ID   HPPD_PSEAE              Reviewed;         357 AA.
AC   Q9I576;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=4-hydroxyphenylpyruvate dioxygenase;
DE            Short=4HPPD;
DE            Short=HPD;
DE            Short=HPPDase;
DE            EC=1.13.11.27;
GN   Name=hpd; OrderedLocusNames=PA0865;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 3/6.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 4HPPD family. {ECO:0000305}.
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DR   EMBL; AE004091; AAG04254.1; -; Genomic_DNA.
DR   PIR; F83537; F83537.
DR   RefSeq; NP_249556.1; NC_002516.2.
DR   RefSeq; WP_003106569.1; NZ_QZGE01000007.1.
DR   AlphaFoldDB; Q9I576; -.
DR   SMR; Q9I576; -.
DR   STRING; 287.DR97_1078; -.
DR   PaxDb; Q9I576; -.
DR   PRIDE; Q9I576; -.
DR   EnsemblBacteria; AAG04254; AAG04254; PA0865.
DR   GeneID; 882225; -.
DR   KEGG; pae:PA0865; -.
DR   PATRIC; fig|208964.12.peg.899; -.
DR   PseudoCAP; PA0865; -.
DR   HOGENOM; CLU_034004_1_0_6; -.
DR   InParanoid; Q9I576; -.
DR   OMA; DPFPVKG; -.
DR   PhylomeDB; Q9I576; -.
DR   BioCyc; PAER208964:G1FZ6-880-MON; -.
DR   UniPathway; UPA00139; UER00362.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006572; P:tyrosine catabolic process; IBA:GO_Central.
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   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW   Reference proteome; Repeat; Tyrosine catabolism.
FT   CHAIN           1..357
FT                   /note="4-hydroxyphenylpyruvate dioxygenase"
FT                   /id="PRO_0000287741"
FT   DOMAIN          17..137
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          165..316
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         168
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         325
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   357 AA;  39913 MW;  016A5C233DE0E2F9 CRC64;
     MNAVAKIEQH NPIGTDGFEF VEFTAPDAKG IEQLRQLFNM MGFTETAKHR SKEVFLFQQN
     DINIVLNGSP TGHVHEFALK HGPSACAMAF RVKNASQAAA YAESQGAKLV GSHANFGELN
     IPSLEGIGGS LLYLVDRYGD RSIYDVDFEF IEGRSANDNS VGLTYIDHLT HNVKRGQMDV
     WSGFYERIAN FREIRYFDIE GKLTGLFSRA MTAPCGKIRI PINESADDTS QIEEFIREYH
     GEGIQHIALT TDDIYATVRK LRDNGVKFMS TPDTYYEKVD TRVAGHGEPL EQLRELNLLI
     DGAPGDDGIL LQIFTDTVIG PIFFEIIQRK GNQGFGEGNF KALFESIEED QIRRGVI