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P85430

- LAC2D_CERUI

UniProt

P85430 - LAC2D_CERUI

Protein

Laccase-2d

Gene
N/A
Organism
Cerrena unicolor (Canker rot fungus) (Daedalea unicolor)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Lignin degradation and detoxification of lignin-derived products Probable. Has highest activity towards ABTS, also active towards ferulic acid and guaiacol, but is not active towards tyrosine, vanillic acid, 2,5-dimethyl aniline, p-anisidine or violuric acid.1 PublicationCurated

    Catalytic activityi

    4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.By similarity1 Publication

    Cofactori

    Binds 4 copper ions per monomer.By similarity

    Enzyme regulationi

    Inhibited by sodium azide, SDS and mercaptoethanol, but not by 4-hexyl resocinol, L-cysteine and dithiothreitol. Activity is inhibited by the heavy metal ions Cr, W, Sn, Ag+ and Hg2+, but not by Pb2+, Fe3+, Ni2+, Li2+, Co2+ or Cd2+.1 Publication

    Kineticsi

    1. KM=54.1 µM for ABTS (at 70 degrees Celsius)1 Publication
    2. KM=57.1 µM for ABTS (at 30 degrees Celsius)1 Publication
    3. KM=19.2 µM for syringaldizine (at 30 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 3.0 at 70 degrees Celsius with ABTS as substrate, and 6.0 with guaiacol and syringaldazine as substrate.1 Publication

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius at pH 3.0 with ABTS as substrate. Retains 100% of its activity after 1 hour at 30 degrees Celsius at pH 9.0. Retains more than 60% of its activity after 180 minutes at 60 degrees Celsius at pH 9.0. Retains approximately 50% of its activity after 90 minutes at 70 degrees Celsius at pH 9.0.1 Publication

    GO - Molecular functioni

    1. hydroquinone:oxygen oxidoreductase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. lignin catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lignin degradation

    Keywords - Ligandi

    Copper, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laccase-2d1 Publication (EC:1.10.3.2)
    Alternative name(s):
    Benzenediol:oxygen oxidoreductaseBy similarity
    Diphenol oxidaseBy similarity
    Laccase-IId1 Publication
    Short name:
    Lac-IId1 Publication
    Urishiol oxidaseBy similarity
    OrganismiCerrena unicolor (Canker rot fungus) (Daedalea unicolor)
    Taxonomic identifieri90312 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPolyporaceaeCerrena

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›47›47Laccase-2dPRO_0000320022Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated; contains 17% carbohydrates.1 Publication

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini? – ›47Plastocyanin-like 3Sequence Analysis
    Domaini2 – ?Plastocyanin-like 1Sequence Analysis

    Sequence similaritiesi

    Belongs to the multicopper oxidase family.Sequence Analysis
    Contains 3 plastocyanin-like domains.Sequence Analysis

    Keywords - Domaini

    Repeat

    Sequencei

    Sequence statusi: Fragments.

    P85430-1 [UniParc]FASTAAdd to Basket

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    GTGPVADLHI INKDLSPDGF QRPTVVAGGG RDVVSIGRAG DNVTIRF      47
    Length:47
    Mass (Da):4,846
    Last modified:September 2, 2008 - v2
    Checksum:iDFC1942A188FC2B9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-adjacent residuesi30 – 3121 Publication
    Non-terminal residuei47 – 4711 Publication

    Cross-referencesi

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "A thermostable metal-tolerant laccase with bioremediation potential from a marine-derived fungus."
      D'Souza-Ticlo D., Sharma D., Raghukumar C.
      Mar. Biotechnol. 11:725-737(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION.
      Strain: MTCC 51591 Publication.

    Entry informationi

    Entry nameiLAC2D_CERUI
    AccessioniPrimary (citable) accession number: P85430
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 22 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    On the 2D-gel the determined pI of this protein is: 5.3, its MW is: 59 kDa.1 Publication

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3