ID   E13A_HORVU              Reviewed;         310 AA.
AC   P34742;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase GI;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase GI;
DE   AltName: Full=(1->3)-beta-glucanase isoenzyme GI;
DE   AltName: Full=Beta-1,3-endoglucanase GI;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 5-310.
RC   STRAIN=cv. Clipper; TISSUE=Leaf, and Root;
RX   PubMed=1398132; DOI=10.1016/0378-1119(92)90089-8;
RA   Xu P., Wang J., Fincher G.B.;
RT   "Evolution and differential expression of the (1-->3)-beta-glucan
RT   endohydrolase-encoding gene family in barley, Hordeum vulgare.";
RL   Gene 120:157-165(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-46.
RC   TISSUE=Seed;
RA   Hoej P.B., Slade A.M., Wettenhall R.E.H., Fincher G.B.;
RT   "Isolation and characterization of a (1-->3)-beta-glucan endohydrolase from
RT   germinating barley (Hordeum vulgare): amino acid sequence similarity with
RT   barley (1-->3,1-->4)-beta-glucanases.";
RL   FEBS Lett. 230:67-71(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-13, AND CHARACTERIZATION.
RX   PubMed=8424790; DOI=10.1042/bj2890453;
RA   Hrmova M., Fincher G.B.;
RT   "Purification and properties of three (1-->3)-beta-D-glucanase isoenzymes
RT   from young leaves of barley (Hordeum vulgare).";
RL   Biochem. J. 289:453-461(1993).
CC   -!- FUNCTION: May provide a degree of protection against microbial invasion
CC       of germinated barley grain through its ability to degrade fungal cell
CC       wall polysaccharides. Does not hydrolyze (1,3;1,4)-beta-D-glucans,
CC       (1,6)-beta-D-glucan, CM-cellulose, insoluble (1,3)-beta-D-glucans or
CC       aryl beta-D-glycosides.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.8.;
CC   -!- SUBUNIT: Monomer.
CC   -!- TISSUE SPECIFICITY: Young leaves and roots.
CC   -!- DEVELOPMENTAL STAGE: First detected in young leaves ten days after
CC       initiation of germination. Also detected in young roots but not in
CC       mature leaves or roots.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; M96938; AAA32960.1; -; mRNA.
DR   PIR; JC1434; JC1434.
DR   AlphaFoldDB; P34742; -.
DR   SMR; P34742; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   PRIDE; P34742; -.
DR   SABIO-RK; P34742; -.
DR   ExpressionAtlas; P34742; baseline and differential.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Plant defense.
FT   CHAIN           1..310
FT                   /note="Glucan endo-1,3-beta-glucosidase GI"
FT                   /id="PRO_0000205273"
FT   ACT_SITE        96
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        234
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   CONFLICT        36..38
FT                   /note="ADA -> TDT (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        45
FT                   /note="R -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   310 AA;  32954 MW;  CD10EF40C3A232C2 CRC64;
     TIGVCYGVVA NNLPPANEVV QLYRSNGLTG MRIYFADAKA LSALRGSGIG LILDVGGNDV
     LASLAANASN AANWVRDNVR PYYPAVNIKY IAAGNEVWGG DTQNIVPAMR NLGAALKAPG
     LGTIKVSTSI RFDAVTNTFP PSNGVFAQAY MTDVARLLAS TGAPLLTNVY PYFAYKDNPR
     DIQLNYATFR PGTTTVRDPN TGLTSQCLFD AMVDAVVAAL ERSGAPGVRV VVSESGWPSA
     SGFAATADNA RAYNQGLIDH VGGGTPKRPG ALETYIFAMF NENFKTGELT EKHFGLFNPD
     KSPAYPIRFQ