Reviewed,
UniProtKB/Swiss-Prot P85026 (PPO_ZINOF)
Last modified
November 4, 2008.
Version 10.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Polyphenol oxidase Short name=PPO EC=1.10.3.1 Alternative name(s): Catechol oxidase |
| Organism | Zingiber officinale (Ginger) (Amomum zingiber) |
| Taxonomic identifier | 94328 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Zingiberales › Zingiberaceae › Zingiber |
Protein attributes
| Sequence length | 10 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 | |
|---|---|
| Ligand | Copper Metal-binding |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | catechol oxidase activity Inferred from electronic annotation. Source: EC copper ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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 | |
|---|---|
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR002227. Tyrosinase. [Graphical view] |
| PROSITE | PS00497. TYROSINASE_1. Partial match. PS00498. TYROSINASE_2. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PPO_ZINOF | ||||||||
| Accession | Primary (citable) accession number: P85026 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


