E13F_HORVU
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 03-AUG-2022, entry version 88.
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}.
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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 ExpressionAtlas; Q02439; 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 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