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Q12628

- EXG_KLULA

UniProt

Q12628 - EXG_KLULA

Protein

Glucan 1,3-beta-glucosidase

Gene

KLLA0C05324g

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 88 (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 sitei215 – 2151Proton 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.
    mycoCLAPiEXG5A_KLULA.

    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
    Ordered Locus Names:KLLA0C05324g
    OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
    Taxonomic identifieri284590 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
    ProteomesiUP000000598: Chromosome C

    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
    Propeptidei20 – 278By similarityPRO_0000007884
    Chaini28 – 429402Glucan 1,3-beta-glucosidaseBy similarityPRO_0000007885Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi299 ↔ 425By similarity
    Disulfide bondi324 ↔ 354By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Zymogen

    Interactioni

    Protein-protein interaction databases

    STRINGi28985.Q12628.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12628.
    SMRiQ12628. Positions 28-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2730.
    HOGENOMiHOG000114462.
    KOiK01210.
    OMAiANGWIPV.
    OrthoDBiEOG7JT75H.

    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.

    Q12628-1 [UniParc]FASTAAdd to Basket

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    MLSMQVVSLI SLLVSVCLAQ PLPLSKRYFE YENYKVRGVN LGGWLVLEPF    50
    ITPSLFETFR TNEYNDDGIP YDEYHYCQYL GEDLARDRLK QHWSTWITEA 100
    DFEDISNTGL NTVRIPIGYW AFELLDDDPY VSGLQEAYLD QAIEWARSYG 150
    LKVWVDLHGA PGSQNGFDNS GLRDQVEFQQ DGNWDVFKNV LAYVIEKYSR 200
    DEFTDTVVGV EVLNEPLGPV IDMDKLKELY NWAYDYLRND LQRDQILVIH 250
    DAFQKANYFD DQLTVEQGAF GVLVDHHHYQ VFSPEEVGRT IDEHISVVCE 300
    QGKETLTEAH WNVVGEWSAA LTDCTKWLNG VGIGARYDGS FVKNQDTSYW 350
    IGSCEGSQDI STWTSDKKDN YRKYIEAQLD AYEIRNGWIY WCYKTEDTLE 400
    WDYRKLVQSG LFPQPLTNRQ FPNQCSSTY 429
    Length:429
    Mass (Da):49,811
    Last modified:November 1, 1996 - v1
    Checksum:i64DA906BCE450B8B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46869 Genomic DNA. Translation: CAA86949.1.
    CR382123 Genomic DNA. Translation: CAH01288.1.
    RefSeqiXP_452437.1. XM_452437.1.

    Genome annotation databases

    GeneIDi2892517.
    KEGGikla:KLLA0C05324g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46869 Genomic DNA. Translation: CAA86949.1 .
    CR382123 Genomic DNA. Translation: CAH01288.1 .
    RefSeqi XP_452437.1. XM_452437.1.

    3D structure databases

    ProteinModelPortali Q12628.
    SMRi Q12628. Positions 28-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 28985.Q12628.

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.
    mycoCLAPi EXG5A_KLULA.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2892517.
    KEGGi kla:KLLA0C05324g.

    Phylogenomic databases

    eggNOGi COG2730.
    HOGENOMi HOG000114462.
    KOi K01210.
    OMAi ANGWIPV.
    OrthoDBi EOG7JT75H.

    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 76492 / CBS 2359/152 / CLIB 210.
    2. "Genome evolution in yeasts."
      Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
      , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
      Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

    Entry informationi

    Entry nameiEXG_KLULA
    AccessioniPrimary (citable) accession number: Q12628
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    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