ID   ARGC2_LACPL             Reviewed;         341 AA.
AC   O08318;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 2.
DT   16-JUN-2009, entry version 67.
DE   RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase 2;
DE            Short=AGPR 2;
DE            EC=1.2.1.38;
DE   AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase 2;
DE            Short=NAGSA dehydrogenase 2;
GN   Name=argC2; Synonyms=argC; OrderedLocusNames=lp_0528;
OS   Lactobacillus plantarum.
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8014 / CCM 1904 / DSM 20205 / NCDO 82 / NCIB 6376;
RX   MEDLINE=97252500; PubMed=9098069;
RA   Bringel F., Frey L., Boivin S., Hubert J.-C.;
RT   "Arginine biosynthesis and regulation in Lactobacillus plantarum: the
RT   carA gene and the argCJBDF cluster are divergently transcribed.";
RL   J. Bacteriol. 179:2697-2706(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   MEDLINE=22480296; PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D.,
RA   Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M.,
RA   Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A.,
RA   Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B.,
RA   De Vos W.M., Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
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; X99978; CAA68239.1; -; Genomic_DNA.
DR   EMBL; AL935253; CAD63147.1; -; Genomic_DNA.
DR   RefSeq; NP_784306.1; -.
DR   GeneID; 1061865; -.
DR   GenomeReviews; AL935263_GR; lp_0528.
DR   KEGG; lpl:lp_0528; -.
DR   NMPDR; fig|220668.1.peg.440; -.
DR   HOGENOM; O08318; -.
DR   BioCyc; LPLA220668:LP_0528-MON; -.
DR   BRENDA; 1.2.1.38; 593.
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 2.
FT                                /FTId=PRO_0000112413.
FT   ACT_SITE    146    146       By similarity.
FT   CONFLICT    119    119       S -> P (in Ref. 1; CAA68239).
FT   CONFLICT    234    234       V -> A (in Ref. 1; CAA68239).
SQ   SEQUENCE   341 AA;  36940 MW;  CD35D297041CC42A CRC64;
     MQVALVGVTG YSGMVLYRLL KQHPEIDRIQ LYGHVGATTV ALKTVAAMYQ KETAVIRPFD
     ATAIMRDNAI VFFATSAGIT RQLALPFIAA HFPVIDLSGD FRLHDPEQYQ RWYQRDPASA
     TALAQASYGL ADMPAPLSTY IANPGCYATA TLLGLAPLAQ QQLVEPTSIV VDAKSGLSGA
     GKRATAASHY VAVNDNLSLY KLNQHQHIPE MMQQLQQWWS AISAIEFTTT LIPVTRGIMT
     TIYAKAKSAL TTTQVRAAFT ATYHEQPFVQ VLPTGMPTLK DVVGSNNCAL GVDYNPVTNT
     IVVVSVIDNL MKGAAGQAVQ NFNRYFDFAV TAGLPTLPVF P
//