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Database: UniProt
Entry: F1L587_ASCSU
LinkDB: F1L587_ASCSU
Original site: F1L587_ASCSU 
ID   F1L587_ASCSU            Unreviewed;       378 AA.
AC   F1L587;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   13-SEP-2023, entry version 29.
DE   RecName: Full=4-hydroxyphenylpyruvate dioxygenase {ECO:0000256|PIRNR:PIRNR009283};
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY45291.1};
RN   [1] {ECO:0000313|EMBL:ADY45291.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
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   -!- SIMILARITY: Belongs to the 4HPPD family.
CC       {ECO:0000256|ARBA:ARBA00005877, ECO:0000256|PIRNR:PIRNR009283}.
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DR   EMBL; JI171611; ADY45291.1; -; mRNA.
DR   AlphaFoldDB; F1L587; -.
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:SF3; PROTEIN C31H2.4-RELATED; 1.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   PIRSF; PIRSF009283; HPP_dOase; 1.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR   PROSITE; PS51819; VOC; 2.
PE   2: Evidence at transcript level;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR009283-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR009283-1}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          8..135
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   DOMAIN          165..325
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   BINDING         168
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT   BINDING         253
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
FT   BINDING         336
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009283-1"
SQ   SEQUENCE   378 AA;  43506 MW;  AD7A7DE9A0BB129C CRC64;
     MDSANLNAFH HVEFFVSNAQ QAAYWYCISF GFERFAIRKT ISSTSIAIRN GIVKFVFTSF
     AYGNDDYESH IIEHGDNVKD IAFKVDNLDV TVTCILKNGG CLLNAIQTLN DKYGTIKMTA
     ISTKHSDMRH TLIDISNYKG FFLPEFERCD NYSFASKFED IPIDALDHIV ENFPIGALDD
     ITQWYSNTFK LQRFWSIDEK ICHSEFSAMK SMLLTNETHL IQVAIAEPVL NTRRGRSQIQ
     EYIDYNGGPG VQHMALRVSN IISTVQKMKT RGVEFLTVPS SYYDDLEERL KCSKIEVIED
     LKMIRQLNIL IDFDDNGYLL QIFTQPVQDR PTLFIEIIQR YNFYGFGAGN FKALFDAVER
     EQAKRGTLIV DDLPIRHY
//
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