ID   EXG_SACU7               Reviewed;         448 AA.
AC   Q876J3;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 67.
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   Saccharomyces uvarum (strain ATCC 76518 / CBS 7001 / CLIB 283 / NBRC 10550
OS   / MCYC 623 / NCYC 2669 / NRRL Y-11845) (Yeast) (Saccharomyces bayanus var.
OS   uvarum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=659244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=623-6C / CBS 9787 / CLIB 533;
RX   PubMed=12594514; DOI=10.1038/nature01419;
RA   Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.;
RT   "Yeast genome duplication was followed by asynchronous differentiation of
RT   duplicated genes.";
RL   Nature 421:848-852(2003).
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; AY144818; AAO32382.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q876J3; -.
DR   SMR; Q876J3; -.
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..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..40
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000007890"
FT   CHAIN           41..448
FT                   /note="Glucan 1,3-beta-glucosidase"
FT                   /id="PRO_0000007889"
FT   ACT_SITE        232
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        334
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        317..443
FT                   /evidence="ECO:0000250"
FT   DISULFID        342..372
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   448 AA;  51229 MW;  80AAF86129D16F1C CRC64;
     MLSLKTLLCT LLTVSSVIAN PVPARDPSSI QFVHEENKKR YYDYDNGALG EPIRGVNIGG
     WLVLEPYITP SLFEAFRTND NNDDGIPVDE YHYCQYLGND LAKSRLQSHW STFYQEQDFA
     NIASQGFNLV RIPIGYWAFA TLDNDPYVTG LQESYLDQAI GWARNNSLKV WVDLHGAAGS
     QNGFDNSGLR DSYEFLEDSN LAVTTKALNY ILKKYSAEEY LDTVIGIELI NEPLGPVLDM
     DKMKNDYLLP AYEYLRNTIE SNQIIIMHDA FQQFNYWDDF MTETDGYWGV TIDHHHYQVF
     DSSQLESSMD EHIQVACQWG TGVLDEAHWT VCGEFAAALT DCTKWVNSVG FGARYDGSWV
     NGDETSTYIG SCANNDDITS WSDQRKENTR RYVEAQLDAF EMRGGWIIWC YKTESSLEWD
     VQRLMYNGLF PQPLTDRQYP NQCNTTSS