HPPD_ARATH
ID HPPD_ARATH Reviewed; 445 AA.
AC P93836; F4IDP1; O04330; Q9SHK1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=4-hydroxyphenylpyruvate dioxygenase;
DE EC=1.13.11.27 {ECO:0000269|PubMed:15301540};
DE AltName: Full=4-hydroxyphenylpyruvic acid oxidase;
DE Short=4HPPD;
DE Short=HPD;
DE Short=HPPDase;
GN Name=HPD; Synonyms=PDS1; OrderedLocusNames=At1g06570; ORFNames=F12K11.9;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Wassilewskija;
RA Bartley G.E., Maxwell C.A., Wittenbach V.A., Scolnik P.A.;
RT "Cloning of an Arabidopsis thaliana cDNA for p-hydroxyphenylpyruvate
RT dioxygenase.";
RL (er) Plant Gene Register PGR97-065(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Norris S.R., Dellapenna D.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=10198110; DOI=10.1104/pp.119.4.1507;
RA Garcia I., Rodgers M., Pepin R., Hsieh T.-F., Matringe M.;
RT "Characterization and subcellular compartmentation of recombinant 4-
RT hydroxyphenylpyruvate dioxygenase from Arabidopsis in transgenic tobacco.";
RL Plant Physiol. 119:1507-1516(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-445 IN COMPLEX WITH IRON,
RP COFACTOR, METAL-BINDING SITES, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15301540; DOI=10.1021/bi049323o;
RA Yang C., Pflugrath J.W., Camper D.L., Foster M.L., Pernich D.J.,
RA Walsh T.A.;
RT "Structural basis for herbicidal inhibitor selectivity revealed by
RT comparison of crystal structures of plant and mammalian 4-
RT hydroxyphenylpyruvate dioxygenases.";
RL Biochemistry 43:10414-10423(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND SUBUNIT.
RX PubMed=15084729; DOI=10.1104/pp.103.034082;
RA Fritze I.M., Linden L., Freigang J., Auerbach G., Huber R., Steinbacher S.;
RT "The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate
RT dioxygenase.";
RL Plant Physiol. 134:1388-1400(2004).
CC -!- FUNCTION: Catalyzes the conversion of 4-hydroxyphenylpyruvic acid to
CC homogentisic acid, one of the steps in tyrosine catabolism.
CC {ECO:0000269|PubMed:15301540}.
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 Evidence={ECO:0000269|PubMed:15301540};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16190;
CC Evidence={ECO:0000305|PubMed:15301540};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:15301540};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:15301540};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 uM for 4-hydroxyphenylpyruvic acid
CC {ECO:0000269|PubMed:15301540};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 3/6.
CC -!- PATHWAY: Cofactor biosynthesis; prenylquinone biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15084729,
CC ECO:0000269|PubMed:15301540}.
CC -!- INTERACTION:
CC P93836; P93836: HPD; NbExp=2; IntAct=EBI-1251387, EBI-1251387;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10198110}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P93836-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the 4HPPD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24813.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U89267; AAB70025.1; -; mRNA.
DR EMBL; AF000228; AAB58404.1; -; mRNA.
DR EMBL; AF047834; AAC15697.1; -; mRNA.
DR EMBL; AC007592; AAF24813.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE28006.2; -; Genomic_DNA.
DR EMBL; AF428446; AAL16215.1; -; mRNA.
DR EMBL; AY072329; AAL61936.1; -; mRNA.
DR EMBL; AY128745; AAM91145.1; -; mRNA.
DR PIR; B86201; B86201.
DR PIR; T51585; T51585.
DR RefSeq; NP_172144.3; NM_100536.4. [P93836-1]
DR PDB; 1SP9; X-ray; 3.00 A; A/B=1-445.
DR PDB; 1SQD; X-ray; 1.80 A; A=23-445.
DR PDB; 1TFZ; X-ray; 1.80 A; A=23-445.
DR PDB; 1TG5; X-ray; 1.90 A; A=23-445.
DR PDB; 5XGK; X-ray; 2.80 A; A/B/C/D=1-445.
DR PDB; 5YWG; X-ray; 2.60 A; A/B=1-445.
DR PDB; 5YWH; X-ray; 2.72 A; A/B=1-445.
DR PDB; 5YWI; X-ray; 2.58 A; A=32-445.
DR PDB; 5YWK; X-ray; 2.80 A; A/B=1-445.
DR PDB; 5YY6; X-ray; 2.40 A; A=32-445.
DR PDB; 5YY7; X-ray; 3.30 A; A/B=1-445.
DR PDB; 6ISD; X-ray; 2.40 A; A/B=1-445.
DR PDB; 6J63; X-ray; 2.62 A; A/B/C/D=1-445.
DR PDB; 6JX9; X-ray; 1.80 A; A=1-445.
DR PDB; 6LGT; X-ray; 1.79 A; A=1-445.
DR PDB; 6M6D; X-ray; 1.84 A; A=1-445.
DR PDB; 7CJK; X-ray; 1.70 A; A=1-445.
DR PDB; 7CQR; X-ray; 1.95 A; A=35-436.
DR PDB; 7CQS; X-ray; 2.00 A; A=35-435.
DR PDB; 7E0X; X-ray; 1.89 A; A=35-439.
DR PDBsum; 1SP9; -.
DR PDBsum; 1SQD; -.
DR PDBsum; 1TFZ; -.
DR PDBsum; 1TG5; -.
DR PDBsum; 5XGK; -.
DR PDBsum; 5YWG; -.
DR PDBsum; 5YWH; -.
DR PDBsum; 5YWI; -.
DR PDBsum; 5YWK; -.
DR PDBsum; 5YY6; -.
DR PDBsum; 5YY7; -.
DR PDBsum; 6ISD; -.
DR PDBsum; 6J63; -.
DR PDBsum; 6JX9; -.
DR PDBsum; 6LGT; -.
DR PDBsum; 6M6D; -.
DR PDBsum; 7CJK; -.
DR PDBsum; 7CQR; -.
DR PDBsum; 7CQS; -.
DR PDBsum; 7E0X; -.
DR AlphaFoldDB; P93836; -.
DR SMR; P93836; -.
DR STRING; 3702.AT1G06570.1; -.
DR BindingDB; P93836; -.
DR ChEMBL; CHEMBL2242740; -.
DR iPTMnet; P93836; -.
DR PaxDb; P93836; -.
DR PRIDE; P93836; -.
DR ProteomicsDB; 230267; -. [P93836-1]
DR EnsemblPlants; AT1G06570.1; AT1G06570.1; AT1G06570. [P93836-1]
DR GeneID; 837168; -.
DR Gramene; AT1G06570.1; AT1G06570.1; AT1G06570. [P93836-1]
DR KEGG; ath:AT1G06570; -.
DR Araport; AT1G06570; -.
DR eggNOG; KOG0638; Eukaryota.
DR HOGENOM; CLU_034004_1_1_1; -.
DR InParanoid; P93836; -.
DR OMA; DPFPVKG; -.
DR OrthoDB; 1087836at2759; -.
DR PhylomeDB; P93836; -.
DR BRENDA; 1.13.11.27; 399.
DR SABIO-RK; P93836; -.
DR UniPathway; UPA00139; UER00362.
DR UniPathway; UPA00975; -.
DR EvolutionaryTrace; P93836; -.
DR PRO; PR:P93836; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P93836; baseline and differential.
DR Genevisible; P93836; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
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; 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; Alternative splicing; Cytoplasm; Dioxygenase; Iron;
KW Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW Reference proteome; Repeat; Tyrosine catabolism.
FT CHAIN 1..445
FT /note="4-hydroxyphenylpyruvate dioxygenase"
FT /id="PRO_0000088397"
FT DOMAIN 46..192
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 223..383
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:15301540"
FT BINDING 308
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:15301540"
FT BINDING 394
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:15301540"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:7CJK"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:7CJK"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:7CJK"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:7CJK"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:7CJK"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 137..147
FT /evidence="ECO:0007829|PDB:7CJK"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:7CJK"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:7CJK"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 219..230
FT /evidence="ECO:0007829|PDB:7CJK"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 264..271
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:5YWI"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:6JX9"
FT HELIX 293..301
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 305..314
FT /evidence="ECO:0007829|PDB:7CJK"
FT HELIX 316..325
FT /evidence="ECO:0007829|PDB:7CJK"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:7CJK"
FT HELIX 340..344
FT /evidence="ECO:0007829|PDB:7CJK"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:7CJK"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:7CJK"
FT HELIX 356..365
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 373..382
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 392..400
FT /evidence="ECO:0007829|PDB:7CJK"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:1SP9"
FT TURN 414..417
FT /evidence="ECO:0007829|PDB:7CJK"
FT HELIX 422..430
FT /evidence="ECO:0007829|PDB:7CJK"
FT HELIX 431..435
FT /evidence="ECO:0007829|PDB:7CJK"
SQ SEQUENCE 445 AA; 48816 MW; FD0442F93556B3F5 CRC64;
MGHQNAAVSE NQNHDDGAAS SPGFKLVGFS KFVRKNPKSD KFKVKRFHHI EFWCGDATNV
ARRFSWGLGM RFSAKSDLST GNMVHASYLL TSGDLRFLFT APYSPSLSAG EIKPTTTASI
PSFDHGSCRS FFSSHGLGVR AVAIEVEDAE SAFSISVANG AIPSSPPIVL NEAVTIAEVK
LYGDVVLRYV SYKAEDTEKS EFLPGFERVE DASSFPLDYG IRRLDHAVGN VPELGPALTY
VAGFTGFHQF AEFTADDVGT AESGLNSAVL ASNDEMVLLP INEPVHGTKR KSQIQTYLEH
NEGAGLQHLA LMSEDIFRTL REMRKRSSIG GFDFMPSPPP TYYQNLKKRV GDVLSDDQIK
ECEELGILVD RDDQGTLLQI FTKPLGDRPT IFIEIIQRVG CMMKDEEGKA YQSGGCGGFG
KGNFSELFKS IEEYEKTLEA KQLVG
