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Q02497

- LAC1_TRAHI

UniProt

Q02497 - LAC1_TRAHI

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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

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 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 bindingi473 – 4731Copper 3; type 3 By similarity
Metal bindingi474 – 4741Copper 4; type 1 By similarity
Metal bindingi475 – 4751Copper 2; type 3 By similarity
Metal bindingi479 – 4791Copper 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
OrganismiTrametes hirsuta (White-rot fungus) (Coriolus hirsutus)
Taxonomic identifieri5327 [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 – 2121Add
BLAST
Chaini22 – 520499LaccasePRO_0000002939Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ02497.
SMRiQ02497. Positions 22-520.

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

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

« Hide

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

Polymorphismi

2 allelic forms exist in position 111.

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti378 – 3792SG → RR in AAA33104. 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: February 19, 2014
This is version 70 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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