ID   E13B_BRACM              Reviewed;         342 AA.
AC   P49236;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 88.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase;
DE            Short=(1->3)-beta-glucanase;
DE   AltName: Full=Beta-1,3-endoglucanase;
DE   Flags: Precursor;
GN   Name=BGL;
OS   Brassica campestris (Field mustard).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3711;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 99-117.
RC   STRAIN=cv. Just Right; TISSUE=Leaf;
RX   PubMed=7949324; DOI=10.1094/mpmi-7-0553;
RA   Newman M.-A., Conrads-Strauch J., Scofield G., Daniels M.J., Dow J.M.;
RT   "Defense-related gene induction in Brassica campestris in response to
RT   defined mutants of Xanthomonas campestris with altered pathogenicity.";
RL   Mol. Plant Microbe Interact. 7:553-563(1994).
CC   -!- FUNCTION: Is thought to be an important plant defense-related product
CC       against fungal pathogens. Accumulation of the glucanase can be detected
CC       as early as 4 hours after inoculation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC         beta-D-glucans.; EC=3.2.1.39;
CC   -!- SUBCELLULAR LOCATION: Vacuole. Note=In intact tissues.
CC   -!- INDUCTION: Following incompatible or compatible interaction with
CC       pathogenic bacteria, but not by wounding or salicylic acid. The
CC       induction is localized and does not seem to result from a systemic
CC       response. Induction occurs more rapidly with an incompatible
CC       interaction.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; X77990; CAA54952.1; -; mRNA.
DR   PIR; S42885; S42885.
DR   AlphaFoldDB; P49236; -.
DR   SMR; P49236; -.
DR   Proteomes; UP000011750; Unplaced.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd00448; YjgF_YER057c_UK114_family; 1.
DR   FunFam; 3.20.20.80:FF:000010; glucan endo-1,3-beta-glucosidase, basic; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR044965; Glyco_hydro_17_plant.
DR   InterPro; IPR061911; GLYCOSYL_HYDROL_F17_CS.
DR   PANTHER; PTHR32227; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE BG1-RELATED-RELATED; 1.
DR   Pfam; PF00332; Glyco_hydro_17; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Plant defense;
KW   Reference proteome; Signal; Vacuole.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   CHAIN           27..342
FT                   /note="Glucan endo-1,3-beta-glucosidase"
FT                   /id="PRO_0000011842"
FT   ACT_SITE        119
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        261
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
SQ   SEQUENCE   342 AA;  38180 MW;  7AE6B1EA445957F7 CRC64;
     MLASSPMLLF LLSLLMAYNF DTTAGQIGVC FGQMGNNIPN PSEVVAMFKQ YSIPRMRMYG
     PNPDALNALR GSNIEFILDV PNGDLKRLAD SQAEANTWVR DNVQKYNDVR FKYISVGNEV
     KPGEPGAAAL IQAMQNIDRA LSAAGLSNIK VSTTTFMGPS RNTYPPSRGR FKDEYRNFLQ
     PVIGFLVNKR SPLLVNIYTY FGYMNRDVSL QFALLQPNSN NEFTDPNNQL RYLNFFDANL
     DSVYAALEKS GGGSLDVVVS ESGWPTQGGP GASVPNAEAY VNNLRLHVNK NGSPKRQEAI
     ETYIFAMFDE APRQTSPNDE YEKYWGMFSP TTRQLKYGVK FN
//