ID   ARGC2_THET2             Reviewed;         344 AA.
AC   O50146; Q9ZND6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   16-JUN-2009, entry version 68.
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=argC2; Synonyms=argC, lysY; OrderedLocusNames=TT_C1542;
OS   Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T.,
RA   Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R.,
RA   Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R.,
RA   Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus
RT   thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-236.
RX   MEDLINE=99173891; PubMed=10074061;
RA   Kobashi N., Nishiyama M., Tanokura M.;
RT   "Aspartate kinase-independent lysine synthesis in an extremely
RT   thermophilic bacterium, Thermus thermophilus: lysine is synthesized
RT   via alpha-aminoadipic acid not via diaminopimelic acid.";
RL   J. Bacteriol. 181:1713-1718(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-344.
RX   MEDLINE=98079437; PubMed=9418242; DOI=10.1016/S0378-1097(97)00456-4;
RA   Kosuge T., Hoshino T.;
RT   "Molecular cloning and sequence analysis of the lysR gene from the
RT   extremely thermophilic eubacterium, Thermus thermophilus HB27.";
RL   FEMS Microbiol. Lett. 157:73-79(1997).
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; AE017221; AAS81884.1; -; Genomic_DNA.
DR   EMBL; AB017109; BAA74767.1; -; mRNA.
DR   EMBL; AB006681; BAA23878.1; ALT_INIT; Genomic_DNA.
DR   PIR; T43947; T43947.
DR   RefSeq; YP_005511.1; -.
DR   GeneID; 2776302; -.
DR   GenomeReviews; AE017221_GR; TT_C1542.
DR   HOGENOM; O50146; -.
DR   OMA; O50146; GCNATAT.
DR   BioCyc; MetaCyc:MON-6802; -.
DR   BioCyc; TTHE262724:TT_C1542-MON; -.
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; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome;
KW   Cytoplasm; Lysine biosynthesis; NADP; Oxidoreductase.
FT   CHAIN         1    344       N-acetyl-gamma-glutamyl-phosphate/N-
FT                                acetyl-gamma-aminoadipyl-phosphate
FT                                reductase.
FT                                /FTId=PRO_0000112501.
FT   ACT_SITE    148    148       By similarity.
SQ   SEQUENCE   344 AA;  38051 MW;  B11CE66CB2F04C15 CRC64;
     MDKKTLSIVG ASGYAGGEFL RLALSHPYLE VKQVTSRRFA GEPVHFVHPN LRGRTNLKFI
     PPEKLEPADI LVLALPHGVF AREFDRYSAL APILIDLSAD FRLKDPELYR RYYGEHPRPD
     LLGCFVYAVP ELYREALKGA DWIAGAGCNA TATLLGLYPL LKAGVLKPTP IFVTLLISTS
     AAGAEASPAS HHPERAGSIR VYKPTGHRHT AEVVENLPGR PEVHLTAIAT DRVRGILMTA
     QCFVQDGWSE RDVWQAYREA YAGEPFIRLV KQKKGVHRYP DPRFVQGTNY ADIGFELEED
     TGRLVVMTAI DNLVKGTAGH ALQALNVRMG WPETLGLDFP GLHP
//