HPPD_BOVIN
ID HPPD_BOVIN Reviewed; 393 AA.
AC Q5EA20;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 115.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Rumen reticulum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; BT020749; AAX08766.1; -; mRNA.
DR EMBL; BC105225; AAI05226.1; -; mRNA.
DR RefSeq; NP_001015611.1; NM_001015611.1.
DR AlphaFoldDB; Q5EA20; -.
DR SMR; Q5EA20; -.
DR STRING; 9913.ENSBTAP00000005469; -.
DR PaxDb; Q5EA20; -.
DR PeptideAtlas; Q5EA20; -.
DR Ensembl; ENSBTAT00000005469; ENSBTAP00000005469; ENSBTAG00000004175.
DR GeneID; 516058; -.
DR KEGG; bta:516058; -.
DR CTD; 3242; -.
DR VEuPathDB; HostDB:ENSBTAG00000004175; -.
DR VGNC; VGNC:29939; HPD.
DR eggNOG; KOG0638; Eukaryota.
DR GeneTree; ENSGT00530000063474; -.
DR HOGENOM; CLU_034004_3_1_1; -.
DR InParanoid; Q5EA20; -.
DR OMA; DPFPVKG; -.
DR OrthoDB; 1087836at2759; -.
DR TreeFam; TF300622; -.
DR UniPathway; UPA00139; UER00362.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000004175; Expressed in liver and 65 other tissues.
DR ExpressionAtlas; Q5EA20; baseline and differential.
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; 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.
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 Acetylation; Cytoplasm; Dioxygenase; Endoplasmic reticulum;
KW Golgi apparatus; Iron; Membrane; Metal-binding; Oxidoreductase;
KW Phenylalanine catabolism; Phosphoprotein; Reference proteome; Repeat;
KW Tyrosine catabolism.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P32754"
FT CHAIN 2..393
FT /note="4-hydroxyphenylpyruvate dioxygenase"
FT /id="PRO_0000088387"
FT DOMAIN 18..149
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:0000250|UniProtKB:P32754"
FT MOD_RES 132
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49429"
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; 44963 MW; 03036A1CD0B7BBD1 CRC64;
MTTYSDKGEK PERGRFLHFH SVTFWVGNAK QAASYYCSKL GFEPLAYKGL ETGSREVVSH
VVKQGQIVFV FSSALNPWNK EMGDHLVKHG DGVKDIAFEV EDCDYIVQKA RERGAKIVRE
PWVEQDKLGK VKFAVLQTYG DTTHTLVEKM NYTGRFLPGF EAPPFMDPQL SKLPSCSLEI
IDHIVGNQPD QEMVSASEWY LKNLQFHRFW SVDDTQVHTE YSSLRSVVVA NYEESIKMPI
NEPAPGKKKS QIQEYVDYNG GAGVQHIALK TKDIITAIRH LRERGVEFLA VPSTYYKQLR
EKLKMAKIRV KENIDILEEL KILVDYDEKG YLLQIFTKPM QDRPTLFLEV IQRHNHQGFG
AGNFNSLFKA FEEEQDLRGN LTDMEPNGVV SGM
