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O59896

- LAC1_PYCCI

UniProt

O59896 - LAC1_PYCCI

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Protein

Laccase

Gene
LCC3-1, LAC3, LCC1
Organism
Pycnoporus cinnabarinus (Cinnabar-red polypore)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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). May also be involved in synthesis of phenoxazinone pigments.

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 2 By similarity
Metal bindingi87 – 871Copper 2; type 3 By similarity
Metal bindingi130 – 1301Copper 2; type 3 By similarity
Metal bindingi132 – 1321Copper 3; type 3 By similarity
Metal bindingi416 – 4161Copper 4; type 1 By similarity
Metal bindingi419 – 4191Copper 1; type 2 By similarity
Metal bindingi421 – 4211Copper 3; type 3 By similarity
Metal bindingi471 – 4711Copper 3; type 3 By similarity
Metal bindingi472 – 4721Copper 4; type 1 By similarity
Metal bindingi473 – 4731Copper 2; type 3 By similarity
Metal bindingi477 – 4771Copper 4; type 1 By 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
Complete GO annotation...

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:LCC3-1
Synonyms:LAC3, LCC1
OrganismiPycnoporus cinnabarinus (Cinnabar-red polypore)
Taxonomic identifieri5643 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesTrametes

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 518497LaccasePRO_0000002934Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi72 – 721N-linked (GlcNAc...) Reviewed prediction
Glycosylationi75 – 751N-linked (GlcNAc...) Reviewed prediction
Glycosylationi229 – 2291N-linked (GlcNAc...) Reviewed prediction
Glycosylationi354 – 3541N-linked (GlcNAc...) Reviewed prediction
Glycosylationi362 – 3621N-linked (GlcNAc...) Reviewed prediction
Glycosylationi398 – 3981N-linked (GlcNAc...) Reviewed prediction
Glycosylationi455 – 4551N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Expressioni

Inductioni

By lignosulfonate, veratryl alcohol and 2,5-xylidine.1 Publication

Structurei

3D structure databases

ProteinModelPortaliO59896.
SMRiO59896. Positions 22-517.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 148126Plastocyanin-like 1Add
BLAST
Domaini160 – 302143Plastocyanin-like 2Add
BLAST
Domaini369 – 489121Plastocyanin-like 3Add
BLAST

Sequence similaritiesi

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.

O59896-1 [UniParc]FASTAAdd to Basket

« Hide

MSRFQSLLSF VLVSLAAVAN AAIGPVADLT LTNAAVSPDG FSREAVVVNG    50
ITPAPLIAGQ KGDRFQLNVI DNLTNHTMLK TTSIHWHGFF QHGTNWADGV 100
SFVNQCPIAS GHSFLYDFQV PDQAGTFWYH SHLSTQYCDG LRGPFVVYDP 150
NDPQASLYDI DNDDTVITLA DWYHVAAKLG PRFPLGADAT LINGLGRSPG 200
TTTADLAVIK VTQGKRYRFR LVSLSCDPNH TFSIDGHTMT VIEADSVNTQ 250
PLEVDSIQIF AAQRYSFVLD ASQPVDNYWI RANPAFGNVG FAGGINSAIL 300
RYDGAPEVEP TTTQTTSTKP LNEADLHPLT PMPVPGRPEA GGVDKPLNMV 350
FNFNGTNFFI NNHSFVPPSV PVLLQILSGA QAAQDLVPDG SVYVLPSNSS 400
IEISFPATAN APGTPHPFHL HGHTFAVVRS AGSSEYNYDN PIFRDVVSTG 450
QPGDNVTIRF QTNNPGPWFL HCHIDFHLEA GFAVVLAEDT PDTAAVNPVP 500
QSWSDLCPIY DALDPSDL 518
Length:518
Mass (Da):55,986
Last modified:August 1, 1998 - v1
Checksum:i31B4386AFDB8DF9D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti348 – 3481N → S in AAN71597. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF025481 Genomic DNA. Translation: AAC39469.1.
AY147188 Genomic DNA. Translation: AAN71597.1.
AJ420334 mRNA. Translation: CAD12461.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF025481 Genomic DNA. Translation: AAC39469.1 .
AY147188 Genomic DNA. Translation: AAN71597.1 .
AJ420334 mRNA. Translation: CAD12461.1 .

3D structure databases

ProteinModelPortali O59896.
SMRi O59896. Positions 22-517.
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. "Molecular analysis of a laccase gene from the white rot fungus Pycnoporus cinnabarinus."
    Eggert C., LaFayette P.R., Temp U., Eriksson K.-E.L., Dean J.F.D.
    Appl. Environ. Microbiol. 64:1766-1772(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 200478 / PB.
    Tissue: Mycelium.
  2. "Cloning, characterization and expression of laccase gene from white rot fungus Pycnoporus cinnabarinus."
    Dhawan S., Lal R., Kuhad R.C.
    Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Molecular biological monitoring of soil fungi with laccase genes."
    Luis P., Buscot F.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE OF 85-131.
    Tissue: Mycelium.
  4. "The ligninolytic system of the white rot fungus Pycnoporus cinnabarinus: purification and characterization of the laccase."
    Eggert C., Temp U., Eriksson K.-E.L.
    Appl. Environ. Microbiol. 62:1151-1158(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-42, CHARACTERIZATION, INDUCTION.
    Strain: ATCC 200478 / PB.
    Tissue: Mycelium.

Entry informationi

Entry nameiLAC1_PYCCI
AccessioniPrimary (citable) accession number: O59896
Secondary accession number(s): Q8J1Y2, Q8WZN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: August 1, 1998
Last modified: October 16, 2013
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

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