Q8RYM9 · LAC2_ORYSJ

Function

function

Lignin degradation and detoxification of lignin-derived products.

Catalytic activity

Cofactor

Cu cation (UniProtKB | Rhea| CHEBI:23378 )

Note: Binds 4 Cu cations per monomer.

Features

Showing features for binding site.

156250100150200250300350400450500550
TypeIDPosition(s)Description
Binding site84Cu cation 1 (UniProtKB | ChEBI)
Binding site86Cu cation 2 (UniProtKB | ChEBI)
Binding site129Cu cation 2 (UniProtKB | ChEBI)
Binding site131Cu cation 3 (UniProtKB | ChEBI)
Binding site463Cu cation 4 (UniProtKB | ChEBI)
Binding site466Cu cation 1 (UniProtKB | ChEBI)
Binding site468Cu cation 3 (UniProtKB | ChEBI)
Binding site525Cu cation 3 (UniProtKB | ChEBI)
Binding site526Cu cation 4 (UniProtKB | ChEBI)
Binding site527Cu cation 2 (UniProtKB | ChEBI)
Binding site531Cu cation 4 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentapoplast
Molecular Functioncopper ion binding
Molecular Functionhydroquinone:oxygen oxidoreductase activity
Molecular Functionoxidoreductase activity
Biological Processlignin catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Laccase-2
  • EC number
  • Alternative names
    • Benzenediol:oxygen oxidoreductase 2
    • Diphenol oxidase 2
    • Urishiol oxidase 2

Gene names

    • Name
      LAC2
    • ORF names
      OsJ_002637, P0663E10.27
    • Ordered locus names
      Os01g0634500, LOC_Os01g44330

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Nipponbare
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa

Accessions

  • Primary accession
    Q8RYM9
  • Secondary accessions
    • A2ZVR5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-26
ChainPRO_000029188727-562Laccase-2
Glycosylation39N-linked (GlcNAc...) asparagine
Glycosylation53N-linked (GlcNAc...) asparagine
Glycosylation72N-linked (GlcNAc...) asparagine
Glycosylation80N-linked (GlcNAc...) asparagine
Glycosylation118N-linked (GlcNAc...) asparagine
Glycosylation189N-linked (GlcNAc...) asparagine
Glycosylation244N-linked (GlcNAc...) asparagine
Glycosylation300N-linked (GlcNAc...) asparagine
Glycosylation328N-linked (GlcNAc...) asparagine
Glycosylation376N-linked (GlcNAc...) asparagine
Glycosylation386N-linked (GlcNAc...) asparagine
Glycosylation421N-linked (GlcNAc...) asparagine
Glycosylation445N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain34-150Plastocyanin-like 1
Domain160-312Plastocyanin-like 2
Domain411-546Plastocyanin-like 3

Sequence similarities

Belongs to the multicopper oxidase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    562
  • Mass (Da)
    61,296
  • Last updated
    2002-06-01 v1
  • Checksum
    0BF4F84B9E7996A9
MASAASSLPLLVSSLLLALFALGAHADVKRYQFDIVMSNVSRLCHEKAMVTVNGSYPGPTIYAREGDRVIVNVTNHVKHNMTIHWHGLKQRRNGWADGPAYVTQCPIGSGGSYVYDFNVTRQRGTLWWHAHIAWMRATVHGAIVILPAAGVPYPFPKPDDEAEIVLGEWWHADVETVERQGSMLGMAPNMSDAHTINGKPGPLVPFCSEKHTYALQVQSGKTYLLRIINAAVNDELFFSIAGHNMTVVEIDATYTKPFAASTVQLSPGQTMNVLVSADQSPGRYFMVAKPFNDVPIPADNKTATAILQYAGVPTSVVPALPQTMPATNSTGSVAAFHDKLRSLNSPRYPADVPLAVDRHLLYTIGLNIDPCETCLNRSRLAASLNNITFVMPRTALLQAHYYGQKGVFAADFPDRPPARFNYTGVPLTAGLGTSLGTRLSKIAYNATVELVLQDTNLLSVESHPFHLHGYNFFVVGRGVGNFDPAKDPAKYNLVDPPERNTVGVPAGGWTAIRFRADNPGVWFLHCHLEVHTSWGLKMAFLVEDGSGPDESVLPPPKDLPKC

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0P0V5L8A0A0P0V5L8_ORYSJOs01g0634500528

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict168in Ref. 4; EAZ12812

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP004317
EMBL· GenBank· DDBJ
BAB90733.1
EMBL· GenBank· DDBJ
Genomic DNA
AP014957
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CM000138
EMBL· GenBank· DDBJ
EAZ12812.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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