ID   TYRA_STAA8              Reviewed;         363 AA.
AC   Q2FYS1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Prephenate dehydrogenase;
DE            Short=PDH;
DE            EC=1.3.1.12;
GN   Name=tyrA; OrderedLocusNames=SAOUHSC_01364;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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}.
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DR   EMBL; CP000253; ABD30459.1; -; Genomic_DNA.
DR   RefSeq; WP_000214264.1; NZ_LS483365.1.
DR   RefSeq; YP_499891.1; NC_007795.1.
DR   AlphaFoldDB; Q2FYS1; -.
DR   SMR; Q2FYS1; -.
DR   STRING; 1280.SAXN108_1381; -.
DR   EnsemblBacteria; ABD30459; ABD30459; SAOUHSC_01364.
DR   GeneID; 3920069; -.
DR   KEGG; sao:SAOUHSC_01364; -.
DR   PATRIC; fig|93061.5.peg.1248; -.
DR   eggNOG; COG0287; Bacteria.
DR   HOGENOM; CLU_055968_2_1_9; -.
DR   OMA; MWRDICL; -.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IBA:GO_Central.
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; Reference proteome; Tyrosine biosynthesis.
FT   CHAIN           1..363
FT                   /note="Prephenate dehydrogenase"
FT                   /id="PRO_0000282661"
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;  40407 MW;  07DEF8CC0AB6293E CRC64;
     MTTVLFVGLG LIGGSLASNI KYHNPNTNII AYDADISQLD 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