ID HPPD_ARATH STANDARD; PRT; 445 AA. AC P93836; O04330; Q9SHK1; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 2. DT 07-FEB-2006, entry version 46. DE 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) (4HPPD) (HPD) DE (HPPDase) (4-hydroxyphenylpyruvic acide oxidase). GN Name=HPD; OrderedLocusNames=At1g06570; ORFNames=F12K11.9; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; 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 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 [6] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-445, METAL-BINDING SITES, RP 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 [7] 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: Phenylalanine catabolism; third step. CC -!- PATHWAY: Tyrosine catabolism; second step. CC -!- PATHWAY: Prenylquinones biosynthesis. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the 4HPPD family. 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; AF428446; AAL16215.1; -; mRNA. DR EMBL; AY072329; AAL61936.1; -; mRNA. DR EMBL; AY128745; AAM91145.1; -; mRNA. DR PIR; T51585; T51585. DR PDB; 1SP9; X-ray; A/B=1-445. DR PDB; 1SQD; X-ray; A=23-445. DR PDB; 1TFZ; X-ray; A=23-445. DR PDB; 1TG5; X-ray; A=23-445. DR TAIR; At1g06570; -. DR InterPro; IPR005956; 4HPP_dOase. DR InterPro; IPR004360; Glyas_bleo_dOase. DR Pfam; PF00903; Glyoxalase; 1. DR TIGRFAMs; TIGR01263; 4HPPD; 1. KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase; KW Phenylalanine catabolism; Tyrosine catabolism. FT CHAIN 1 445 4-hydroxyphenylpyruvate dioxygenase. FT /FTId=PRO_0000088397. FT METAL 226 226 Iron (By similarity). FT METAL 308 308 Iron (By similarity). FT METAL 394 394 Iron (By similarity). FT DISULFID 401 416 FT STRAND 41 42 FT STRAND 44 53 FT STRAND 55 55 FT HELIX 57 68 FT TURN 69 69 FT STRAND 71 77 FT HELIX 78 80 FT TURN 81 81 FT STRAND 83 92 FT TURN 93 94 FT STRAND 95 102 FT HELIX 105 107 FT TURN 108 110 FT HELIX 113 115 FT STRAND 119 120 FT TURN 121 122 FT HELIX 125 135 FT STRAND 137 147 FT HELIX 149 158 FT TURN 159 160 FT STRAND 163 170 FT TURN 171 173 FT STRAND 174 182 FT TURN 183 184 FT STRAND 185 192 FT TURN 204 205 FT STRAND 207 208 FT TURN 211 213 FT STRAND 219 230 FT STRAND 232 232 FT HELIX 234 245 FT STRAND 248 253 FT STRAND 265 271 FT TURN 273 274 FT STRAND 275 275 FT STRAND 277 284 FT HELIX 293 301 FT TURN 302 302 FT STRAND 303 303 FT STRAND 305 314 FT HELIX 316 329 FT TURN 330 330 FT STRAND 331 331 FT STRAND 334 334 FT HELIX 340 350 FT TURN 351 353 FT STRAND 354 354 FT HELIX 356 365 FT TURN 366 366 FT STRAND 368 371 FT STRAND 373 382 FT STRAND 385 389 FT STRAND 392 400 FT STRAND 402 402 FT STRAND 412 412 FT TURN 414 417 FT STRAND 419 420 FT TURN 421 422 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 //