ID   E13B_PHAVU              Reviewed;         348 AA.
AC   P23535;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase, basic isoform;
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;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1909591; DOI=10.1007/bf00017919;
RA   Edington B.V., Lamb C.J., Dixon R.A.;
RT   "cDNA cloning and characterization of a putative 1,3-beta-D-glucanase
RT   transcript induced by fungal elicitor in bean cell suspension cultures.";
RL   Plant Mol. Biol. 16:81-94(1991).
CC   -!- FUNCTION: Implicated in the defense of plants against pathogens.
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 {ECO:0000250}.
CC   -!- INDUCTION: By fungal elicitor.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; X53129; CAA37289.1; -; mRNA.
DR   PIR; S13323; S13323.
DR   AlphaFoldDB; P23535; -.
DR   SMR; P23535; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   eggNOG; ENOG502QQ3M; Eukaryota.
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   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR044965; Glyco_hydro_17_plant.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR32227:SF440; GLUCAN ENDO-1,3-BETA-D-GLUCOSIDASE; 1.
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   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Plant defense; Pyrrolidone carboxylic acid;
KW   Vacuole.
FT   CHAIN           1..316
FT                   /note="Glucan endo-1,3-beta-glucosidase, basic isoform"
FT                   /id="PRO_0000011857"
FT   PROPEP          317..348
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011858"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        240
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P15797"
SQ   SEQUENCE   348 AA;  38869 MW;  83177308F77429D6 CRC64;
     QIGVCYGMMG NNLPSANEVI NLYRSNNIRR MRLYDPNQAA LQALRNSGIE LILGVPNSDL
     QGLATNADTA RQWVQRNVLN FWPSVKIKYI AVGNEVSPVG GSSWYAQYVL PAVQNVYQAV
     RAQGLHDQIK VSTAIDMTLI GNSYPPSQGS FRGDVRSYLD PIIGYLLYAS APLHVNVYPY
     FSYSGNPRDI SLPYALFTSP NVVVRDGQYG YQNLFDAMLD SVHAAIDNTR IGYVEVVVSE
     SGWPSDGGFG ATYDNARVYL DNLVRRAGRG SPRRPSKPTE TYIFAMFDEN QKSPEIEKHF
     GLFKPSKEKK YPFGFGAQRM QRLLLMSSMQ HIPLRVTCKL EPSSQSLL
//