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P85026 (PPO_ZINOF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyphenol oxidase

Short name=PPO
EC=1.10.3.1
Alternative name(s):
Catechol oxidase
OrganismZingiber officinale (Ginger) (Amomum zingiber)
Taxonomic identifier94328 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaZingiberalesZingiberaceaeZingiber

Protein attributes

Sequence length10 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of mono- and o-diphenols to o-diquinones. Ref.1

Catalytic activity

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

Cofactor

Binds 2 copper ions per subunit By similarity. UniProtKB Q9ZP19

Subunit structure

Homodimer. Ref.1

Tissue specificity

Expressed in the rhizome. Not detected in leaves. Ref.1

Developmental stage

Expressed throughout rhizome development. Ref.1

Post-translational modification

Glycosylated. Ref.1

Sequence similarities

Belongs to the tyrosinase family. Ref.1

Biophysicochemical properties

pH dependence:

Optimum pH is 4.5. Active from pH 3.0 to 8.0. The activity decreases sharply above pH 7.5. Ref.1

Temperature dependence:

Optimum temperature is 60 degrees Celsius. There is only a slight decrease in activity at 75 degrees Celsius and a sharp decrease in activity at 90 degrees Celsius. Ref.1

Ontologies

Keywords
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_functioncatechol oxidase activity

Inferred from electronic annotation. Source: UniProtKB-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

Chain1 – ›10›10Polyphenol oxidase
PRO_0000259621

Experimental info

Non-terminal residue101

Sequences

Sequence LengthMass (Da)Tools
P85026 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: 38286BAAA87862C8

FASTA10946
        10 
EQGVGGDDGL 

« Hide

References

[1]"Purification and characterization of a polyphenol oxidase from the rhizome of Zingiber officinale."
Joseph A., Thayumanavan B., Manickam A., Panicker P.R.
Submitted (SEP-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION.
Tissue: Rhizome.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry namePPO_ZINOF
AccessionPrimary (citable) accession number: P85026
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: February 19, 2014
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families