -.
DR   OMA; A5CSI9; 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    349       N-acetyl-gamma-glutamyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_1000010988.
FT   ACT_SITE    152    152       By similarity.
SQ   SEQUENCE   349 AA;  36032 MW;  4D8717CAD0CD8BF9 CRC64;
     MSFSVAVAGA SGYAGGELLR LLADHPRLEV QTLTAFQNAG ERLRQVHPHL TSYADRTFVE
     TTAERLAGHD VVFLALPHGK SGAITAELDD QTLVVDCGAD HRLVDEAAWD AFYGGDFAGA
     WPYGLPELLH AEEGGTQRTR LSGVKRIAVP GCNVTAITLG LQPGIRAGVI EPEDIVAVLA
     VGPSGAGRSL RTNLLASEIL GSASAYAVGG THRHTPEIRQ NLETAGGGHV SVSFTPVLVP
     MARGILATAT ARLAPGFSAH DVRAAWELAY ADEPFVHLLP EGSFPNVSDV TGSNTALVGL
     AIDEAAGRVV TVTAIDNLVK GTAGAAIQSA NIALGLPEAM GLPVNGVAP
//