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A7BHQ9

- TYRO_PHONA

UniProt

A7BHQ9 - TYRO_PHONA

Protein

Tyrosinase

Gene

tyr1

Organism
Pholiota nameko
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 27 (01 Oct 2014)
      Sequence version 1 (11 Sep 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.By similarity

    Catalytic activityi

    2 L-dopa + O2 = 2 dopaquinone + 2 H2O.1 Publication
    L-tyrosine + O2 = dopaquinone + H2O.1 Publication

    Cofactori

    Binds 2 copper ions per subunit.1 Publication

    Kineticsi

    1. KM=1930 µM for L-dopa1 Publication
    2. KM=119 µM for t-butylphenol1 Publication
    3. KM=30.6 µM for p-cresol1 Publication
    4. KM=163 µM for t-butylcatechol1 Publication
    5. KM=1240 µM for 3-(3,4-dihydroxyphenyl) propionic acid1 Publication
    6. KM=122 µM for dopamine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi58 – 581Copper ABy similarity
    Metal bindingi86 – 861Copper ABy similarity
    Metal bindingi95 – 951Copper ABy similarity
    Metal bindingi258 – 2581Copper BBy similarity
    Metal bindingi262 – 2621Copper BBy similarity
    Metal bindingi287 – 2871Copper BBy similarity

    GO - Molecular functioni

    1. copper ion binding Source: UniProtKB
    2. monophenol monooxygenase activity Source: UniProtKB

    GO - Biological processi

    1. melanin biosynthetic process Source: UniProtKB-KW
    2. oxidation-reduction process Source: UniProtKB

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Melanin biosynthesis

    Keywords - Ligandi

    Copper, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TyrosinaseImported1 Publication (EC:1.14.18.1)
    Gene namesi
    Name:tyr1Imported
    OrganismiPholiota nameko
    Taxonomic identifieri61267 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesStrophariaceaePholiota

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 387387Tyrosinase1 PublicationPRO_0000352767Add
    BLAST
    Propeptidei388 – 6252381 PublicationPRO_0000352768Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.1 Publication

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliA7BHQ9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi367 – 45185Ala-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the tyrosinase family.Sequence Analysis

    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.

    A7BHQ9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRVVITGVS GTIANRLEIN DFVKNDKFFS LYIQALQVMS SVPPQENVRS    50
    FFQIGGIHGL PYTPWDGITG DQPFDPNTQW GGYCTHGSVL FPTWHRPYVL 100
    LYEQILHKHV QDIAATYTTS DKAAWVQAAA NLRQPYWDWA ANAVPPDQVI 150
    VSKKVTITGS NGHKVEVDNP LYHYKFHPID SSFPRPYSEW PTTLRQPNSS 200
    RPNATDNVAK LRNVLRASQE NITSNTYSML TRVHTWKAFS NHTVGDGGST 250
    SNSLEAIHDG IHVDVGGGGH MGDPAVAAFD PIFFLHHCNV DRLLSLWAAI 300
    NPGVWVSPGD SEDGTFILPP EAPVDVSTPL TPFSNTETTF WASGGITDTT 350
    KLGYTYPEFN GLDLGNAQAV KAAIGNIVNR LYGASVFSGF AAATSAIGAG 400
    SVASLAADVP LEKAPAPAPE AAAQPPVPAP AHVEPAVRAV SVHAAAAQPH 450
    AEPPVHVSAG GHPSPHGFYD WTARIEFKKY EFGSSFSVLL FLGPVPEDPE 500
    QWLVSPNFVG AHHAFVNSAA GHCANCRSQG NVVVEGFVHL TKYISEHAGL 550
    RSLNPEVVEP YLTNELHWRV LKADGSVGQL ESLEVSVYGT PMNLPVGAMF 600
    PVPGNRRHFH GITHGRVGGS RHAIV 625
    Length:625
    Mass (Da):67,499
    Last modified:September 11, 2007 - v1
    Checksum:i26E8AEFA285F871B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131I → V in BAF74396. (PubMed:17617709)Curated
    Sequence conflicti151 – 1511V → A in BAF74396. (PubMed:17617709)Curated
    Sequence conflicti272 – 2721G → A in BAF74396. (PubMed:17617709)Curated
    Sequence conflicti425 – 4251P → S in BAF74396. (PubMed:17617709)Curated
    Sequence conflicti528 – 5281S → N in BAF74396. (PubMed:17617709)Curated

    Mass spectrometryi

    Molecular mass is 42424.39 Da from positions 1 - 387. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB275646 mRNA. Translation: BAF74395.1.
    AB275647 mRNA. Translation: BAF74396.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB275646 mRNA. Translation: BAF74395.1 .
    AB275647 mRNA. Translation: BAF74396.1 .

    3D structure databases

    ProteinModelPortali A7BHQ9.
    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. "Purification, characterization, and molecular cloning of tyrosinase from Pholiota nameko."
      Kawamura-Konishi Y., Tsuji M., Hatana S., Asanuma M., Kakuta D., Kawano T., Mukouyama E.B., Goto H., Suzuki H.
      Biosci. Biotechnol. Biochem. 71:1752-1760(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 154-164; 175-195; 351-362 AND 384-387, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MASS SPECTROMETRY.
      Tissue: Fruiting body1 Publication.

    Entry informationi

    Entry nameiTYRO_PHONA
    AccessioniPrimary (citable) accession number: A7BHQ9
    Secondary accession number(s): A7BHR0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 14, 2008
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 27 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3