HPPD_STRAW
ID HPPD_STRAW Reviewed; 381 AA.
AC Q53586; Q93HN6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 145.
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=SAV_5149;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31272 / MA-4848;
RX PubMed=8071207; DOI=10.1128/jb.176.17.5312-5319.1994;
RA Denoya C.D., Skinner D.D., Morgenstern M.R.;
RT "A Streptomyces avermitilis gene encoding a 4-hydroxyphenylpyruvic acid
RT dioxygenase-like protein that directs the production of homogentisic acid
RT and an ochronotic pigment in Escherichia coli.";
RL J. Bacteriol. 176:5312-5319(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), METAL-BINDING SITES, AND SUBUNIT.
RX PubMed=15157070; DOI=10.1021/bi049317s;
RA Brownlee J.M., Johnson-Winters K., Harrison D.H.T., Moran G.R.;
RT "Structure of the ferrous form of (4-hydroxyphenyl)pyruvate dioxygenase
RT from Streptomyces avermitilis in complex with the therapeutic herbicide,
RT NTBC.";
RL Biochemistry 43:6370-6377(2004).
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: Homodimer. {ECO:0000269|PubMed:15157070}.
CC -!- SIMILARITY: Belongs to the 4HPPD family. {ECO:0000305}.
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DR EMBL; U11864; AAA50231.1; -; Genomic_DNA.
DR EMBL; AB070935; BAB69150.1; -; Genomic_DNA.
DR EMBL; BA000030; BAC72861.1; -; Genomic_DNA.
DR RefSeq; WP_010986553.1; NZ_JZJK01000072.1.
DR PDB; 1T47; X-ray; 2.50 A; A/B=1-381.
DR PDBsum; 1T47; -.
DR AlphaFoldDB; Q53586; -.
DR SMR; Q53586; -.
DR STRING; 227882.SAV_5149; -.
DR DrugBank; DB08307; 2-{HYDROXY[2-NITRO-4-(TRIFLUOROMETHYL)PHENYL]METHYLENE}CYCLOHEXANE-1,3-DIONE.
DR PRIDE; Q53586; -.
DR EnsemblBacteria; BAC72861; BAC72861; SAVERM_5149.
DR KEGG; sma:SAVERM_5149; -.
DR eggNOG; COG3185; Bacteria.
DR HOGENOM; CLU_034004_1_1_11; -.
DR OMA; DPFPVKG; -.
DR OrthoDB; 402639at2; -.
DR BRENDA; 1.13.11.27; 5980.
DR SABIO-RK; Q53586; -.
DR UniPathway; UPA00139; UER00362.
DR EvolutionaryTrace; Q53586; -.
DR Proteomes; UP000000428; Chromosome.
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; 2.
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; Iron; Metal-binding; Oxidoreductase;
KW Phenylalanine catabolism; Reference proteome; Repeat; Tyrosine catabolism.
FT CHAIN 1..381
FT /note="4-hydroxyphenylpyruvate dioxygenase"
FT /id="PRO_0000088409"
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 BINDING 270
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 349
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT CONFLICT 40
FT /note="Missing (in Ref. 1; AAA50231)"
FT /evidence="ECO:0000305"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:1T47"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:1T47"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:1T47"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:1T47"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 150..159
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:1T47"
FT HELIX 197..208
FT /evidence="ECO:0007829|PDB:1T47"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:1T47"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:1T47"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:1T47"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:1T47"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1T47"
FT HELIX 303..307
FT /evidence="ECO:0007829|PDB:1T47"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:1T47"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:1T47"
FT HELIX 363..376
FT /evidence="ECO:0007829|PDB:1T47"
SQ SEQUENCE 381 AA; 41863 MW; 4A3B3E7B646165D7 CRC64;
MTQTTHHTPD TARQADPFPV KGMDAVVFAV GNAKQAAHYY STAFGMQLVA YSGPENGSRE
TASYVLTNGS ARFVLTSVIK PATPWGHFLA DHVAEHGDGV VDLAIEVPDA RAAHAYAIEH
GARSVAEPYE LKDEHGTVVL AAIATYGKTR HTLVDRTGYD GPYLPGYVAA APIVEPPAHR
TFQAIDHCVG NVELGRMNEW VGFYNKVMGF TNMKEFVGDD IATEYSALMS KVVADGTLKV
KFPINEPALA KKKSQIDEYL EFYGGAGVQH IALNTGDIVE TVRTMRAAGV QFLDTPDSYY
DTLGEWVGDT RVPVDTLREL KILADRDEDG YLLQIFTKPV QDRPTVFFEI IERHGSMGFG
KGNFKALFEA IEREQEKRGN L
