ID   TYRA_STAAS              Reviewed;         363 AA.
AC   Q6G9J4;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Prephenate dehydrogenase;
DE            Short=PDH;
DE            EC=1.3.1.12;
GN   Name=tyrA; OrderedLocusNames=SAS1305;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- CATALYTIC ACTIVITY: Prephenate + NAD(+) = 4-hydroxyphenylpyruvate
CC       + CO(2) + NADH.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; L-
CC       tyrosine from prephenate: step 1/2.
CC   -!- SIMILARITY: Contains 1 prephenate/arogenate dehydrogenase domain.
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DR   EMBL; BX571857; CAG43082.1; -; Genomic_DNA.
DR   RefSeq; YP_043429.1; -.
DR   GeneID; 2861989; -.
DR   GenomeReviews; BX571857_GR; SAS1305.
DR   KEGG; sas:SAS1305; -.
DR   HOGENOM; Q6G9J4; -.
DR   OMA; Q6G9J4; QRAIRWG.
DR   BioCyc; SAUR282459:SAS1305-MON; -.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0008977; F:prephenate dehydrogenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002912; ACT_bd.
DR   InterPro; IPR003099; Prephen_DH.
DR   PANTHER; PTHR21363; Prephen_DH; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF02153; PDH; 1.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; NAD; Oxidoreductase; Tyrosine biosynthesis.
FT   CHAIN         1    363       Prephenate dehydrogenase.
FT                                /FTId=PRO_0000282657.
FT   DOMAIN        2    291       Prephenate/arogenate dehydrogenase.
FT   NP_BIND       3     33       NAD (Potential).
SQ   SEQUENCE   363 AA;  40395 MW;  8F16333DC3B816C6 CRC64;
     MTTVLFVGLG LIGGSLASNI KYHNPNTNII AYDADTSQLD KAKSIGIINE KCLNYSEAIK
     KADVIIYATP VAITNKYLSE LIDMPTKPGV IVSDTGSTKA MIQQHECNLL KHNIHLVSGH
     PMAGSHKSGV LNAKKHLFEN AYYILVYNEP RNEQAANTLK ELLSPTLAKF IVTTAEEHDY
     VTSVVSHLPH IVASSLVHVS QKNGQEHHLV NKLAAGGFRD ITRIASSNAQ MWKDITLSNK
     TYILEMIRQL KSQFQDLERL IESNDSEKLL SFFAQAKSYR DALPAKQLGG LNTAYDLYVD
     IPDESGMISK VTYILSLHNI SISNLRILEV REDIYGALKI SFKNPTDRER GMQALSDFDC
     YIQ
//