P15737 (E13B_HORVU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Glucan endo-1,3-beta-glucosidase GII EC=3.2.1.39 Alternative name(s): (1->3)-beta-glucan endohydrolase GII (1->3)-beta-glucanase isoenzyme GII Beta-1,3-endoglucanase GII
Organism	Hordeum vulgare (Barley)
Taxonomic identifier	4513 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

Protein attributes

Sequence length	334 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May provide a degree of protection against microbial invasion of germinated barley grain through its ability to degrade fungal cell wall polysaccharides.
Catalytic activity	Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Sequence similarities	Belongs to the glycosyl hydrolase 17 family.

Ontologies

Keywords
Biological process	Plant defense
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro defense response Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	glucan endo-1,3-beta-D-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Ref.1 Ref.4

Chain

29 – 334

306

Glucan endo-1,3-beta-glucosidase GII

PRO_0000011848

Sites

Active site

259

1

Nucleophile

Active site

316

1

Proton donor

Experimental info

Sequence conflict

12

1

A → V in AAA32939. Ref.2

Sequence conflict

71

1

L → V in AAA32939. Ref.2

Secondary structure

1

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334

Helix Strand Turn

Details...

Beta strand

30 – 32

3

Beta strand

37 – 39

3

Helix

43 – 53

11

Beta strand

57 – 62

6

Helix

65 – 70

6

Turn

71 – 73

3

Beta strand

77 – 81

5

Helix

84 – 86

3

Helix

87 – 92

6

Helix

94 – 104

11

Turn

105 – 111

7

Beta strand

112 – 122

11

Helix

125 – 130

6

Helix

131 – 145

15

Beta strand

150 – 157

8

Helix

158 – 160

3

Helix

167 – 169

3

Beta strand

171 – 174

4

Helix

176 – 187

12

Beta strand

191 – 194

4

Helix

197 – 203

7

Turn

205 – 207

3

Helix

210 – 214

5

Turn

224 – 226

3

Helix

233 – 248

16

Beta strand

255 – 260

6

Beta strand

264 – 267

4

Helix

272 – 283

12

Helix

286 – 288

3

Beta strand

299 – 302

4

Helix

314 – 318

5

Beta strand

328 – 330

3

Sequences

	Sequence		Length	Mass (Da)
	P15737 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 552D66A29A08C703	FASTA	334	35,194
	10 20 30 40 50 60 MARKDVASMF AAALFIGAFA AVPTSVQSIG VCYGVIGNNL PSRSDVVQLY RSKGINGMRI 70 80 90 100 110 120 YFADGQALSA LRNSGIGLIL DIGNDQLANI AASTSNAASW VQNNVRPYYP AVNIKYIAAG 130 140 150 160 170 180 NEVQGGATQS ILPAMRNLNA ALSAAGLGAI KVSTSIRFDE VANSFPPSAG VFKNAYMTDV 190 200 210 220 230 240 ARLLASTGAP LLANVYPYFA YRDNPGSISL NYATFQPGTT VRDQNNGLTY TSLFDAMVDA 250 260 270 280 290 300 VYAALEKAGA PAVKVVVSES GWPSAGGFAA SAGNARTYNQ GLINHVGGGT PKKREALETY 310 320 330 IFAMFNENQK TGDATERSFG LFNPDKSPAY NIQF

References

[1]	"Purification of (1-->3)-beta-glucan endohydrolase isoenzyme II from germinated barley and determination of its primary structure from a cDNA clone." Hoej P.B., Hartman D.J., Morrice N.A., Doan D.N.P., Fincher G.B. Plant Mol. Biol. 13:31-42(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-68. Strain: cv. Clipper.
[2]	"Biochemical and molecular characterization of three barley seed proteins with antifungal properties." Leah R., Tommerup H., Svendsen I., Mundy J. J. Biol. Chem. 266:1564-1573(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Piggy.
[3]	Jutidamrongphan W., Mackinnon G., Manners J., Simpson R.S., Scott K.J. Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 258-332. Tissue: Leaf.
[4]	"Purification and amino acid sequence determination of an endo-1,3-beta-glucanase from barley." Ballance G.M., Svendsen I. Carlsberg Res. Commun. 53:411-419(1988) Cited for: PROTEIN SEQUENCE OF 29-334.
[5]	"Three-dimensional structures of two plant beta-glucan endohydrolases with distinct substrate specificities." Varghese J.N., Garrett T.P.J., Colman P.M., Chen L., Hoej P.B., Fincher G.B. Proc. Natl. Acad. Sci. U.S.A. 91:2785-2789(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M62907 mRNA. Translation: AAA32939.1.
X16274 mRNA. Translation: CAA34350.1.
M23548 mRNA. Translation: AAA32958.1.

PIR

S05510.

UniGene

Hv.18110.
Hv.25599.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GHS	X-ray	2.30	A/B	29-334	[»]

ProteinModelPortal

P15737.

SMR

P15737. Positions 29-334.

ModBase

Search...

Protein family/group databases

CAZy

GH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

Gramene

P15737.

Enzyme and pathway databases

SABIO-RK

P15737.

Gene expression databases

Genevestigator

P15737.

Family and domain databases

Gene3D

3.20.20.80. 1 hit.

InterPro

IPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF00332. Glyco_hydro_17. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P15737.

Entry information

Entry name

E13B_HORVU

Accession

Primary (citable) accession number: P15737

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program