Q0CRX0 · TYRP_ASPTN

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).

Catalytic activity

Cofactor

Cu2+ (UniProtKB | Rhea| CHEBI:29036 )

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.

TypeIDPosition(s)Description
Binding site87Cu cation A (UniProtKB | ChEBI)
Binding site96Cu cation A (UniProtKB | ChEBI)
Binding site203Cu cation B (UniProtKB | ChEBI)
Binding site263Cu cation B (UniProtKB | ChEBI)
Binding site286Cu cation B (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum lumen
Cellular ComponentGolgi lumen
Molecular Functionmetal ion binding
Molecular Functionoxidoreductase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Tyrosinase P
  • EC number
  • Alternative names
    • Melanin biosynthesis protein B

Gene names

    • Name
      tyrP
    • Synonyms
      melB
    • ORF names
      ATEG_03564

Organism names

Accessions

  • Primary accession
    Q0CRX0

Proteomes

Subcellular Location

Golgi apparatus lumen
Note: The oxidizing environment of Golgi or endoplasmic reticulum (ER) is required for tyrP to be active.

Keywords

Phenotypes & Variants

Disruption phenotype

Impairs the production of Asp-melanin (PubMed:28791090).
Results in yellow fluorescent conidia and accumulates aspulvinone E in conidia (PubMed:27133313).

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

Type
IDPosition(s)Description
Signal1-19
ChainPRO_000044862320-356Tyrosinase P
Glycosylation81N-linked (GlcNAc...) asparagine
Glycosylation148N-linked (GlcNAc...) asparagine
Glycosylation193N-linked (GlcNAc...) asparagine
Glycosylation226N-linked (GlcNAc...) asparagine
Glycosylation309N-linked (GlcNAc...) asparagine

Post-translational modification

Glycosylated.

Keywords

PTM databases

Expression

Induction

Expression is induced during conidiation.

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the tyrosinase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    356
  • Mass (Da)
    40,470
  • Last updated
    2019-12-11 v2
  • Checksum
    8B6D196601BF66CD
MGFYRNLVLVAASCTQALGLCPAPRCDSPDIRHEWGELSREDRLSYISAVQCMKDRPPELSVEEVPAVRSRYDDFTAVHINYTLQIHNSGIFLPWHRHFIWLWEKALREECGFTGTLPYWDWVMWPNLAASPLFDGTETSLSGDGEFNATEQPTELNPEPGLTITIPRGAGGGCVRTGPFKDWVINMGPFAFNESYEPALPDHAFDYNPRCLVRSLNDWVIQTYNNQTVVDTLLDSPDIVEFQNIMGGFPNPPIPIGPHAMGHRSLGPDMLDFFASPQDPAFWQHHGMVDRLWTVWQDADEPWRRFALNGSSTTWYKDDTPEVTLQTTVEFGILDEPRPLYELMSPTAGPYCYTYT

Sequence caution

The sequence EAU36838.1 differs from that shown. Reason: Erroneous gene model prediction

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CH476597
EMBL· GenBank· DDBJ
EAU36838.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.

Genome annotation databases

Similar Proteins

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