ID   HPPD_STRCO              Reviewed;         381 AA.
AC   Q9S2F4;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=SCO2927; ORFNames=SCE19A.27c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 4HPPD family. {ECO:0000305}.
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DR   EMBL; AL939114; CAB51008.1; -; Genomic_DNA.
DR   PIR; T36150; T36150.
DR   RefSeq; NP_627153.1; NC_003888.3.
DR   RefSeq; WP_003975883.1; NZ_VNID01000010.1.
DR   AlphaFoldDB; Q9S2F4; -.
DR   SMR; Q9S2F4; -.
DR   STRING; 100226.SCO2927; -.
DR   GeneID; 1098360; -.
DR   KEGG; sco:SCO2927; -.
DR   PATRIC; fig|100226.15.peg.2985; -.
DR   eggNOG; COG3185; Bacteria.
DR   HOGENOM; CLU_034004_1_1_11; -.
DR   InParanoid; Q9S2F4; -.
DR   OMA; DPFPVKG; -.
DR   PhylomeDB; Q9S2F4; -.
DR   UniPathway; UPA00139; UER00362.
DR   Proteomes; UP000001973; 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; 2.
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..381
FT                   /note="4-hydroxyphenylpyruvate dioxygenase"
FT                   /id="PRO_0000088410"
FT   DOMAIN          22..156
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          184..338
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         187
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         349
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   381 AA;  41876 MW;  326B241FF9BAC49E CRC64;
     MTQTTHHTPD TARQADPFPV KGMDAVVFAV GNAKQAAHYY STAFGMKLVA YSGPENGSRE
     TASYVLESGS ARFVFTSVIK PSTDWGTFLA QHVAEHGDGV VDLAIEVPDA RAAHAYAVEH
     GARSLAEPHE VKDEHGTVVL AAIATYGETR HTLVERTGYD GPYLPGYVAA KPMVAPPAQR
     VFQAVDHCVG NVELGRMNEW VGFYNKVMGF TNMKEFVGDD IATEYSALMS KVVADGTLKV
     KFPINEPAIA KKKSQIDEYL EFYGGAGVQH IALNTNDIVA TVRAMRAAGV EFLDTPDSYY
     DTLGEWAGET RVPVDVLREL KILVDRDEDG YLLQIFTKPV QDRPTVFFEM IERHGSMGFG
     KGNFKALFEA IEREQEKRGN L