ID   HPPD_ZYMTR              Reviewed;         419 AA.
AC   O42764;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=4-hydroxyphenylpyruvate dioxygenase;
DE            Short=4HPPD;
DE            Short=HPD;
DE            Short=HPPDase;
DE            EC=1.13.11.27;
GN   Name=HPPD;
OS   Zymoseptoria tritici (Speckled leaf blotch fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047171;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LAST93;
RX   PubMed=9570125; DOI=10.1111/j.1574-6968.1998.tb12966.x;
RA   Keon J.P.R., Hargreaves J.A.;
RT   "Isolation and heterologous expression of a gene encoding 4-
RT   hydroxyphenylpyruvate dioxygenase from the wheat leaf-spot pathogen,
RT   Mycosphaerella graminicola.";
RL   FEMS Microbiol. Lett. 161:337-343(1998).
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   -!- SIMILARITY: Belongs to the 4HPPD family. {ECO:0000305}.
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DR   EMBL; AF038152; AAC15884.1; -; Genomic_DNA.
DR   AlphaFoldDB; O42764; -.
DR   SMR; O42764; -.
DR   VEuPathDB; FungiDB:ZT3D1_G6039; -.
DR   VEuPathDB; FungiDB:ZTRI_5.480; -.
DR   OMA; FRPIAYR; -.
DR   UniPathway; UPA00139; UER00362.
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   3: Inferred from homology;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW   Repeat; Tyrosine catabolism.
FT   CHAIN           1..419
FT                   /note="4-hydroxyphenylpyruvate dioxygenase"
FT                   /id="PRO_0000088405"
FT   DOMAIN          41..187
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          218..376
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         221
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         304
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   419 AA;  46740 MW;  07951CCE0CB50EE3 CRC64;
     MAPGALLVTS QNGRTSPLYD SDGYVPAPAA LVVGGEVNYR GYHHAEWWVG NAKQVAQFYI
     TRMGFEPVAH KGLETGSRFF ASHVVQNNGV RFVFTSPVRS SARQTLKAAP LADQARLDEM
     YDHLDKHGDG VKDVAFEVDD VLAVYENAVA NGAESVSSPH TDSCDEGDVI SAAIKTYGDT
     THTFIQRTTY TGPFLPGYRS CTTVDSANKF LPPVNLEAID HCVGNQDWDE MSDACDFYER
     CLGFHRFWSV DDKDICTEFS ALKSIVMSSP NQVVKMPINE PAHGKKKSQI EEYVDFYNGP
     GVQHIALRTP NIIEAVSNLR SRGVEFISVP DTYYENMRLR LKAAGMKLEE SFDIIQKLNI
     LIDFDEGGYL LQLFTKPLMD RPTVFIEIIQ RNNFDGFGAG NFKSLFEAIE REQDLRGNL