ID   EXG_BLUGR               Reviewed;         426 AA.
AC   Q96V64;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 73.
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   Blumeria graminis (Powdery mildew) (Oidium monilioides).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Blumeria.
OX   NCBI_TaxID=34373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Zhang Z., Gurr S.J.;
RT   "A 1,3-beta glucanase from Blumeria graminis related to the fungal cell
RT   wall.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
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; AF317734; AAL26905.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q96V64; -.
DR   SMR; Q96V64; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   EnsemblFungi; BLGH_02382-mRNA-1; BLGH_02382-mRNA-1; BLGH_02382.
DR   VEuPathDB; FungiDB:BGT96224V316_LOCUS3035; -.
DR   OMA; DTHHYQV; -.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Disulfide bond; Glycosidase; Hydrolase;
KW   Secreted; Signal; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..426
FT                   /note="Glucan 1,3-beta-glucosidase"
FT                   /id="PRO_0000007877"
FT   ACT_SITE        208
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        307
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        290..416
FT                   /evidence="ECO:0000250"
FT   DISULFID        315..343
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   426 AA;  47446 MW;  F9B2E13D33616CA3 CRC64;
     MLYPRALLPA AVALASLVLA VPLEERQLAF DFNNQKVRGV NLGGWFVLEP WITPSIFQQW
     ANGGDVIDEY SYTAALGKDE AFTRLNNHWA TWITEEDFAE IASMGLNHVR IPIGYWALVA
     IPNDPYVQGQ LSYVDRAIDW ARKNGLKVML DLHGAPGSQN GFDNSGRTGT IAWQSGDNVP
     NTLRAIQALA ERYAPQTDVV TAIELLNEPA NWGNDLSQIK KFYYDGWGNV RTQGQTAVTI
     HDAFLDPRSW NGFMNSEAGV NNVILDTHIY QVFSQNEVAM KPCAHVQTAC SSIDKIKPTD
     KWTIVGEWTG AQTDCAKWLN GLGKGARYDG TLPGHSEGYY GSCDKKYEGT VDSMLPVDKT
     NLQYFVEAQL DAYESHTGWF FWTWKTESAP EWHFQNLTRA GLIPQPLDSR KVPSQCGTSQ
     CLVPGN