ID H3B607_LATCH Unreviewed; 395 AA.
AC H3B607;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=4-hydroxyphenylpyruvate dioxygenase {ECO:0000256|ARBA:ARBA00018452, ECO:0000256|PIRNR:PIRNR009283};
GN Name=HPDA {ECO:0000313|Ensembl:ENSLACP00000017328.2};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000017328.2, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000017328.2}
RP IDENTIFICATION.
RG Ensembl;
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 -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004395}.
CC -!- SIMILARITY: Belongs to the 4HPPD family.
CC {ECO:0000256|ARBA:ARBA00005877, ECO:0000256|PIRNR:PIRNR009283}.
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DR EMBL; AFYH01038729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01038730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01038731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01038732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01038733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005992305.1; XM_005992243.2.
DR AlphaFoldDB; H3B607; -.
DR STRING; 7897.ENSLACP00000017328; -.
DR Ensembl; ENSLACT00000017455.2; ENSLACP00000017328.2; ENSLACG00000015263.2.
DR GeneID; 102364955; -.
DR KEGG; lcm:102364955; -.
DR CTD; 394142; -.
DR eggNOG; KOG0638; Eukaryota.
DR GeneTree; ENSGT00530000063474; -.
DR HOGENOM; CLU_034004_3_1_1; -.
DR InParanoid; H3B607; -.
DR OMA; WANFYKD; -.
DR OrthoDB; 34818at2759; -.
DR TreeFam; TF300622; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000015263; Expressed in muscle tissue and 1 other cell type or tissue.
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: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 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR009283-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR009283-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 18..149
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 181..339
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT BINDING 184
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT BINDING 267
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT BINDING 350
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
SQ SEQUENCE 395 AA; 45548 MW; A604CD9E30618531 CRC64;
MTSYTDKGQK PERGRFVKFH HLTFWVGNAK QAAAYYCDKL GFEPLAYKGL ETRSRDVVSH
VLKQDKILFV FQSPLNPGNE EMGEHLIKHG DGVKDVAFQV EDCDFLIQKA RERGAVIVKD
PWVEQDEFGK VKFAVVQTYG DTTHTFIEYQ EPYKGLFLPG YKKPLFQDPL LQHLPPALLS
FIDHIVGNQP DDDMVSVVEW YQKCLFFHRF WSVDDKQVHT EYSALRSIVV TNYEETIKMP
INEPAPGKKK SQIQEYVDYY GGPGVQHIAL NTSNIIQAIV NLKARGMEFL IAPDSYYDQL
REKLKTAKIK VKEDLKKLQE LKILVDFDDK GYLLQIFTKP VQDRPTLFLE VIQRYNHYGF
GAGNFKSLFE AIELDQDARG NLTVYTEDGV SKSFY
//
