HPPD_PIG
ID HPPD_PIG Reviewed; 393 AA.
AC Q02110;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 119.
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;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT THR-2, PARTIAL PROTEIN SEQUENCE,
RP SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=1339442; DOI=10.1016/s0021-9258(18)35755-7;
RA Endo F., Awata H., Tanoue A., Ishiguro M., Eda Y., Titani K., Matsuda I.;
RT "Primary structure deduced from complementary DNA sequence and expression
RT in cultured cells of mammalian 4-hydroxyphenylpyruvic acid dioxygenase.
RT Evidence that the enzyme is a homodimer of identical subunits homologous to
RT rat liver-specific alloantigen F.";
RL J. Biol. Chem. 267:24235-24240(1992).
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:0000269|PubMed:1339442}.
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 -!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:1339442}.
CC -!- SIMILARITY: Belongs to the 4HPPD family. {ECO:0000305}.
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DR EMBL; D13390; BAA02660.1; -; mRNA.
DR PIR; S32821; S32821.
DR AlphaFoldDB; Q02110; -.
DR SMR; Q02110; -.
DR STRING; 9823.ENSSSCP00000010467; -.
DR BindingDB; Q02110; -.
DR ChEMBL; CHEMBL3203; -.
DR DrugCentral; Q02110; -.
DR iPTMnet; Q02110; -.
DR PeptideAtlas; Q02110; -.
DR PRIDE; Q02110; -.
DR eggNOG; KOG0638; Eukaryota.
DR InParanoid; Q02110; -.
DR UniPathway; UPA00139; UER00362.
DR PRO; PR:Q02110; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA: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.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Dioxygenase; Direct protein sequencing;
KW Endoplasmic reticulum; Golgi apparatus; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Phenylalanine catabolism; Phosphoprotein;
KW Reference proteome; Repeat; Tyrosine catabolism.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1339442"
FT CHAIN 2..393
FT /note="4-hydroxyphenylpyruvate dioxygenase"
FT /id="PRO_0000088390"
FT DOMAIN 18..152
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 180..338
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 183
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P32755"
FT BINDING 266
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P32755"
FT BINDING 349
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P32755"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:1339442"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32754"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49429"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49429"
SQ SEQUENCE 393 AA; 45064 MW; C1A1D42EB2600182 CRC64;
MTSYSDKGEK PERGRFLHFH SVTFWVGNAK QAASYYCSKI GFEPLAYKGL ETGSREVVSH
VVKQDKIVFV FSSALNPWNK EMGDHLVKHG DGVKDIAFEV EDCDYIVQKA RERGAIIVRE
EVCCAADVRG HHTPLDRARQ VWEGTLVEKM TFCLDSRPQP SQTLLHRLLL SKLPKCGLEI
IDHIVGNQPD QEMESASQWY MRNLQFHRFW SVDDTQIHTE YSALRSVVMA NYEESIKMPI
NEPAPGKKKS QIQEYVDYNG GAGVQHIALK TEDIITAIRS LRERGVEFLA VPFTYYKQLQ
EKLKSAKIRV KESIDVLEEL KILVDYDEKG YLLQIFTKPM QDRPTVFLEV IQRNNHQGFG
AGNFNSLFKA FEEEQELRGN LTDTDPNGVP FRL
