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Protein

4-hydroxyphenylpyruvate dioxygenase

Gene

HPD

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

4-hydroxyphenylpyruvate + O2 = homogentisate + CO2.

Cofactori

Fe cation1 PublicationNote: Binds 1 Fe cation per subunit.1 Publication

Pathwayi: L-phenylalanine degradation

This protein is involved in step 3 of the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Tyrosine aminotransferase (TAT)
  3. 4-hydroxyphenylpyruvate dioxygenase (HPD)
  4. Homogentisate 1,2-dioxygenase (HGO)
  5. no protein annotated in this organism
  6. no protein annotated in this organism
This subpathway is part of the pathway L-phenylalanine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine, the pathway L-phenylalanine degradation and in Amino-acid degradation.

Pathwayi: prenylquinone biosynthesis

This protein is involved in the pathway prenylquinone biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway prenylquinone biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi226 – 2261Iron1 Publication
Metal bindingi308 – 3081Iron1 Publication
Metal bindingi394 – 3941Iron1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Phenylalanine catabolism, Tyrosine catabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciARA:GQT-1626-MONOMER.
BRENDAi1.13.11.27. 399.
ReactomeiR-ATH-71182. Phenylalanine and tyrosine catabolism.
SABIO-RKP93836.
UniPathwayiUPA00139; UER00362.
UPA00975.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxyphenylpyruvate dioxygenase (EC:1.13.11.27)
Alternative name(s):
4-hydroxyphenylpyruvic acid oxidase
Short name:
4HPPD
Short name:
HPD
Short name:
HPPDase
Gene namesi
Name:HPD
Synonyms:PDS1
Ordered Locus Names:At1g06570
ORF Names:F12K11.9
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G06570.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2242740.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4454454-hydroxyphenylpyruvate dioxygenasePRO_0000088397Add
BLAST

Proteomic databases

PaxDbiP93836.
PRIDEiP93836.

Expressioni

Gene expression databases

ExpressionAtlasiP93836. baseline and differential.
GenevisibleiP93836. AT.

Interactioni

Subunit structurei

Homodimer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1251387,EBI-1251387

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

STRINGi3702.AT1G06570.1.

Structurei

Secondary structure

1
445
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 5310Combined sources
Helixi57 – 6812Combined sources
Beta strandi71 – 777Combined sources
Helixi78 – 803Combined sources
Beta strandi83 – 9210Combined sources
Beta strandi95 – 1028Combined sources
Helixi105 – 1073Combined sources
Turni108 – 1103Combined sources
Helixi113 – 1153Combined sources
Helixi125 – 13511Combined sources
Beta strandi137 – 14711Combined sources
Helixi149 – 15810Combined sources
Beta strandi163 – 1708Combined sources
Turni171 – 1733Combined sources
Beta strandi174 – 1829Combined sources
Beta strandi185 – 1928Combined sources
Turni211 – 2133Combined sources
Beta strandi219 – 23012Combined sources
Helixi234 – 24512Combined sources
Beta strandi248 – 2536Combined sources
Beta strandi265 – 2717Combined sources
Beta strandi277 – 2848Combined sources
Beta strandi287 – 2904Combined sources
Helixi293 – 3019Combined sources
Beta strandi305 – 31410Combined sources
Helixi316 – 32611Combined sources
Helixi327 – 3293Combined sources
Helixi340 – 35011Combined sources
Turni351 – 3533Combined sources
Helixi356 – 36510Combined sources
Beta strandi368 – 3714Combined sources
Beta strandi373 – 38210Combined sources
Beta strandi385 – 3895Combined sources
Beta strandi392 – 4009Combined sources
Beta strandi406 – 4083Combined sources
Turni414 – 4174Combined sources
Helixi423 – 4308Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SP9X-ray3.00A/B1-445[»]
1SQDX-ray1.80A23-445[»]
1TFZX-ray1.80A23-445[»]
1TG5X-ray1.90A23-445[»]
5CTOX-ray2.62A/B/C/D1-445[»]
ProteinModelPortaliP93836.
SMRiP93836. Positions 35-431.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP93836.

Family & Domainsi

Sequence similaritiesi

Belongs to the 4HPPD family.Curated

Phylogenomic databases

eggNOGiKOG0638. Eukaryota.
COG3185. LUCA.
InParanoidiP93836.
PhylomeDBiP93836.

Family and domain databases

Gene3Di3.10.180.10. 2 hits.
InterProiIPR005956. 4OHPhenylPyrv_dOase.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
[Graphical view]
PANTHERiPTHR11959. PTHR11959. 1 hit.
PfamiPF00903. Glyoxalase. 1 hit.
[Graphical view]
PIRSFiPIRSF009283. HPP_dOase. 1 hit.
SUPFAMiSSF54593. SSF54593. 1 hit.
TIGRFAMsiTIGR01263. 4HPPD. 1 hit.

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P93836-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGHQNAAVSE NQNHDDGAAS SPGFKLVGFS KFVRKNPKSD KFKVKRFHHI
60 70 80 90 100
EFWCGDATNV ARRFSWGLGM RFSAKSDLST GNMVHASYLL TSGDLRFLFT
110 120 130 140 150
APYSPSLSAG EIKPTTTASI PSFDHGSCRS FFSSHGLGVR AVAIEVEDAE
160 170 180 190 200
SAFSISVANG AIPSSPPIVL NEAVTIAEVK LYGDVVLRYV SYKAEDTEKS
210 220 230 240 250
EFLPGFERVE DASSFPLDYG IRRLDHAVGN VPELGPALTY VAGFTGFHQF
260 270 280 290 300
AEFTADDVGT AESGLNSAVL ASNDEMVLLP INEPVHGTKR KSQIQTYLEH
310 320 330 340 350
NEGAGLQHLA LMSEDIFRTL REMRKRSSIG GFDFMPSPPP TYYQNLKKRV
360 370 380 390 400
GDVLSDDQIK ECEELGILVD RDDQGTLLQI FTKPLGDRPT IFIEIIQRVG
410 420 430 440
CMMKDEEGKA YQSGGCGGFG KGNFSELFKS IEEYEKTLEA KQLVG
Length:445
Mass (Da):48,816
Last modified:January 1, 1998 - v2
Checksum:iFD0442F93556B3F5
GO

Sequence cautioni

The sequence AAF24813.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AEE28006.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89267 mRNA. Translation: AAB70025.1.
AF000228 mRNA. Translation: AAB58404.1.
AF047834 mRNA. Translation: AAC15697.1.
AC007592 Genomic DNA. Translation: AAF24813.1. Different initiation.
CP002684 Genomic DNA. Translation: AEE28006.1. Different initiation.
AF428446 mRNA. Translation: AAL16215.1.
AY072329 mRNA. Translation: AAL61936.1.
AY128745 mRNA. Translation: AAM91145.1.
PIRiB86201.
T51585.
RefSeqiNP_172144.2. NM_100536.3.
UniGeneiAt.48158.
At.71039.

Genome annotation databases

EnsemblPlantsiAT1G06570.1; AT1G06570.1; AT1G06570.
GeneIDi837168.
GrameneiAT1G06570.1; AT1G06570.1; AT1G06570.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89267 mRNA. Translation: AAB70025.1.
AF000228 mRNA. Translation: AAB58404.1.
AF047834 mRNA. Translation: AAC15697.1.
AC007592 Genomic DNA. Translation: AAF24813.1. Different initiation.
CP002684 Genomic DNA. Translation: AEE28006.1. Different initiation.
AF428446 mRNA. Translation: AAL16215.1.
AY072329 mRNA. Translation: AAL61936.1.
AY128745 mRNA. Translation: AAM91145.1.
PIRiB86201.
T51585.
RefSeqiNP_172144.2. NM_100536.3.
UniGeneiAt.48158.
At.71039.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SP9X-ray3.00A/B1-445[»]
1SQDX-ray1.80A23-445[»]
1TFZX-ray1.80A23-445[»]
1TG5X-ray1.90A23-445[»]
5CTOX-ray2.62A/B/C/D1-445[»]
ProteinModelPortaliP93836.
SMRiP93836. Positions 35-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G06570.1.

Chemistry

ChEMBLiCHEMBL2242740.

Proteomic databases

PaxDbiP93836.
PRIDEiP93836.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G06570.1; AT1G06570.1; AT1G06570.
GeneIDi837168.
GrameneiAT1G06570.1; AT1G06570.1; AT1G06570.

Organism-specific databases

TAIRiAT1G06570.

Phylogenomic databases

eggNOGiKOG0638. Eukaryota.
COG3185. LUCA.
InParanoidiP93836.
PhylomeDBiP93836.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00362.
UPA00975.
BioCyciARA:GQT-1626-MONOMER.
BRENDAi1.13.11.27. 399.
ReactomeiR-ATH-71182. Phenylalanine and tyrosine catabolism.
SABIO-RKP93836.

Miscellaneous databases

EvolutionaryTraceiP93836.
PROiP93836.

Gene expression databases

ExpressionAtlasiP93836. baseline and differential.
GenevisibleiP93836. AT.

Family and domain databases

Gene3Di3.10.180.10. 2 hits.
InterProiIPR005956. 4OHPhenylPyrv_dOase.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
[Graphical view]
PANTHERiPTHR11959. PTHR11959. 1 hit.
PfamiPF00903. Glyoxalase. 1 hit.
[Graphical view]
PIRSFiPIRSF009283. HPP_dOase. 1 hit.
SUPFAMiSSF54593. SSF54593. 1 hit.
TIGRFAMsiTIGR01263. 4HPPD. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of an Arabidopsis thaliana cDNA for p-hydroxyphenylpyruvate dioxygenase."
    Bartley G.E., Maxwell C.A., Wittenbach V.A., Scolnik P.A.
    Plant Gene Register PGR97-065
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Wassilewskija.
  2. Norris S.R., Dellapenna D.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  3. "Characterization and subcellular compartmentation of recombinant 4-hydroxyphenylpyruvate dioxygenase from Arabidopsis in transgenic tobacco."
    Garcia I., Rodgers M., Pepin R., Hsieh T.-F., Matringe M.
    Plant Physiol. 119:1507-1516(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
  4. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    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.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases."
    Yang C., Pflugrath J.W., Camper D.L., Foster M.L., Pernich D.J., Walsh T.A.
    Biochemistry 43:10414-10423(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-445 IN COMPLEX WITH IRON, COFACTOR, METAL-BINDING SITES, SUBUNIT.
  8. "The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase."
    Fritze I.M., Linden L., Freigang J., Auerbach G., Huber R., Steinbacher S.
    Plant Physiol. 134:1388-1400(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiHPPD_ARATH
AccessioniPrimary (citable) accession number: P93836
Secondary accession number(s): F4IDP1, O04330, Q9SHK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: February 17, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.