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P85026

- PPO_ZINOF

UniProt

P85026 - PPO_ZINOF

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Protein
Polyphenol oxidase
Gene
N/A
Organism
Zingiber officinale (Ginger) (Amomum zingiber)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Binds 2 copper ions per subunit By similarity.By similarity

pH dependencei

Optimum pH is 4.5. Active from pH 3.0 to 8.0. The activity decreases sharply above pH 7.5.1 Publication

Temperature dependencei

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.1 Publication

GO - Molecular functioni

  1. catechol oxidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyphenol oxidase (EC:1.10.3.1)
    Short name:
    PPO
    Alternative name(s):
    Catechol oxidase
    OrganismiZingiber officinale (Ginger) (Amomum zingiber)
    Taxonomic identifieri94328 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaZingiberalesZingiberaceaeZingiber

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›10›10Polyphenol oxidase
    PRO_0000259621

    Post-translational modificationi

    Glycosylated.1 Publication

    Expressioni

    Tissue specificityi

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

    Developmental stagei

    Expressed throughout rhizome development.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tyrosinase family.1 Publication

    Sequencei

    Sequence statusi: Fragment.

    P85026-1 [UniParc]FASTAAdd to Basket

    « Hide

    EQGVGGDDGL                                               10
    Length:10
    Mass (Da):946
    Last modified:October 31, 2006 - v1
    Checksum:i38286BAAA87862C8
    GO

    Non-terminal residue

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei10 – 101

    Cross-referencesi

    3D structure databases

    ModBasei Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiPPO_ZINOF
    AccessioniPrimary (citable) accession number: P85026
    Entry historyi
    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 statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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