Q00234 (TYRO_ASPOR) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 76.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Tyrosinase EC=1.14.18.1 Alternative name(s): Monophenol monooxygenase | ||||
| Gene names |
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| Organism | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome] | ||||
| Taxonomic identifier | 510516 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › ![]() |
Protein attributes
| Sequence length | 539 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. |
| Catalytic activity | 2 L-dopa + O2 = 2 dopaquinone + 2 H2O. L-tyrosine + O2 = dopaquinone + H2O. |
| Cofactor | Binds 2 copper ions per subunit. |
| Enzyme regulation | Activated by acidifying treatment at pH 3.0. |
| Subunit structure | Homotetramer. |
| Post-translational modification | The N-terminus is blocked. |
| Sequence similarities | Belongs to the tyrosinase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Melanin biosynthesis |
| Ligand | Copper Metal-binding |
| Molecular function | Monooxygenase Oxidoreductase |
| PTM | Thioether bond |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | melanin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW monophenol monooxygenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 539 | 539 | Tyrosinase | PRO_0000186733 | |||||||
Sites | |||||||||||
| Metal binding | 63 | 1 | Copper A By similarity | ||||||||
| Metal binding | 84 | 1 | Copper A By similarity | ||||||||
| Metal binding | 93 | 1 | Copper A By similarity | ||||||||
| Metal binding | 290 | 1 | Copper B By similarity | ||||||||
| Metal binding | 294 | 1 | Copper B By similarity | ||||||||
| Metal binding | 333 | 1 | Copper B By similarity | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 82 ↔ 84 | 2'-(S-cysteinyl)-histidine (Cys-His) By similarity | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning and nucleotide sequence of the protyrosinase gene, melO, from Aspergillus oryzae and expression of the gene in yeast cells." Fujita Y., Uraga Y., Ichishima E. Biochim. Biophys. Acta 1261:151-154(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 22788 / RIB 128 / CBS 819.72 / IFO 30113 / JCM 2248. |
| [2] | "Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. Kikuchi H.Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D37929 Genomic DNA. Translation: BAA07149.1. AP007169 Genomic DNA. Translation: BAE63910.1. |
| PIR | S53529. |
| RefSeq | XP_001825043.1. XM_001824991.2. |
3D structure databases | |
| ProteinModelPortal | Q00234. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 5062.CADAORAP00008707. |
Proteomic databases | |
| PRIDE | Q00234. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | CADAORAT00008890; CADAORAP00008707; CADAORAG00008890. |
| GeneID | 5997138. |
| KEGG | aor:AOR_1_92074. |
Phylogenomic databases | |
| HOGENOM | HOG000250264. |
| OrthoDB | EOG46X2JC. |
Family and domain databases | |
| Gene3D | 1.10.1280.10. 3 hits. |
| InterPro | IPR016216. Monophenol_mOase_fun. IPR002227. Tyrosinase. IPR008922. Unchr_di-copper_centre. [Graphical view] |
| Pfam | PF00264. Tyrosinase. 1 hit. [Graphical view] |
| PIRSF | PIRSF000340. MPO_fungal. 1 hit. |
| PRINTS | PR00092. TYROSINASE. |
| SUPFAM | SSF48056. Di-copper_centre. 1 hit. |
| PROSITE | PS00497. TYROSINASE_1. 1 hit. PS00498. TYROSINASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TYRO_ASPOR | ||||||||
| Accession | Primary (citable) accession number: Q00234 Secondary accession number(s): Q2U3F5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
