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P15737 (E13B_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processPlant defense
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

defense response

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionglucan endo-1,3-beta-D-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.1 Ref.4
Chain29 – 334306Glucan endo-1,3-beta-glucosidase GII
PRO_0000011848

Sites

Active site2591Nucleophile
Active site3161Proton donor

Experimental info

Sequence conflict121A → V in AAA32939. Ref.2
Sequence conflict711L → V in AAA32939. Ref.2

Secondary structure

........................................................... 334
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15737 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 552D66A29A08C703

FASTA33435,194
        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 

« Hide

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.
PIRS05510.
UniGeneHv.18110.
Hv.25599.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GHSX-ray2.30A/B29-334[»]
ProteinModelPortalP15737.
SMRP15737. Positions 29-334.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP15737.

Enzyme and pathway databases

SABIO-RKP15737.

Gene expression databases

GenevestigatorP15737.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15737.

Entry information

Entry nameE13B_HORVU
AccessionPrimary (citable) accession number: P15737
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 16, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries