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P43311 (PPO_VITVI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Polyphenol oxidase, chloroplastic
Short name=PPO
EC=1.10.3.1
Alternative name(s):
Catechol oxidase
OrganismVitis vinifera (Grape)
Taxonomic identifier29760 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › Vitales › Vitaceae › Vitis

Protein attributes

Sequence length607 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of mono- and o-diphenols to o-diquinones. Ref.2

Catalytic activity

2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O. Ref.2

Cofactor

Binds 2 copper ions per subunit.

Subcellular location

Plastid › chloroplast thylakoid lumen.

Sequence similarities

Belongs to the tyrosinase family.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
Thylakoid
   DomainTransit peptide
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
Thioether bond
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processpigment biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentchloroplast thylakoid lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncatechol oxidase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 103103Chloroplast Potential
Chain104 – 607504Polyphenol oxidase, chloroplastic
PRO_0000035920

Sites

Metal binding1901Copper A
Metal binding2111Copper A
Metal binding2201Copper A
Metal binding3421Copper B
Metal binding3461Copper B
Metal binding3751Copper B

Amino acid modifications

Disulfide bond114 ↔ 129 Ref.2
Disulfide bond128 ↔ 191 Ref.2
Cross-link194 ↔ 2112'-(S-cysteinyl)-histidine (Cys-His) By similarity

Secondary structure

1 ....................................................... 607
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43311 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: B9045598E69BC57B

FASTA60767,347
        10         20         30         40         50         60 
MASLPWSLTT STAIANTTNI SAFPPSPLFQ RASHVPVARN RSRRFAPSKV SCNSANGDPN 

        70         80         90        100        110        120 
SDSTSDVRET SSGKLDRRNV LLGIGGLYGA AGGLGATKPL AFGAPIQAPD ISKCGTATVP 

       130        140        150        160        170        180 
DGVTPTNCCP PVTTKIIDFQ LPSSGSPMRT RPAAHLVSKE YLAKYKKAIE LQKALPDDDP 

       190        200        210        220        230        240 
RSFKQQANVH CTYCQGAYDQ VGYTDLELQV HASWLFLPFH RYYLYFNERI LAKLIDDPTF 

       250        260        270        280        290        300 
ALPYWAWDNP DGMYMPTIYA SSPSSLYDEK RNAKHLPPTV IDLDYDGTEP TIPDDELKTD 

       310        320        330        340        350        360 
NLAIMYKQIV SGATTPKLFL GYPYRAGDAI DPGAGTLEHA PHNIVHKWTG LADKPSEDMG 

       370        380        390        400        410        420 
NFYTAGRDPI FFGHHANVDR MWNIWKTIGG KNRKDFTDTD WLDATFVFYD ENKQLVKVKV 

       430        440        450        460        470        480 
SDCVDTSKLR YQYQDIPIPW LPKNTKAKAK TTTKSSKSGV AKAAELPKTT ISSIGDFPKA 

       490        500        510        520        530        540 
LNSVIRVEVP RPKKSRSKKE KEDEEEVLLI KGIELDRENF VKFDVYINDE DYSVSRPKNS 

       550        560        570        580        590        600 
EFAGSFVNVP HKHMKEMKTK TNLRFAINEL LEDLGAEDDE SVIVTIVPRA GGDDVTIGGI 


EIEFVSD

« Hide

References

[1]"Molecular cloning and characterisation of grape berry polyphenol oxidase."
Dry I.B., Robinson S.P.
Plant Mol. Biol. 26:495-502(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Sultana.
Tissue: Fruit.
[2]"Cloning, sequencing, purification, and crystal structure of Grenache (Vitis vinifera) polyphenol oxidase."
Virador V.M., Reyes Grajeda J.P., Blanco-Labra A., Mendiola-Olaya E., Smith G.M., Moreno A., Whitaker J.R.
J. Agric. Food Chem. 58:1189-1201(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 104-442 IN COMPLEX WITH COPPER IONS, FUNCTION, CATALYTIC ACTIVITY, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z27411 mRNA. Translation: CAA81798.1.
UniGeneVvi.108.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2P3XX-ray2.20A104-442[»]
ProteinModelPortalP43311.
SMRP43311. Positions 104-441.
ModBaseSearch...

Proteomic databases

PRIDEP43311.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG254493.

Enzyme and pathway databases

BRENDA1.10.3.1. 6671.

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
InterProIPR013788. Hemocyanin/hexamerin.
IPR016213. Polyphenol_oxidase.
IPR022740. Polyphenol_oxidase_C.
IPR022739. Polyphenol_oxidase_cen.
IPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamPF12142. PPO1_DWL. 1 hit.
PF12143. PPO1_KFDV. 1 hit.
PF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFPIRSF000290. PPO_plant. 1 hit.
PRINTSPR00092. TYROSINASE.
SUPFAMSSF48056. Di-copper_centre. 1 hit.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP43311.

Entry information

Entry namePPO_VITVI
AccessionPrimary (citable) accession number: P43311
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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