ID   TYRA_STAS1              Reviewed;         363 AA.
AC   Q49XG5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Prephenate dehydrogenase;
DE            Short=PDH;
DE            EC=1.3.1.12;
GN   Name=tyrA; OrderedLocusNames=SSP1387;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18532.1; -; Genomic_DNA.
DR   RefSeq; WP_002483353.1; NZ_MTGA01000038.1.
DR   AlphaFoldDB; Q49XG5; -.
DR   SMR; Q49XG5; -.
DR   GeneID; 66867610; -.
DR   KEGG; ssp:SSP1387; -.
DR   eggNOG; COG0287; Bacteria.
DR   HOGENOM; CLU_055968_2_1_9; -.
DR   OrthoDB; 9802008at2; -.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000006371; 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; 3.30.70.260; -; 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; PF01842; ACT; 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; Reference proteome; Tyrosine biosynthesis.
FT   CHAIN           1..363
FT                   /note="Prephenate dehydrogenase"
FT                   /id="PRO_0000282666"
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;  40963 MW;  130EB5895E8F90DF CRC64;
     MKQILFVGLG LIGGSLASNL RYYHDDIEIT AFDADTSQLD KALSIGIIDY QSTDYKTSVE
     NADIIIYATP VQQTVKYLQD LPNYQLKKHV IITDTGSTKS TIQQYEQFLL NHDIHLVGGH
     PMAGSHKSGV LNAKKHLFEN AFYILVHNET DNDAAFEEIQ HLLQTTSAKF ISTTAEEHDF
     VTGIVSHVPH IIASSLVHLN AQHVEDSSLV KTLAAGGFRD ITRIASSNPI MWRDITIENK
     NTILRILKEW KNQMSDVINI IEHNNPDELY DFFNDAKVYR DQLPLKQQGA LSVEYDLYVD
     IPDKPGMISK VTNILSLHNI SISNLRILEV REDIYGALRV SFKNPQDRKD GADALSDFDT
     YFD
//