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Q12739

- LAC2_PLEOS

UniProt

Q12739 - LAC2_PLEOS

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Protein

Laccase-2

Gene

POX2

Organism
Pleurotus ostreatus (Oyster mushroom) (White-rot fungus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Lignin degradation and detoxification of lignin-derived products.By similarity

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 bindingi98 – 981Copper 1; type 2By similarity
Metal bindingi100 – 1001Copper 2; type 3By similarity
Metal bindingi143 – 1431Copper 2; type 3By similarity
Metal bindingi145 – 1451Copper 3; type 3By similarity
Metal bindingi427 – 4271Copper 4; type 1By similarity
Metal bindingi430 – 4301Copper 1; type 2By similarity
Metal bindingi432 – 4321Copper 3; type 3By similarity
Metal bindingi483 – 4831Copper 3; type 3By similarity
Metal bindingi484 – 4841Copper 4; type 1By similarity
Metal bindingi485 – 4851Copper 2; type 3By similarity
Metal bindingi489 – 4891Copper 4; type 1By 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-2 (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductase 2
Diphenol oxidase 2
Urishiol oxidase 2
Gene namesi
Name:POX2
OrganismiPleurotus ostreatus (Oyster mushroom) (White-rot fungus)
Taxonomic identifieri5322 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPleurotaceaePleurotus

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Add
BLAST
Chaini24 – 533510Laccase-2PRO_0000002930Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi467 – 4671N-linked (GlcNAc...) (high mannose)1 Publication

Post-translational modificationi

N-glycosylated at Asn-467; contains a high-mannose glycan with a varying number of mannose residues.1 Publication

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ12739.
SMRiQ12739. Positions 24-527.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 171147Plastocyanin-like 1Add
BLAST
Domaini173 – 336164Plastocyanin-like 2Add
BLAST
Domaini382 – 501120Plastocyanin-like 3Add
BLAST

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.
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. 2 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q12739-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFPGARILAT LTLALHLLHG AHAAIGPAGN MYIVNEDVSP DGFARSAVVA
60 70 80 90 100
RSVPATDPTP ATASIPGVLV QGNKGDNFQL NVVNQLSDTT MLKTTSIHWH
110 120 130 140 150
GFFQAGSSWA DGPAFVTQCP VASGDSFLYN FNVPDQAGTF WYHSHLSTQY
160 170 180 190 200
CDGLRGPFVV YDPSDPHLSL YDIDNADTVI TLEDWYHIVA PQNAAIPTPD
210 220 230 240 250
STLINGKGRY AGGPTSPLAI INVESNKRYR FRLVSMSCDP NFTFSIDGHS
260 270 280 290 300
LLVIEADAVN IVPITVDSIQ IFAGQRYSFV LTANQAVDNY WIRANPNLGS
310 320 330 340 350
TGFVGGINSA ILRYAGATED DPTTTSSTST PLLETNLVPL ENPGAPGPPV
360 370 380 390 400
PGGADININL AMAFDFTTFE LTINGVPFLP PTAPVLLQIL SGASTAASLL
410 420 430 440 450
PSGSIYELEA NKVVEISMPA LAVGGPHPFH LHGHTFDVIR SAGSTTYNFD
460 470 480 490 500
TPARRDVVNT GTGANDNVTI RFVTDNPGPW FLHCHIDWHL EIGLAVVFAE
510 520 530
DVTSISAPPA AWDDLCPIYN ALSDNDKGGI VPS
Length:533
Mass (Da):56,767
Last modified:November 1, 1996 - v1
Checksum:i7233C41D47E19AE6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49075 Genomic DNA. Translation: CAA88895.1.
Z34848 mRNA. Translation: CAA84357.1.
PIRiS62371.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49075 Genomic DNA. Translation: CAA88895.1 .
Z34848 mRNA. Translation: CAA84357.1 .
PIRi S62371.

3D structure databases

ProteinModelPortali Q12739.
SMRi Q12739. Positions 24-527.
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. 2 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The gene, protein and glycan structures of laccase from Pleurotus ostreatus."
    Giardina P., Aurilia V., Cannio R., Marzullo L., Amoresano A., Siciliano R., Pucci P., Sannia G.
    Eur. J. Biochem. 235:508-515(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], GLYCOSYLATION AT ASN-467, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Mycelium.
  2. "Stability and activity of a phenol oxidase from the ligninolytic fungus Pleurotus ostreatus."
    Palmieri G., Giardina P., Marzullo L., Desiderio B., Nitti G., Cannio R., Sannia G.
    Appl. Microbiol. Biotechnol. 39:632-636(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: Florida.
    Tissue: Mycelium.

Entry informationi

Entry nameiLAC2_PLEOS
AccessioniPrimary (citable) accession number: Q12739
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

POX2 isozyme is the most abundant laccase of P.ostreatus under various growth conditions.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3