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Protein

Laccase

Gene
N/A
Organism
Trametes hirsuta (White-rot fungus) (Coriolus hirsutus)
Status
Reviewed-Annotation score: 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

Cu cationBy similarityNote: Binds 4 Cu cations per monomer.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi85Copper 1; type 2By similarity1
Metal bindingi87Copper 2; type 3By similarity1
Metal bindingi130Copper 2; type 3By similarity1
Metal bindingi132Copper 3; type 3By similarity1
Metal bindingi416Copper 4; type 1By similarity1
Metal bindingi419Copper 1; type 2By similarity1
Metal bindingi421Copper 3; type 3By similarity1
Metal bindingi473Copper 3; type 3By similarity1
Metal bindingi474Copper 4; type 1By similarity1
Metal bindingi475Copper 2; type 3By similarity1
Metal bindingi479Copper 4; type 1By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lignin degradation

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BRENDAi1.10.3.2. 1623.

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Add BLAST21
ChainiPRO_000000293922 – 520LaccaseAdd BLAST499

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi50N-linked (GlcNAc...)Sequence analysis1
Glycosylationi72N-linked (GlcNAc...)Sequence analysis1
Glycosylationi75N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi106 ↔ 509Sequence analysis
Disulfide bondi138 ↔ 226Sequence analysis
Glycosylationi210N-linked (GlcNAc...)Sequence analysis1
Glycosylationi229N-linked (GlcNAc...)Sequence analysis1
Glycosylationi354N-linked (GlcNAc...)Sequence analysis1
Glycosylationi457N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ02497.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 148Plastocyanin-like 1Add BLAST126
Domaini160 – 302Plastocyanin-like 2Add BLAST143
Domaini369 – 491Plastocyanin-like 3Add BLAST123

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.
IPR033138. Cu_oxidase_CS.
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

        10         20         30         40         50
MSRFQSLLAF VVASLAAVAH AAIGPTADLT ISNAEVSPDG FARQAVVVNN
60 70 80 90 100
VTPGPLVAGN KGDRFQLNVI DNLTNHTMLK STSIHWHGFF QKGTNWADGP
110 120 130 140 150
AFVNQCPISS GHSFLYDFQV PDQAGTFWYH SHLSTQYCDG LRGPFVVYDP
160 170 180 190 200
NDPHASLYDV DNDDTVITLA DWYHTAAKLG PAFPLGADAT LINGLGRSPS
210 220 230 240 250
TTAADLAVIN VTKGKRYRFR LVSLSCDPNH TFSIDGHDLT IIEVDSINSQ
260 270 280 290 300
PLVVDSIQIF AAQRYSFVLN ADQDVGNYWI RANPNFGNVG FAGGINSAIL
310 320 330 340 350
RYDGADPVEP TTTQTTPTKP LNEVDLHPLA TMAVPGSPVA GGVDTAINMA
360 370 380 390 400
FNFNGTNFFI NGASFVPPTV PVLLQIISGA QNAQDLLPSG SVYSLPSNAD
410 420 430 440 450
IEISFPATAA APGAPHPFHL HGHAFAVVRS AGSTVYNYDN PIFRDVVSTG
460 470 480 490 500
TPAAGDNVTI RFRTDNPGPW FLHCHIDFHL EAGFAVVFAE DIPDVASANP
510 520
VPQAWSDLCP IYDALDVNDQ
Length:520
Mass (Da):55,688
Last modified:October 1, 1996 - v1
Checksum:i977D8DFA551F7929
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti378 – 379SG → RR in AAA33104 (PubMed:2394718).Curated2

Polymorphismi

2 allelic forms exist in position 111.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti411A → P.1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60560 Genomic DNA. Translation: AAA33103.1.
M60561 Genomic DNA. Translation: AAA33104.1.
PIRiA35883.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60560 Genomic DNA. Translation: AAA33103.1.
M60561 Genomic DNA. Translation: AAA33104.1.
PIRiA35883.

3D structure databases

ProteinModelPortaliQ02497.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.10.3.2. 1623.

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
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]
ProtoNetiSearch...

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: October 5, 2016
This is version 80 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.