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P06845 (TYRO_STRGA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 78. 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 glaucescens
Taxonomic identifier1907 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Miscellaneous

The extra- and intra-cellular tyrosinases are identical.

Sequence similarities

Belongs to the tyrosinase family.

Ontologies

Keywords
   Biological processMelanin biosynthesis
   LigandCopper
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termDirect protein sequencing
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
Chain2 – 274273Tyrosinase
PRO_0000186738

Sites

Metal binding381Copper A
Metal binding541Copper A
Metal binding631Copper A
Metal binding1901Copper B
Metal binding1941Copper B
Metal binding2161Copper B

Experimental info

Mutagenesis381H → Q: Loss of activity.
Mutagenesis541H → Q: Loss of activity.
Mutagenesis631H → N: Loss of activity.
Mutagenesis1901H → N: Loss of activity.
Mutagenesis1911N → Q: Loss of activity.
Mutagenesis1941H → Q: Loss of activity.
Mutagenesis2161H → Q: Loss of activity.
Sequence conflict2161H → N in AAA26834. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P06845 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0FDC67DC2739AA79

FASTA27430,874
        10         20         30         40         50         60 
MTVRKNQATL TADEKRRFVA AVLELKRSGR YDEFVTTHNA FIIGDTDAGE RTGHRSPSFL 

        70         80         90        100        110        120 
PWHRRYLLEF ERALQSVDAS VALPYWDWSA DRTARASLWA PDFLGGTGRS LDGRVMDGPF 

       130        140        150        160        170        180 
AASAGNWPIN VRVDGRAYLR RSLGTAVREL PTRAEVESVL GMATYDTAPW NSASDGFRNH 

       190        200        210        220        230        240 
LEGWRGVNLH NRVHVWVGGQ MATGMSPNDP VFWLHHAYVD KLWAEWQRRH PGSGYLPAAG 

       250        260        270 
TPDVVDLNDR MKPWNDTSPA DLLDHTAHYT FDTD 

« Hide

References

[1]"Primary structure of tyrosinase from Streptomyces glaucescens."
Huber M., Hintermann G., Lerch K.
Biochemistry 24:6038-6044(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: DSM 40716 / ETH 22794 / GLA.0.
[2]"Identification of two histidines as copper ligands in Streptomyces glaucescens tyrosinase."
Huber M., Lerch K.
Biochemistry 27:5610-5615(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: COPPER-LIGANDS, MUTAGENESIS.
Strain: DSM 40716 / ETH 22794 / GLA.0.
[3]"Albino mutants of Streptomyces glaucescens tyrosinase."
Jackman M.P., Hajnal A., Lerch K.
Biochem. J. 274:707-713(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: COPPER-LIGANDS, MUTAGENESIS.
Strain: DSM 40716 / ETH 22794 / GLA.0.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11302 Genomic DNA. Translation: AAA26834.1.
PIRA24089.

3D structure databases

ProteinModelPortalP06845.
SMRP06845. Positions 2-272.
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_STRGA
AccessionPrimary (citable) accession number: P06845
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 78 of the entry and version 3 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