ID   HPPD_DAUCA              Reviewed;         442 AA.
AC   O23920;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=4-hydroxyphenylpyruvate dioxygenase;
DE            EC=1.13.11.27;
DE   AltName: Full=4-hydroxyphenylpyruvic acid oxidase;
DE            Short=4HPPD;
DE            Short=HPD;
DE            Short=HPPDase;
OS   Daucus carota (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9271098; DOI=10.1042/bj3250761;
RA   Garcia I., Rodgers M., Lenne C., Rolland A., Sailland A., Matringe M.;
RT   "Subcellular localization and purification of a p-hydroxyphenylpyruvate
RT   dioxygenase from cultured carrot cells and characterization of the
RT   corresponding cDNA.";
RL   Biochem. J. 325:761-769(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate;
CC         Xref=Rhea:RHEA:16189, ChEBI:CHEBI:15379, ChEBI:CHEBI:16169,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:36242; EC=1.13.11.27;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 3/6.
CC   -!- PATHWAY: Cofactor biosynthesis; prenylquinone biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the 4HPPD family. {ECO:0000305}.
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DR   EMBL; U87257; AAC49815.1; -; mRNA.
DR   PIR; T14353; T14353.
DR   AlphaFoldDB; O23920; -.
DR   SMR; O23920; -.
DR   BindingDB; O23920; -.
DR   ChEMBL; CHEMBL4105881; -.
DR   SABIO-RK; O23920; -.
DR   UniPathway; UPA00139; UER00362.
DR   UniPathway; UPA00975; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07250; HPPD_C_like; 1.
DR   CDD; cd08342; HPPD_N_like; 1.
DR   Gene3D; 3.10.180.10; -; 2.
DR   InterPro; IPR005956; 4OHPhenylPyrv_dOase.
DR   InterPro; IPR041735; 4OHPhenylPyrv_dOase_C.
DR   InterPro; IPR041736; 4OHPhenylPyrv_dOase_N.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR037523; VOC.
DR   PANTHER; PTHR11959; PTHR11959; 1.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   PIRSF; PIRSF009283; HPP_dOase; 1.
DR   SUPFAM; SSF54593; SSF54593; 1.
DR   TIGRFAMs; TIGR01263; 4HPPD; 1.
DR   PROSITE; PS51819; VOC; 2.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Phenylalanine catabolism; Repeat; Tyrosine catabolism.
FT   CHAIN           1..442
FT                   /note="4-hydroxyphenylpyruvate dioxygenase"
FT                   /id="PRO_0000088398"
FT   DOMAIN          45..200
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          216..376
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         219
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         387
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   442 AA;  48148 MW;  A484AFFA267F7BF7 CRC64;
     MGKKQSEAEI LSSNSSNTSP ATFKLVGFNN FVRANPKSDH FAVKRFHHIE FWCGDATNTS
     RRFSWGLGMP LVAKSDLSTG NSVHASYLVR SANLSFVFTA PYSPSTTTSS GSAAIPSFSA
     SGFHSFAAKH GLAVRAIALE VADVAAAFEA SVARGARPAS APVELDDQAW LAEVELYGDV
     VLRFVSFGRE EGLFLPGFEA VEGTASFPDL DYGIRRLDHA VGNVTELGPV VEYIKGFTGF
     HEFAEFTAED VGTLESGLNS VVLANNEEMV LLPLNEPVYG TKRKSQIQTY LEHNEGAGVQ
     HLALVSEDIF RTLREMRKRS CLGGFEFMPS PPPTYYKNLK NRVGDVLSDE QIKECEDLGI
     LVDRDDQGTL LQIFTKPVGD RPTLFIEIIQ RVGCMLKDDA GQMYQKGGCG GFGKGNFSEL
     FKSIEEYEKT LEAKQITGSA AA