ID   EXG2_WICAO              Reviewed;         427 AA.
AC   O93983;
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 2;
DE            EC=3.2.1.58;
DE   AltName: Full=Exo-1,3-beta-glucanase 2;
DE   Flags: Precursor;
GN   Name=EXG2;
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 encoding genes in relation to
RT   the protective activity of Pichia anomala (strain K) against Botrytis
RT   cinerea 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; AJ222862; CAA11018.1; -; Genomic_DNA.
DR   AlphaFoldDB; O93983; -.
DR   SMR; O93983; -.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..427
FT                   /note="Glucan 1,3-beta-glucosidase 2"
FT                   /id="PRO_0000007883"
FT   ACT_SITE        217
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        316
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        299..426
FT                   /evidence="ECO:0000250"
FT   DISULFID        324..355
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   427 AA;  49130 MW;  EDF7865B08538BE2 CRC64;
     MLISTFIISS LLSIALANPI PSRGGTQFYK RGDYWDYQND KIRGVNLGGW FVLEPFITPS
     LFEAFENQGQ DVPVDEYHYT KALGKDLAKE RLDQHWSSWI VEADFQSIAG AGLNFVRIPI
     GYWAFQLLDN DPYVQGQESY LDQALEWAKK YDIKVWIDLH GAPGSQNGFD NSGLRDSYEF
     QNGDNTQVAL DVLQYISNKY GGSDYGDVVI GIELLNEPLG SVLDMGKLND FWQQGYHNLR
     NTGSSQNVII HDAFQTWDSF NDKFHTPDYW NVVIDHHHYQ VFSPGELSRS VDEHVKVACE
     WGANSTKENH WNLCGEWSAA MTDCTKWLNG VGRGSRYDQT FDYDPSQNQN YIGSCQGSQD
     ISTWDDDKKS NYRRYIEAQL DAFEKRSGWI FWTWKTETTL EWDFQKLSYY GIFPSPLTSR
     QYPGQCD