E13B_HORVU
ID E13B_HORVU Reviewed; 334 AA.
AC P15737;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase GII;
DE EC=3.2.1.39 {ECO:0000269|PubMed:8514770};
DE AltName: Full=(1->3)-beta-glucan endohydrolase GII;
DE AltName: Full=(1->3)-beta-glucanase isoenzyme GII;
DE AltName: Full=Beta-1,3-endoglucanase GII;
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 [MRNA], AND PROTEIN SEQUENCE OF 29-68.
RC STRAIN=cv. Clipper;
RX PubMed=2562758; DOI=10.1007/bf00027333;
RA Hoej P.B., Hartman D.J., Morrice N.A., Doan D.N.P., Fincher G.B.;
RT "Purification of (1-->3)-beta-glucan endohydrolase isoenzyme II from
RT germinated barley and determination of its primary structure from a cDNA
RT clone.";
RL Plant Mol. Biol. 13:31-42(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Piggy;
RX PubMed=1899089; DOI=10.1016/s0021-9258(18)52331-0;
RA Leah R., Tommerup H., Svendsen I., Mundy J.;
RT "Biochemical and molecular characterization of three barley seed proteins
RT with antifungal properties.";
RL J. Biol. Chem. 266:1564-1573(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 258-332.
RC TISSUE=Leaf;
RA Jutidamrongphan W., Mackinnon G., Manners J., Simpson R.S., Scott K.J.;
RL Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 29-334.
RA Ballance G.M., Svendsen I.;
RT "Purification and amino acid sequence determination of an endo-1,3-beta-
RT glucanase from barley.";
RL Carlsberg Res. Commun. 53:411-419(1988).
RN [5]
RP PROTEIN SEQUENCE OF 255-266 AND 311-317, CATALYTIC ACTIVITY, ACTIVE SITE,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8514770; DOI=10.1016/s0021-9258(19)38654-5;
RA Chen L., Fincher G.B., Hoej P.B.;
RT "Evolution of polysaccharide hydrolase substrate specificity. Catalytic
RT amino acids are conserved in barley 1,3-1,4- and 1,3-beta-glucanases.";
RL J. Biol. Chem. 268:13318-13326(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 29-334.
RX PubMed=8146192; DOI=10.1073/pnas.91.7.2785;
RA Varghese J.N., Garrett T.P.J., Colman P.M., Chen L., Hoej P.B.,
RA Fincher G.B.;
RT "Three-dimensional structures of two plant beta-glucan endohydrolases with
RT distinct substrate specificities.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2785-2789(1994).
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 (PubMed:1899089). Hydrolyzes laminarin in vitro
CC (PubMed:8514770). {ECO:0000269|PubMed:1899089,
CC ECO:0000269|PubMed:8514770}.
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; Evidence={ECO:0000269|PubMed:8514770};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5 (at 37 degrees Celsius).
CC {ECO:0000269|PubMed:8514770};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR EMBL; M62907; AAA32939.1; -; mRNA.
DR EMBL; X16274; CAA34350.1; -; mRNA.
DR EMBL; M23548; AAA32958.1; -; mRNA.
DR PIR; S05510; S05510.
DR PDB; 1GHS; X-ray; 2.30 A; A/B=29-334.
DR PDBsum; 1GHS; -.
DR AlphaFoldDB; P15737; -.
DR SMR; P15737; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR EnsemblPlants; HORVU.MOREX.r2.3HG0266280.1; HORVU.MOREX.r2.3HG0266280.1; HORVU.MOREX.r2.3HG0266280.
DR EnsemblPlants; HORVU.MOREX.r2.3HG0266280.1.mrna1; HORVU.MOREX.r2.3HG0266280.1.mrna1; HORVU.MOREX.r2.3HG0266280.1.
DR Gramene; HORVU.MOREX.r2.3HG0266280.1; HORVU.MOREX.r2.3HG0266280.1; HORVU.MOREX.r2.3HG0266280.
DR Gramene; HORVU.MOREX.r2.3HG0266280.1.mrna1; HORVU.MOREX.r2.3HG0266280.1.mrna1; HORVU.MOREX.r2.3HG0266280.1.
DR SABIO-RK; P15737; -.
DR EvolutionaryTrace; P15737; -.
DR ExpressionAtlas; P15737; baseline and differential.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0006076; P:(1->3)-beta-D-glucan catabolic process; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
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 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase;
KW Plant defense; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:2562758, ECO:0000269|Ref.4"
FT CHAIN 29..334
FT /note="Glucan endo-1,3-beta-glucosidase GII"
FT /id="PRO_0000011848"
FT ACT_SITE 122
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 259
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CONFLICT 12
FT /note="A -> V (in Ref. 2; AAA32939)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="L -> V (in Ref. 2; AAA32939)"
FT /evidence="ECO:0000305"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1GHS"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:1GHS"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:1GHS"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1GHS"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:1GHS"
FT TURN 105..111
FT /evidence="ECO:0007829|PDB:1GHS"
FT STRAND 112..122
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 131..145
FT /evidence="ECO:0007829|PDB:1GHS"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1GHS"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 176..187
FT /evidence="ECO:0007829|PDB:1GHS"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:1GHS"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:1GHS"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 233..248
FT /evidence="ECO:0007829|PDB:1GHS"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:1GHS"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 272..283
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:1GHS"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:1GHS"
FT HELIX 314..318
FT /evidence="ECO:0007829|PDB:1GHS"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:1GHS"
SQ SEQUENCE 334 AA; 35194 MW; 552D66A29A08C703 CRC64;
MARKDVASMF AAALFIGAFA AVPTSVQSIG VCYGVIGNNL PSRSDVVQLY RSKGINGMRI
YFADGQALSA LRNSGIGLIL DIGNDQLANI AASTSNAASW VQNNVRPYYP AVNIKYIAAG
NEVQGGATQS ILPAMRNLNA ALSAAGLGAI KVSTSIRFDE VANSFPPSAG VFKNAYMTDV
ARLLASTGAP LLANVYPYFA YRDNPGSISL NYATFQPGTT VRDQNNGLTY TSLFDAMVDA
VYAALEKAGA PAVKVVVSES GWPSAGGFAA SAGNARTYNQ GLINHVGGGT PKKREALETY
IFAMFNENQK TGDATERSFG LFNPDKSPAY NIQF
