ID   HPPD_HORVU              Reviewed;         434 AA.
AC   O48604;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 102.
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   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Carina; TISSUE=Meristem;
RA   Krupinska K., Falk J.;
RT   "cDNA sequence encoding a barley 4-hydroxyphenylpyruvate dioxygenase with
RT   enhanced expression in meristematic leaf tissue and during leaf
RT   senescence.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
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; AJ000693; CAA04245.1; -; mRNA.
DR   PIR; T04471; T04471.
DR   AlphaFoldDB; O48604; -.
DR   SMR; O48604; -.
DR   BRENDA; 1.13.11.27; 2687.
DR   UniPathway; UPA00139; UER00362.
DR   UniPathway; UPA00975; -.
DR   ExpressionAtlas; O48604; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblPlants.
DR   GO; GO:0005506; F:iron ion binding; IEA:EnsemblPlants.
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..434
FT                   /note="4-hydroxyphenylpyruvate dioxygenase"
FT                   /id="PRO_0000088399"
FT   DOMAIN          41..192
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          208..368
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         211
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         379
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   434 AA;  46550 MW;  42DE721182654A4C CRC64;
     MPPTPTTPAA TGAAAAVTPE HARPHRMVRF NPRSDRFHTL SFHHVEFWCA DAASAAGRFA
     FALGAPLAAR SDLSTGNSAH ASQLLRSGSL AFLFTAPYAN GCDAATASLP SFSADAARRF
     SADHGIAVRS VALRVADAAE AFRASRRRGA RPAFAPVDLG RGFAFAEVEL YGDVVLRFVS
     HPDGTDVPFL PGFEGVTNPD AVDYGLTRFD HVVGNVPELA PAAAYIAGFT GFHEFAEFTA
     EDVGTTESGL NSVVLANNSE GVLLPLNEPV HGTKRRSQIQ TFLEHHGGPG VQHIAVASSD
     VLRTLRKMRA RSAMGGFDFL PPPLPKYYEG VRRLAGDVLS EAQIKECQEL GVLVDRDDQG
     VLLQIFTKPV GDRPTLFLEM IQRIGCMEKD ERGEEYQKGG CGGFGKGNFS ELFKSIEDYE
     KSLEAKQSAA VQGS