Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9LFD1

- LAC9_ARATH

UniProt

Q9LFD1 - LAC9_ARATH

Protein

Laccase-9

Gene

LAC9

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 bindingi83 – 831Copper 1; type 2By similarity
    Metal bindingi85 – 851Copper 2; type 3By similarity
    Metal bindingi128 – 1281Copper 2; type 3By similarity
    Metal bindingi130 – 1301Copper 3; type 3By similarity
    Metal bindingi469 – 4691Copper 4; type 1By similarity
    Metal bindingi472 – 4721Copper 1; type 2By similarity
    Metal bindingi474 – 4741Copper 3; type 3By similarity
    Metal bindingi531 – 5311Copper 3; type 3By similarity
    Metal bindingi532 – 5321Copper 4; type 1By similarity
    Metal bindingi533 – 5331Copper 2; type 3By similarity
    Metal bindingi537 – 5371Copper 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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lignin degradation

    Keywords - Ligandi

    Copper, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT5G01050-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laccase-9 (EC:1.10.3.2)
    Alternative name(s):
    Benzenediol:oxygen oxidoreductase 9
    Diphenol oxidase 9
    Urishiol oxidase 9
    Gene namesi
    Name:LAC9
    Ordered Locus Names:At5g01050
    ORF Names:F7J8.30
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G01050.

    Subcellular locationi

    GO - Cellular componenti

    1. apoplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Apoplast, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 586561Laccase-9PRO_0000283637Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi52 – 521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi385 – 3851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi403 – 4031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi451 – 4511N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiQ9LFD1.

    Expressioni

    Tissue specificityi

    Predominantly expressed in roots.2 Publications

    Gene expression databases

    GenevestigatoriQ9LFD1.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT5G01050.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LFD1.
    SMRiQ9LFD1. Positions 29-555.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 149117Plastocyanin-like 1Add
    BLAST
    Domaini159 – 307149Plastocyanin-like 2Add
    BLAST
    Domaini411 – 552142Plastocyanin-like 3Add
    BLAST

    Sequence similaritiesi

    Belongs to the multicopper oxidase family.Curated
    Contains 3 plastocyanin-like domains.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG2132.
    HOGENOMiHOG000241916.
    InParanoidiQ9LFD1.
    OMAiNDIPTAH.
    PhylomeDBiQ9LFD1.

    Family and domain databases

    Gene3Di2.60.40.420. 4 hits.
    InterProiIPR001117. Cu-oxidase.
    IPR011706. Cu-oxidase_2.
    IPR011707. Cu-oxidase_3.
    IPR008972. Cupredoxin.
    IPR017761. Laccase.
    [Graphical view]
    PfamiPF00394. Cu-oxidase. 1 hit.
    PF07731. Cu-oxidase_2. 1 hit.
    PF07732. Cu-oxidase_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF49503. SSF49503. 4 hits.
    TIGRFAMsiTIGR03389. laccase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9LFD1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRVHHSLSN QAFLVLLLFS SIASAAIVEH VLHVKDVVVT PLCKEQMIPI    50
    VNGSLPGPTI NVREGDTLVV HVINKSTYNV TIHWHGVFQL KSVWMDGANM 100
    ITQCPIQPSN NFTYQFDITG QEGTLLWHAH VVNLRATIHG ALIIRPRSGR 150
    PYPFPKPYKE VPLIFQQWWD TDVRLLELRP APVSDAYLIN GLAGDSYPCS 200
    KNRMFNLKVV QGKTYLLRII NAALNTHLFF KIANHNVTVV AVDAVYTTPY 250
    LTDVMILTPG QTIDAILTAD QPIGTYYMAI IPYFSAIGVP ASPDTKPTRG 300
    LIVYEGATSS SSPTKPWMPP ANDIPTAHRF SSNITSLVGG PHWTPVPRHV 350
    DEKMFITMGL GLDPCPSNAK CVGPLDQRLA GSLNNRTFMI PERISMQEAY 400
    FYNITGVYTD DFPDQPPLKF DFTKFEQHPT NSDMEMMFPE RKTSVKTIRF 450
    NSTVEIVLQN TGILTPESHP MHLHGFNFYV LGYGFGNYDP IRDARKLNLF 500
    NPQMHNTVGV PPGGWVVLRF IANNPGIWLF HCHMDAHLPL GIMMAFIVQN 550
    GPTRETSLPS PPSNLPQCTR DPTIYDSRTT NVDMSY 586
    Length:586
    Mass (Da):65,589
    Last modified:October 1, 2000 - v1
    Checksum:i84FFF22C99A35451
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL137189 Genomic DNA. Translation: CAB69833.1.
    CP002688 Genomic DNA. Translation: AED90292.1.
    PIRiT45945.
    RefSeqiNP_195725.1. NM_120182.2.
    UniGeneiAt.33978.

    Genome annotation databases

    EnsemblPlantsiAT5G01050.1; AT5G01050.1; AT5G01050.
    GeneIDi831812.
    KEGGiath:AT5G01050.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL137189 Genomic DNA. Translation: CAB69833.1 .
    CP002688 Genomic DNA. Translation: AED90292.1 .
    PIRi T45945.
    RefSeqi NP_195725.1. NM_120182.2.
    UniGenei At.33978.

    3D structure databases

    ProteinModelPortali Q9LFD1.
    SMRi Q9LFD1. Positions 29-555.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT5G01050.1-P.

    Proteomic databases

    PRIDEi Q9LFD1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G01050.1 ; AT5G01050.1 ; AT5G01050 .
    GeneIDi 831812.
    KEGGi ath:AT5G01050.

    Organism-specific databases

    TAIRi AT5G01050.

    Phylogenomic databases

    eggNOGi COG2132.
    HOGENOMi HOG000241916.
    InParanoidi Q9LFD1.
    OMAi NDIPTAH.
    PhylomeDBi Q9LFD1.

    Enzyme and pathway databases

    BioCyci ARA:AT5G01050-MONOMER.

    Gene expression databases

    Genevestigatori Q9LFD1.

    Family and domain databases

    Gene3Di 2.60.40.420. 4 hits.
    InterProi IPR001117. Cu-oxidase.
    IPR011706. Cu-oxidase_2.
    IPR011707. Cu-oxidase_3.
    IPR008972. Cupredoxin.
    IPR017761. Laccase.
    [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. 4 hits.
    TIGRFAMsi TIGR03389. laccase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "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] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    4. "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] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiLAC9_ARATH
    AccessioniPrimary (citable) accession number: Q9LFD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3