ID   EXG_KLULA               Reviewed;         429 AA.
AC   Q12628;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 119.
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   OrderedLocusNames=KLLA0C05324g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX   PubMed=10029988;
RX   DOI=10.1002/(sici)1097-0061(19990130)15:2<91::aid-yea343>3.0.co;2-#;
RA   Esteban P.F., Vazquez de Aldana C.R., del Rey F.;
RT   "Cloning and characterization of 1,3-beta-glucanase-encoding genes from
RT   non-conventional yeasts.";
RL   Yeast 15:91-109(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; Z46869; CAA86949.1; -; Genomic_DNA.
DR   EMBL; CR382123; CAH01288.1; -; Genomic_DNA.
DR   RefSeq; XP_452437.1; XM_452437.1.
DR   AlphaFoldDB; Q12628; -.
DR   SMR; Q12628; -.
DR   STRING; 28985.XP_452437.1; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   CLAE; EXG5A_KLULA; -.
DR   EnsemblFungi; CAH01288; CAH01288; KLLA0_C05324g.
DR   GeneID; 2892517; -.
DR   KEGG; kla:KLLA0_C05324g; -.
DR   eggNOG; ENOG502QPYU; Eukaryota.
DR   HOGENOM; CLU_004624_0_1_1; -.
DR   InParanoid; Q12628; -.
DR   OMA; YWTWKAE; -.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:1990819; C:actin fusion focus; IEA:EnsemblFungi.
DR   GO; GO:0000935; C:division septum; IEA:EnsemblFungi.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046557; F:glucan endo-1,6-beta-glucosidase activity; IEA:EnsemblFungi.
DR   GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070879; P:fungal-type cell wall beta-glucan metabolic process; IEA:EnsemblFungi.
DR   GO; GO:1904541; P:fungal-type cell wall disassembly involved in conjugation with cellular fusion; IEA:EnsemblFungi.
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; Cleavage on pair of basic residues;
KW   Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Secreted;
KW   Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..27
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000007884"
FT   CHAIN           28..429
FT                   /note="Glucan 1,3-beta-glucosidase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000007885"
FT   ACT_SITE        215
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        316
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        299..425
FT                   /evidence="ECO:0000250"
FT   DISULFID        324..354
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   429 AA;  49811 MW;  64DA906BCE450B8B CRC64;
     MLSMQVVSLI SLLVSVCLAQ PLPLSKRYFE YENYKVRGVN LGGWLVLEPF ITPSLFETFR
     TNEYNDDGIP YDEYHYCQYL GEDLARDRLK QHWSTWITEA DFEDISNTGL NTVRIPIGYW
     AFELLDDDPY VSGLQEAYLD QAIEWARSYG LKVWVDLHGA PGSQNGFDNS GLRDQVEFQQ
     DGNWDVFKNV LAYVIEKYSR DEFTDTVVGV EVLNEPLGPV IDMDKLKELY NWAYDYLRND
     LQRDQILVIH DAFQKANYFD DQLTVEQGAF GVLVDHHHYQ VFSPEEVGRT IDEHISVVCE
     QGKETLTEAH WNVVGEWSAA LTDCTKWLNG VGIGARYDGS FVKNQDTSYW IGSCEGSQDI
     STWTSDKKDN YRKYIEAQLD AYEIRNGWIY WCYKTEDTLE WDYRKLVQSG LFPQPLTNRQ
     FPNQCSSTY