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Database: UniProt
Entry: A0A2K5ZNC7_MANLE
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ID   A0A2K5ZNC7_MANLE        Unreviewed;       393 AA.
AC   A0A2K5ZNC7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=4-hydroxyphenylpyruvate dioxygenase {ECO:0000256|ARBA:ARBA00018452, ECO:0000256|PIRNR:PIRNR009283};
GN   Name=HPD {ECO:0000313|Ensembl:ENSMLEP00000029342.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000029342.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000029342.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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_011819872.1; XM_011964482.1.
DR   AlphaFoldDB; A0A2K5ZNC7; -.
DR   STRING; 9568.ENSMLEP00000029342; -.
DR   Ensembl; ENSMLET00000052898.1; ENSMLEP00000029342.1; ENSMLEG00000038880.1.
DR   GeneID; 105527962; -.
DR   KEGG; mleu:105527962; -.
DR   CTD; 3242; -.
DR   GeneTree; ENSGT00530000063474; -.
DR   OMA; DPFPVKG; -.
DR   OrthoDB; 34818at2759; -.
DR   Proteomes; UP000233140; 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   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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140};
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;  44914 MW;  5D7B3F722CDD7710 CRC64;
     MTTYSDKGAK PERGRFLHFH SVTFWVGNAK QAASFYCSKM GFEPLAYRGL ETGSREVVSH
     VIKQGKIVFV LSSALNPWNK EMGDHLVKHG DGVKDIAFEV EDCDYIVQKA RERGAKIVRE
     PWVEQDKFGK VKFAVLQTYG DTTHTLVEKM NYTGQFLPGY EAPVFMDPLL PKLPKCSLEI
     IDHIVGNQPD QEMVSASEWY LKNLQFHRFW SVDDTQVHTE YSSLRSIVVA NYEESIKMPI
     NEPAPGKKKS QIQEYVDYNG GAGVQHIALN TQDIITAIRH LRERGMEFLS VPSTYYKQLR
     EKLKTAKIKV KENIDVLEEL KILVDYDEKG YLLQIFTKPV QDRPTLFLEV IQRHNHQGFG
     AGNFNSLFKA FEEEQNLRGN LTDLETNGVV PGM
//
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