Essential maintenance is planned to begin on Tue Jan 28 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ during this time.

A0A384KUM7 · A0A384KUM7_ARATH

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.

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentapoplast
Molecular Functioncopper ion binding
Molecular Functionhydroquinone:oxygen oxidoreductase activity
Biological Processlignin catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • ORF names
      AT9943_LOCUS10505
    • Ordered locus names
      AXX17_At3g08840

Organism names

  • Taxonomic identifier
  • Strains
    • cv. Landsberg erecta
    • cv. Cdm-0
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    A0A384KUM7

Proteomes

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Keywords

Expression

Gene expression databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-49Plastocyanin-like
Domain61-213Plastocyanin-like
Domain315-453Plastocyanin-like

Sequence similarities

Belongs to the multicopper oxidase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    470
  • Mass (Da)
    51,858
  • Last updated
    2018-11-07 v1
  • MD5 Checksum
    B045E88ECDC808F1598E09FA41DD9317
MITQCPIQPGQRYAYRFNITGQEGTLWWHAHASFLRATVYGALVIRPKSGHSYPFPKPHKEVPILFGEWWNTDVVALEEAAIATGVPPNNSDAYTINGRPGNLYPCSKDRMFSLNVVKGKRYLLRIINAAMNIQLFFKIANHRLTVVAADAVYTAPYVTDVIVIAPGQTIDALLFADQSVDTSYYMAAHPYASAPAVPFPNTTTRGVIHYGGASKTGRSKPVLMPKLPSFFDTLTAYRFYSNLTALVNGPHWVPVPRYVDEEMLVTIGLGLEACADNTTCPKFSASMSNHSFVLPKKLSILEAVFHDVKGIFTADFPDQPPVKFDYTNPNVTQTNPGLLFTQKSTSAKILKFNTTVEVVLQNHALIAAESHPMHLHGFNFHVLAQGFGNYDPSRDRSKLNLVDPQSRNTLAVPVGGWAVIRFTANNPGAWIFHCHIDVHLPFGLGMIFVVKNGPTKSTTLPPPPPDLPKC

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LR881468
EMBL· GenBank· DDBJ
CAD5322497.1
EMBL· GenBank· DDBJ
Genomic DNA
LUHQ01000003
EMBL· GenBank· DDBJ
OAP01519.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help