ID   EXG_CANOL               Reviewed;         425 AA.
AC   Q8NKF9;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Glucan 1,3-beta-glucosidase;
DE            EC=3.2.1.58;
DE   AltName: Full=Exo-1,3-beta-glucanase;
DE   Flags: Precursor;
GN   Name=EXG1;
OS   Candida oleophila (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Kurtzmaniella.
OX   NCBI_TaxID=45573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC MYA-1208 / I-182 / NRRL Y-18846;
RX   PubMed=12237858; DOI=10.1002/yea.910;
RA   Segal E., Yehuda H., Droby S., Wisniewski M., Goldway M.;
RT   "Cloning and analysis of CoEXG1, a secreted 1,3-beta-glucanase of the yeast
RT   biocontrol agent Candida oleophila.";
RL   Yeast 19:1171-1182(2002).
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:0000269|PubMed:12237858}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; AF393806; AAM21469.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NKF9; -.
DR   SMR; Q8NKF9; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   CLAE; EXG5A_CANOL; -.
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..425
FT                   /note="Glucan 1,3-beta-glucosidase"
FT                   /id="PRO_0000007880"
FT   ACT_SITE        214
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        328
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        301..423
FT                   /evidence="ECO:0000250"
FT   DISULFID        326..352
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   425 AA;  48774 MW;  C374EB3438AD5D1D CRC64;
     MLLTFAPIFL LISSIVAAPT LQLQRKGLEW DYQNDKIRGV NLGGWFVLEP YITPSLFSVW
     SNGEDDLNTP VDEYHYTQKL GKETALSRLE AHWSSWYTEA DFAQMKYLGI NAVRIPIGYW
     AFQLLDNDPY VQGQVKYLDQ ALEWCRNNGL YAWVDLHGAP GSQNGFDNSG LRDSYKFQDD
     DDVKVTLEVL KTIGAKYGGS DYEDVVIGIE LLNEPLGPVL DMDGLRQFYQ DGYSEIRNND
     GVESYNAIII HDAFQQTDHY WDNFMQVSGG YWNVVVDHHH YQVFDQAALE LLIEDHIKTA
     CNWGTTHKDE AHWNIVGEWS SALTDCAKWL NGVGHGARWS GNYDNCPYID SCLSYTDLSG
     WTDEYKTNVR KYTEAQLDAW EQVGGWFFWC WKTESAPEWD FQALTNAGLI PQPLNDRQYP
     NQCGY