LLY_LEGPH
ID LLY_LEGPH Reviewed; 348 AA.
AC Q5ZT84; Q53407;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 99.
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; Synonyms=hpd; OrderedLocusNames=lpg2278;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8112844; DOI=10.1128/iai.62.3.1109-1117.1994;
RA Wintermeyer E., Flugel M., Ott M., Steinert M., Rdest U., Mann K.H.,
RA Hacker J.;
RT "Sequence determination and mutational analysis of the lly locus of
RT Legionella pneumophila.";
RL Infect. Immun. 62:1109-1117(1994).
RN [2]
RP SEQUENCE REVISION TO 94, AND CHARACTERIZATION.
RA Flugel M., Steinert M., Wintermeyer E., Supriyono A., Proksch P.,
RA Hacker J.;
RT "Homogentisic acid is a product of the p-hydroxyphenylpyruvate dioxygenase
RT activity of the Lly-protein, which mediates melanogenesis in Legionella
RT pneumophila.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
CC -!- FUNCTION: Catalyzes the transformation of p-hydroxyphenylpyruvate into
CC HGA. Has hemolytic and brown pigment production activity.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAU28343.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF075724; AAC32843.1; -; Genomic_DNA.
DR EMBL; AE017354; AAU28343.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011216180.1; NC_002942.5.
DR RefSeq; YP_096290.1; NC_002942.5.
DR AlphaFoldDB; Q5ZT84; -.
DR SMR; Q5ZT84; -.
DR STRING; 272624.lpg2278; -.
DR PaxDb; Q5ZT84; -.
DR PRIDE; Q5ZT84; -.
DR EnsemblBacteria; AAU28343; AAU28343; lpg2278.
DR GeneID; 66491406; -.
DR KEGG; lpn:lpg2278; -.
DR PATRIC; fig|272624.6.peg.2395; -.
DR eggNOG; COG3185; Bacteria.
DR HOGENOM; CLU_034004_1_0_6; -.
DR Proteomes; UP000000609; Chromosome.
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 1: Evidence at protein level;
KW Cytolysis; Dioxygenase; Direct protein sequencing; Hemolysis; Iron;
KW Metal-binding; Oxidoreductase; Reference proteome; Repeat; Toxin;
KW Virulence.
FT CHAIN 1..348
FT /note="4-hydroxyphenylpyruvate dioxygenase"
FT /id="PRO_0000088412"
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"
SQ SEQUENCE 348 AA; 38923 MW; DA822AAFB019DB8F CRC64;
MQNNNPCGLD GFAFLEFSGP DRNKLHQQFS EMGFQAVAHH KNQDITLFKQ GEIQFIVNAA
SHCQAEAHAS THGPGACAMG FKVKDAKAAF QHAIAHGGIA FQDAPHANHG LPAIQAIGGS
VIYFVDEEHQ PFSHEWNITS PEPVVGNGLT AIDHLTHNVY RGNMDKWASF YASIFNFQEI
RFFNIKGKMT GLVSRALGSP CGKIKIPLNE SKDDLSQIEE FLHEYHGEGI QHIALNTNDI
YKTVNGLRKQ GVKFLDVPDT YYEMINDRLP WHKEPLNQLH AEKILIDGEA DPKDGLLLQI
FTENIFGPVF FEIIQRKGNQ GFGEGNFQAL FEAIERDQVR RGTLKELS
