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D0VWU3

- LAC1_TRAMX

UniProt

D0VWU3 - LAC1_TRAMX

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

Functioni

Lignin degradation and detoxification of lignin-derived products Inferred.2 Publications

Catalytic activityi

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

Cofactori

Binds 4 copper ions per monomer.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Copper 1; type 21 Publication
Metal bindingi66 – 661Copper 2; type 31 Publication
Metal bindingi109 – 1091Copper 2; type 31 Publication
Metal bindingi111 – 1111Copper 3; type 31 Publication
Metal bindingi395 – 3951Copper 4; type 11 Publication
Metal bindingi398 – 3981Copper 1; type 21 Publication
Metal bindingi400 – 4001Copper 3; type 31 Publication
Metal bindingi452 – 4521Copper 3; type 31 Publication
Metal bindingi453 – 4531Copper 4; type 11 Publication
Metal bindingi454 – 4541Copper 2; type 31 Publication
Metal bindingi458 – 4581Copper 4; type 11 Publication

GO - Molecular functioni

  1. copper ion binding Source: UniProtKB
  2. hydroquinone:oxygen oxidoreductase activity Source: UniProtKB-EC
  3. oxidoreductase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. 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:
Laccase (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductase
Diphenol oxidase
Urishiol oxidase
OrganismiTrametes maxima (White-rot fungus) (Cerrena maxima)
Taxonomic identifieri259368 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesTrametes

Subcellular locationi

Secreted 2 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Laccase
PRO_0000401149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi51 – 511N-linked (GlcNAc...) Reviewed prediction
Glycosylationi54 – 541N-linked (GlcNAc...)3 Publications
Disulfide bondi85 ↔ 4883 Publications
Disulfide bondi117 ↔ 2053 Publications
Modified residuei196 – 19613'-nitrotyrosine3 Publications
Glycosylationi208 – 2081N-linked (GlcNAc...) Reviewed prediction
Glycosylationi217 – 2171N-linked (GlcNAc...)3 Publications
Glycosylationi292 – 2921N-linked (GlcNAc...) Reviewed prediction
Glycosylationi333 – 3331N-linked (GlcNAc...)1 Publication
Modified residuei372 – 37213'-nitrotyrosine3 Publications
Glycosylationi377 – 3771N-linked (GlcNAc...) Reviewed prediction
Glycosylationi416 – 4161N-linked (GlcNAc...) Reviewed prediction
Glycosylationi436 – 4361N-linked (GlcNAc...)2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1512
Beta strandi22 – 276
Beta strandi30 – 323
Beta strandi36 – 394
Beta strandi43 – 508
Helixi55 – 573
Beta strandi63 – 664
Helixi74 – 763
Turni80 – 823
Beta strandi92 – 987
Beta strandi104 – 1107
Helixi115 – 1184
Beta strandi121 – 1277
Helixi134 – 1363
Helixi142 – 1443
Beta strandi145 – 1517
Turni156 – 1583
Beta strandi167 – 1715
Beta strandi187 – 1904
Beta strandi195 – 2028
Beta strandi209 – 2135
Beta strandi218 – 2236
Beta strandi226 – 23813
Beta strandi243 – 2497
Beta strandi254 – 26714
Helixi271 – 2733
Beta strandi276 – 2816
Beta strandi297 – 2993
Helixi302 – 3043
Beta strandi307 – 3093
Beta strandi322 – 3276
Beta strandi330 – 3323
Beta strandi337 – 3393
Helixi351 – 3566
Turni362 – 3643
Beta strandi365 – 3673
Beta strandi370 – 3745
Beta strandi379 – 3857
Beta strandi396 – 3994
Beta strandi404 – 4085
Beta strandi417 – 4193
Beta strandi422 – 4276
Turni431 – 4344
Beta strandi436 – 4427
Beta strandi447 – 4559
Helixi456 – 4605
Beta strandi464 – 4707
Helixi471 – 4733
Helixi474 – 4774
Helixi482 – 4854
Helixi487 – 4926
Helixi496 – 4983

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H5UX-ray1.90A2-499[»]
3DIVX-ray1.76A1-499[»]

Miscellaneous databases

EvolutionaryTraceiD0VWU3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 127126Plastocyanin-like 1
Add
BLAST
Domaini139 – 281143Plastocyanin-like 2
Add
BLAST
Domaini348 – 470123Plastocyanin-like 3
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

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.

D0VWU3-1 [UniParc]FASTAAdd to Basket

« Hide

AVGPVADNTI TDAATSPDGF SRQAVVVNGV TPGPLVAGNI GDRFQLNVID    50
NLTNHTMLKT TSVHWHGFFQ QGTNWADGPA FINQCPISPG HSFLYDFQVP 100
NQAGTFWYHS HLSTQYCDGL RGPFVVYDPN DPHASRYDVD NDDTVITLAD 150
WYHTAAKLGP RFPAGADATL INGKGRAPSD TSAELSVIKV TKGKRYRFRL 200
VSLSCDPNFT FSIDGHNLTI IEVDSSNSQP LSVDSIQIFA AQRYSFVLNA 250
NQAVDNYWIR ANPNFGNVGF NGGINSAILR YDGAPAVEPT TNQTTSVKPL 300
NEVNLHPLVS TPVPGSPSSG GVDKAINMAF NFNGSNFFIN GASFVPPSVP 350
VLLQILSGAQ TAQDLLPSGS VYVLPSNASI EISFPATAAA PGAPHPFHLH 400
GHTFAVVRSA GSTVYNYSNP IFRDVVSTGT PAAGDNVTIR FLTNNPGPWF 450
LHCHIDFHLE GGFAVVQAED VPDVKATNPV PQAWSDLCPT YDANAPSDQ 499
Length:499
Mass (Da):53,451
Last modified:December 15, 2009 - v1
Checksum:iF018B0357333CF33
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2H5U X-ray 1.90 A 2-499 [» ]
3DIV X-ray 1.76 A 1-499 [» ]
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei D0VWU3.

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. Cited for: CRYSTALLIZATION, PRELIMINARY X-RAY CRYSTALLOGRAPHY, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, NITRATION AT TYR-196 AND TYR-372, GLYCOSYLATION AT ASN-54; ASN-217 AND ASN-436, DISULFIDE BONDS.
    Strain: 0275.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, NITRATION AT TYR-196 AND TYR-372, GLYCOSYLATION AT ASN-54; ASN-217; ASN-333 AND ASN-436, DISULFIDE BONDS.
    Strain: 0275.
  3. Lyashenko A.V., Zhukova Y.N., Mikhailov A.M.
    Submitted (JUN-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS), COPPER-BINDING SITES, NITRATION AT TYR-196 AND TYR-372, GLYCOSYLATION AT ASN-54 AND ASN-217, DISULFIDE BONDS.

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: May 14, 2014
This is version 20 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

External Data

Dasty 3

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