ID   HPPD_PLESU              Reviewed;         436 AA.
AC   Q9ARF9;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 83.
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   Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae;
OC   Plectranthinae; Plectranthus.
OX   NCBI_TaxID=4142;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kim K.H.;
RL   Thesis (2001), Philipps-Universitaet Marburg, Germany.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 4HPPD family. {ECO:0000305}.
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DR   EMBL; AJ309203; CAC37394.1; -; mRNA.
DR   AlphaFoldDB; Q9ARF9; -.
DR   SMR; Q9ARF9; -.
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..436
FT                   /note="4-hydroxyphenylpyruvate dioxygenase"
FT                   /id="PRO_0000088400"
FT   DOMAIN          38..194
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          210..370
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         213
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         381
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   436 AA;  47736 MW;  663737B7578C0F13 CRC64;
     MGQESTAAAA VVPAEFKLVG HKNFVRSNPM SDHFPVHRFH HVEFWCGDAT NTSRRFSWGL
     GMPLVAKSDL STGNSAHASY LLRSGELSFV FTAPYSPSLA EPSSASIPTF SFSDHRAFTS
     SHGLAVRAVA IQVDSASSAY SAAVSRGAKP VSPPVVLADC ETAIAEVHLY GDTVLRFVSC
     GSGADGWFLP GFEVVGDGVS CQELDYGIRR LDHAVGNVPK LEPVVDYLKK FTGFHEFAEF
     TAEDVGTAES GLNSVVLANN NENVLFPLNE PVYGTKRKSQ IQTYLDHNEG AGVQHLALIT
     EDIFRTLREM RKRSEVGGFE FMPSPPPTYY RNLKSRAGDV LSDEQIEECE KLGILIDRDD
     QGTLLQIFTK PVGDRPTLFI EIIQRVGCMM KDEEGKMYQK GGCGGFGKGN FSELFKSIEE
     YEKMLESKLV TKTAMA