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D0VWU3

- LAC1_TRAMX

UniProt

D0VWU3 - LAC1_TRAMX

Protein

Laccase

Gene
N/A
Organism
Trametes maxima (White-rot fungus) (Cerrena maxima)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 21 (01 Oct 2014)
      Sequence version 1 (15 Dec 2009)
      Previous versions | rss
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    Functioni

    Lignin degradation and detoxification of lignin-derived products.2 PublicationsCurated

    Catalytic activityi

    4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.2 Publications

    Cofactori

    Binds 4 copper ions per monomer.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi64 – 641Copper 1; type 2
    Metal bindingi66 – 661Copper 2; type 3
    Metal bindingi109 – 1091Copper 2; type 3
    Metal bindingi111 – 1111Copper 3; type 3
    Metal bindingi395 – 3951Copper 4; type 1
    Metal bindingi398 – 3981Copper 1; type 2
    Metal bindingi400 – 4001Copper 3; type 3
    Metal bindingi452 – 4521Copper 3; type 3
    Metal bindingi453 – 4531Copper 4; type 1
    Metal bindingi454 – 4541Copper 2; type 3
    Metal bindingi458 – 4581Copper 4; type 1

    GO - Molecular functioni

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

    GO - Biological processi

    1. lignin catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lignin degradation

    Keywords - Ligandi

    Copper, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    LaccaseImported2 Publications (EC:1.10.3.2)
    Alternative name(s):
    Benzenediol:oxygen oxidoreductaseBy similarity
    Diphenol oxidaseBy similarity
    Urishiol oxidaseBy similarity
    OrganismiTrametes maxima (White-rot fungus) (Cerrena maxima)
    Taxonomic identifieri259368 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesTrametes

    Subcellular locationi

    Secreted 2 Publications

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 499499LaccasePRO_0000401149Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi51 – 511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi54 – 541N-linked (GlcNAc...)3 Publications
    Disulfide bondi85 ↔ 4882 Publications
    Disulfide bondi117 ↔ 2052 Publications
    Modified residuei196 – 19613'-nitrotyrosine3 Publications
    Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi217 – 2171N-linked (GlcNAc...)3 Publications
    Glycosylationi292 – 2921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi333 – 3331N-linked (GlcNAc...)1 Publication
    Modified residuei372 – 37213'-nitrotyrosine3 Publications
    Glycosylationi377 – 3771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi436 – 4361N-linked (GlcNAc...)2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Nitration

    Structurei

    Secondary structure

    1
    499
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 1512
    Beta strandi22 – 276
    Beta strandi30 – 323
    Beta strandi36 – 394
    Beta strandi43 – 508
    Helixi55 – 573
    Beta strandi63 – 664
    Helixi74 – 763
    Turni80 – 823
    Beta strandi92 – 987
    Beta strandi104 – 1107
    Helixi115 – 1184
    Beta strandi121 – 1277
    Helixi134 – 1363
    Helixi142 – 1443
    Beta strandi145 – 1517
    Turni156 – 1583
    Beta strandi167 – 1715
    Beta strandi187 – 1904
    Beta strandi195 – 2028
    Beta strandi209 – 2135
    Beta strandi218 – 2236
    Beta strandi226 – 23813
    Beta strandi243 – 2497
    Beta strandi254 – 26714
    Helixi271 – 2733
    Beta strandi276 – 2816
    Beta strandi297 – 2993
    Helixi302 – 3043
    Beta strandi307 – 3093
    Beta strandi322 – 3276
    Beta strandi330 – 3323
    Beta strandi337 – 3393
    Helixi351 – 3566
    Turni362 – 3643
    Beta strandi365 – 3673
    Beta strandi370 – 3745
    Beta strandi379 – 3857
    Beta strandi396 – 3994
    Beta strandi404 – 4085
    Beta strandi417 – 4193
    Beta strandi422 – 4276
    Turni431 – 4344
    Beta strandi436 – 4427
    Beta strandi447 – 4559
    Helixi456 – 4605
    Beta strandi464 – 4707
    Helixi471 – 4733
    Helixi474 – 4774
    Helixi482 – 4854
    Helixi487 – 4926
    Helixi496 – 4983

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H5UX-ray1.90A2-499[»]
    3DIVX-ray1.76A1-499[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiD0VWU3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 127126Plastocyanin-like 1Add
    BLAST
    Domaini139 – 281143Plastocyanin-like 2Add
    BLAST
    Domaini348 – 470123Plastocyanin-like 3Add
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    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.

    D0VWU3-1 [UniParc]FASTAAdd to Basket

    « Hide

    AVGPVADNTI TDAATSPDGF SRQAVVVNGV TPGPLVAGNI GDRFQLNVID    50
    NLTNHTMLKT TSVHWHGFFQ QGTNWADGPA FINQCPISPG HSFLYDFQVP 100
    NQAGTFWYHS HLSTQYCDGL RGPFVVYDPN DPHASRYDVD NDDTVITLAD 150
    WYHTAAKLGP RFPAGADATL INGKGRAPSD TSAELSVIKV TKGKRYRFRL 200
    VSLSCDPNFT FSIDGHNLTI IEVDSSNSQP LSVDSIQIFA AQRYSFVLNA 250
    NQAVDNYWIR ANPNFGNVGF NGGINSAILR YDGAPAVEPT TNQTTSVKPL 300
    NEVNLHPLVS TPVPGSPSSG GVDKAINMAF NFNGSNFFIN GASFVPPSVP 350
    VLLQILSGAQ TAQDLLPSGS VYVLPSNASI EISFPATAAA PGAPHPFHLH 400
    GHTFAVVRSA GSTVYNYSNP IFRDVVSTGT PAAGDNVTIR FLTNNPGPWF 450
    LHCHIDFHLE GGFAVVQAED VPDVKATNPV PQAWSDLCPT YDANAPSDQ 499
    Length:499
    Mass (Da):53,451
    Last modified:December 15, 2009 - v1
    Checksum:iF018B0357333CF33
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H5U X-ray 1.90 A 2-499 [» ]
    3DIV X-ray 1.76 A 1-499 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei D0VWU3.

    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. Cited for: CRYSTALLIZATION, PRELIMINARY X-RAY CRYSTALLOGRAPHY, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, NITRATION AT TYR-196 AND TYR-372, GLYCOSYLATION AT ASN-54; ASN-217 AND ASN-436, DISULFIDE BONDS.
      Strain: 02751 Publication.
    2. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, NITRATION AT TYR-196 AND TYR-372, GLYCOSYLATION AT ASN-54; ASN-217; ASN-333 AND ASN-436, DISULFIDE BONDS.
      Strain: 02751 Publication.
    3. Lyashenko A.V., Zhukova Y.N., Mikhailov A.M.
      Submitted (JUN-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS), COPPER-BINDING SITES, NITRATION AT TYR-196 AND TYR-372, GLYCOSYLATION AT ASN-54 AND ASN-217, DISULFIDE BONDS.

    Entry informationi

    Entry nameiLAC1_TRAMX
    AccessioniPrimary (citable) accession number: D0VWU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 30, 2010
    Last sequence update: December 15, 2009
    Last modified: October 1, 2014
    This is version 21 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

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3