ID   E13B_PEA                Reviewed;         370 AA.
AC   Q03467;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 85.
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;
OS   Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Alcan; TISSUE=Leaf;
RX   PubMed=8310053; DOI=10.1104/pp.101.3.1121;
RA   Chang M.-M., Culley D.E., Hadwiger L.A.;
RT   "Nucleotide sequence of a pea (Pisum sativum L.) beta-1,3-glucanase gene.";
RL   Plant Physiol. 101:1121-1122(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-370.
RC   STRAIN=cv. Alcan; TISSUE=Leaf;
RX   PubMed=1450378; DOI=10.1007/bf00046446;
RA   Chang M.-M., Hadwiger L.A., Horovitz D.;
RT   "Molecular characterization of a pea beta-1,3-glucanase induced by Fusarium
RT   solani and chitosan challenge.";
RL   Plant Mol. Biol. 20:609-618(1992).
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   -!- TISSUE SPECIFICITY: Constitutively expressed in seedling roots.
CC   -!- INDUCTION: By fungal elicitors.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; S51479; AAB24398.1; -; Genomic_DNA.
DR   EMBL; L02212; AAA33648.1; -; Genomic_DNA.
DR   EMBL; S69419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; T06552; T06552.
DR   AlphaFoldDB; Q03467; -.
DR   SMR; Q03467; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   EnsemblPlants; Psat1g161880.1; Psat1g161880.1.cds1; Psat1g161880.
DR   Gramene; Psat1g161880.1; Psat1g161880.1.cds1; Psat1g161880.
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   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR044965; Glyco_hydro_17_plant.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR32227; PTHR32227; 1.
DR   Pfam; PF00332; Glyco_hydro_17; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosidase; Hydrolase; Plant defense;
KW   Pyrrolidone carboxylic acid; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..347
FT                   /note="Glucan endo-1,3-beta-glucosidase"
FT                   /id="PRO_0000011855"
FT   PROPEP          348..370
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011856"
FT   ACT_SITE        127
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        272
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   MOD_RES         33
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P15797"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   370 AA;  41050 MW;  93847A4CF99B6186 CRC64;
     MASFFARTRR FSLVSLFLLE LFTINLIPTT DAQIGICYGM MGNNLPPANE VIALYKANNI
     KRMRLYDPNQ PALNALRDSG IELILGIPNS DLQTLATNQD SARQWVQRNV LNFYPSVKIK
     YIAVGNEVSP VGGSSWLAQY VLPATQNVYQ AIRAQGLHDQ IKVTTAIDMT LIGNSFPPSK
     GSFRSDVRSY LDPFIGYLVY AGAPLLVNVY PYFSHIGNPR DISLPYALFT SPGVMVQDGP
     NGYQNLFDAM LDSVHAALDN TGIGWVNVVV SESGWPSDGG SATSYDNARI YLDNLIRHVG
     KGTPRRPWAT EAYLFAMFDE NQKSPELEKH FGVFYPNKQK KYPFGFGGER RDGEIVEGDF
     NGTVSLKSDM