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Q8NKF9

- EXG_CANOL

UniProt

Q8NKF9 - EXG_CANOL

Protein

Glucan 1,3-beta-glucosidase

Gene

EXG1

Organism
Candida oleophila (Yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase By similarity.By similarity

    Catalytic activityi

    Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei214 – 2141Proton donorBy similarity
    Active sitei328 – 3281NucleophileBy similarity

    GO - Molecular functioni

    1. glucan exo-1,3-beta-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.
    mycoCLAPiEXG5A_CANOL.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucan 1,3-beta-glucosidase (EC:3.2.1.58)
    Alternative name(s):
    Exo-1,3-beta-glucanase
    Gene namesi
    Name:EXG1
    OrganismiCandida oleophila (Yeast)
    Taxonomic identifieri45573 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 425408Glucan 1,3-beta-glucosidasePRO_0000007880Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi301 ↔ 423By similarity
    Disulfide bondi326 ↔ 352By similarity

    Keywords - PTMi

    Disulfide bond, Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliQ8NKF9.
    SMRiQ8NKF9. Positions 30-425.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8NKF9-1 [UniParc]FASTAAdd to Basket

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    MLLTFAPIFL LISSIVAAPT LQLQRKGLEW DYQNDKIRGV NLGGWFVLEP    50
    YITPSLFSVW SNGEDDLNTP VDEYHYTQKL GKETALSRLE AHWSSWYTEA 100
    DFAQMKYLGI NAVRIPIGYW AFQLLDNDPY VQGQVKYLDQ ALEWCRNNGL 150
    YAWVDLHGAP GSQNGFDNSG LRDSYKFQDD DDVKVTLEVL KTIGAKYGGS 200
    DYEDVVIGIE LLNEPLGPVL DMDGLRQFYQ DGYSEIRNND GVESYNAIII 250
    HDAFQQTDHY WDNFMQVSGG YWNVVVDHHH YQVFDQAALE LLIEDHIKTA 300
    CNWGTTHKDE AHWNIVGEWS SALTDCAKWL NGVGHGARWS GNYDNCPYID 350
    SCLSYTDLSG WTDEYKTNVR KYTEAQLDAW EQVGGWFFWC WKTESAPEWD 400
    FQALTNAGLI PQPLNDRQYP NQCGY 425
    Length:425
    Mass (Da):48,774
    Last modified:October 1, 2002 - v1
    Checksum:iC374EB3438AD5D1D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF393806 Genomic DNA. Translation: AAM21469.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF393806 Genomic DNA. Translation: AAM21469.1 .

    3D structure databases

    ProteinModelPortali Q8NKF9.
    SMRi Q8NKF9. Positions 30-425.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.
    mycoCLAPi EXG5A_CANOL.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and analysis of CoEXG1, a secreted 1,3-beta-glucanase of the yeast biocontrol agent Candida oleophila."
      Segal E., Yehuda H., Droby S., Wisniewski M., Goldway M.
      Yeast 19:1171-1182(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
      Strain: ATCC MYA-1208 / I-182 / NRRL Y-18846.

    Entry informationi

    Entry nameiEXG_CANOL
    AccessioniPrimary (citable) accession number: Q8NKF9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 53 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3