ID   TYRA_STAAC              Reviewed;         363 AA.
AC   Q5HG54;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Prephenate dehydrogenase;
DE            Short=PDH;
DE            EC=1.3.1.12;
GN   Name=tyrA; OrderedLocusNames=SACOL1401;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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; CP000046; AAW36649.1; -; Genomic_DNA.
DR   RefSeq; WP_000214266.1; NC_002951.2.
DR   AlphaFoldDB; Q5HG54; -.
DR   SMR; Q5HG54; -.
DR   KEGG; sac:SACOL1401; -.
DR   HOGENOM; CLU_055968_2_1_9; -.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000000530; Chromosome.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
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   CDD; cd04909; ACT_PDH-BS; 1.
DR   Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR046825; PDH_C.
DR   InterPro; IPR046826; PDH_N.
DR   InterPro; IPR003099; Prephen_DH.
DR   PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF20463; PDH_C; 1.
DR   Pfam; PF02153; PDH_N; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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_0000282655"
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
//