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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+2 PublicationsNote: Binds 2 copper ions per subunit.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi38Copper A2 Publications1
Metal bindingi54Copper A2 Publications1
Metal bindingi63Copper A2 Publications1
Metal bindingi190Copper B2 Publications1
Metal bindingi194Copper B2 Publications1
Metal bindingi216Copper B2 Publications1

GO - Molecular functioni

GO - Biological processi

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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi38H → Q: Loss of activity. 2 Publications1
Mutagenesisi54H → Q: Loss of activity. 2 Publications1
Mutagenesisi63H → N: Loss of activity. 2 Publications1
Mutagenesisi190H → N: Loss of activity. 2 Publications1
Mutagenesisi191N → Q: Loss of activity. 2 Publications1
Mutagenesisi194H → Q: Loss of activity. 2 Publications1
Mutagenesisi216H → Q: Loss of activity. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001867382 – 274TyrosinaseAdd BLAST273

Structurei

3D structure databases

ProteinModelPortaliP06845.
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 23, 2007 - v3
Checksum:i0FDC67DC2739AA79
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti216H → N in AAA26834 (PubMed:3002431).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11302 Genomic DNA. Translation: AAA26834.1.
PIRiA24089.
RefSeqiWP_043498008.1. NZ_CP009438.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11302 Genomic DNA. Translation: AAA26834.1.
PIRiA24089.
RefSeqiWP_043498008.1. NZ_CP009438.1.

3D structure databases

ProteinModelPortaliP06845.
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...

Entry informationi

Entry nameiTYRO_STRGA
AccessioniPrimary (citable) accession number: P06845
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: October 5, 2016
This is version 87 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

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 one 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.