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Q02497

- LAC1_TRAHI

UniProt

Q02497 - LAC1_TRAHI

Protein

Laccase

Gene
N/A
Organism
Trametes hirsuta (White-rot fungus) (Coriolus hirsutus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Most probably plays an important role in lignin degradation. Cleaves the C-C and C-O bonds of some phenolic lignin model compounds (such as O- and P-quinols, aminophenols and phenylenediamine).

    Catalytic activityi

    4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

    Cofactori

    Binds 4 copper ions per monomer.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi85 – 851Copper 1; type 2By similarity
    Metal bindingi87 – 871Copper 2; type 3By similarity
    Metal bindingi130 – 1301Copper 2; type 3By similarity
    Metal bindingi132 – 1321Copper 3; type 3By similarity
    Metal bindingi416 – 4161Copper 4; type 1By similarity
    Metal bindingi419 – 4191Copper 1; type 2By similarity
    Metal bindingi421 – 4211Copper 3; type 3By similarity
    Metal bindingi473 – 4731Copper 3; type 3By similarity
    Metal bindingi474 – 4741Copper 4; type 1By similarity
    Metal bindingi475 – 4751Copper 2; type 3By similarity
    Metal bindingi479 – 4791Copper 4; type 1By similarity

    GO - Molecular functioni

    1. copper ion binding Source: InterPro
    2. hydroquinone:oxygen oxidoreductase activity Source: UniProtKB-EC

    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 (EC:1.10.3.2)
    Alternative name(s):
    Benzenediol:oxygen oxidoreductase
    Diphenol oxidase
    Ligninolytic phenoloxidase
    Urishiol oxidase
    OrganismiTrametes hirsuta (White-rot fungus) (Coriolus hirsutus)
    Taxonomic identifieri5327 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesTrametes

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Add
    BLAST
    Chaini22 – 520499LaccasePRO_0000002939Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi50 – 501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi106 ↔ 509Sequence Analysis
    Disulfide bondi138 ↔ 226Sequence Analysis
    Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi229 – 2291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ02497.
    SMRiQ02497. Positions 22-520.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 148126Plastocyanin-like 1Add
    BLAST
    Domaini160 – 302143Plastocyanin-like 2Add
    BLAST
    Domaini369 – 491123Plastocyanin-like 3Add
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di2.60.40.420. 3 hits.
    InterProiIPR001117. Cu-oxidase.
    IPR011706. Cu-oxidase_2.
    IPR011707. Cu-oxidase_3.
    IPR002355. Cu_oxidase_Cu_BS.
    IPR008972. Cupredoxin.
    [Graphical view]
    PfamiPF00394. Cu-oxidase. 1 hit.
    PF07731. Cu-oxidase_2. 1 hit.
    PF07732. Cu-oxidase_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF49503. SSF49503. 3 hits.
    PROSITEiPS00079. MULTICOPPER_OXIDASE1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q02497-1 [UniParc]FASTAAdd to Basket

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    MSRFQSLLAF VVASLAAVAH AAIGPTADLT ISNAEVSPDG FARQAVVVNN    50
    VTPGPLVAGN KGDRFQLNVI DNLTNHTMLK STSIHWHGFF QKGTNWADGP 100
    AFVNQCPISS GHSFLYDFQV PDQAGTFWYH SHLSTQYCDG LRGPFVVYDP 150
    NDPHASLYDV DNDDTVITLA DWYHTAAKLG PAFPLGADAT LINGLGRSPS 200
    TTAADLAVIN VTKGKRYRFR LVSLSCDPNH TFSIDGHDLT IIEVDSINSQ 250
    PLVVDSIQIF AAQRYSFVLN ADQDVGNYWI RANPNFGNVG FAGGINSAIL 300
    RYDGADPVEP TTTQTTPTKP LNEVDLHPLA TMAVPGSPVA GGVDTAINMA 350
    FNFNGTNFFI NGASFVPPTV PVLLQIISGA QNAQDLLPSG SVYSLPSNAD 400
    IEISFPATAA APGAPHPFHL HGHAFAVVRS AGSTVYNYDN PIFRDVVSTG 450
    TPAAGDNVTI RFRTDNPGPW FLHCHIDFHL EAGFAVVFAE DIPDVASANP 500
    VPQAWSDLCP IYDALDVNDQ 520
    Length:520
    Mass (Da):55,688
    Last modified:October 1, 1996 - v1
    Checksum:i977D8DFA551F7929
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti378 – 3792SG → RR in AAA33104. (PubMed:2394718)Curated

    Polymorphismi

    2 allelic forms exist in position 111.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti411 – 4111A → P.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60560 Genomic DNA. Translation: AAA33103.1.
    M60561 Genomic DNA. Translation: AAA33104.1.
    PIRiA35883.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60560 Genomic DNA. Translation: AAA33103.1 .
    M60561 Genomic DNA. Translation: AAA33104.1 .
    PIRi A35883.

    3D structure databases

    ProteinModelPortali Q02497.
    SMRi Q02497. Positions 22-520.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.40.420. 3 hits.
    InterProi IPR001117. Cu-oxidase.
    IPR011706. Cu-oxidase_2.
    IPR011707. Cu-oxidase_3.
    IPR002355. Cu_oxidase_Cu_BS.
    IPR008972. Cupredoxin.
    [Graphical view ]
    Pfami PF00394. Cu-oxidase. 1 hit.
    PF07731. Cu-oxidase_2. 1 hit.
    PF07732. Cu-oxidase_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49503. SSF49503. 3 hits.
    PROSITEi PS00079. MULTICOPPER_OXIDASE1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequence analysis, and expression of ligninolytic phenoloxidase genes of the white-rot basidiomycete Coriolus hirsutus."
      Kojima Y., Tsukuda Y., Kawai Y., Tsukamoto A., Sugiura J., Sakaino M., Kita Y.
      J. Biol. Chem. 265:15224-15230(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, VARIANT PRO-411.
      Strain: NBRC 4917.

    Entry informationi

    Entry nameiLAC1_TRAHI
    AccessioniPrimary (citable) accession number: Q02497
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 71 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