HPPD_PSEUJ
ID HPPD_PSEUJ Reviewed; 357 AA.
AC P80064;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=4-hydroxyphenylpyruvate dioxygenase;
DE Short=4HPPD;
DE Short=HPD;
DE Short=HPPDase;
DE EC=1.13.11.27;
GN Name=hpd;
OS Pseudomonas sp. (strain P.J. 874).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=72587;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1572351; DOI=10.1111/j.1432-1033.1992.tb16800.x;
RA Rueetschi U., Odelhoeg B., Lindstedt S., Barros-Soederling J., Persson B.,
RA Joernvall H.;
RT "Characterization of 4-hydroxyphenylpyruvate dioxygenase. Primary structure
RT of the Pseudomonas enzyme.";
RL Eur. J. Biochem. 205:459-466(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=10467142; DOI=10.1016/s0969-2126(99)80124-5;
RA Serre L., Sailland A., Sy D., Boudec P., Rolland A., Pebay-Peyroula E.,
RA Cohen-Addad C.;
RT "Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate
RT dioxygenase: an enzyme involved in the tyrosine degradation pathway.";
RL Structure 7:977-988(1999).
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;
CC Note=Binds 1 Fe cation per subunit.;
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 3/6.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the 4HPPD family. {ECO:0000305}.
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DR PIR; S21209; S21209.
DR PDB; 1CJX; X-ray; 2.40 A; A/B/C/D=1-357.
DR PDBsum; 1CJX; -.
DR AlphaFoldDB; P80064; -.
DR SMR; P80064; -.
DR World-2DPAGE; 0008:P80064; -.
DR PRIDE; P80064; -.
DR BioCyc; MetaCyc:MON-12032; -.
DR BRENDA; 1.13.11.27; 5121.
DR UniPathway; UPA00139; UER00362.
DR EvolutionaryTrace; P80064; -.
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:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006572; P:tyrosine catabolic process; 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 3D-structure; Dioxygenase; Direct protein sequencing; Iron; Metal-binding;
KW Oxidoreductase; Phenylalanine catabolism; Repeat; Tyrosine catabolism.
FT CHAIN 1..357
FT /note="4-hydroxyphenylpyruvate dioxygenase"
FT /id="PRO_0000088408"
FT DOMAIN 12..129
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 158..313
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 240
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 322
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT STRAND 10..19
FT /evidence="ECO:0007829|PDB:1CJX"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 36..51
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1CJX"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 74..85
FT /evidence="ECO:0007829|PDB:1CJX"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1CJX"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1CJX"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:1CJX"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:1CJX"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:1CJX"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:1CJX"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:1CJX"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:1CJX"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 303..312
FT /evidence="ECO:0007829|PDB:1CJX"
FT STRAND 319..328
FT /evidence="ECO:0007829|PDB:1CJX"
FT HELIX 334..351
FT /evidence="ECO:0007829|PDB:1CJX"
SQ SEQUENCE 357 AA; 40061 MW; 26CF4A80B1484BD0 CRC64;
ADLYENPMGL MGFEFIELAS PTPNTLEPIF EIMGFTKVAT HRSKDVHLYR QGAINLILNN
EPHSVASYFA AEHGPSVCGM AFRVKDSQKA YKRALELGAQ PIHIETGPME LNLPAIKGIG
GAPLYLIDRF GEGSSIYDID FVFLEGVDRH PVGAGLKIID HLTHNVYRGR MAYWANFYEK
LFNFREIRYF DIKGEYTGLT SKAMTAPDGM IRIPLNEESS KGAGQIEEFL MQFNGEGIQH
VAFLSDDLIK TWDHLKSIGM RFMTAPPDTY YEMLEGRLPN HGEPVGELQA RGILLDGSSE
SGDKRLLLQI FSETLMGPVF FEFIQRKGDD GFGEGNFKAL FESIERDQVR RGVLSTD
