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 23-MAY-2018, entry version 145. DE RecName: Full=4-hydroxyphenylpyruvate dioxygenase; DE EC=1.13.11.27; DE AltName: Full=4-hydroxyphenylpyruvic acid oxidase; DE Short=4HPPD; DE Short=HPD; DE Short=HPPDase; GN Name=HPD; Synonyms=PDS1; OrderedLocusNames=At1g06570; GN ORFNames=F12K11.9; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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 RT 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., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA 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., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT 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 RT reference 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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, AND SUBUNIT. 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., RA Steinbacher S.; RT "The crystal structures of Zea mays and Arabidopsis 4- RT hydroxyphenylpyruvate dioxygenase."; RL Plant Physiol. 134:1388-1400(2004). CC -!- CATALYTIC ACTIVITY: 4-hydroxyphenylpyruvate + O(2) = homogentisate CC + CO(2). 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 -!- 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 Self; 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=Translation N-terminally shortened.; 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 UniGene; At.48158; -. DR UniGene; At.71039; -. 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; 5CTO; X-ray; 2.62 A; A/B/C/D=1-445. DR PDB; 5DHW; X-ray; 2.62 A; A/B=1-445. DR PDBsum; 1SP9; -. DR PDBsum; 1SQD; -. DR PDBsum; 1TFZ; -. DR PDBsum; 1TG5; -. DR PDBsum; 5CTO; -. DR PDBsum; 5DHW; -. DR ProteinModelPortal; P93836; -. DR SMR; P93836; -. DR STRING; 3702.AT1G06570.1; -. DR ChEMBL; CHEMBL2242740; -. DR iPTMnet; P93836; -. DR PaxDb; P93836; -. DR PRIDE; P93836; -. 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 eggNOG; COG3185; LUCA. DR InParanoid; P93836; -. DR KO; K00457; -. DR OrthoDB; EOG09360BAR; -. DR PhylomeDB; P93836; -. DR BRENDA; 1.13.11.27; 399. DR Reactome; R-ATH-71182; Phenylalanine and tyrosine catabolism. 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; IEA:UniProtKB-EC. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. 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 Gene3D; 3.10.180.10; -; 2. DR InterPro; IPR005956; 4OHPhenylPyrv_dOase. 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; Complete proteome; Cytoplasm; KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; KW Phenylalanine catabolism; Reference proteome; Repeat; KW Tyrosine catabolism. FT CHAIN 1 445 4-hydroxyphenylpyruvate dioxygenase. FT /FTId=PRO_0000088397. FT DOMAIN 46 192 VOC 1. {ECO:0000255|PROSITE- FT ProRule:PRU01163}. FT DOMAIN 223 383 VOC 2. {ECO:0000255|PROSITE- FT ProRule:PRU01163}. FT METAL 226 226 Iron. {ECO:0000269|PubMed:15301540}. FT METAL 308 308 Iron. {ECO:0000269|PubMed:15301540}. FT METAL 394 394 Iron. {ECO:0000269|PubMed:15301540}. FT STRAND 44 53 {ECO:0000244|PDB:1SQD}. FT HELIX 57 68 {ECO:0000244|PDB:1SQD}. FT STRAND 71 77 {ECO:0000244|PDB:1SQD}. FT HELIX 78 80 {ECO:0000244|PDB:1SQD}. FT STRAND 83 92 {ECO:0000244|PDB:1SQD}. FT STRAND 95 102 {ECO:0000244|PDB:1SQD}. FT HELIX 105 107 {ECO:0000244|PDB:1SQD}. FT TURN 108 110 {ECO:0000244|PDB:1SQD}. FT HELIX 113 115 {ECO:0000244|PDB:1SQD}. FT HELIX 125 135 {ECO:0000244|PDB:1SQD}. FT STRAND 137 147 {ECO:0000244|PDB:1SQD}. FT HELIX 149 158 {ECO:0000244|PDB:1SQD}. FT STRAND 163 170 {ECO:0000244|PDB:1SQD}. FT TURN 171 173 {ECO:0000244|PDB:1SQD}. FT STRAND 174 182 {ECO:0000244|PDB:1SQD}. FT STRAND 185 192 {ECO:0000244|PDB:1SQD}. FT TURN 211 213 {ECO:0000244|PDB:1SQD}. FT STRAND 219 230 {ECO:0000244|PDB:1SQD}. FT HELIX 234 245 {ECO:0000244|PDB:1SQD}. FT STRAND 248 253 {ECO:0000244|PDB:1SQD}. FT STRAND 265 271 {ECO:0000244|PDB:1SQD}. FT STRAND 277 284 {ECO:0000244|PDB:1SQD}. FT STRAND 287 290 {ECO:0000244|PDB:1SP9}. FT HELIX 293 301 {ECO:0000244|PDB:1SQD}. FT STRAND 305 314 {ECO:0000244|PDB:1SQD}. FT HELIX 316 326 {ECO:0000244|PDB:1SQD}. FT HELIX 327 329 {ECO:0000244|PDB:1SQD}. FT HELIX 340 350 {ECO:0000244|PDB:1SQD}. FT TURN 351 353 {ECO:0000244|PDB:1SQD}. FT HELIX 356 365 {ECO:0000244|PDB:1SQD}. FT STRAND 368 371 {ECO:0000244|PDB:1SQD}. FT STRAND 373 382 {ECO:0000244|PDB:1SQD}. FT STRAND 385 389 {ECO:0000244|PDB:1SQD}. FT STRAND 392 400 {ECO:0000244|PDB:1SQD}. FT STRAND 406 408 {ECO:0000244|PDB:1SP9}. FT TURN 414 417 {ECO:0000244|PDB:1SQD}. FT HELIX 423 430 {ECO:0000244|PDB:1SQD}. 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 //