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Reviewed, UniProtKB/Swiss-Prot P43311 (PPO_VITVI)

Last modified June 16, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsVitalesVitaceaeVitis

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.

Catalytic activity

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

Cofactor

Binds 2 copper ions per subunit By similarity.

Subcellular location

Plastidchloroplast thylakoid lumen.

Sequence similarities

Belongs to the tyrosinase family.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
Thioether bond
   Technical term3D-structure
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast thylakoid lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncatechol oxidase activity

Inferred from electronic annotation. Source: EC

copper 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 By similarity
Metal binding2111Copper A By similarity
Metal binding2201Copper A By similarity
Metal binding3421Copper B By similarity
Metal binding3461Copper B By similarity
Metal binding3751Copper B By similarity

Amino acid modifications

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

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P43311-1 [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: 7948897] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Sultana.
Tissue: Fruit.

Cross-references

Sequence databases

Z27411 mRNA. Translation: CAA81798.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2P3XX-ray2.20A104-442[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.10.3.1. 81671.

Family and domain databases

InterProIPR008922. Di-copper_centre.
IPR016213. Polyphenol_Oxase_pln.
IPR002227. Tyrosinase.
[Graphical view]
Gene3DG3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
PfamPF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFPIRSF000290. PPO_plant. 1 hit.
PRINTSPR00092. TYROSINASE.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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: June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents