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Protein

Tyrosinase

Gene

melC2

Organism
Streptomyces glaucescens
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.

Catalytic activityi

2 L-dopa + O2 = 2 dopaquinone + 2 H2O.
L-tyrosine + O2 = dopaquinone + H2O.

Cofactori

Cu2+Note: Binds 2 copper ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi38 – 381Copper A
Metal bindingi54 – 541Copper A
Metal bindingi63 – 631Copper A
Metal bindingi190 – 1901Copper B
Metal bindingi194 – 1941Copper B
Metal bindingi216 – 2161Copper B

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. monophenol monooxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. melanin biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Melanin biosynthesis

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosinase (EC:1.14.18.1)
Alternative name(s):
Monophenol monooxygenase
Gene namesi
Name:melC2
Synonyms:mel
OrganismiStreptomyces glaucescens
Taxonomic identifieri1907 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381H → Q: Loss of activity.
Mutagenesisi54 – 541H → Q: Loss of activity.
Mutagenesisi63 – 631H → N: Loss of activity.
Mutagenesisi190 – 1901H → N: Loss of activity.
Mutagenesisi191 – 1911N → Q: Loss of activity.
Mutagenesisi194 – 1941H → Q: Loss of activity.
Mutagenesisi216 – 2161H → Q: Loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 274273TyrosinasePRO_0000186738Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP06845.
SMRiP06845. Positions 2-272.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 1 hit.
PROSITEiPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06845-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVRKNQATL TADEKRRFVA AVLELKRSGR YDEFVTTHNA FIIGDTDAGE
60 70 80 90 100
RTGHRSPSFL PWHRRYLLEF ERALQSVDAS VALPYWDWSA DRTARASLWA
110 120 130 140 150
PDFLGGTGRS LDGRVMDGPF AASAGNWPIN VRVDGRAYLR RSLGTAVREL
160 170 180 190 200
PTRAEVESVL GMATYDTAPW NSASDGFRNH LEGWRGVNLH NRVHVWVGGQ
210 220 230 240 250
MATGMSPNDP VFWLHHAYVD KLWAEWQRRH PGSGYLPAAG TPDVVDLNDR
260 270
MKPWNDTSPA DLLDHTAHYT FDTD
Length:274
Mass (Da):30,874
Last modified:January 22, 2007 - v3
Checksum:i0FDC67DC2739AA79
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti216 – 2161H → N in AAA26834 (PubMed:3002431).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11302 Genomic DNA. Translation: AAA26834.1.
PIRiA24089.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11302 Genomic DNA. Translation: AAA26834.1.
PIRiA24089.

3D structure databases

ProteinModelPortaliP06845.
SMRiP06845. Positions 2-272.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 1 hit.
PROSITEiPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Primary structure of tyrosinase from Streptomyces glaucescens."
    Huber M., Hintermann G., Lerch K.
    Biochemistry 24:6038-6044(1984) [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(1987) [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(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: COPPER-LIGANDS, MUTAGENESIS.
    Strain: DSM 40716 / ETH 22794 / GLA.0.

Entry informationi

Entry nameiTYRO_STRGA
AccessioniPrimary (citable) accession number: P06845
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 31, 1987
Last sequence update: January 22, 2007
Last modified: November 25, 2014
This is version 80 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The extra- and intra-cellular tyrosinases are identical.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.