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P80064

- HPPD_PSEUJ

UniProt

P80064 - HPPD_PSEUJ

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Protein

4-hydroxyphenylpyruvate dioxygenase

Gene

hpd

Organism
Pseudomonas sp. (strain P.J. 874)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

4-hydroxyphenylpyruvate + O2 = homogentisate + CO2.

Cofactori

Fe cationNote: Binds 1 Fe cation per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi161 – 1611Iron
Metal bindingi240 – 2401Iron
Metal bindingi322 – 3221Iron

GO - Molecular functioni

  1. 4-hydroxyphenylpyruvate dioxygenase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. L-phenylalanine catabolic process Source: UniProtKB-UniPathway
  2. tyrosine catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Phenylalanine catabolism, Tyrosine catabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12032.
UniPathwayiUPA00139; UER00362.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxyphenylpyruvate dioxygenase (EC:1.13.11.27)
Short name:
4HPPD
Short name:
HPD
Short name:
HPPDase
Gene namesi
Name:hpd
OrganismiPseudomonas sp. (strain P.J. 874)
Taxonomic identifieri72587 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3573574-hydroxyphenylpyruvate dioxygenasePRO_0000088408Add
BLAST

2D gel databases

World-2DPAGE0008:P80064.

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
357
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 1910Combined sources
Helixi27 – 326Combined sources
Beta strandi36 – 5116Combined sources
Beta strandi54 – 596Combined sources
Beta strandi62 – 643Combined sources
Helixi65 – 739Combined sources
Beta strandi74 – 8512Combined sources
Helixi87 – 9610Combined sources
Beta strandi115 – 1173Combined sources
Helixi119 – 1213Combined sources
Beta strandi123 – 1275Combined sources
Beta strandi131 – 1333Combined sources
Helixi136 – 1405Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi155 – 1628Combined sources
Helixi170 – 18213Combined sources
Beta strandi185 – 1939Combined sources
Beta strandi198 – 2058Combined sources
Beta strandi212 – 2187Combined sources
Helixi225 – 2339Combined sources
Beta strandi235 – 2373Combined sources
Beta strandi240 – 2467Combined sources
Helixi248 – 25710Combined sources
Helixi268 – 2725Combined sources
Helixi274 – 2774Combined sources
Helixi285 – 2917Combined sources
Beta strandi294 – 3007Combined sources
Beta strandi303 – 31210Combined sources
Beta strandi319 – 32810Combined sources
Helixi334 – 35118Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CJXX-ray2.40A/B/C/D1-357[»]
ProteinModelPortaliP80064.
SMRiP80064. Positions 4-355.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80064.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi167 – 19630Tyr-richAdd
BLAST

Sequence similaritiesi

Belongs to the 4HPPD family.Curated

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.

P80064-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
ADLYENPMGL MGFEFIELAS PTPNTLEPIF EIMGFTKVAT HRSKDVHLYR
60 70 80 90 100
QGAINLILNN EPHSVASYFA AEHGPSVCGM AFRVKDSQKA YKRALELGAQ
110 120 130 140 150
PIHIETGPME LNLPAIKGIG GAPLYLIDRF GEGSSIYDID FVFLEGVDRH
160 170 180 190 200
PVGAGLKIID HLTHNVYRGR MAYWANFYEK LFNFREIRYF DIKGEYTGLT
210 220 230 240 250
SKAMTAPDGM IRIPLNEESS KGAGQIEEFL MQFNGEGIQH VAFLSDDLIK
260 270 280 290 300
TWDHLKSIGM RFMTAPPDTY YEMLEGRLPN HGEPVGELQA RGILLDGSSE
310 320 330 340 350
SGDKRLLLQI FSETLMGPVF FEFIQRKGDD GFGEGNFKAL FESIERDQVR

RGVLSTD
Length:357
Mass (Da):40,061
Last modified:May 1, 1992 - v1
Checksum:i26CF4A80B1484BD0
GO

Sequence databases

PIRiS21209.

Cross-referencesi

Sequence databases

PIRi S21209.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CJX X-ray 2.40 A/B/C/D 1-357 [» ]
ProteinModelPortali P80064.
SMRi P80064. Positions 4-355.
ModBasei Search...
MobiDBi Search...

2D gel databases

World-2DPAGE 0008:P80064.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00139 ; UER00362 .
BioCyci MetaCyc:MONOMER-12032.

Miscellaneous databases

EvolutionaryTracei P80064.

Family and domain databases

Gene3Di 3.10.180.10. 2 hits.
InterProi IPR005956. 4OHPhenylPyrv_dOase.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
[Graphical view ]
PANTHERi PTHR11959. PTHR11959. 1 hit.
Pfami PF00903. Glyoxalase. 1 hit.
[Graphical view ]
PIRSFi PIRSF009283. HPP_dOase. 1 hit.
SUPFAMi SSF54593. SSF54593. 1 hit.
TIGRFAMsi TIGR01263. 4HPPD. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Characterization of 4-hydroxyphenylpyruvate dioxygenase. Primary structure of the Pseudomonas enzyme."
    Rueetschi U., Odelhoeg B., Lindstedt S., Barros-Soederling J., Persson B., Joernvall H.
    Eur. J. Biochem. 205:459-466(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway."
    Serre L., Sailland A., Sy D., Boudec P., Rolland A., Pebay-Peyroula E., Cohen-Addad C.
    Structure 7:977-988(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Entry informationi

Entry nameiHPPD_PSEUJ
AccessioniPrimary (citable) accession number: P80064
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 26, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3