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Q01679

- LAC1_PHLRA

UniProt

Q01679 - LAC1_PHLRA

Protein

Laccase

Gene

LAC

Organism
Phlebia radiata (White-rot fungus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 2 (10 May 2004)
      Previous versions | rss
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    Functioni

    Most probably plays an important role in lignin degradation.

    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 bindingi418 – 4181Copper 4; type 1By similarity
    Metal bindingi421 – 4211Copper 1; type 2By similarity
    Metal bindingi423 – 4231Copper 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
    Gene namesi
    Name:LAC
    OrganismiPhlebia radiata (White-rot fungus)
    Taxonomic identifieri5308 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesCorticialesCorticiaceaePhlebia

    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_0000002928Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi352 – 3521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ01679.
    SMRiQ01679. Positions 22-520.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 148127Plastocyanin-like 1Add
    BLAST
    Domaini160 – 304145Plastocyanin-like 2Add
    BLAST
    Domaini373 – 496124Plastocyanin-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.

    Q01679-1 [UniParc]FASTAAdd to Basket

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    MHTFLRSTAL VVAGLSARAL ASIGPVTDFH IVNAAVSPDG FSRQAVLAEG    50
    VFPGPLIAGN KGDNFQINVI DELTNATMLK TTTIHWHGFF QHGTNWADGP 100
    AFINQCPIAS GDSFLYNFQV PDQAGTFWYH SHLSTQYCDG LRGPFVVYDP 150
    ADPYLDQYDV DDDSTVITLA DWYHTAARLG SPFPAADTTL INGLGRCGEA 200
    GCPVSDLAVI SVTKGKRYRF RLVSISCDSF FTFSIDGHSL NVIEVDATNH 250
    QPLTVDELTI YAGQRYSFIL TADQDVDNYW IRANPGIGIT TGFAGGINSA 300
    ILRYDGADVV EPTTTQATSP VVLSESNLAP LTNAAAPGLP EVGGVDLALN 350
    FNLTFDGPSL KFQINGVTFV PPTVPVLLQI LSGAQSAADL LPSGSVYALP 400
    SNATIELSLP AGALGGPHPF HLHGHTFSVV RPAGSTTYNY VNPVQRDVVS 450
    IGNTGDNVTI RFDTNNPGPW FLHCHIDWHL EAGFAVVFAE DIPDVASINP 500
    VPQDWSNLCP IYNALDASDH 520
    Length:520
    Mass (Da):55,704
    Last modified:May 10, 2004 - v2
    Checksum:iB566CE3CA2791D36
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52134 Genomic DNA. Translation: CAA36379.2.
    PIRiS18746.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52134 Genomic DNA. Translation: CAA36379.2 .
    PIRi S18746.

    3D structure databases

    ProteinModelPortali Q01679.
    SMRi Q01679. 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. "Isolation and structural analysis of the laccase gene from the lignin-degrading fungus Phlebia radiata."
      Saloheimo M., Niku-Paavola M.L., Knowles J.K.
      J. Gen. Microbiol. 137:1537-1544(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: ATCC 64658 / 79.
    2. Saloheimo M.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO C-TERMINUS.

    Entry informationi

    Entry nameiLAC1_PHLRA
    AccessioniPrimary (citable) accession number: Q01679
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: May 10, 2004
    Last modified: October 1, 2014
    This is version 77 of the entry and version 2 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