ID   HPPD_TETTH              Reviewed;         404 AA.
AC   Q27203;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
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;
DE   AltName: Full=F-antigen homolog;
DE   AltName: Full=TF-AG;
GN   Name=TFA;
OS   Tetrahymena thermophila.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B1868;
RX   PubMed=1469718; DOI=10.1016/0022-2836(92)90869-l;
RA   Hummel R., Noergaard P., Andreasen P.H., Neve S., Skjoedt K., Tornehave D.,
RA   Kristiansen K.;
RT   "Tetrahymena gene encodes a protein that is homologous with the liver-
RT   specific F-antigen and associated with membranes of the Golgi apparatus and
RT   transport vesicles.";
RL   J. Mol. Biol. 228:850-861(1992).
CC   -!- FUNCTION: Key enzyme in the degradation of tyrosine. {ECO:0000250}.
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; M59429; AAA96492.1; -; Genomic_DNA.
DR   PIR; S27339; S27339.
DR   AlphaFoldDB; Q27203; -.
DR   SMR; Q27203; -.
DR   OMA; DPFPVKG; -.
DR   UniPathway; UPA00139; UER00362.
DR   GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
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..404
FT                   /note="4-hydroxyphenylpyruvate dioxygenase"
FT                   /id="PRO_0000088396"
FT   DOMAIN          28..163
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          194..353
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         197
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         364
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   404 AA;  46046 MW;  48DADC8AEE5D1837 CRC64;
     MSENKDHVVV GYTEKPVGER PTGGKFLGYD HLHFWVGNAK QAAGWYTSRF GFEYYAYKGL
     ETGSREVATH VVRNKQGVTL AFSTPYGNDK DNQREMNQHQ SLHGDGVKDV AFAVEDCHSI
     YNKAIQRGAK CAYPPQDLKD EHGSVTIAAV HTYGEVIHTF IQRNDYKGFF MPGFVAHPLK
     DPLNNVLPDI SYNYVDHIVG NQPDNMMTSA ADWYEKTLDF HRFWSVDDSM IHTEFSSLRS
     IVMTDYDQKI KMPINEPADG KRKSQIQEYI DFYAGPGVQH IALNTSDVIN TVEGLRARGV
     EFLSIPTSYY DNLRKALTAQ TSITVKEDLD VLQKNHILVD YDEKGYLLQI FTKPVEDRPT
     LFYEIIQRNN HQGFGAGNFK SLFVSLELEQ EKRGNLTEIV KNIY