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-OCT-2012, entry version 106. 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; core eudicotyledons; 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. 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 MEDLINE=21016719; 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; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; 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: Binds 1 iron ion per subunit. 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. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-1251387, EBI-1251387; CC -!- SUBCELLULAR LOCATION: Cytoplasm. 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. CC -!- SEQUENCE CAUTION: CC Sequence=AAF24813.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC Sequence=AEE28006.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; 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; AEE28006.1; ALT_INIT; Genomic_DNA. DR EMBL; AF428446; AAL16215.1; -; mRNA. DR EMBL; AY072329; AAL61936.1; -; mRNA. DR EMBL; AY128745; AAM91145.1; -; mRNA. DR IPI; IPI00531512; -. DR PIR; B86201; B86201. DR PIR; T51585; T51585. DR RefSeq; NP_172144.2; NM_100536.3. 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 PDBsum; 1SP9; -. DR PDBsum; 1SQD; -. DR PDBsum; 1TFZ; -. DR PDBsum; 1TG5; -. DR ProteinModelPortal; P93836; -. DR SMR; P93836; 35-431. DR STRING; P93836; -. DR PRIDE; P93836; -. DR GeneID; 837168; -. DR KEGG; ath:AT1G06570; -. DR TAIR; At1g06570; -. DR eggNOG; COG3185; -. DR InParanoid; P93836; -. DR KO; K00457; -. DR OMA; LDTPDSY; -. DR PhylomeDB; P93836; -. DR ProtClustDB; PLN02875; -. DR BRENDA; 1.13.11.27; 399. DR UniPathway; UPA00139; UER00362. DR UniPathway; UPA00975; -. DR EvolutionaryTrace; P93836; -. DR Genevestigator; P93836; -. DR GermOnline; AT1G06570; Arabidopsis thaliana. DR GO; GO:0009507; C:chloroplast; NAS:TAIR. DR GO; GO:0005829; C:cytosol; IDA:TAIR. DR GO; GO:0005739; C:mitochondrion; IDA:TAIR. DR GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; IDA:TAIR. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016117; P:carotenoid biosynthetic process; IMP:TAIR. DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-KW. DR GO; GO:0010236; P:plastoquinone biosynthetic process; IMP:TAIR. DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW. DR GO; GO:0010189; P:vitamin E biosynthetic process; IMP:TAIR. DR InterPro; IPR005956; 4OHPhenylPyrv_dOase. DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom. DR PANTHER; PTHR11959; PTHR11959; 1. DR Pfam; PF00903; Glyoxalase; 1. DR PIRSF; PIRSF009283; HPP_dOase; 1. DR TIGRFAMs; TIGR01263; 4HPPD; 1. 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; Tyrosine catabolism. FT CHAIN 1 445 4-hydroxyphenylpyruvate dioxygenase. FT /FTId=PRO_0000088397. FT METAL 226 226 Iron. FT METAL 308 308 Iron. FT METAL 394 394 Iron. FT STRAND 44 53 FT HELIX 57 68 FT STRAND 71 77 FT HELIX 78 80 FT STRAND 83 92 FT STRAND 95 102 FT HELIX 105 107 FT TURN 108 110 FT HELIX 113 115 FT HELIX 125 135 FT STRAND 137 147 FT HELIX 149 158 FT STRAND 163 170 FT TURN 171 173 FT STRAND 174 182 FT STRAND 185 192 FT TURN 211 213 FT STRAND 219 230 FT HELIX 234 245 FT STRAND 248 253 FT STRAND 265 271 FT STRAND 277 284 FT STRAND 287 290 FT HELIX 293 301 FT STRAND 305 314 FT HELIX 316 326 FT HELIX 327 329 FT HELIX 340 350 FT TURN 351 353 FT HELIX 356 365 FT STRAND 368 371 FT STRAND 373 382 FT STRAND 385 389 FT STRAND 392 400 FT STRAND 406 408 FT TURN 414 417 FT HELIX 423 430 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 //