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   03-AUG-2022, entry version 98.
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; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
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., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC         NADH; Xref=Rhea:RHEA:13869, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC         ChEBI:CHEBI:36242, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.12;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC       hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC   -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX571857; CAG43082.1; -; Genomic_DNA.
DR   RefSeq; WP_000214266.1; NC_002953.3.
DR   AlphaFoldDB; Q6G9J4; -.
DR   SMR; Q6G9J4; -.
DR   KEGG; sas:SAS1305; -.
DR   HOGENOM; CLU_055968_2_1_9; -.
DR   OMA; MWRDICL; -.
DR   UniPathway; UPA00122; UER00961.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003099; Prephen_DH.
DR   Pfam; PF02153; PDH; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NAD;
KW   Oxidoreductase; Tyrosine biosynthesis.
FT   CHAIN           1..363
FT                   /note="Prephenate dehydrogenase"
FT                   /id="PRO_0000282657"
FT   DOMAIN          2..291
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
FT   DOMAIN          296..363
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   BINDING         3..33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
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