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P06845

- TYRO_STRGA

UniProt

P06845 - TYRO_STRGA

Protein

Tyrosinase

Gene

melC2

Organism
Streptomyces glaucescens
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    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

    MTVRKNQATL TADEKRRFVA AVLELKRSGR YDEFVTTHNA FIIGDTDAGE    50
    RTGHRSPSFL PWHRRYLLEF ERALQSVDAS VALPYWDWSA DRTARASLWA 100
    PDFLGGTGRS LDGRVMDGPF AASAGNWPIN VRVDGRAYLR RSLGTAVREL 150
    PTRAEVESVL GMATYDTAPW NSASDGFRNH LEGWRGVNLH NRVHVWVGGQ 200
    MATGMSPNDP VFWLHHAYVD KLWAEWQRRH PGSGYLPAAG TPDVVDLNDR 250
    MKPWNDTSPA DLLDHTAHYT FDTD 274
    Length:274
    Mass (Da):30,874
    Last modified:January 23, 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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11302 Genomic DNA. Translation: AAA26834.1.
    PIRiA24089.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11302 Genomic DNA. Translation: AAA26834.1 .
    PIRi A24089.

    3D structure databases

    ProteinModelPortali P06845.
    SMRi P06845. Positions 2-272.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.10.1280.10. 1 hit.
    InterProi IPR002227. Tyrosinase_Cu-bd.
    IPR008922. Unchr_di-copper_centre.
    [Graphical view ]
    Pfami PF00264. Tyrosinase. 1 hit.
    [Graphical view ]
    PRINTSi PR00092. TYROSINASE.
    SUPFAMi SSF48056. SSF48056. 1 hit.
    PROSITEi PS00497. TYROSINASE_1. 1 hit.
    PS00498. TYROSINASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    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 1, 2014
    This is version 79 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