ID   TYRA_STAAR              Reviewed;         363 AA.
AC   Q6GH39;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Prephenate dehydrogenase;
DE            Short=PDH;
DE            EC=1.3.1.12;
GN   Name=tyrA; OrderedLocusNames=SAR1378;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282458;
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; BX571856; CAG40376.1; -; Genomic_DNA.
DR   RefSeq; YP_040783.1; -.
DR   GeneID; 2861438; -.
DR   GenomeReviews; BX571856_GR; SAR1378.
DR   KEGG; sar:SAR1378; -.
DR   HOGENOM; Q6GH39; -.
DR   OMA; Q6GH39; QRAIRWG.
DR   BioCyc; SAUR282458:SAR1378-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_0000282656.
FT   DOMAIN        2    291       Prephenate/arogenate dehydrogenase.
FT   NP_BIND       3     33       NAD (Potential).
SQ   SEQUENCE   363 AA;  40421 MW;  6BE50F4A89852C49 CRC64;
     MTTVLFVGLG LIGGSLASNI KYHNPNTNII AYDADTSQLD KAKSIGIINE KCLNYSEAIK
     KADVIIYATP VAITNKYLSE LIHMPTKPGV IVSDTGSTKA MIQQHECSLL KHNIHLVSGH
     PMAGSHKSGV LNAKKHLFEN AYYILVYNEP RNEQAANTLK ELLSPTLAKF IVTTAEEHDY
     VTSVVSHLPH IVASSLVHVS QKNSQEHHLV NKLAAGGFRD ITRIASSNAQ MWKDITLSNK
     TYILEMIRQL KSQFQDLERL IESNDSEKLL SFFAEAKSYR DALPAKQLGG LNTAYDLYVD
     IPDESGMISK VTYILSLHNI SISNLRILEV REDIYGALKI SFKNPTDRER GMQALSDFDC
     YIQ
//