ID   BGL2_CANAX              Reviewed;         308 AA.
AC   P43070;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=BGL2;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061 / FMJ 1011;
RA   Scadden A.D., Sullivan P.A.;
RT   "The glucanosyl transferase (BGL2) of Candida albicans.";
RL   Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
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, cell wall. Note=Tightly bound to cell
CC       wall.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; U12975; AAA21151.1; -; Genomic_DNA.
DR   AlphaFoldDB; P43070; -.
DR   SMR; P43070; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   COMPLUYEAST-2DPAGE; P43070; -.
DR   VEuPathDB; FungiDB:C4_02250C_A; -.
DR   VEuPathDB; FungiDB:CAWG_03569; -.
DR   PHI-base; PHI:61; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0009277; C:fungal-type cell wall; IEA:EnsemblFungi.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:EnsemblFungi.
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:0031505; P:fungal-type cell wall organization; IEA:EnsemblFungi.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00332; Glyco_hydro_17; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE   3: Inferred from homology;
KW   Cell wall; Cell wall biogenesis/degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..308
FT                   /note="Glucan 1,3-beta-glucosidase"
FT                   /id="PRO_0000011894"
FT   ACT_SITE        119
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        228
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   308 AA;  33540 MW;  82E5AB9A5D9D1855 CRC64;
     MQIKFLTTLA TVLTSVAAMG DLAFNLGVKN DDGTCKDVST FEGDLDFLKS HSKIIKTYAV
     SDCNTLQNLG PAAEAEGFQI QLGIWPNDDA HFEAEKEALQ NYLPKISVST IKIFLVGSEA
     LYREDLTASE LASKINDIKG LVKGIKGKNG KSYSSVPVGT VDSWDVLVDG ASKPAIDAAD
     VVYSNSFSYW QKNSQANASY SLFDDVMQAL QTLQTAKGST DIEFWVGETG WPTDGSSYGD
     SVPSVENAAD QWQKGICALR AWGINVAVYE AFDEAWKPDT SGTSSVEKHW GVWQSDKTLK
     YSIDCKFN