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Reviewed, UniProtKB/Swiss-Prot Q9LFD1 (LAC9_ARATH)

Last modified June 16, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Laccase-9
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 9
    Urishiol oxidase 9
    Diphenol oxidase 9
Gene names
Name: LAC9
Ordered Locus Names: At5g01050
ORF Names: F7J8.30
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

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

Catalytic activity

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

Cofactor

Binds 4 copper ions per monomer By similarity.

Subcellular location

Secreted › extracellular space › apoplast Potential.

Tissue specificity

Predominantly expressed in roots. Ref.2 Ref.3

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

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Ontologies

Keywords
   Biological processLignin degradation
   Cellular componentApoplast
Secreted
   DomainRepeat
Signal
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processlignin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentapoplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

laccase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 586561Laccase-9
PRO_0000283637

Regions

Domain33 – 149117Plastocyanin-like 1
Domain159 – 307149Plastocyanin-like 2
Domain411 – 552142Plastocyanin-like 3

Sites

Metal binding831Copper 1; type 2 By similarity
Metal binding851Copper 2; type 3 By similarity
Metal binding1281Copper 2; type 3 By similarity
Metal binding1301Copper 3; type 3 By similarity
Metal binding4691Copper 4; type 1 By similarity
Metal binding4721Copper 1; type 2 By similarity
Metal binding4741Copper 3; type 3 By similarity
Metal binding5311Copper 3; type 3 By similarity
Metal binding5321Copper 4; type 1 By similarity
Metal binding5331Copper 2; type 3 By similarity
Metal binding5371Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation521N-linked (GlcNAc...) Potential
Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation2361N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Potential
Glycosylation3851N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential
Glycosylation4511N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q9LFD1-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 84FFF22C99A35451

FASTA58665,589
        10         20         30         40         50         60 
MPRVHHSLSN QAFLVLLLFS SIASAAIVEH VLHVKDVVVT PLCKEQMIPI VNGSLPGPTI 

        70         80         90        100        110        120 
NVREGDTLVV HVINKSTYNV TIHWHGVFQL KSVWMDGANM ITQCPIQPSN NFTYQFDITG 

       130        140        150        160        170        180 
QEGTLLWHAH VVNLRATIHG ALIIRPRSGR PYPFPKPYKE VPLIFQQWWD TDVRLLELRP 

       190        200        210        220        230        240 
APVSDAYLIN GLAGDSYPCS KNRMFNLKVV QGKTYLLRII NAALNTHLFF KIANHNVTVV 

       250        260        270        280        290        300 
AVDAVYTTPY LTDVMILTPG QTIDAILTAD QPIGTYYMAI IPYFSAIGVP ASPDTKPTRG 

       310        320        330        340        350        360 
LIVYEGATSS SSPTKPWMPP ANDIPTAHRF SSNITSLVGG PHWTPVPRHV DEKMFITMGL 

       370        380        390        400        410        420 
GLDPCPSNAK CVGPLDQRLA GSLNNRTFMI PERISMQEAY FYNITGVYTD DFPDQPPLKF 

       430        440        450        460        470        480 
DFTKFEQHPT NSDMEMMFPE RKTSVKTIRF NSTVEIVLQN TGILTPESHP MHLHGFNFYV 

       490        500        510        520        530        540 
LGYGFGNYDP IRDARKLNLF NPQMHNTVGV PPGGWVVLRF IANNPGIWLF HCHMDAHLPL 

       550        560        570        580 
GIMMAFIVQN GPTRETSLPS PPSNLPQCTR DPTIYDSRTT NVDMSY

« Hide

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References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed: 11130714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Gene structure and molecular analysis of the laccase-like multicopper oxidase (LMCO) gene family in Arabidopsis thaliana."
McCaig B.C., Meagher R.B., Dean J.F.D.
Planta 221:619-636(2005) [PubMed: 15940465] [Abstract]
Cited for: TISSUE SPECIFICITY.
[3]"Mutant identification and characterization of the laccase gene family in Arabidopsis."
Cai X., Davis E.J., Ballif J., Liang M., Bushman E., Haroldsen V., Torabinejad J., Wu Y.
J. Exp. Bot. 57:2563-2569(2006) [PubMed: 16804053] [Abstract]
Cited for: TISSUE SPECIFICITY.

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Cross-references

Sequence databases

AL137189 Genomic DNA. Translation: CAB69833.1.
IPIIPI00548494.
PIRT45945.
RefSeqNP_195725.1.
UniGeneAt.33978

3D structure databases

HSSPHSSP built from PDB template 1AOZ based on UniProtKB P37064.
ModBaseSearch...

Genome annotation databases

GeneID831812.
GenomeReviewsGene locus AT5G01050 in contig BA000015_GR.
KEGGath:AT5G01050.
NMPDRfig|3702.1.peg.22166.

Organism-specific databases

TAIRAt5g01050.

Phylogenomic databases

OMAQ9LFD1. EFINIAN.

Enzyme and pathway databases

BRENDA1.10.3.2. 302.

Family and domain databases

InterProIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR017761. Laccase.
[Graphical view]
Gene3DG3DSA:2.60.40.420. Cupredoxin. 3 hits.
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
TIGRFAMsTIGR03389. laccase. 1 hit.
PROSITEPS00079. MULTICOPPER_OXIDASE1. False negative.
PS00080. MULTICOPPER_OXIDASE2. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameLAC9_ARATH
AccessionPrimary (citable) accession number: Q9LFD1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents