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O93983

- EXG2_HANAN

UniProt

O93983 - EXG2_HANAN

Protein

Glucan 1,3-beta-glucosidase 2

Gene

EXG2

Organism
Hansenula anomala (Yeast) (Candida pelliculosa)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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 sitei217 – 2171Proton donorBy similarity
    Active sitei316 – 3161NucleophileBy 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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucan 1,3-beta-glucosidase 2 (EC:3.2.1.58)
    Alternative name(s):
    Exo-1,3-beta-glucanase 2
    Gene namesi
    Name:EXG2
    OrganismiHansenula anomala (Yeast) (Candida pelliculosa)
    Taxonomic identifieri4927 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeWickerhamomyces

    Subcellular locationi

    Secreted Curated

    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 – 427410Glucan 1,3-beta-glucosidase 2PRO_0000007883Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi299 ↔ 426By similarity
    Disulfide bondi324 ↔ 355By similarity

    Keywords - PTMi

    Disulfide bond, Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliO93983.
    SMRiO93983. Positions 35-426.
    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.

    O93983-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLISTFIISS LLSIALANPI PSRGGTQFYK RGDYWDYQND KIRGVNLGGW    50
    FVLEPFITPS LFEAFENQGQ DVPVDEYHYT KALGKDLAKE RLDQHWSSWI 100
    VEADFQSIAG AGLNFVRIPI GYWAFQLLDN DPYVQGQESY LDQALEWAKK 150
    YDIKVWIDLH GAPGSQNGFD NSGLRDSYEF QNGDNTQVAL DVLQYISNKY 200
    GGSDYGDVVI GIELLNEPLG SVLDMGKLND FWQQGYHNLR NTGSSQNVII 250
    HDAFQTWDSF NDKFHTPDYW NVVIDHHHYQ VFSPGELSRS VDEHVKVACE 300
    WGANSTKENH WNLCGEWSAA MTDCTKWLNG VGRGSRYDQT FDYDPSQNQN 350
    YIGSCQGSQD ISTWDDDKKS NYRRYIEAQL DAFEKRSGWI FWTWKTETTL 400
    EWDFQKLSYY GIFPSPLTSR QYPGQCD 427
    Length:427
    Mass (Da):49,130
    Last modified:May 1, 1999 - v1
    Checksum:iEDF7865B08538BE2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ222862 Genomic DNA. Translation: CAA11018.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ222862 Genomic DNA. Translation: CAA11018.1 .

    3D structure databases

    ProteinModelPortali O93983.
    SMRi O93983. Positions 35-426.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.

    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. "Preliminary study of exo-beta-1,3-glucanase encoding genes in relation to the protective activity of Pichia anomala (strain K) against Botrytis cinerea on postharvest apples."
      Grevesse C., Jijakli M.H., Duterme O., Colinet D., Lepoivre P.
      Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K.

    Entry informationi

    Entry nameiEXG2_HANAN
    AccessioniPrimary (citable) accession number: O93983
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 59 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