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Q00234

- TYRO_ASPOR

UniProt

Q00234 - TYRO_ASPOR

Protein

Tyrosinase

Gene

melO

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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.

    Enzyme regulationi

    Activated by acidifying treatment at pH 3.0.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi63 – 631Copper ABy similarity
    Metal bindingi84 – 841Copper ABy similarity
    Metal bindingi93 – 931Copper ABy similarity
    Metal bindingi290 – 2901Copper BBy similarity
    Metal bindingi294 – 2941Copper BBy similarity
    Metal bindingi333 – 3331Copper BBy similarity

    GO - Molecular functioni

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

    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:melO
    ORF Names:AO090038000061
    OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
    Taxonomic identifieri510516 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006564: Chromosome 6

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 539539TyrosinasePRO_0000186733Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki82 ↔ 842'-(S-cysteinyl)-histidine (Cys-His)By similarity

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Thioether bond

    Proteomic databases

    PRIDEiQ00234.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    STRINGi5062.CADAORAP00008707.

    Structurei

    3D structure databases

    ProteinModelPortaliQ00234.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tyrosinase family.Curated

    Phylogenomic databases

    HOGENOMiHOG000250264.
    OMAiENDTASF.
    OrthoDBiEOG7JX3D0.

    Family and domain databases

    Gene3Di1.10.1280.10. 3 hits.
    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. 2 hits.
    PROSITEiPS00497. TYROSINASE_1. 1 hit.
    PS00498. TYROSINASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q00234-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASVEPIKTF EIRQKGPVET KAERKSIRDL NEEELDKLIE AWRWIQDPAR    50
    TGEDSFFYLA GLHGEPFRGA GYNNSHWWGG YCHHGNILFP TWHRAYLMAV 100
    EKALRKACPD VSLPYWDESD DETAKKGIPL IFTQKEYKGK PNPLYSYTFS 150
    ERIVDRLAKF PDADYSKPQG YKTCRYPYSG LCGQDDIAIA QQHNNFLDAN 200
    FNQEQITGLL NSNVTSWLNL GQFTDIEGKQ VKADTRWKIR QCLLTEEYTV 250
    FSNTTSAQRW NDEQFHPLES GGKETEAKAT SLAVPLESPH NDMHLAIGGV 300
    QIPGFNVDQY AGANGDMGEN DTASFDPIFY FHHCFIDYLF WTWQTMHKKT 350
    DASQITILPE YPGTNSVDSQ GPTPGISGNT WLTLDTPLDP FRENGDKVTS 400
    NKLLTLKDLP YTYKAPTSGT GSVFNDVPRL NYPLSPPILR VSGINRASIA 450
    GSFALAISQT DHTGKAQVKG IESVLSRWHV QGCANCQTHL STTAFVPLFE 500
    LNEDDAKRKH ANNELAVHLH TRGNPGGQRV RNVTVGTMR 539
    Length:539
    Mass (Da):60,605
    Last modified:November 1, 1996 - v1
    Checksum:iCD2ECD702A018E15
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D37929 Genomic DNA. Translation: BAA07149.1.
    AP007169 Genomic DNA. Translation: BAE63910.1.
    PIRiS53529.
    RefSeqiXP_001825043.1. XM_001824991.2.

    Genome annotation databases

    EnsemblFungiiCADAORAT00008890; CADAORAP00008707; CADAORAG00008890.
    GeneIDi5997138.
    KEGGiaor:AOR_1_92074.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D37929 Genomic DNA. Translation: BAA07149.1 .
    AP007169 Genomic DNA. Translation: BAE63910.1 .
    PIRi S53529.
    RefSeqi XP_001825043.1. XM_001824991.2.

    3D structure databases

    ProteinModelPortali Q00234.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5062.CADAORAP00008707.

    Proteomic databases

    PRIDEi Q00234.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAORAT00008890 ; CADAORAP00008707 ; CADAORAG00008890 .
    GeneIDi 5997138.
    KEGGi aor:AOR_1_92074.

    Phylogenomic databases

    HOGENOMi HOG000250264.
    OMAi ENDTASF.
    OrthoDBi EOG7JX3D0.

    Family and domain databases

    Gene3Di 1.10.1280.10. 3 hits.
    InterProi IPR016216. Monophenol_mOase_fun.
    IPR002227. Tyrosinase_Cu-bd.
    IPR008922. Unchr_di-copper_centre.
    [Graphical view ]
    Pfami PF00264. Tyrosinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000340. MPO_fungal. 1 hit.
    PRINTSi PR00092. TYROSINASE.
    SUPFAMi SSF48056. SSF48056. 2 hits.
    PROSITEi PS00497. TYROSINASE_1. 1 hit.
    PS00498. TYROSINASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and nucleotide sequence of the protyrosinase gene, melO, from Aspergillus oryzae and expression of the gene in yeast cells."
      Fujita Y., Uraga Y., Ichishima E.
      Biochim. Biophys. Acta 1261:151-154(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: ATCC 22788 / RIB 128 / CBS 819.72 / IFO 30113 / JCM 2248.
    2. "Genome sequencing and analysis of Aspergillus oryzae."
      Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
      , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
      Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 42149 / RIB 40.

    Entry informationi

    Entry nameiTYRO_ASPOR
    AccessioniPrimary (citable) accession number: Q00234
    Secondary accession number(s): Q2U3F5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 81 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3