ID E13F_HORVU Reviewed; 321 AA. AC Q02439; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 27-MAR-2024, entry version 92. DE RecName: Full=Putative glucan endo-1,3-beta-glucosidase GVI; DE EC=3.2.1.39; DE AltName: Full=(1->3)-beta-glucan endohydrolase GVI; DE AltName: Full=(1->3)-beta-glucanase isoenzyme GVI; DE AltName: Full=Beta-1,3-endoglucanase GVI; DE Flags: Precursor; Fragment; 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]. RC STRAIN=cv. Clipper, and cv. NK 1558; TISSUE=Seedling; 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). 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M96941; AAA32957.1; -; Genomic_DNA. DR PIR; JC1439; JC1439. DR AlphaFoldDB; Q02439; -. DR SMR; Q02439; -. DR CAZy; GH17; Glycoside Hydrolase Family 17. 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:SF250; GLUCAN ENDO-1,3-BETA-D-GLUCOSIDASE-RELATED; 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 3: Inferred from homology; KW Glycosidase; Hydrolase; Plant defense; Signal. FT SIGNAL <1..6 FT /evidence="ECO:0000250" FT CHAIN 7..321 FT /note="Putative glucan endo-1,3-beta-glucosidase GVI" FT /id="PRO_0000011850" FT ACT_SITE 100 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:O22317" FT ACT_SITE 241 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:O22317" FT NON_TER 1 SQ SEQUENCE 321 AA; 33344 MW; D95BC94BF91573D9 CRC64; LAGVEGIGVN YGMMGSDLPS PDKVVALYKA NNITDVRIFH PDTNVLEALR NSGLGVVLGT LNSDLAPLAS DASYAASWVH SYVQPFAGAV SFRYINAGNE VIPGESAALV LPAMKNLEAA LQAAGLSVPV TTAMATSVLG TSYPPSQGTF SEAALPTVGP IVSHLASSGT PLLVNVYPYF AYSADPSSVR LDYALLSSSA AVAVTDNGVE YANMFDAILD AVYAAVEKAG GGESLELVVS ETGWPSGGGG YGASVENAAA YINNLVRHVG GTPRRPGKAV ETYIFAMFNE NQKPEGVEQN FGMFQPDMSQ VYHVDFTASS S //