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Q12700

- EXG_SCHOC

UniProt

Q12700 - EXG_SCHOC

Protein

Glucan 1,3-beta-glucosidase

Gene
N/A
Organism
Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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 sitei219 – 2191Proton donorBy similarity
    Active sitei318 – 3181NucleophileBy 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_DEBOC.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucan 1,3-beta-glucosidase (EC:3.2.1.58)
    Alternative name(s):
    Exo-1,3-beta-glucanase
    OrganismiSchwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis)
    Taxonomic identifieri27300 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeSchwanniomyces

    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 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 425406Glucan 1,3-beta-glucosidasePRO_0000007881Add
    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

    ProteinModelPortaliQ12700.
    SMRiQ12700. Positions 35-425.
    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.

    Q12700-1 [UniParc]FASTAAdd to Basket

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    MNLTLLLLAL IFSPSLIFSL PTANKVKLVK KGLNWDYQNA KIHGVNLGGW    50
    FVLEPFITPS LFDIYSKPND DSQVPVDEYH FTQKLGKDAA QQVLEQHWKT 100
    WYKENDFKMM LKYGLNAVRI PIGYWAFKLL DYDPYVQGQV KYLDRALDWA 150
    RKYNLKVWID LHGAPGSQNG FDNSGLRDSL GFQQGNNVNF TLEVLEIIGK 200
    KYGGPEYEDV VIGIELLNEP LGPSLDLNYL KEFFQQGYQN LRNSGSVQAV 250
    IIQDAFQPMG YWDNFLTLDQ YWNVVVDHHH YQVFSAGELQ RSIDDHITVA 300
    CNWGWDAKKE YHWNVAGEWS AALTDCARWL NGVGRGARFS GDFDNSPYFG 350
    SCDCYVNIAT WPSEYRTNVR RYIEAQLDAF EQTGGWFFWN WKCENAIEWD 400
    LQGLITAGVF PYPFYNRQFP NQCGF 425
    Length:425
    Mass (Da):49,127
    Last modified:November 1, 1996 - v1
    Checksum:i57F063ABE2FBF274
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46871 Genomic DNA. Translation: CAA86951.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46871 Genomic DNA. Translation: CAA86951.1 .

    3D structure databases

    ProteinModelPortali Q12700.
    SMRi Q12700. Positions 35-425.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.
    mycoCLAPi EXG5A_DEBOC.

    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 characterization of 1,3-beta-glucanase-encoding genes from non-conventional yeasts."
      Esteban P.F., Vazquez de Aldana C.R., del Rey F.
      Yeast 15:91-109(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 26077 / CBS 2863 / JCM 8124 / BCRC 20332 / NBRC 1840 / NRRL Y-2477.

    Entry informationi

    Entry nameiEXG_SCHOC
    AccessioniPrimary (citable) accession number: Q12700
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 68 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