ID HPPD_DANRE Reviewed; 397 AA.
AC Q6TGZ5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=4-hydroxyphenylpyruvate dioxygenase;
DE EC=1.13.11.27 {ECO:0000250|UniProtKB:P32755};
DE AltName: Full=4-hydroxyphenylpyruvic acid oxidase;
DE Short=4HPPD;
DE Short=HPD;
DE Short=HPPDase;
GN Name=hpd; ORFNames=zgc:56326;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
CC -!- FUNCTION: Catalyzes the conversion of 4-hydroxyphenylpyruvic acid to
CC homogentisic acid, one of the steps in tyrosine catabolism.
CC {ECO:0000250|UniProtKB:P32755}.
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 Evidence={ECO:0000250|UniProtKB:P32755};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16190;
CC Evidence={ECO:0000250|UniProtKB:P32755};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:P32755};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:P32755};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 3/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P32755}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32755}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P32755};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P32755}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:P32755}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P32755}.
CC -!- SIMILARITY: Belongs to the 4HPPD family. {ECO:0000305}.
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DR EMBL; AY398361; AAQ97794.1; -; mRNA.
DR AlphaFoldDB; Q6TGZ5; -.
DR SMR; Q6TGZ5; -.
DR STRING; 7955.ENSDARP00000016115; -.
DR PaxDb; 7955-ENSDARP00000016115; -.
DR AGR; ZFIN:ZDB-GENE-040426-986; -.
DR ZFIN; ZDB-GENE-040426-986; hpda.
DR eggNOG; KOG0638; Eukaryota.
DR InParanoid; Q6TGZ5; -.
DR PhylomeDB; Q6TGZ5; -.
DR UniPathway; UPA00139; UER00362.
DR PRO; PR:Q6TGZ5; -.
DR Proteomes; UP000000437; Genome assembly.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 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; IPR018146; Glyoxalase_1_CS.
DR InterPro; IPR037523; VOC.
DR NCBIfam; TIGR01263; 4HPPD; 1.
DR PANTHER; PTHR11959; 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE; 1.
DR PANTHER; PTHR11959:SF11; 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE; 1.
DR Pfam; PF00903; Glyoxalase; 2.
DR PIRSF; PIRSF009283; HPP_dOase; 1.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR PROSITE; PS51819; VOC; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Dioxygenase; Endoplasmic reticulum; Golgi apparatus; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW Reference proteome; Repeat; Tyrosine catabolism.
FT CHAIN 1..397
FT /note="4-hydroxyphenylpyruvate dioxygenase"
FT /id="PRO_0000088392"
FT DOMAIN 18..149
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 181..339
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 184
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P32755"
FT BINDING 267
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P32755"
FT BINDING 350
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P32755"
SQ SEQUENCE 397 AA; 45211 MW; E689B499A97C8C33 CRC64;
MTSYTDKGEK PERGKFLNFH HIKFWVGNAK QAAVFYCDKF GFEPLAYKGL ETGSREVVSH
AVRQDKIIFV FESALNPGNE EMGEHMIKHG DGVKDVAFLV EDCDFLVKKA KERGAAVLKE
PWVEQDAGGK VKYAIVQTYG DTTHTFVEYL GPYKGLFLPG YKEPLFRDPL LPKLPSGHLS
FIDHIVGNQP DDEMVPVSDW YQKCLLFHRF WSIDDKQIHT EYSALRSIVV TNYEETIKMP
INEPAMGKKK SQIQEYIDYN GGPGVQHIAL NTSNIIQAIV NLRARGLEFL SAPDNYYESL
REKLKTAKIK VKEDLKTLQE LKILVDFDDK GYLLQIFTKP VQDRPTLFLE VIQRNNHFGF
GAGNFKSLFE AIEKDQDARG NLTVLTAQNQ SVSKAFQ
//
