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Protein

Laccase

Gene
N/A
Organism
Trametes maxima (White-rot fungus) (Cerrena maxima)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lignin degradation and detoxification of lignin-derived products.Curated2 Publications

Catalytic activityi

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

Cofactori

Cu cation2 PublicationsNote: Binds 4 Cu cations per monomer.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi64Copper 1; type 21
Metal bindingi66Copper 2; type 31
Metal bindingi109Copper 2; type 31
Metal bindingi111Copper 3; type 31
Metal bindingi395Copper 4; type 11
Metal bindingi398Copper 1; type 21
Metal bindingi400Copper 3; type 31
Metal bindingi452Copper 3; type 31
Metal bindingi453Copper 4; type 11
Metal bindingi454Copper 2; type 31
Metal bindingi458Copper 4; type 11

GO - Molecular functioni

  • copper ion binding Source: UniProtKB
  • hydroquinone:oxygen oxidoreductase activity Source: UniProtKB-EC
  • oxidoreductase activity Source: UniProtKB

GO - Biological processi

  • lignin catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lignin degradation

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Laccase2 PublicationsImported (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

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004011491 – 499LaccaseAdd BLAST499

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi51N-linked (GlcNAc...)Sequence analysis1
Glycosylationi54N-linked (GlcNAc...)3 Publications1
Disulfide bondi85 ↔ 4882 Publications
Disulfide bondi117 ↔ 2052 Publications
Modified residuei1963'-nitrotyrosine3 Publications1
Glycosylationi208N-linked (GlcNAc...)Sequence analysis1
Glycosylationi217N-linked (GlcNAc...)3 Publications1
Glycosylationi292N-linked (GlcNAc...)Sequence analysis1
Glycosylationi333N-linked (GlcNAc...)1 Publication1
Modified residuei3723'-nitrotyrosine3 Publications1
Glycosylationi377N-linked (GlcNAc...)Sequence analysis1
Glycosylationi416N-linked (GlcNAc...)Sequence analysis1
Glycosylationi436N-linked (GlcNAc...)2 Publications1

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration

Structurei

Secondary structure

1499
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 15Combined sources12
Beta strandi22 – 27Combined sources6
Beta strandi30 – 32Combined sources3
Beta strandi36 – 39Combined sources4
Beta strandi43 – 50Combined sources8
Helixi55 – 57Combined sources3
Beta strandi63 – 66Combined sources4
Helixi74 – 76Combined sources3
Turni80 – 82Combined sources3
Beta strandi92 – 98Combined sources7
Beta strandi104 – 110Combined sources7
Helixi115 – 118Combined sources4
Beta strandi121 – 127Combined sources7
Helixi134 – 136Combined sources3
Helixi142 – 144Combined sources3
Beta strandi145 – 151Combined sources7
Turni156 – 158Combined sources3
Beta strandi167 – 171Combined sources5
Beta strandi187 – 190Combined sources4
Beta strandi195 – 202Combined sources8
Beta strandi209 – 213Combined sources5
Beta strandi218 – 223Combined sources6
Beta strandi226 – 238Combined sources13
Beta strandi243 – 249Combined sources7
Beta strandi254 – 267Combined sources14
Helixi271 – 273Combined sources3
Beta strandi276 – 281Combined sources6
Beta strandi297 – 299Combined sources3
Helixi302 – 304Combined sources3
Beta strandi307 – 309Combined sources3
Beta strandi322 – 327Combined sources6
Beta strandi330 – 332Combined sources3
Beta strandi337 – 339Combined sources3
Helixi351 – 356Combined sources6
Turni362 – 364Combined sources3
Beta strandi365 – 367Combined sources3
Beta strandi370 – 374Combined sources5
Beta strandi379 – 385Combined sources7
Beta strandi396 – 399Combined sources4
Beta strandi404 – 408Combined sources5
Beta strandi417 – 419Combined sources3
Beta strandi422 – 427Combined sources6
Turni431 – 434Combined sources4
Beta strandi436 – 442Combined sources7
Beta strandi447 – 455Combined sources9
Helixi456 – 460Combined sources5
Beta strandi464 – 470Combined sources7
Helixi471 – 473Combined sources3
Helixi474 – 477Combined sources4
Helixi482 – 485Combined sources4
Helixi487 – 492Combined sources6
Helixi496 – 498Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H5UX-ray1.90A2-499[»]
3DIVX-ray1.76A1-499[»]
SMRiD0VWU3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiD0VWU3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 127Plastocyanin-like 1Add BLAST126
Domaini139 – 281Plastocyanin-like 2Add BLAST143
Domaini348 – 470Plastocyanin-like 3Add BLAST123

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.
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.

D0VWU3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AVGPVADNTI TDAATSPDGF SRQAVVVNGV TPGPLVAGNI GDRFQLNVID
60 70 80 90 100
NLTNHTMLKT TSVHWHGFFQ QGTNWADGPA FINQCPISPG HSFLYDFQVP
110 120 130 140 150
NQAGTFWYHS HLSTQYCDGL RGPFVVYDPN DPHASRYDVD NDDTVITLAD
160 170 180 190 200
WYHTAAKLGP RFPAGADATL INGKGRAPSD TSAELSVIKV TKGKRYRFRL
210 220 230 240 250
VSLSCDPNFT FSIDGHNLTI IEVDSSNSQP LSVDSIQIFA AQRYSFVLNA
260 270 280 290 300
NQAVDNYWIR ANPNFGNVGF NGGINSAILR YDGAPAVEPT TNQTTSVKPL
310 320 330 340 350
NEVNLHPLVS TPVPGSPSSG GVDKAINMAF NFNGSNFFIN GASFVPPSVP
360 370 380 390 400
VLLQILSGAQ TAQDLLPSGS VYVLPSNASI EISFPATAAA PGAPHPFHLH
410 420 430 440 450
GHTFAVVRSA GSTVYNYSNP IFRDVVSTGT PAAGDNVTIR FLTNNPGPWF
460 470 480 490
LHCHIDFHLE GGFAVVQAED VPDVKATNPV PQAWSDLCPT YDANAPSDQ
Length:499
Mass (Da):53,451
Last modified:December 15, 2009 - v1
Checksum:iF018B0357333CF33
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H5UX-ray1.90A2-499[»]
3DIVX-ray1.76A1-499[»]
SMRiD0VWU3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiD0VWU3.

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_TRAMX
AccessioniPrimary (citable) accession number: D0VWU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: December 15, 2009
Last modified: November 2, 2016
This is version 25 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

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.