Q10ND7 · LAC10_ORYSJ
- ProteinLaccase-10
- GeneLAC10
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids578 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Lignin degradation and detoxification of lignin-derived products.
Catalytic activity
- 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Cofactor
Note: Binds 4 Cu cations per monomer.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 87 | Cu cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 89 | Cu cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 132 | Cu cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 134 | Cu cation 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 479 | Cu cation 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 482 | Cu cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 484 | Cu cation 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 541 | Cu cation 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 542 | Cu cation 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 543 | Cu cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 547 | Cu cation 4 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apoplast | |
Molecular Function | copper ion binding | |
Molecular Function | hydroquinone:oxygen oxidoreductase activity | |
Molecular Function | oxidoreductase activity | |
Biological Process | lignin catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLaccase-10
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ10ND7
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-29 | |||||
Sequence: MGARCLALLLLYGTLLLLLLLPQLPLAGA | ||||||
Chain | PRO_0000291895 | 30-578 | Laccase-10 | |||
Sequence: ATRYYTFNVKLQNVTRLCNTRAIPTVNGKFPGPKIVTREGDRVVVKVVNNIKDNITIHWHGVRQMRTGWSDGPAYVTQCPIQTGQSYVYNFTINGQRGTLFWHAHVSWLRSTLYGPIIILPKAGLPLPFTEPHKDVPIIFGEWFNADPEAIVAQALQTGGGPNVSDAYTINGLPGPLYNCSSKDTFRLKVQPGKMYLLRLINAALNDELFFSVANHTLTVVDVDASYVKPFDTDVVLITPGQTTNVLLRAKPTAEAAGATHLMMARPYATGRPGTYDNTTVAAVLEYAPPGHIKSLPLLRPSLPALNDTAFAAGFAAKLRSLACPDYPSNVPRRVDKPFFFAVGLGTTPCPGSNNQTCQGPTNTTKFTASINNVSFDMPTTALLQAHYTGQSAGVYTADFPASPLEPFNYTGTPPNNTNVSNGTRVVVLPYNASVEVVLQDTSILGAESHPLHLHGFDFFVVGQGTGNYDPSKHPAEFNLVDPVQRNTVGVPAGGWVAIRFFADNPGVWFMHCHLEVHTTWGLKMAWVVNDGPLPEQKLMPPPSDLPMC | ||||||
Glycosylation | 42 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 83 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 119 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 192 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 208 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 244 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 307 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 336 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 384 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 392 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 402 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 438 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 445 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 448 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 451 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 461 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 37-153 | Plastocyanin-like 1 | ||||
Sequence: NVKLQNVTRLCNTRAIPTVNGKFPGPKIVTREGDRVVVKVVNNIKDNITIHWHGVRQMRTGWSDGPAYVTQCPIQTGQSYVYNFTINGQRGTLFWHAHVSWLRSTLYGPIIILPKAG | ||||||
Domain | 163-319 | Plastocyanin-like 2 | ||||
Sequence: KDVPIIFGEWFNADPEAIVAQALQTGGGPNVSDAYTINGLPGPLYNCSSKDTFRLKVQPGKMYLLRLINAALNDELFFSVANHTLTVVDVDASYVKPFDTDVVLITPGQTTNVLLRAKPTAEAAGATHLMMARPYATGRPGTYDNTTVAAVLEYAPP | ||||||
Domain | 428-562 | Plastocyanin-like 3 | ||||
Sequence: DFPASPLEPFNYTGTPPNNTNVSNGTRVVVLPYNASVEVVLQDTSILGAESHPLHLHGFDFFVVGQGTGNYDPSKHPAEFNLVDPVQRNTVGVPAGGWVAIRFFADNPGVWFMHCHLEVHTTWGLKMAWVVNDGP |
Sequence similarities
Belongs to the multicopper oxidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length578
- Mass (Da)62,829
- Last updated2006-08-22 v1
- Checksum4493AA05FF1E36D7
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DP000009 EMBL· GenBank· DDBJ | ABF95230.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP008209 EMBL· GenBank· DDBJ | BAF11613.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014959 EMBL· GenBank· DDBJ | BAS83490.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CM000140 EMBL· GenBank· DDBJ | EEE58784.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK060579 EMBL· GenBank· DDBJ | BAG87502.1 EMBL· GenBank· DDBJ | mRNA | ||
AK072397 EMBL· GenBank· DDBJ | BAG92951.1 EMBL· GenBank· DDBJ | mRNA |