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Reviewed, UniProtKB/Swiss-Prot P85026 (PPO_ZINOF)

Last modified November 4, 2008. Version 10. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
      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.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

2 catechol + O(2) = 2 1,2-benzoquinone + 2 H(2)O.

Cofactor

Binds 2 copper ions per subunit By similarity.

Subunit structure

Homodimer.

Tissue specificity

Expressed in the rhizome. Not detected in leaves.

Developmental stage

Expressed throughout rhizome development.

Post-translational modification

Glycosylated.

Sequence similarities

Belongs to the tyrosinase family.

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.

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.

Ontologies

Keywords

   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   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

Chain1 – ›10›10Polyphenol oxidase
PRO_0000259621

Experimental info

Non-terminal residue101

Sequences

Sequence LengthMass (Da)Tools
P85026-1 [UniParc].

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

FASTA10946
        10 
EQGVGGDDGL 

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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...

Family and domain databases

InterProIPR002227. Tyrosinase.
[Graphical view]
PROSITEPS00497. TYROSINASE_1. Partial match.
PS00498. TYROSINASE_2. Partial match.
[Graphical view]
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: November 4, 2008
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

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