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Q875R9

- EXG_LACK1

UniProt

Q875R9 - EXG_LACK1

Protein

Glucan 1,3-beta-glucosidase

Gene

EXG1

Organism
Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / CCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543 / NRRL Y-12651) (Yeast) (Saccharomyces kluyveri)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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 sitei227 – 2271Proton 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.

    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
    OrganismiLachancea kluyveri (strain ATCC 58438 / CBS 3082 / CCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543 / NRRL Y-12651) (Yeast) (Saccharomyces kluyveri)
    Taxonomic identifieri226302 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeLachancea

    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 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 439421Glucan 1,3-beta-glucosidasePRO_0000007891Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi311 ↔ 437By similarity
    Disulfide bondi336 ↔ 366By similarity

    Keywords - PTMi

    Disulfide bond, Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliQ875R9.
    SMRiQ875R9. Positions 40-438.
    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.

    Q875R9-1 [UniParc]FASTAAdd to Basket

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    MLLSLLFLLS TFAFGALTQP VPAKSENNVQ FLHSKNKKRF YDYSTELIRG    50
    VNIGGWLLLE PYITPSLFEA FRTDENSDAG IPVDEYHYCE ALGSEVAESR 100
    LEAHWSTFYT EQDFKNIASA GLNMVRIPIG YWAFKTLDSD PYVTGKQESY 150
    LDKAIQWSKD AGLKVWVDLH GAPGSQNGFD NSGLRDHWSF LEDENLNLTK 200
    EVIKYLLEKY SREEYLDTVI GIELINEPLG PVLDMDKLKE YYQFGYDYLR 250
    NELGSDQIVV IHDAFEAYNY WDSTLTVEDG SWGVVVDHHH YQCFSSDQLA 300
    RSIDEHVSVA CEWGTGVLTE SHWTVAGEWS AALTDCAKWI NGVGYGARYD 350
    GSFTKDSESS YYIGSCENNE DVSTWSEERK SNNRKYVEAQ LDAFELRGGW 400
    IFWCYKTETT VEWDLQRLMY SGLFPQPVTD RQYPNQCGF 439
    Length:439
    Mass (Da):50,349
    Last modified:June 1, 2003 - v1
    Checksum:i7EFCB8E266C92729
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY145000 Genomic DNA. Translation: AAO32563.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY145000 Genomic DNA. Translation: AAO32563.1 .

    3D structure databases

    ProteinModelPortali Q875R9.
    SMRi Q875R9. Positions 40-438.
    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. "Yeast genome duplication was followed by asynchronous differentiation of duplicated genes."
      Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.
      Nature 421:848-852(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 58438 / CBS 3082 / CCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543 / NRRL Y-12651.

    Entry informationi

    Entry nameiEXG_LACK1
    AccessioniPrimary (citable) accession number: Q875R9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 56 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