[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. DOI=10.1111/j.1574-6968.2001.tb10818.x; PubMed=11557138 [NCBI, ExPASy, EBI, Israel, Japan] Steinert M., Flugel M., Schuppler M., Helbig J.H., Supriyono A., Proksch P., Lueck P.C.; "The Lly protein is essential for p-hydroxyphenylpyruvate dioxygenase activity in Legionella pneumophila."; FEMS Microbiol. Lett. 203:41-47(2001).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E., Steinert M., Buchrieser C., Hacker J., Heuner K.; "Identification and characterization of a new conjugation/ type IVA secretion system (trb/tra) of L. pneumophila Corby localized on a mobile genomic island."; Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Catalyzes the transformation of p-hydroxyphenylpyruvate into HGA. Has hemolytic and brown pigment production activity.
CATALYTIC ACTIVITY: 4-hydroxyphenylpyruvate + O₂ = homogentisate + CO₂.
COFACTOR: Binds 1 iron ion per subunit (By similarity).
SIMILARITY: Belongs to the 4HPPD family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ001357; CAA04693.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000675; ABQ55683.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001251029.1; -.

3D structure databases

HSSP

P80064; 1CJX. [HSSP ENTRY / PDB]

ModBase

P69053.

Family and domain databases

InterPro

IPR005956; 4OHPhenylPyrv_dOase.
IPR004360; Glyas_bleo-R_dOase.
Graphical view of domain structure.

Pfam

PF00903; Glyoxalase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF009283; HPP_dOase; 1.

TIGRFAMs

TIGR01263; 4HPPD; 1.

BLOCKS

P69053.

Genome annotation databases

GeneID

5181555; -.

GenomeReviews

CP000675_GR; LPC_1747.

KEGG

lpc:LPC_1747; -.

CMR

P69053; LPC_1747.

Other

ProtoNet

P69053.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytolysis; Dioxygenase; Hemolysis; Iron; Metal-binding; Oxidoreductase; Toxin.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 348`	`348`	`4-hydroxyphenylpyruvate dioxygenase.`	`PRO_0000088413`
`METAL`	`154 154`		`Iron (By similarity).`
`METAL`	`232 232`		`Iron (By similarity).`
`METAL`	`312 312`		`Iron (By similarity).`
`CONFLICT`	`94 94`		`I -> S (in Ref. 1; CAA04693).`
`CONFLICT`	`141 141`		`S -> P (in Ref. 1; CAA04693).`
`CONFLICT`	`348 348`		`T -> S (in Ref. 1; CAA04693).`

Sequence information

Length: 348 AA [This is the length of the unprocessed precursor]

Molecular weight: 38927 Da [This is the MW of the unprocessed precursor]

CRC64: F25DE43DDCD749E3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQNNNPCGLD GFAFLEFSGP DRNKLHQQFS EMGFQAVAHH KNQDITLFKQ GEIQFIVNAA 

        70         80         90        100        110        120 
SHCQAEAHAS THGPGACAMG FKVKDAKAAF QHAIAHGGIA FQDAPHANHG LPAIQAIGGS 

       130        140        150        160        170        180 
VIYFVDEEHQ PFSHEWNITS SEPVVGNGLT AIDHLTHNVY RGNMDKWASF YASIFNFQEI 

       190        200        210        220        230        240 
RFFNIKGKMT GLVSRALGSP CGKIKIPLNE SKDDLSQIEE FLHEYHGEGI QHIALNTNDI 

       250        260        270        280        290        300 
YKTVNGLRKQ GVKFLDVPDT YYEMINDRLP WHKEPLNQLH AEKILIDGEA DPKDGLLLQI 

       310        320        330        340 
FTENIFGPVF FEIIQRKGNQ GFGEGNFQAL FEAIERDQVR RGTLKELT

P69053 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools