ID   EXG_LACK1               Reviewed;         439 AA.
AC   Q875R9;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-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   Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 /
OS   JCM 7257 / NCYC 543 / NRRL Y-12651) (Yeast) (Saccharomyces kluyveri).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=226302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543
RC   / NRRL Y-12651;
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; AY145000; AAO32563.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q875R9; -.
DR   SMR; Q875R9; -.
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..439
FT                   /note="Glucan 1,3-beta-glucosidase"
FT                   /id="PRO_0000007891"
FT   ACT_SITE        227
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        328
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        311..437
FT                   /evidence="ECO:0000250"
FT   DISULFID        336..366
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   439 AA;  50349 MW;  7EFCB8E266C92729 CRC64;
     MLLSLLFLLS TFAFGALTQP VPAKSENNVQ FLHSKNKKRF YDYSTELIRG VNIGGWLLLE
     PYITPSLFEA FRTDENSDAG IPVDEYHYCE ALGSEVAESR LEAHWSTFYT EQDFKNIASA
     GLNMVRIPIG YWAFKTLDSD PYVTGKQESY LDKAIQWSKD AGLKVWVDLH GAPGSQNGFD
     NSGLRDHWSF LEDENLNLTK EVIKYLLEKY SREEYLDTVI GIELINEPLG PVLDMDKLKE
     YYQFGYDYLR NELGSDQIVV IHDAFEAYNY WDSTLTVEDG SWGVVVDHHH YQCFSSDQLA
     RSIDEHVSVA CEWGTGVLTE SHWTVAGEWS AALTDCAKWI NGVGYGARYD GSFTKDSESS
     YYIGSCENNE DVSTWSEERK SNNRKYVEAQ LDAFELRGGW IFWCYKTETT VEWDLQRLMY
     SGLFPQPVTD RQYPNQCGF