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   25-NOV-2008, entry version 22.
DE   RecName: Full=4-hydroxyphenylpyruvate dioxygenase;
DE            Short=HPPDase;
DE            Short=4HPPD;
DE            Short=HPD;
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].
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S.,
RA   Schunder E., 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
RT   mobile genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transformation of p-hydroxyphenylpyruvate
CC       into HGA. Has hemolytic and brown pigment production activity.
CC   -!- CATALYTIC ACTIVITY: 4-hydroxyphenylpyruvate + O(2) = homogentisate
CC       + CO(2).
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the 4HPPD family.
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DR   EMBL; AJ001357; CAA04693.1; -; Genomic_DNA.
DR   EMBL; CP000675; ABQ55683.1; -; Genomic_DNA.
DR   RefSeq; YP_001251029.1; -.
DR   HSSP; P80064; 1CJX.
DR   GeneID; 5181555; -.
DR   GenomeReviews; CP000675_GR; LPC_1747.
DR   KEGG; lpc:LPC_1747; -.
DR   GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009072; P:aromatic amino acid family metabolic process; IEA:InterPro.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0019836; P:hemolysis by symbiont of host red blood cells; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR005956; 4OHPhenylPyrv_dOase.
DR   InterPro; IPR004360; Glyas_bleo-R_dOase.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   PIRSF; PIRSF009283; HPP_dOase; 1.
DR   TIGRFAMs; TIGR01263; 4HPPD; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytolysis; Dioxygenase; Hemolysis; Iron;
KW   Metal-binding; Oxidoreductase; Toxin.
FT   CHAIN         1    348       4-hydroxyphenylpyruvate dioxygenase.
FT                                /FTId=PRO_0000088413.
FT   METAL       154    154       Iron (By similarity).
FT   METAL       232    232       Iron (By similarity).
FT   METAL       312    312       Iron (By similarity).
FT   CONFLICT     94     94       I -> S (in Ref. 1; CAA04693).
FT   CONFLICT    141    141       S -> P (in Ref. 1; CAA04693).
FT   CONFLICT    348    348       T -> S (in Ref. 1; CAA04693).
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
//