ID A0A3Q7UN83_VULVU Unreviewed; 393 AA.
AC A0A3Q7UN83;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=4-hydroxyphenylpyruvate dioxygenase {ECO:0000256|ARBA:ARBA00018452, ECO:0000256|PIRNR:PIRNR009283};
GN Name=HPD {ECO:0000313|RefSeq:XP_025874672.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025874672.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025874672.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025874672.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025874672.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the conversion of 4-hydroxyphenylpyruvic acid to
CC homogentisic acid, one of the steps in tyrosine catabolism.
CC {ECO:0000256|ARBA:ARBA00033727}.
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:0000256|ARBA:ARBA00033692};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16190;
CC Evidence={ECO:0000256|ARBA:ARBA00033692};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|PIRSR:PIRSR009283-1};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000256|PIRSR:PIRSR009283-1};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 3/6.
CC {ECO:0000256|ARBA:ARBA00005162}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}. Golgi
CC apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane
CC protein {ECO:0000256|ARBA:ARBA00004395}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the 4HPPD family.
CC {ECO:0000256|ARBA:ARBA00005877, ECO:0000256|PIRNR:PIRNR009283}.
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DR RefSeq; XP_025874672.1; XM_026018887.1.
DR AlphaFoldDB; A0A3Q7UN83; -.
DR STRING; 9627.ENSVVUP00000022802; -.
DR KEGG; vvp:112935237; -.
DR OrthoDB; 34818at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
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; IPR037523; VOC.
DR NCBIfam; TIGR01263; 4HPPD; 1.
DR PANTHER; PTHR11959; 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE; 1.
DR PANTHER; PTHR11959:SF12; 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 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Dioxygenase {ECO:0000313|RefSeq:XP_025874672.1};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR009283-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR009283-1};
KW Oxidoreductase {ECO:0000313|RefSeq:XP_025874672.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 18..149
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 180..338
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT BINDING 183
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT BINDING 266
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT BINDING 349
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
SQ SEQUENCE 393 AA; 44824 MW; 095B4F62EFE7F8CC CRC64;
MTTYSDKGKK PERGRFLHFH SVTFWVGNAK QAASFYCNKM GFEPLAYKGL ETGSREVVSH
VIKQGKIVFV FSSALNPWNK EMGDHLVKHG DGVKDIAFEV EDCDYIVQKA REQGAKIVRE
PWIEEDKFGK VKLAVLQTYG DTTHTLVEKM NYTGRFLPGF EAPACVDPLL SKLPSCSLEI
IDHIVGNQPD QEMVSASEWY LKNLQFHRFW SVDDTQVHTE YSSLRSIVVA NYEESIKMPI
NEPAPGKKKS QIQEYVDYNG GAGVQHIALK TQDIITAIRH LRDRGMEFLA VPSTYYKQLR
EKLKSAKIQV KESIDVLEEL KILVDYDEKG YLLQIFTKPM QDRPTLFLEV IQRHNHQGFG
AGNFNSLFKA FEEEQDLRGN LTDLETNGTM PGM
//
