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Q12725

- EXG_YARLI

UniProt

Q12725 - EXG_YARLI

Protein

Glucan 1,3-beta-glucosidase

Gene

EXG1

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    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 sitei213 – 2131Proton donorBy similarity
    Active sitei313 – 3131NucleophileBy 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
    Ordered Locus Names:YALI0F05390g
    OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
    Taxonomic identifieri284591 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
    ProteomesiUP000001300: Chromosome F

    Subcellular locationi

    Secreted By similarity

    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 – 1515Sequence AnalysisAdd
    BLAST
    Chaini16 – 421406Glucan 1,3-beta-glucosidasePRO_0000007888Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi296 ↔ 419By similarity
    Disulfide bondi321 ↔ 347By similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    STRINGi4952.Q12725.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12725.
    SMRiQ12725. Positions 29-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2730.
    HOGENOMiHOG000114462.
    KOiK01210.
    OMAiQYPNICG.
    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.

    Q12725-1 [UniParc]FASTAAdd to Basket

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    MKLTKLVALA GAALASPIQL VPREGSFLGF NYGSEKVHGV NLGGWFVLEP    50
    FITPSLFEAF GNNDANVPVD EYHYTAWLGK EEAEKRLTDH WNTWITEYDI 100
    KAIAENYKLN LVRIPIGYWA FSLLPNDPYV QGQEAYLDRA LGWCRKYGVK 150
    AWVDVHGVPG SQNGFDNSGL RDHWDWPNAD NVQHSINVIN YIAGKYGAPE 200
    YNDIVVGIEL VNEPLGPAIG MEVIEKYFQE GFWTVRHAGS DTAVVIHDAF 250
    QEKNYFNNFM TTEQGFWNVV LDHHQYQVFS PGELARNIDQ HIAEVCNVGR 300
    QASTEYHWRI FGEWSAALTD CTHWLNGVGK GPRLDGSFPG SYYQRSCQGR 350
    GDIQTWSEQD KQESRRYVEA QLDAWEHGGD GWIYWTYKTE NALEWDFRRL 400
    VDNGIFPFPY WDRQFPNQCG F 421
    Length:421
    Mass (Da):48,275
    Last modified:October 11, 2004 - v2
    Checksum:i2BB03184758252CC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti333 – 3331R → S in CAA86952. (PubMed:10029988)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46872 Genomic DNA. Translation: CAA86952.1.
    CR382132 Genomic DNA. Translation: CAG77837.1.
    RefSeqiXP_505030.1. XM_505030.1.

    Genome annotation databases

    EnsemblFungiiCAG77837; CAG77837; YALI0_F05390g.
    GeneIDi2908269.
    KEGGiyli:YALI0F05390g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46872 Genomic DNA. Translation: CAA86952.1 .
    CR382132 Genomic DNA. Translation: CAG77837.1 .
    RefSeqi XP_505030.1. XM_505030.1.

    3D structure databases

    ProteinModelPortali Q12725.
    SMRi Q12725. Positions 29-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 4952.Q12725.

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CAG77837 ; CAG77837 ; YALI0_F05390g .
    GeneIDi 2908269.
    KEGGi yli:YALI0F05390g.

    Phylogenomic databases

    eggNOGi COG2730.
    HOGENOMi HOG000114462.
    KOi K01210.
    OMAi QYPNICG.
    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 20460 / W29 / CBS 7504 / IFP29.
    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: CLIB 122 / E 150.

    Entry informationi

    Entry nameiEXG_YARLI
    AccessioniPrimary (citable) accession number: Q12725
    Secondary accession number(s): Q6C2T2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 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