ID   EXG_SCHOC               Reviewed;         425 AA.
AC   Q12700;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 81.
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;
OS   Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Schwanniomyces.
OX   NCBI_TaxID=27300;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 26077 / CBS 2863 / JCM 8124 / BCRC 20332 / NBRC 1840 / NRRL
RC   Y-2477;
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).
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; Z46871; CAA86951.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q12700; -.
DR   SMR; Q12700; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   CLAE; EXG5A_DEBOC; -.
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   CHAIN           20..425
FT                   /note="Glucan 1,3-beta-glucosidase"
FT                   /id="PRO_0000007881"
FT   ACT_SITE        219
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        318
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;  49127 MW;  57F063ABE2FBF274 CRC64;
     MNLTLLLLAL IFSPSLIFSL PTANKVKLVK KGLNWDYQNA KIHGVNLGGW FVLEPFITPS
     LFDIYSKPND DSQVPVDEYH FTQKLGKDAA QQVLEQHWKT WYKENDFKMM LKYGLNAVRI
     PIGYWAFKLL DYDPYVQGQV KYLDRALDWA RKYNLKVWID LHGAPGSQNG FDNSGLRDSL
     GFQQGNNVNF TLEVLEIIGK KYGGPEYEDV VIGIELLNEP LGPSLDLNYL KEFFQQGYQN
     LRNSGSVQAV IIQDAFQPMG YWDNFLTLDQ YWNVVVDHHH YQVFSAGELQ RSIDDHITVA
     CNWGWDAKKE YHWNVAGEWS AALTDCARWL NGVGRGARFS GDFDNSPYFG SCDCYVNIAT
     WPSEYRTNVR RYIEAQLDAF EQTGGWFFWN WKCENAIEWD LQGLITAGVF PYPFYNRQFP
     NQCGF