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Q70KY3

- LAC1_MELAO

UniProt

Q70KY3 - LAC1_MELAO

Protein

Laccase-1

Gene

LAC1

Organism
Melanocarpus albomyces
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Lignin degradation and detoxification of lignin-derived products.1 PublicationCurated

    Catalytic activityi

    4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.1 Publication

    Cofactori

    Binds 4 copper ions per monomer.2 Publications

    Absorptioni

    Abs(max)=280 nm2 Publications

    Exhibits a shoulder at 360 nm, a smaller absorption peak at 450 nm, and a second, larger peak at 590 nm.1 Publication

    pH dependencei

    Optimum pH is 3.5 with 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulphonate) as substrate, 5.0-7.5 with guiacol as substrate, and 6.0-7.0 with syringaldazine as substrate.2 Publications

    Temperature dependencei

    Optimum temperature is 60-70 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi143 – 1431Copper 11 Publication
    Metal bindingi145 – 1451Copper 21 Publication
    Metal bindingi188 – 1881Copper 21 Publication
    Metal bindingi190 – 1901Copper 31 Publication
    Metal bindingi481 – 4811Copper 41 Publication
    Metal bindingi484 – 4841Copper 11 Publication
    Metal bindingi486 – 4861Copper 31 Publication
    Metal bindingi552 – 5521Copper 31 Publication
    Metal bindingi553 – 5531Copper 41 Publication
    Metal bindingi554 – 5541Copper 21 Publication
    Metal bindingi558 – 5581Copper 41 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB
    2. 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-1 (EC:1.10.3.2)
    Alternative name(s):
    Benzenediol:oxygen oxidoreductase 1
    Diphenol oxidase 1
    Ligninolytic phenoloxidase
    Urishiol oxidase 1
    Gene namesi
    Name:LAC1
    OrganismiMelanocarpus albomyces
    Taxonomic identifieri204285 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariales incertae sedisMelanocarpus

    Subcellular locationi

    GO - Cellular componenti

    1. extraorganismal space Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 50281 PublicationSequence AnalysisPRO_0000235826Add
    BLAST
    Chaini51 – 609559Laccase-11 PublicationPRO_0000235827Add
    BLAST
    Propeptidei610 – 623141 PublicationPRO_0000235828Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 621 Publication
    Glycosylationi89 – 891N-linked (GlcNAc...)1 Publication
    Glycosylationi138 – 1381N-linked (GlcNAc...)1 Publication
    Disulfide bondi164 ↔ 5901 Publication
    Glycosylationi251 – 2511N-linked (GlcNAc...)1 Publication
    Glycosylationi266 – 2661N-linked (GlcNAc...)1 Publication
    Glycosylationi294 – 2941N-linked (GlcNAc...)1 Publication
    Glycosylationi339 – 3391N-linked (GlcNAc...)1 Publication
    Disulfide bondi348 ↔ 3821 Publication
    Glycosylationi426 – 4261N-linked (GlcNAc...)1 Publication
    Glycosylationi446 – 4461N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Secreted protein; extracellular space.1 Publication

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    623
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi61 – 644
    Turni73 – 753
    Beta strandi83 – 9715
    Beta strandi103 – 1108
    Beta strandi113 – 1153
    Beta strandi119 – 1224
    Beta strandi126 – 1349
    Beta strandi142 – 1454
    Helixi153 – 1553
    Turni159 – 1613
    Turni168 – 1703
    Beta strandi171 – 1788
    Beta strandi183 – 1897
    Helixi194 – 1974
    Beta strandi200 – 2067
    Beta strandi214 – 22512
    Helixi230 – 2378
    Beta strandi245 – 2506
    Turni257 – 2593
    Beta strandi266 – 2694
    Beta strandi274 – 2818
    Beta strandi288 – 2925
    Beta strandi297 – 3026
    Beta strandi305 – 3139
    Beta strandi315 – 3173
    Beta strandi322 – 3287
    Beta strandi333 – 3419
    Helixi344 – 3463
    Beta strandi351 – 3544
    Beta strandi357 – 3626
    Beta strandi390 – 3923
    Beta strandi398 – 4003
    Helixi405 – 4073
    Beta strandi408 – 4147
    Beta strandi416 – 4205
    Beta strandi422 – 4254
    Beta strandi434 – 4363
    Helixi438 – 4447
    Helixi451 – 4533
    Beta strandi455 – 4584
    Beta strandi464 – 4718
    Beta strandi481 – 4888
    Beta strandi490 – 4967
    Helixi511 – 5144
    Helixi515 – 5173
    Beta strandi525 – 5317
    Beta strandi535 – 5428
    Beta strandi547 – 5537
    Helixi556 – 5605
    Beta strandi564 – 5696
    Helixi571 – 5744
    Helixi575 – 5773
    Helixi580 – 59617
    Helixi597 – 5993

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GW0X-ray2.40A/B51-609[»]
    2IH8X-ray2.00A/B51-609[»]
    2IH9X-ray2.00A/B51-609[»]
    2Q9OX-ray1.30A/B51-609[»]
    3DKHX-ray2.40A/B51-609[»]
    3FU7X-ray1.67A/B51-609[»]
    3FU8X-ray1.80A/B51-609[»]
    3FU9X-ray2.00A/B51-609[»]
    3QPKX-ray1.90A/B51-609[»]
    ProteinModelPortaliQ70KY3.
    SMRiQ70KY3. Positions 51-609.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ70KY3.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the multicopper oxidase family.Sequence Analysis

    Keywords - Domaini

    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.
    PS00080. MULTICOPPER_OXIDASE2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q70KY3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTFTSALAL VVGMLAPGAV VAAPPSTPAQ RDLVELREAR QEGGKDLRPR    50
    EPTCNTPSNR ACWSDGFDIN TDYEVSTPDT GVTQSYVFNL TEVDNWMGPD 100
    GVVKEKVMLI NGNIMGPNIV ANWGDTVEVT VINNLVTNGT SIHWHGIHQK 150
    DTNLHDGANG VTECPIPPKG GQRTYRWRAR QYGTSWYHSH FSAQYGNGVV 200
    GTIQINGPAS LPYDIDLGVF PITDYYYRAA DDLVHFTQNN APPFSDNVLI 250
    NGTAVNPNTG EGQYANVTLT PGKRHRLRIL NTSTENHFQV SLVNHTMTVI 300
    AADMVPVNAM TVDSLFLAVG QRYDVVIDAS RAPDNYWFNV TFGGQAACGG 350
    SLNPHPAAIF HYAGAPGGLP TDEGTPPVDH QCLDTLDVRP VVPRSVPVNS 400
    FVKRPDNTLP VALDLTGTPL FVWKVNGSDI NVDWGKPIID YILTGNTSYP 450
    VSDNIVQVDA VDQWTYWLIE NDPEGPFSLP HPMHLHGHDF LVLGRSPDVP 500
    AASQQRFVFD PAVDLARLNG DNPPRRDTTM LPAGGWLLLA FRTDNPGAWL 550
    FHCHIAWHVS GGLSVDFLER PADLRQRISQ EDEDDFNRVC DEWRAYWPTN 600
    PYPKIDSGLK RRRWVEESEW LVR 623
    Length:623
    Mass (Da):68,958
    Last modified:July 5, 2004 - v1
    Checksum:iA322F89B438784E1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ571698 Genomic DNA. Translation: CAE00180.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ571698 Genomic DNA. Translation: CAE00180.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GW0 X-ray 2.40 A/B 51-609 [» ]
    2IH8 X-ray 2.00 A/B 51-609 [» ]
    2IH9 X-ray 2.00 A/B 51-609 [» ]
    2Q9O X-ray 1.30 A/B 51-609 [» ]
    3DKH X-ray 2.40 A/B 51-609 [» ]
    3FU7 X-ray 1.67 A/B 51-609 [» ]
    3FU8 X-ray 1.80 A/B 51-609 [» ]
    3FU9 X-ray 2.00 A/B 51-609 [» ]
    3QPK X-ray 1.90 A/B 51-609 [» ]
    ProteinModelPortali Q70KY3.
    SMRi Q70KY3. Positions 51-609.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q70KY3.

    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.
    PS00080. MULTICOPPER_OXIDASE2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression in Saccharomyces cerevisiae of a laccase gene from the ascomycete Melanocarpus albomyces."
      Kiiskinen L.-L., Saloheimo M.
      Appl. Environ. Microbiol. 70:137-144(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Purification and characterisation of a novel laccase from the ascomycete Melanocarpus albomyces."
      Kiiskinen L.-L., Viikari L., Kruus K.
      Appl. Microbiol. Biotechnol. 59:198-204(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 51-78; 214-228 AND 507-517, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
      Strain: VTT D-964901 Publication.
    3. "Laccase from Melanocarpus albomyces binds effectively to cellulose."
      Kiiskinen L.-L., Palonen H., Linder M., Viikari L., Kruus K.
      FEBS Lett. 576:251-255(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROBABLE FUNCTION.
    4. "Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site."
      Hakulinen N., Kiiskinen L.-L., Kruus K., Saloheimo M., Paananen A., Koivula A., Rouvinen J.
      Nat. Struct. Biol. 9:601-605(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 51-609 IN COMPLEX WITH COFACTOR AND OXYGEN, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GLYCOSYLATION AT ASN-89; ASN-138; ASN-251; ASN-266; ASN-294; ASN-339; ASN-426 AND ASN-446, DISULFIDE BONDS.

    Entry informationi

    Entry nameiLAC1_MELAO
    AccessioniPrimary (citable) accession number: Q70KY3
    Secondary accession number(s): Q7SIE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2006
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 60 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, Direct protein sequencing

    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