ID   ARGC_CENSY              Reviewed;         348 AA.
AC   A0RWW0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase;
DE            Short=AGPR;
DE            EC=1.2.1.38;
DE            EC=1.2.1.-;
DE   AltName: Full=N-acetyl-glutamate semialdehyde/N-acetyl-aminoadipate semialdehyde dehydrogenase;
DE            Short=NAGSA dehydrogenase;
GN   Name=argC; Synonyms=lysY; OrderedLocusNames=CENSYa_1203;
OS   Cenarchaeum symbiosum.
OC   Archaea; Crenarchaeota; Thermoprotei; Cenarchaeales; Cenarchaeaceae;
OC   Cenarchaeum.
OX   NCBI_TaxID=46770;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
CC   -!- FUNCTION: Involved in both the arginine and lysine biosynthetic
CC       pathways (By similarity).
CC   -!- CATALYTIC ACTIVITY: N-acetyl-L-glutamate 5-semialdehyde + NADP(+)
CC       + phosphate = N-acetyl-5-glutamyl phosphate + NADPH.
CC   -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-aminoadipate-semialdehyde +
CC       NADP(+) + phosphate = N(2)-acetyl-L-gamma-aminoadipyl phosphate +
CC       NADPH.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 3/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step
CC       3/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1
CC       subfamily.
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DR   EMBL; DP000238; ABK77827.1; -; Genomic_DNA.
DR   GenomeReviews; DP000238_GR; CENSYa_1203.
DR   OMA; A0RWW0; GCNATAT.
DR   BRENDA; 1.2.1.38; 281607.
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:0009085; P:lysine biosynthetic process; IEA:UniProtKB-KW.
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; FALSE_NEG.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome;
KW   Cytoplasm; Lysine biosynthesis; NADP; Oxidoreductase.
FT   CHAIN         1    348       N-acetyl-gamma-glutamyl-phosphate/N-
FT                                acetyl-gamma-aminoadipyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_1000010987.
FT   ACT_SITE    149    149       By similarity.
SQ   SEQUENCE   348 AA;  38320 MW;  62FB3BA2351B940E CRC64;
     MKVGVVGASG YVGGETLRLL VNHPDVEIAA VTSRQHVGEY LHRVQPSLRG FTDLTFSELD
     YDRLSDSCDL VFTAVPHGTA TDIVRALYDR DIKVIDLSAD YRLHDPADYT KWYGWEHPHP
     DYLSKSVFGI PELHREEIRS AKLVSCPGCM AVTSILALAP PVREGLVDTE HIVVDSKIGS
     SGAGAGAGTA HAMRAGVIRP YKPAKHRHTG EIEQELSGIA GKKIRVSMSP HAVDVVRGIL
     CTNHVFLTRE ASEKDLWKMY RQAYGEERFV RLIRDKKGLY KFPDPKFLVG SNFCDIGFDL
     DEDNNRLVAI SASDNLMKGA AGSAIQNMNI MAGLDEMSGL RYTPLTPV
//