TYRA_STAAR
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 03-AUG-2022, entry version 101.
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; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
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}.
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DR EMBL; BX571856; CAG40376.1; -; Genomic_DNA.
DR RefSeq; WP_000214282.1; NC_002952.2.
DR AlphaFoldDB; Q6GH39; -.
DR SMR; Q6GH39; -.
DR KEGG; sar:SAR1378; -.
DR HOGENOM; CLU_055968_2_1_9; -.
DR OMA; MWRDICL; -.
DR OrthoDB; 533829at2; -.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000000596; 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_0000282656"
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; 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