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HPPD_XENTR
ID   HPPD_XENTR              Reviewed;         394 AA.
AC   Q5BKL0;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
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   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-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; BC091035; AAH91035.1; -; mRNA.
DR   RefSeq; NP_001025588.1; NM_001030417.1.
DR   AlphaFoldDB; Q5BKL0; -.
DR   SMR; Q5BKL0; -.
DR   STRING; 8364.ENSXETP00000062603; -.
DR   PaxDb; Q5BKL0; -.
DR   PRIDE; Q5BKL0; -.
DR   DNASU; 594976; -.
DR   Ensembl; ENSXETT00000085370; ENSXETP00000064696; ENSXETG00000007789.
DR   GeneID; 594976; -.
DR   KEGG; xtr:594976; -.
DR   CTD; 594976; -.
DR   Xenbase; XB-GENE-986330; hpd-like.2.
DR   eggNOG; KOG0638; Eukaryota.
DR   HOGENOM; CLU_034004_3_1_1; -.
DR   InParanoid; Q5BKL0; -.
DR   OrthoDB; 1087836at2759; -.
DR   PhylomeDB; Q5BKL0; -.
DR   UniPathway; UPA00139; UER00362.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000007789; Expressed in liver and 7 other tissues.
DR   ExpressionAtlas; Q5BKL0; 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; 2.
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   Cytoplasm; Dioxygenase; Endoplasmic reticulum; Golgi apparatus; Iron;
KW   Membrane; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW   Reference proteome; Repeat; Tyrosine catabolism.
FT   CHAIN           1..394
FT                   /note="4-hydroxyphenylpyruvate dioxygenase"
FT                   /id="PRO_0000088393"
FT   DOMAIN          18..149
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          181..339
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         184
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P32755"
FT   BINDING         267
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P32755"
FT   BINDING         350
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P32755"
SQ   SEQUENCE   394 AA;  44989 MW;  A0347A1DE03EC07C CRC64;
     MTSYTDKGEK HARGRFLSFH HLTFWVGNAK QAASFYCDKF GFEPCAYKGL ETGSRDVVSH
     AIKQDKIIFV FQSPLNPGNQ EMGQHMIKHG DGVKDVAFQV EDCDFLFQKA KDHGAVVVRE
     PWIEEDEGGK VKYAVLQTYG DTTHTLLEYL GPYRGVFLPG YKEPLFRDPL LPTLPSGCLS
     FIDHIVGNQP DNEMVPIVEW YQKCLLFHRF WSVDDKQIHT EYSSLRSIVV TNYEETIKMP
     INEPAAGKKK SQIQEYVDYY GSAGVQHIAL NTSNIIKAVK NLKSRGIEFL SAPDTYYEEL
     RKKLKTAKIT VKEDLNVLQE LKILVDYDDK GYLLQIFTKP MQDRPTLFLE VIQRYNHFGF
     GAGNFKSLFE AIETDQDARG NLTIYAANGE HQVL
 
 
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