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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.2 PublicationsCurated

Catalytic activityi

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

Cofactori

Binds 4 copper ions per monomer.2 Publications

Sites

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

GO - Molecular functioni

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

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:
LaccaseImported2 Publications (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

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 – 499499LaccasePRO_0000401149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi51 – 511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi54 – 541N-linked (GlcNAc...)3 Publications
Disulfide bondi85 ↔ 4882 Publications
Disulfide bondi117 ↔ 2052 Publications
Modified residuei196 – 19613'-nitrotyrosine3 Publications
Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi217 – 2171N-linked (GlcNAc...)3 Publications
Glycosylationi292 – 2921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi333 – 3331N-linked (GlcNAc...)1 Publication
Modified residuei372 – 37213'-nitrotyrosine3 Publications
Glycosylationi377 – 3771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi436 – 4361N-linked (GlcNAc...)2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration

Structurei

Secondary structure

1
499
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1512Combined sources
Beta strandi22 – 276Combined sources
Beta strandi30 – 323Combined sources
Beta strandi36 – 394Combined sources
Beta strandi43 – 508Combined sources
Helixi55 – 573Combined sources
Beta strandi63 – 664Combined sources
Helixi74 – 763Combined sources
Turni80 – 823Combined sources
Beta strandi92 – 987Combined sources
Beta strandi104 – 1107Combined sources
Helixi115 – 1184Combined sources
Beta strandi121 – 1277Combined sources
Helixi134 – 1363Combined sources
Helixi142 – 1443Combined sources
Beta strandi145 – 1517Combined sources
Turni156 – 1583Combined sources
Beta strandi167 – 1715Combined sources
Beta strandi187 – 1904Combined sources
Beta strandi195 – 2028Combined sources
Beta strandi209 – 2135Combined sources
Beta strandi218 – 2236Combined sources
Beta strandi226 – 23813Combined sources
Beta strandi243 – 2497Combined sources
Beta strandi254 – 26714Combined sources
Helixi271 – 2733Combined sources
Beta strandi276 – 2816Combined sources
Beta strandi297 – 2993Combined sources
Helixi302 – 3043Combined sources
Beta strandi307 – 3093Combined sources
Beta strandi322 – 3276Combined sources
Beta strandi330 – 3323Combined sources
Beta strandi337 – 3393Combined sources
Helixi351 – 3566Combined sources
Turni362 – 3643Combined sources
Beta strandi365 – 3673Combined sources
Beta strandi370 – 3745Combined sources
Beta strandi379 – 3857Combined sources
Beta strandi396 – 3994Combined sources
Beta strandi404 – 4085Combined sources
Beta strandi417 – 4193Combined sources
Beta strandi422 – 4276Combined sources
Turni431 – 4344Combined sources
Beta strandi436 – 4427Combined sources
Beta strandi447 – 4559Combined sources
Helixi456 – 4605Combined sources
Beta strandi464 – 4707Combined sources
Helixi471 – 4733Combined sources
Helixi474 – 4774Combined sources
Helixi482 – 4854Combined sources
Helixi487 – 4926Combined sources
Helixi496 – 4983Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiD0VWU3.

Family & Domainsi

Domains and Repeats

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

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.
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

        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:
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...
MobiDBi 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: 02751 Publication.
  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: 02751 Publication.
  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: October 29, 2014
This is version 22 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

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