ID   EXG1_WICAO              Reviewed;         498 AA.
AC   O93939;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Glucan 1,3-beta-glucosidase 1;
DE            EC=3.2.1.58;
DE   AltName: Full=Exo-1,3-beta-glucanase 1;
DE   Flags: Precursor;
GN   Name=EXG1;
OS   Wickerhamomyces anomalus (Yeast) (Hansenula anomala).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX   NCBI_TaxID=4927;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K;
RA   Grevesse C., Jijakli M.H., Duterme O., Colinet D., Lepoivre P.;
RT   "Preliminary study of exo-beta-1,3-glucanase genes in relation to the
RT   protective activity of Pichia anomala (strain K) against Botrytis cinerea
RT   on postharvest apples.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan,
CC       the main structural component of the cell wall. It could also function
CC       biosynthetically as a transglycosylase (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC         reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC         EC=3.2.1.58;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; AJ002195; CAA05243.1; -; Genomic_DNA.
DR   AlphaFoldDB; O93939; -.
DR   SMR; O93939; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Disulfide bond; Glycosidase; Hydrolase;
KW   Secreted; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..498
FT                   /note="Glucan 1,3-beta-glucosidase 1"
FT                   /id="PRO_0000007882"
FT   ACT_SITE        218
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        341
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        349..394
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   498 AA;  58063 MW;  04B129CAD6ED6D31 CRC64;
     MLFNILILSA LSLQLCTCFH IKRNLNGSND VIWDYYDDSK KVQGVSLGGW FVLEPYITPS
     LFEQFGEDEK KIPVDEYTFT EQLGKDEAQK QLDKHWATYF TESDFKDIKD YGLNLVRIPI
     GYWAFYLLED DPYVQGQEPY LDKALEWAKQ NDLKVWIDLH GVPGSQNGFD NSGKRGNVTW
     QDDEENIELS YKTLNYIFGK YGGENLTDTV IGIEIVNEPF HSKLNETDML DFYYNSYYDF
     RIKHNSRNFF LIQEAFEPIG FWNTHLNNDY TNVSKPFLND ELLEEGVPKN YFHDIVLDHH
     HYEVFSVDQL DKSENARIQD IKNYGESVAK EQEYHPSLVG EWSGAITDCA KWLNGVGTGA
     RYDGTFDESQ LVRTNAINGT AESQFKFKDK KRSCENVTFV EDFSKQHKEN IRKFIEIQLL
     TYENSNSGWI FWNYKTENAI EWDFKKLVEH KLFPHPFNEY KYFYENGTQI VESAASGNPQ
     NLLFITLSAL LVSLSTLL