ID   E13A_SOLLC              Reviewed;         336 AA.
AC   Q01412;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase A;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase A;
DE            Short=(1->3)-beta-glucanase A;
DE   AltName: Full=Acidic beta-1,3-glucanase;
DE   AltName: Full=Beta-1,3-endoglucanase A;
DE   Flags: Precursor;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 312-330.
RC   STRAIN=cv. Moneymaker; TISSUE=Leaf;
RX   PubMed=1421154; DOI=10.1007/bf00040610;
RA   van Kan J.A.L., Joosten M.H.A.J., Wagemakers C.A.M.,
RA   van den Berg-Velthuis G.C.M., de Wit P.J.G.M.;
RT   "Differential accumulation of mRNAs encoding extracellular and
RT   intracellular PR proteins in tomato induced by virulent and avirulent races
RT   of Cladosporium fulvum.";
RL   Plant Mol. Biol. 20:513-527(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   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- DEVELOPMENTAL STAGE: Maximum expression found during days 4 to 8 and
CC       days 8 to 12 after inoculation with an avirulent and a virulent
CC       pathogen respectively.
CC   -!- INDUCTION: Upon infection by virulent and avirulent races of pathogens,
CC       for example fungal pathogen C.fulvum.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; M80604; AAA03617.1; -; mRNA.
DR   PIR; S26240; S26240.
DR   RefSeq; NP_001234798.2; NM_001247869.2.
DR   AlphaFoldDB; Q01412; -.
DR   SMR; Q01412; -.
DR   STRING; 4081.Solyc01g008620.2.1; -.
DR   Allergome; 2549; Sola l Glucanase.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   PaxDb; Q01412; -.
DR   GeneID; 543986; -.
DR   KEGG; sly:543986; -.
DR   eggNOG; ENOG502RRK1; Eukaryota.
DR   OrthoDB; 966331at2759; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q01412; baseline.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; 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   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;
KW   Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..336
FT                   /note="Glucan endo-1,3-beta-glucosidase A"
FT                   /id="PRO_0000011851"
FT   ACT_SITE        118
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        257
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   MOD_RES         24
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P15797"
SQ   SEQUENCE   336 AA;  37572 MW;  5335FDF40DEF9488 CRC64;
     MAFLSSLLAS LLLVGLLIQI TGAQPIGVCY GKIANNLPSD QDVIKLYNSN NIKKMRIYFP
     ETNVFNALKG SNIEIILDVP NQDLEALANP SKRQGWVQDN IRNHFPDVKF KYIAVGNEVD
     PGRDSGKYAR FVGPAMENIY NALSSAGLQN QIKVSTATYL GLLTNTYPPR DSIFRDEYKS
     FINPIIGFLS RHNLPLLANI YPYFGHADDN VPLPYALFKQ QGLNDAGYQN LFDALVDSMY
     FATEKLGGQN IEIIVSESGW PSEGHPSATL ENAMTYYTNL INHVKGGAGT PKKPGRTIET
     YLFAMFDENR KDGKPSEQHF GLFKPDQRPK YQLKFD