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 14-DEC-2022, entry version 168. 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}; 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 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 PDB; 7EZQ; X-ray; 1.89 A; A=33-438. DR PDB; 7V6X; X-ray; 1.80 A; A=33-445. DR PDB; 7VC8; X-ray; 1.61 A; A=33-445. DR PDB; 7X5R; X-ray; 1.64 A; A=33-445. DR PDB; 7X5S; X-ray; 1.71 A; A=33-445. DR PDB; 7X5U; X-ray; 1.60 A; A=33-445. DR PDB; 7X5W; X-ray; 1.60 A; A=33-445. DR PDB; 7X5X; X-ray; 2.20 A; A=33-445. DR PDB; 7X5Y; X-ray; 1.50 A; A=33-445. DR PDB; 7X5Z; X-ray; 1.69 A; A=33-445. DR PDB; 7X62; X-ray; 2.00 A; A=33-445. DR PDB; 7X64; X-ray; 2.29 A; A=33-445. DR PDB; 7X65; X-ray; 2.30 A; A=33-445. DR PDB; 7X67; X-ray; 2.00 A; A=33-445. DR PDB; 7X69; X-ray; 1.80 A; A=33-445. DR PDB; 7X6M; X-ray; 1.81 A; A=33-445. DR PDB; 7X6N; X-ray; 1.69 A; A=33-445. DR PDB; 7X8D; X-ray; 1.70 A; A=33-445. DR PDB; 7X8H; X-ray; 1.99 A; A=33-445. DR PDB; 7X8I; X-ray; 2.10 A; A=33-445. 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 PDBsum; 7EZQ; -. DR PDBsum; 7V6X; -. DR PDBsum; 7VC8; -. DR PDBsum; 7X5R; -. DR PDBsum; 7X5S; -. DR PDBsum; 7X5U; -. DR PDBsum; 7X5W; -. DR PDBsum; 7X5X; -. DR PDBsum; 7X5Y; -. DR PDBsum; 7X5Z; -. DR PDBsum; 7X62; -. DR PDBsum; 7X64; -. DR PDBsum; 7X65; -. DR PDBsum; 7X67; -. DR PDBsum; 7X69; -. DR PDBsum; 7X6M; -. DR PDBsum; 7X6N; -. DR PDBsum; 7X8D; -. DR PDBsum; 7X8H; -. DR PDBsum; 7X8I; -. DR AlphaFoldDB; P93836; -. DR SMR; P93836; -. DR STRING; 3702.AT1G06570.1; -. DR BindingDB; P93836; -. DR ChEMBL; CHEMBL2242740; -. DR iPTMnet; P93836; -. DR PaxDb; 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; 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE; 1. DR Pfam; PF00903; Glyoxalase; 1. DR PIRSF; PIRSF009283; HPP_dOase; 1. DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 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 //