Reviewed,
UniProtKB/Swiss-Prot Q00024 (PPO1_AGABI)
Last modified
November 4, 2008.
Version 47.
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 names | Recommended name: Polyphenol oxidase Short name=PPO EC=1.10.3.1 Alternative name(s): Catechol oxidase | ||
| Gene names |
| ||
| Organism | Agaricus bisporus (Common mushroom) | ||
| Taxonomic identifier | 5341 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Agaricomycetidae › Agaricales › Agaricaceae › Agaricus |
Protein attributes
| Sequence length | 568 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript 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. |
| Sequence similarities | Belongs to the tyrosinase family. |
Ontologies
Keywords | |
|---|---|
| Ligand | Copper Metal-binding |
| Molecular function | Oxidoreductase |
| PTM | Thioether bond |
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)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 568 | 568 | Polyphenol oxidase | PRO_0000186740 | |||||||
Sites | |||||||||||
| Metal binding | 57 | 1 | Copper A By similarity | ||||||||
| Metal binding | 85 | 1 | Copper A By similarity | ||||||||
| Metal binding | 94 | 1 | Copper A By similarity | ||||||||
| Metal binding | 257 | 1 | Copper B By similarity | ||||||||
| Metal binding | 261 | 1 | Copper B By similarity | ||||||||
| Metal binding | 286 | 1 | Copper B By similarity | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 83 ↔ 85 | 2'-(S-cysteinyl)-histidine (Cys-His) By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Cloning, expression and characterisation of two tyrosinase cDNAs from Agaricus bisporus." Wichers H., Recourt K., Hendriks M., Ebbelaar C.E.M., Biancone G., Hoeberichts F., Mooibroek H., Soler-Rivas C. Appl. Microbiol. Biotechnol. 61:336-341(2003) [PubMed: 12743763] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Horst U1. |
Cross-references
Sequence databases | |
|---|---|
| X85113 mRNA. Translation: CAA59432.1. | |
| PIR | S53017. |
3D structure databases | |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR008922. Di-copper_centre. IPR016216. Monophenol_mOase_fun. IPR002227. Tyrosinase. [Graphical view] |
| Gene3D | G3DSA:1.10.1280.10. Di-copper_centre. 1 hit. |
| Pfam | PF00264. Tyrosinase. 1 hit. [Graphical view] |
| PIRSF | PIRSF000340. MPO_fungal. 1 hit. |
| PRINTS | PR00092. TYROSINASE. |
| PROSITE | PS00497. TYROSINASE_1. 1 hit. PS00498. TYROSINASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PPO1_AGABI | ||||||||
| Accession | Primary (citable) accession number: Q00024 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

Clusters with


