ID   TYRA_STAHJ              Reviewed;         363 AA.
AC   Q4L672;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Prephenate dehydrogenase;
DE            Short=PDH;
DE            EC=1.3.1.12;
GN   Name=tyrA; OrderedLocusNames=SH1544;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04853.1; -; Genomic_DNA.
DR   RefSeq; WP_011275835.1; NC_007168.1.
DR   AlphaFoldDB; Q4L672; -.
DR   SMR; Q4L672; -.
DR   STRING; 279808.SH1544; -.
DR   EnsemblBacteria; BAE04853; BAE04853; SH1544.
DR   KEGG; sha:SH1544; -.
DR   eggNOG; COG0287; Bacteria.
DR   HOGENOM; CLU_055968_2_1_9; -.
DR   OMA; MWRDICL; -.
DR   OrthoDB; 533829at2; -.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000000543; Chromosome.
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_0000282665"
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;  40442 MW;  4E34B068A10921BC CRC64;
     MKNILFIGLG LIGGSLASNL KYYQPNLTIS AFDADKDQLE KALSIGIIDK KIEDYSEGVK
     NADIIIYATP VQQTELYLKE LPNYQTQSHL IVTDTGSTKS NIQSYEKFLL NNDIHLVGGH
     PMAGSHKSGV LNSKKHLFEN AYYILVYDDA RNAESAKKLQ TLLSTTSAKF ITTSAQEHDY
     VTGVVSHIPH IIASSLVHLS ETNSKNHTLV TQLAAGGFRD VTRIASSNAD MWRDITFSNQ
     ENILHLLEML QQQLDSISSH IRLNDTNEVH SFFSGAKKFR DQLPVKQQGA LSIAYDLYVD
     IPDKSGMISK VTSILSLHNI SISNLKILEI REDILGALQI SFKTPEDRER GIKALSDFET
     YIL