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 22-FEB-2023, entry version 122. 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}. 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; 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 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:SF94; BETA 1,3-GLUCANASE; 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 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 //