HPPD_CAEEL
ID HPPD_CAEEL Reviewed; 393 AA.
AC Q22633;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=4-hydroxyphenylpyruvate dioxygenase;
DE EC=1.13.11.27;
DE AltName: Full=4-hydroxyphenylpyruvic acid oxidase;
DE Short=4HPPD;
DE Short=HPD;
DE Short=HPPDase;
GN Name=hpd-1 {ECO:0000312|WormBase:T21C12.2};
GN ORFNames=T21C12.2 {ECO:0000312|WormBase:T21C12.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18227072; DOI=10.1074/jbc.m708341200;
RA Fisher A.L., Page K.E., Lithgow G.J., Nash L.;
RT "The Caenorhabditis elegans K10C2.4 gene encodes a member of the
RT fumarylacetoacetate hydrolase family: a Caenorhabditis elegans model of
RT type I tyrosinemia.";
RL J. Biol. Chem. 283:9127-9135(2008).
CC -!- FUNCTION: Key enzyme in the degradation of tyrosine. {ECO:0000250,
CC ECO:0000305|PubMed:18227072}.
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 3/6.
CC -!- TISSUE SPECIFICITY: Expressed in the hypodermis and intestine.
CC {ECO:0000269|PubMed:18227072}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown together with fah-1 RNAi
CC rescues the impaired growth and fertility defects in the single fah-1
CC RNAi mutant. {ECO:0000269|PubMed:18227072}.
CC -!- SIMILARITY: Belongs to the 4HPPD family. {ECO:0000305}.
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DR EMBL; BX284603; CAA90315.1; -; Genomic_DNA.
DR PIR; T25063; T25063.
DR RefSeq; NP_499324.1; NM_066923.6.
DR AlphaFoldDB; Q22633; -.
DR SMR; Q22633; -.
DR BioGRID; 41664; 11.
DR STRING; 6239.T21C12.2; -.
DR World-2DPAGE; 0020:Q22633; -.
DR EPD; Q22633; -.
DR PaxDb; Q22633; -.
DR PeptideAtlas; Q22633; -.
DR EnsemblMetazoa; T21C12.2.1; T21C12.2.1; WBGene00001993.
DR GeneID; 176473; -.
DR UCSC; T21C12.2; c. elegans.
DR CTD; 176473; -.
DR WormBase; T21C12.2; CE02347; WBGene00001993; hpd-1.
DR eggNOG; KOG0638; Eukaryota.
DR GeneTree; ENSGT00530000063474; -.
DR HOGENOM; CLU_034004_3_1_1; -.
DR InParanoid; Q22633; -.
DR OMA; DPFPVKG; -.
DR OrthoDB; 1087836at2759; -.
DR PhylomeDB; Q22633; -.
DR Reactome; R-CEL-8963684; Tyrosine catabolism.
DR UniPathway; UPA00139; UER00362.
DR PRO; PR:Q22633; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001993; Expressed in larva and 4 other tissues.
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: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 Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW Reference proteome; Repeat; Tyrosine catabolism.
FT CHAIN 1..393
FT /note="4-hydroxyphenylpyruvate dioxygenase"
FT /id="PRO_0000088395"
FT DOMAIN 17..148
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 179..339
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 182
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 393 AA; 44383 MW; B2D66424ED2CE998 CRC64;
MTTFDKGAKP DIGTFVAFDH VRFVVGNAKQ AAYWYCANFG FEPFAYKGLE TGSRITAQHA
IRQDKIVFIF ESALLPDNSE LGNHLVQHGD GVKDVCFEVE DLDSIIAHAK AAGATIVHDI
TEESDADGSI RYATLRTYGE TDHTLLERKN YRGAFLPGFK AHPMPATFFK TLPRVGLNFL
DHCVGNQPDL QMDSAVQWYE KVLKFHRFWS VDDSMIHTEY SALRSIVVTN FEETIKMPIN
EPATSDKKAI SQIQEYVDYY GGSGVQHIAL NTSDIITAIE ALRARGCEFL SIPSSYYDNL
KERLAASSMV VKEDMDRLQK LHILVDFDEN GYLLQIFSKP CQDRPTLFLE IIQRQNHEGF
GAGNFKALFE SIELEQTKRG NLFYDNVKDG NTK
