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 27-MAR-2024, entry version 118.
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; Pseudomonadota; 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; 208964.PA0865; -.
DR PaxDb; 208964-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 OrthoDB; 9780241at2; -.
DR PhylomeDB; Q9I576; -.
DR BioCyc; PAER208964:G1FZ6-880-MONOMER; -.
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; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 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 NCBIfam; TIGR01263; 4HPPD; 1.
DR PANTHER; PTHR11959; 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE; 1.
DR PANTHER; PTHR11959:SF1; 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE; 1.
DR Pfam; PF00903; Glyoxalase; 1.
DR Pfam; PF14696; Glyoxalase_5; 1.
DR PIRSF; PIRSF009283; HPP_dOase; 1.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 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
//
