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Protein

Tyrosinase

Gene

tyr1

Organism
Pholiota nameko
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.By similarity

Catalytic activityi

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

Cofactori

Cu2+1 PublicationNote: 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

    • copper ion binding Source: UniProtKB
    • monophenol monooxygenase activity Source: UniProtKB

    GO - Biological processi

    • melanin biosynthetic process Source: UniProtKB-KW
    • oxidation-reduction process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Melanin biosynthesis

    Keywords - Ligandi

    Copper, Metal-binding

    Enzyme and pathway databases

    BRENDAi1.14.18.1. 4764.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosinase1 PublicationImported (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.
    InterProiIPR016216. Monophenol_mOase_fun.
    IPR002227. Tyrosinase_Cu-bd.
    IPR008922. Unchr_di-copper_centre.
    [Graphical view]
    PfamiPF00264. Tyrosinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000340. MPO_fungal. 1 hit.
    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

            10         20         30         40         50
    MSRVVITGVS GTIANRLEIN DFVKNDKFFS LYIQALQVMS SVPPQENVRS
    60 70 80 90 100
    FFQIGGIHGL PYTPWDGITG DQPFDPNTQW GGYCTHGSVL FPTWHRPYVL
    110 120 130 140 150
    LYEQILHKHV QDIAATYTTS DKAAWVQAAA NLRQPYWDWA ANAVPPDQVI
    160 170 180 190 200
    VSKKVTITGS NGHKVEVDNP LYHYKFHPID SSFPRPYSEW PTTLRQPNSS
    210 220 230 240 250
    RPNATDNVAK LRNVLRASQE NITSNTYSML TRVHTWKAFS NHTVGDGGST
    260 270 280 290 300
    SNSLEAIHDG IHVDVGGGGH MGDPAVAAFD PIFFLHHCNV DRLLSLWAAI
    310 320 330 340 350
    NPGVWVSPGD SEDGTFILPP EAPVDVSTPL TPFSNTETTF WASGGITDTT
    360 370 380 390 400
    KLGYTYPEFN GLDLGNAQAV KAAIGNIVNR LYGASVFSGF AAATSAIGAG
    410 420 430 440 450
    SVASLAADVP LEKAPAPAPE AAAQPPVPAP AHVEPAVRAV SVHAAAAQPH
    460 470 480 490 500
    AEPPVHVSAG GHPSPHGFYD WTARIEFKKY EFGSSFSVLL FLGPVPEDPE
    510 520 530 540 550
    QWLVSPNFVG AHHAFVNSAA GHCANCRSQG NVVVEGFVHL TKYISEHAGL
    560 570 580 590 600
    RSLNPEVVEP YLTNELHWRV LKADGSVGQL ESLEVSVYGT PMNLPVGAMF
    610 620
    PVPGNRRHFH GITHGRVGGS RHAIV
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB275646 mRNA. Translation: BAF74395.1.
    AB275647 mRNA. Translation: BAF74396.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB275646 mRNA. Translation: BAF74395.1.
    AB275647 mRNA. Translation: BAF74396.1.

    3D structure databases

    ProteinModelPortaliA7BHQ9.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi1.14.18.1. 4764.

    Family and domain databases

    Gene3Di1.10.1280.10. 1 hit.
    InterProiIPR016216. Monophenol_mOase_fun.
    IPR002227. Tyrosinase_Cu-bd.
    IPR008922. Unchr_di-copper_centre.
    [Graphical view]
    PfamiPF00264. Tyrosinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000340. MPO_fungal. 1 hit.
    PRINTSiPR00092. TYROSINASE.
    SUPFAMiSSF48056. SSF48056. 1 hit.
    PROSITEiPS00497. TYROSINASE_1. 1 hit.
    PS00498. TYROSINASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    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: May 27, 2015
    This is version 30 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

    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.