ID HPPD_ARATH STANDARD; PRT; 445 AA. AC P93836; O04330; Q9SHK1; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-MAY-2005 (Rel. 47, Last annotation update) DE 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) (4HPPD) (HPD) DE (HPPDase). 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 eudicots; rosids; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE. 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. 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, AND SUBCELLULAR LOCATION. RC STRAIN=cv. Columbia; RX PubMed=10198110; 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). CC -!- CATALYTIC ACTIVITY: 4-hydroxyphenylpyruvate + O(2) = homogentisate CC + CO(2). CC -!- COFACTOR: Iron (By similarity). CC -!- PATHWAY: Phenylalanine catabolism; third step. CC -!- PATHWAY: Tyrosine catabolism; second step. CC -!- PATHWAY: Prenylquinones biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. 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 InterPro; IPR005956; 4-OHPPdiox. DR InterPro; IPR004360; Gly_bleo_diox. DR Pfam; PF00903; Glyoxalase; 1. DR TIGRFAMs; TIGR01263; 4HPPD; 1. KW 3D-structure; Dioxygenase; Iron; Oxidoreductase; KW Phenylalanine catabolism; Tyrosine catabolism. 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 //