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 02-SEP-2026, 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; OS Pseudomonas sp. (strain P.J. 874). OC Bacteria; Pseudomonadati; Pseudomonadota. 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 = homogentisate + CO2; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PIR; S21209; S21209. DR PDB; 1CJX; X-ray; 2.40 A; A/B/C/D=1-357. DR AlphaFoldDB; P80064; -. DR SMR; P80064; -. DR BioCyc; MetaCyc:MONOMER-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:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006572; P:L-tyrosine catabolic process; IEA:TreeGrafter. DR CDD; cd07250; HPPD_C_like; 1. DR CDD; cd08342; HPPD_N_like; 1. DR FunFam; 3.10.180.10:FF:000007; 4-hydroxyphenylpyruvate dioxygenase; 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_core. 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. DR PDBsum; 1CJX; -. 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 263..267 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 //