ID   LLY_LEGPC               Reviewed;         348 AA.
AC   P69053; A5IE83; Q53407;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=4-hydroxyphenylpyruvate dioxygenase;
DE            Short=4HPPD;
DE            Short=HPD;
DE            Short=HPPDase;
DE            EC=1.13.11.27;
DE   AltName: Full=Legiolysin;
GN   Name=lly; OrderedLocusNames=LPC_1747;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=11557138; DOI=10.1111/j.1574-6968.2001.tb10818.x;
RA   Steinert M., Flugel M., Schuppler M., Helbig J.H., Supriyono A.,
RA   Proksch P., Lueck P.C.;
RT   "The Lly protein is essential for p-hydroxyphenylpyruvate dioxygenase
RT   activity in Legionella pneumophila.";
RL   FEMS Microbiol. Lett. 203:41-47(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transformation of p-hydroxyphenylpyruvate into
CC       HGA. Has hemolytic and brown pigment production activity.
CC       {ECO:0000269|PubMed:11557138}.
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   -!- SIMILARITY: Belongs to the 4HPPD family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ001357; CAA04693.1; -; Genomic_DNA.
DR   EMBL; CP000675; ABQ55683.1; -; Genomic_DNA.
DR   RefSeq; WP_011947137.1; NC_009494.2.
DR   AlphaFoldDB; P69053; -.
DR   SMR; P69053; -.
DR   KEGG; lpc:LPC_1747; -.
DR   HOGENOM; CLU_034004_1_0_6; -.
DR   OMA; DPFPVKG; -.
DR   GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0009072; P:aromatic amino acid family metabolic process; IEA:InterPro.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cytolysis; Dioxygenase; Hemolysis; Iron; Metal-binding; Oxidoreductase;
KW   Repeat; Toxin; Virulence.
FT   CHAIN           1..348
FT                   /note="4-hydroxyphenylpyruvate dioxygenase"
FT                   /id="PRO_0000088413"
FT   DOMAIN          11..141
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          151..303
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         154
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        94
FT                   /note="I -> S (in Ref. 1; CAA04693)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="S -> P (in Ref. 1; CAA04693)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        348
FT                   /note="T -> S (in Ref. 1; CAA04693)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   348 AA;  38927 MW;  F25DE43DDCD749E3 CRC64;
     MQNNNPCGLD GFAFLEFSGP DRNKLHQQFS EMGFQAVAHH KNQDITLFKQ GEIQFIVNAA
     SHCQAEAHAS THGPGACAMG FKVKDAKAAF QHAIAHGGIA FQDAPHANHG LPAIQAIGGS
     VIYFVDEEHQ PFSHEWNITS SEPVVGNGLT AIDHLTHNVY RGNMDKWASF YASIFNFQEI
     RFFNIKGKMT GLVSRALGSP CGKIKIPLNE SKDDLSQIEE FLHEYHGEGI QHIALNTNDI
     YKTVNGLRKQ GVKFLDVPDT YYEMINDRLP WHKEPLNQLH AEKILIDGEA DPKDGLLLQI
     FTENIFGPVF FEIIQRKGNQ GFGEGNFQAL FEAIERDQVR RGTLKELT