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O42713

- PPO2_AGABI

UniProt

O42713 - PPO2_AGABI

Protein

Polyphenol oxidase 2

Gene

PPO2

Organism
Agaricus bisporus (White button mushroom)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Copper-containing oxidase that catalyzes both the o-hydroxylation of monophenols and the subsequent oxidation of the resulting o-diphenols into reactive o-quinones, which evolve spontaneously to produce intermediates, which associate in dark brown pigments. Involved in the initial step of melanin synthesis. Melanins constitute a mechanism of defense and resistance to stress such as UV radiations, free radicals, gamma rays, dehydratation and extreme temperatures, and contribute to the fungal cell-wall resistance against hydrolytic enzymes in avoiding cellular lysis. Fungal pigments are also involved in the formation and stability of spores By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 2 copper ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi57 – 571Copper 1; via tele nitrogenBy similarity
    Metal bindingi81 – 811Copper 1; via tele nitrogenBy similarity
    Metal bindingi90 – 901Copper 1; via tele nitrogenBy similarity
    Metal bindingi250 – 2501Copper 2; via tele nitrogenBy similarity
    Metal bindingi254 – 2541Copper 2; via tele nitrogenBy similarity
    Binding sitei254 – 2541SubstrateBy similarity
    Metal bindingi282 – 2821Copper 2; via tele nitrogenBy similarity
    Sitei378 – 3792CleavageCurated

    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

    Enzyme and pathway databases

    SABIO-RKO42713.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyphenol oxidase 2 (EC:1.14.18.1)
    Short name:
    PPO2
    Short name:
    Phenolase 2
    Alternative name(s):
    Cresolase 2
    Tyrosinase 2
    Gene namesi
    Name:PPO2
    OrganismiAgaricus bisporus (White button mushroom)
    Taxonomic identifieri5341 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 378378Polyphenol oxidase 2PRO_0000186731Add
    BLAST
    Propeptidei379 – 556178Removed in mature formCuratedPRO_0000416863Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki79 ↔ 812'-(S-cysteinyl)-histidine (Cys-His)By similarity

    Post-translational modificationi

    The C-ter is probably cleaved after Gly-378 since the mature active protein is smaller than the protein encoded by the gene.By similarity

    Keywords - PTMi

    Thioether bond

    Expressioni

    Developmental stagei

    Expressed during the fruiting body stage.1 Publication

    Interactioni

    Subunit structurei

    Heterotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO42713.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tyrosinase family.Curated

    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.

    O42713-1 [UniParc]FASTAAdd to Basket

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    MSLIATVGPT GGVKNRLNIV DFVKNEKFFT LYVRSLELLQ AKEQHDYSSF    50
    FQLAGIHGLP FTEWAKERPS MNLYKAGYCT HGQVLFPTWH RTYLSVLEQI 100
    LQGAAIEVAK KFTSNQTDWV QAAQDLRQPY WDWGFELMPP DEVIKNEEVN 150
    ITNYDGKKIS VKNPILRYHF HPIDPSFKPY GDFATWRTTV RNPDRNRRED 200
    IPGLIKKMRL EEGQIREKTY NMLKFNDAWE RFSNHGISDD QHANSLESVH 250
    DDIHVMVGYG KIEGHMDHPF FAAFDPIFWL HHTNVDRLLS LWKAINPDVW 300
    VTSGRNRDGT MGIAPNAQIN SETPLEPFYQ SGDKVWTSAS LADTARLGYS 350
    YPDFDKLVGG TKELIRDAID DLIDERYGSK PSSGARNTAF DLLADFKGIT 400
    KEHKEDLKMY DWTIHVAFKK FELKESFSLL FYFASDGGDY DQENCFVGSI 450
    NAFRGTAPET CANCQDNENL IQEGFIHLNH YLARDLESFE PQDVHKFLKE 500
    KGLSYKLYSR GDKPLTSLSV KIEGRPLHLP PGEHRPKYDH TQARVVFDDV 550
    AVHVIN 556
    Length:556
    Mass (Da):63,927
    Last modified:June 1, 1998 - v1
    Checksum:iDE10827A209895DA
    GO

    Sequence cautioni

    The sequence CAA61562.1 differs from that shown. Reason: Frameshift at position 445.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ223816 mRNA. Translation: CAA11562.1.
    X89382 mRNA. Translation: CAA61562.1. Frameshift.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ223816 mRNA. Translation: CAA11562.1 .
    X89382 mRNA. Translation: CAA61562.1 . Frameshift.

    3D structure databases

    ProteinModelPortali O42713.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi O42713.
    ChEMBLi CHEMBL3318.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK O42713.

    Family and domain databases

    Gene3Di 1.10.1280.10. 1 hit.
    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. 1 hit.
    PROSITEi PS00497. TYROSINASE_1. 1 hit.
    PS00498. TYROSINASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression and characterisation of two tyrosinase cDNAs from Agaricus bisporus."
      Wichers H., Recourt K., Hendriks M., Ebbelaar C.E.M., Biancone G., Hoeberichts F., Mooibroek H., Soler-Rivas C.
      Appl. Microbiol. Biotechnol. 61:336-341(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Horst U1.
    2. "Characterization of a fruiting body-expressed gene encoding a putative polyphenol oxidase of Agaricus bisporus."
      Ebbelar C.E.M., Wichers H.J., Van Den Bosch T., Oyevaar J.I., Recourt K.
      Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-556.
      Strain: Horst U1.
    3. "Expression of phenol oxidase and heat-shock genes during the development of Agaricus bisporus fruiting bodies, healthy and infected by Lecanicillium fungicola."
      Largeteau M.L., Latapy C., Minvielle N., Regnault-Roger C., Savoie J.M.
      Appl. Microbiol. Biotechnol. 85:1499-1507(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiPPO2_AGABI
    AccessioniPrimary (citable) accession number: O42713
    Secondary accession number(s): Q12543
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 63 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3