Q0CRX0 · TYRP_ASPTN
- ProteinTyrosinase P
- GenetyrP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids356 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Tyrosinase; part of the gene cluster that mediates the biosynthesis of Asp-melanin, a pigment that confers resistance against UV light and hampers phagocytosis by soil amoeba (PubMed:27133313, PubMed:28791090, PubMed:29270299).
The nonribosomal peptide synthase melA converts 4-hydroxyphenylpyruvate (4-HPPA) to aspulvinone E (PubMed:27133313, PubMed:29270299).
The tyrosinase tyrP then performs hydroxylations of both aromatic moieties of aspulvinone E (PubMed:27133313).
The product of tyrP is highly unstable, and, due to the high reactivity of methides and ortho-diquinones, the polymeric Asp-melanin forms spontaneously (PubMed:27133313).
The nonribosomal peptide synthase melA converts 4-hydroxyphenylpyruvate (4-HPPA) to aspulvinone E (PubMed:27133313, PubMed:29270299).
The tyrosinase tyrP then performs hydroxylations of both aromatic moieties of aspulvinone E (PubMed:27133313).
The product of tyrP is highly unstable, and, due to the high reactivity of methides and ortho-diquinones, the polymeric Asp-melanin forms spontaneously (PubMed:27133313).
Catalytic activity
- aspulvinone E + O2 = (5Z)-3-(3,4-dihydroxyphenyl)-5-[(3,4-dihydroxyphenyl)methylidene]-5-oxo-2,5-dihydrofuran-3-olateThis reaction proceeds in the forward direction.
- aspulvinone E + O2 = (2Z)-2-[(3,4-dioxocyclohexa-1,5-dien-1-yl)methylidene]-4-(4-hydroxyphenyl)-5-oxo-2,5-dihydrofuran-3-olate + H2OThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 copper ions per subunit.
Activity regulation
Activity is inhibited by the presence of dithiothreitol (DTT).
pH Dependence
Optimum pH is 5-7.
Pathway
Secondary metabolite biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 87 | Cu cation A (UniProtKB | ChEBI) | |||
Binding site | 96 | Cu cation A (UniProtKB | ChEBI) | |||
Binding site | 203 | Cu cation B (UniProtKB | ChEBI) | |||
Binding site | 263 | Cu cation B (UniProtKB | ChEBI) | |||
Binding site | 286 | Cu cation B (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | Golgi lumen | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTyrosinase P
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionQ0CRX0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: The oxidizing environment of Golgi or endoplasmic reticulum (ER) is required for tyrP to be active.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-19 | ||||
Chain | PRO_0000448623 | 20-356 | Tyrosinase P | ||
Glycosylation | 81 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 148 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 193 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 226 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 309 | N-linked (GlcNAc...) asparagine | |||
Post-translational modification
Glycosylated.
Keywords
- PTM
PTM databases
Expression
Induction
Expression is induced during conidiation.
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length356
- Mass (Da)40,470
- Last updated2019-12-11 v2
- Checksum8B6D196601BF66CD
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CH476597 EMBL· GenBank· DDBJ | EAU36838.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. |