ID   TYRA_STAES              Reviewed;         362 AA.
AC   Q8CPB5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Prephenate dehydrogenase;
DE            Short=PDH;
DE            EC=1.3.1.12;
GN   Name=tyrA; OrderedLocusNames=SE_1047;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04644.1; -; Genomic_DNA.
DR   RefSeq; NP_764602.1; NC_004461.1.
DR   RefSeq; WP_001831297.1; NZ_WBME01000002.1.
DR   AlphaFoldDB; Q8CPB5; -.
DR   SMR; Q8CPB5; -.
DR   GeneID; 50018826; -.
DR   KEGG; sep:SE_1047; -.
DR   PATRIC; fig|176280.10.peg.1023; -.
DR   eggNOG; COG0287; Bacteria.
DR   HOGENOM; CLU_055968_2_1_9; -.
DR   OrthoDB; 9802008at2; -.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000001411; 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   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; Tyrosine biosynthesis.
FT   CHAIN           1..362
FT                   /note="Prephenate dehydrogenase"
FT                   /id="PRO_0000282663"
FT   DOMAIN          2..291
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
FT   DOMAIN          296..362
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   362 AA;  40710 MW;  BB0D1A12046E0A3B CRC64;
     MRNILFVGLG LIGGSLASNL KYHYSNFNIL AYDSDYTQLD EALSIGIIDQ KVNDYATAVE
     IADIIIFATP VEQTIKYLSE LTNYNTKTHL IVTDTGSTKL TIQSFEKELL KHDIHLISGH
     PMAGSHKSGV LNAKKHLFEN AYYILVFNEI ENNEAATYLK KLLKPTLAKF IVTHANEHDF
     VTGIVSHVPH IIASILVHLS ANHVKDHSLI EKLAAGGFRD ITRIASSNAQ MWKDITLNNQ
     NHILSLLNEI KEQITGIENL IREQNSNSIY DFFVKAKDYR DQLPVKQHGA ISTAYDLYVD
     IPDKPGMISQ ITNIISSHNI SIINLKILEV REDIYGALQI SFKSPEDREN AIKALANFDT
     YY
//