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Q12626

- EXG_PICAN

UniProt

Q12626 - EXG_PICAN

Protein

Glucan 1,3-beta-glucosidase

Gene
N/A
Organism
Pichia angusta (Yeast) (Hansenula polymorpha)
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 sitei222 – 2221Proton donorBy similarity
    Active sitei323 – 3231NucleophileBy 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_PICAN.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucan 1,3-beta-glucosidase (EC:3.2.1.58)
    Alternative name(s):
    Exo-1,3-beta-glucanase
    OrganismiPichia angusta (Yeast) (Hansenula polymorpha)
    Taxonomic identifieri870730 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetales incertae sedisOgataea

    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 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 435405Glucan 1,3-beta-glucosidasePRO_0000007886Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi306 ↔ 432By similarity
    Disulfide bondi331 ↔ 357By similarity

    Keywords - PTMi

    Disulfide bond, Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliQ12626.
    SMRiQ12626. Positions 41-435.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    PhylomeDBiQ12626.

    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.

    Q12626-1 [UniParc]FASTAAdd to Basket

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    MLFPVLHLPK AMKFSSFSLI ASSLLSLVAA APVTLLKRDS RWDYANDKIY    50
    GVNIGGWLVL EPFITPSLFE AVSSDVPVDE YHYTEALGKE EAEKRLQEHW 100
    STWIKEEDFK GMANAGLNFV RIPIGYWAFQ LAEGDPYVQG QQEYLDKALE 150
    WCAKYGLKAW VDLHGAPGSQ NGFDNSGKRG EIGWQNTTGY VDLTVQVLDQ 200
    LTSKYGGSNY SDVIIGIELL NEPLGSYLDF DQLVDFYNKG YQLVRNNGNA 250
    PVIIHDAYLP DHTFDNVLNT EQDPNVWEVI VDHHHYQVFD EGSLSQSIDE 300
    HVSTACGWGQ SENTEYHYSL CGEWTAALTD CAKWLNGAGR GARYDATFGG 350
    GNYIGSCDQL YTANYDYFTP EVISNYRRYV EAQMDSFLYG KNAGWVFWCW 400
    KTENTIEWDM QRLLGLGIIP QPLDDRQYPN QCGFS 435
    Length:435
    Mass (Da):49,264
    Last modified:November 1, 1996 - v1
    Checksum:i840C22F271CC87A0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46868 Genomic DNA. Translation: CAA86948.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46868 Genomic DNA. Translation: CAA86948.1 .

    3D structure databases

    ProteinModelPortali Q12626.
    SMRi Q12626. Positions 41-435.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.
    mycoCLAPi EXG5A_PICAN.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    PhylomeDBi Q12626.

    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 14754 / CBS 1976 / JCM 3620 / NBRC 0799 / NCYC 495 / NRRL Y-1798 / VKM Y-1397.

    Entry informationi

    Entry nameiEXG_PICAN
    AccessioniPrimary (citable) accession number: Q12626
    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