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P55023 (TYRO_STRLN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosinase

EC=1.14.18.1
Alternative name(s):
Monophenol monooxygenase
Gene names
Name:melC2
Synonyms:mel
OrganismStreptomyces lincolnensis
Taxonomic identifier1915 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 By similarity.

Sequence similarities

Belongs to the tyrosinase family.

Ontologies

Keywords
   Biological processMelanin biosynthesis
   LigandCopper
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
Gene Ontology (GO)
   Biological_processmelanin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

monophenol monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 273272Tyrosinase
PRO_0000186739

Sites

Metal binding371Copper A By similarity
Metal binding531Copper A By similarity
Metal binding621Copper A By similarity
Metal binding1891Copper B By similarity
Metal binding1931Copper B By similarity
Metal binding2151Copper B By similarity

Sequences

Sequence LengthMass (Da)Tools
P55023 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E9D8616C99DD4DB9

FASTA27330,854
        10         20         30         40         50         60 
MTVRKNQATL TADEKRRFVT AVLSSSAARY DTFVTTHNEF IVADTDNGER TGHRSPSFLP 

        70         80         90        100        110        120 
WHRRFLLEFE RALQSVDASV ALPYWDWSTD RSARSSLWAP DFLGGTGRSR NGRVTDGPFR 

       130        140        150        160        170        180 
AATGVWPITV RLDGRTYLRR ALGGAGRELP TRAEVDSVLS IPTYDMAPWN SASDGFRNHL 

       190        200        210        220        230        240 
EGWRGVNLHN RVHVWVGGQM ATGVSPNDPV FWLHHAYIDK LWAQWQRRHR TPAYVPAAGT 

       250        260        270 
PDVVDLDETM KPWHDSSPAD LLDHTGHYTF DTD 

« Hide

References

[1]Zhang H.Z., Piepersberg W.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 78-11.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X95703 Genomic DNA. Translation: CAA65000.1.

3D structure databases

ProteinModelPortalP55023.
SMRP55023. Positions 2-271.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
InterProIPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSPR00092. TYROSINASE.
SUPFAMSSF48056. SSF48056. 1 hit.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTYRO_STRLN
AccessionPrimary (citable) accession number: P55023
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families