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UniProtKB/Swiss-Prot entry P93836


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HPPD_ARATH
Primary accession number P93836
Secondary accession numbers O04330 Q9SHK1
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on January 1, 1998 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 70)
Name and origin of the protein
Protein name 4-hydroxyphenylpyruvate dioxygenase
Synonyms EC 1.13.11.27
4-hydroxyphenylpyruvic acid oxidase
HPPDase
4HPPD
HPD
Gene name
Name: HPD
OrderedLocusNames: At1g06570
ORFNames: F12K11.9
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Wassilewskija;
Bartley G.E., Maxwell C.A., Wittenbach V.A., Scolnik P.A.;
"Cloning of an Arabidopsis thaliana cDNA for p-hydroxyphenylpyruvate dioxygenase.";
(er) Plant Gene Register PGR97-065.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Norris S.R., Dellapenna D.;
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
DOI=10.1104/pp.119.4.1507; PubMed=10198110 [NCBI, ExPASy, EBI, Israel, Japan]
Garcia I., Rodgers M., Pepin R., Hsieh T.-F., Matringe M.;
"Characterization and subcellular compartmentation of recombinant 4-hydroxyphenylpyruvate dioxygenase from Arabidopsis in transgenic tobacco.";
Plant Physiol. 119:1507-1516(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[6]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-445, METAL-BINDING SITES, AND SUBUNIT.
DOI=10.1021/bi049323o; PubMed=15301540 [NCBI, ExPASy, EBI, Israel, Japan]
Yang C., Pflugrath J.W., Camper D.L., Foster M.L., Pernich D.J., Walsh T.A.;
"Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases.";
Biochemistry 43:10414-10423(2004).
[7]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND SUBUNIT.
DOI=10.1104/pp.103.034082; PubMed=15084729 [NCBI, ExPASy, EBI, Israel, Japan]
Fritze I.M., Linden L., Freigang J., Auerbach G., Huber R., Steinbacher S.;
"The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase.";
Plant Physiol. 134:1388-1400(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U89267; AAB70025.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF000228; AAB58404.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF047834; AAC15697.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC007592; AAF24813.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF428446; AAL16215.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY072329; AAL61936.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128745; AAM91145.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B86201; B86201.
T51585; T51585.
UniGene At.48158
3D structure databases
PDB
1SP9; X-ray; 3.00 A; A/B=1-445.[ExPASy / RCSB / EBI]
1SQD; X-ray; 1.80 A; A=23-445.[ExPASy / RCSB / EBI]
1TFZ; X-ray; 1.80 A; A=23-445.[ExPASy / RCSB / EBI]
1TG5; X-ray; 1.90 A; A=23-445.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1SP9; -.
1SQD; -.
1TFZ; -.
1TG5; -.
ModBase P93836.
Protein-protein interaction databases
IntAct P93836; -.
Organism-specific databases
TAIR At1g06570; -.
Gene expression databases
GermOnline AT1G06570; Arabidopsis thaliana.
Ontologies
GO
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR005956; 4OHPhenylPyrv_dOase.
IPR004360; Glyas_bleo-R_dOase.
Graphical view of domain structure.
PANTHER PTHR11959; HPP_dOase; 1.
Pfam PF00903; Glyoxalase; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF009283; HPP_dOase; 1.
TIGRFAMs TIGR01263; 4HPPD; 1.
BLOCKS P93836.
Genome annotation databases
NMPDR fig|3702.1.peg.833; -.
Other
ProtoNet P93836.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism; Tyrosine catabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   445  445     4-hydroxyphenylpyruvate dioxygenase. PRO_0000088397
METAL   226   226        Iron (By similarity). 
METAL   308   308        Iron (By similarity). 
METAL   394   394        Iron (By similarity). 
DISULFID   401   416         
STRAND   44    53  10      
HELIX   57    68  12      
STRAND   71    77  7      
HELIX   78    80  3      
STRAND   83    92  10      
STRAND   95   102  8      
HELIX   105   107  3      
TURN   108   110  3      
HELIX   113   115  3      
HELIX   125   135  11      
STRAND   137   147  11      
HELIX   149   158  10      
STRAND   163   170  8      
TURN   171   173  3      
STRAND   174   182  9      
STRAND   185   192  8      
TURN   211   213  3      
STRAND   219   230  12      
HELIX   234   245  12      
STRAND   248   253  6      
STRAND   265   271  7      
STRAND   277   284  8      
HELIX   293   301  9      
STRAND   305   314  10      
HELIX   316   326  11      
HELIX   327   329  3      
HELIX   340   350  11      
TURN   351   353  3      
HELIX   356   365  10      
STRAND   368   371  4      
STRAND   373   382  10      
STRAND   385   389  5      
STRAND   392   400  9      
TURN   414   417  4      
HELIX   423   430  8      
Sequence information
Length: 445 AA [This is the length of the unprocessed precursor] Molecular weight: 48816 Da [This is the MW of the unprocessed precursor] CRC64: FD0442F93556B3F5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGHQNAAVSE NQNHDDGAAS SPGFKLVGFS KFVRKNPKSD KFKVKRFHHI EFWCGDATNV 

        70         80         90        100        110        120 
ARRFSWGLGM RFSAKSDLST GNMVHASYLL TSGDLRFLFT APYSPSLSAG EIKPTTTASI 

       130        140        150        160        170        180 
PSFDHGSCRS FFSSHGLGVR AVAIEVEDAE SAFSISVANG AIPSSPPIVL NEAVTIAEVK 

       190        200        210        220        230        240 
LYGDVVLRYV SYKAEDTEKS EFLPGFERVE DASSFPLDYG IRRLDHAVGN VPELGPALTY 

       250        260        270        280        290        300 
VAGFTGFHQF AEFTADDVGT AESGLNSAVL ASNDEMVLLP INEPVHGTKR KSQIQTYLEH 

       310        320        330        340        350        360 
NEGAGLQHLA LMSEDIFRTL REMRKRSSIG GFDFMPSPPP TYYQNLKKRV GDVLSDDQIK 

       370        380        390        400        410        420 
ECEELGILVD RDDQGTLLQI FTKPLGDRPT IFIEIIQRVG CMMKDEEGKA YQSGGCGGFG 

       430        440 
KGNFSELFKS IEEYEKTLEA KQLVG 

P93836 in FASTA format

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