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P86102 (E13B_VITRO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

EC=3.2.1.39
Alternative name(s):
(1->3)-beta-glucan endohydrolase
Short name=(1->3)-beta-glucanase
Beta-1,3-endoglucanase
OrganismVitis rotundifolia (Muscadine grape)
Taxonomic identifier103349 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsVitalesVitaceaeVitis

Protein attributes

Sequence length34 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Is thought to be an important plant defense-related product against fungal pathogens.

Catalytic activity

Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. UniProtKB Q03773

Miscellaneous

On the 2D-gel the determined pI of this protein is: 6, its MW is: 25 kDa. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Ontologies

Keywords
   Biological processPlant defense
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect 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

Chain‹1 – ›34›34Glucan endo-1,3-beta-glucosidase
PRO_0000358869

Experimental info

Non-terminal residue11
Non-terminal residue341

Sequences

Sequence LengthMass (Da)Tools
P86102 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: F58BE59A84C58419

FASTA343,406
        10         20         30 
NIFNAISAAG LGNQIKVSTA IDTGVLGTSY PPSK 

« Hide

References

[1]"Proteomics approach to identify unique xylem sap proteins in Pierce's disease-tolerant Vitis species."
Basha S.M., Mazhar H., Vasanthaiah H.K.N.
Appl. Biochem. Biotechnol. 160:932-944(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Xylem.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
[Graphical view]
PfamPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE13B_VITRO
AccessionPrimary (citable) accession number: P86102
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 16, 2008
Last modified: February 19, 2014
This is version 14 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries