ID   E13C_HORVU              Reviewed;         330 AA.
AC   Q02126;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase GIII;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase GIII;
DE   AltName: Full=(1->3)-beta-glucanase isoenzyme GIII;
DE   AltName: Full=Beta-1,3-endoglucanase GIII;
DE   Flags: Precursor;
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 [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Clipper, and cv. NK 1558;
RX   PubMed=1396688; DOI=10.1111/j.1432-1033.1992.tb17266.x;
RA   Wang J., Xu P., Fincher G.B.;
RT   "Purification, characterization and gene structure of (1-->3)-beta-
RT   glucanase isoenzyme GIII from barley (Hordeum vulgare).";
RL   Eur. J. Biochem. 209:103-109(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-330.
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   [3]
RP   PROTEIN SEQUENCE OF 26-37.
RC   STRAIN=cv. Clipper;
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.
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   -!- DEVELOPMENTAL STAGE: Accumulates in developing leaves.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; X67099; CAA47473.1; -; Genomic_DNA.
DR   PIR; S29311; S29311.
DR   AlphaFoldDB; Q02126; -.
DR   SMR; Q02126; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   BRENDA; 3.2.1.39; 2687.
DR   SABIO-RK; Q02126; -.
DR   ExpressionAtlas; Q02126; 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; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:8424790"
FT   CHAIN           26..330
FT                   /note="Glucan endo-1,3-beta-glucosidase GIII"
FT                   /id="PRO_0000011849"
FT   ACT_SITE        117
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        255
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   CONFLICT        169
FT                   /note="D -> S (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   330 AA;  34887 MW;  B8A262CF345A79E7 CRC64;
     MARKGVDVAV ALVLVALAAF PAVHSIGVCN GVLGNNLPAP SDVVTLYRSK RIDAMRIYEP
     ESKVLTALSG TGIAVLMDVG PALPSLASSP SAAAAWVKAN VSSFPGVSFR YIAVRNEVMD
     SAGQSTILPA MRNVQRALAA AGSPIKVSTS VRFDVFNNTS PPSNGVLADK SGFLRPILNF
     LARPARPLLA NVYPYFAYKG NPRDIQLTFA TFVPGSTTVN DNGLTYTNLF DAMVDSIYAA
     LEKAGTPGVK VVISESGWPS DQGFGATAQN ARAYNQGLIN HVGNGSPKKA GALESYIFAM
     FNENLKDGDE LEKNFGLFKP NMSPAYAITF