Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P34742 (E13A_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 66. 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 GI

EC=3.2.1.39
Alternative name(s):
(1->3)-beta-glucan endohydrolase GI
(1->3)-beta-glucanase isoenzyme GI
Beta-1,3-endoglucanase GI
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
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. Does not hydrolyze (1,3;1,4)-beta-D-glucans, (1,6)-beta-D-glucan, CM-cellulose, insoluble (1,3)-beta-D-glucans or aryl beta-D-glycosides.

Catalytic activity

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

Subunit structure

Monomer.

Tissue specificity

Young leaves and roots.

Developmental stage

First detected in young leaves ten days after initiation of germination. Also detected in young roots but not in mature leaves or roots.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.8.

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

Chain1 – 310310Glucan endo-1,3-beta-glucosidase GI
PRO_0000205273

Sites

Active site2341Nucleophile By similarity
Active site2911Proton donor By similarity

Experimental info

Sequence conflict36 – 383ADA → TDT AA sequence Ref.2
Sequence conflict451R → S AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P34742 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: CD10EF40C3A232C2

FASTA31032,954
        10         20         30         40         50         60 
TIGVCYGVVA NNLPPANEVV QLYRSNGLTG MRIYFADAKA LSALRGSGIG LILDVGGNDV 

        70         80         90        100        110        120 
LASLAANASN AANWVRDNVR PYYPAVNIKY IAAGNEVWGG DTQNIVPAMR NLGAALKAPG 

       130        140        150        160        170        180 
LGTIKVSTSI RFDAVTNTFP PSNGVFAQAY MTDVARLLAS TGAPLLTNVY PYFAYKDNPR 

       190        200        210        220        230        240 
DIQLNYATFR PGTTTVRDPN TGLTSQCLFD AMVDAVVAAL ERSGAPGVRV VVSESGWPSA 

       250        260        270        280        290        300 
SGFAATADNA RAYNQGLIDH VGGGTPKRPG ALETYIFAMF NENFKTGELT EKHFGLFNPD 

       310 
KSPAYPIRFQ 

« Hide

References

[1]"Evolution and differential expression of the (1-->3)-beta-glucan endohydrolase-encoding gene family in barley, Hordeum vulgare."
Xu P., Wang J., Fincher G.B.
Gene 120:157-165(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-310.
Strain: cv. Clipper.
Tissue: Leaf and Root.
[2]"Isolation and characterization of a (1-->3)-beta-glucan endohydrolase from germinating barley (Hordeum vulgare): amino acid sequence similarity with barley (1-->3,1-->4)-beta-glucanases."
Hoej P.B., Slade A.M., Wettenhall R.E.H., Fincher G.B.
FEBS Lett. 230:67-71(1988)
Cited for: PROTEIN SEQUENCE OF 1-46.
Tissue: Seed.
[3]"Purification and properties of three (1-->3)-beta-D-glucanase isoenzymes from young leaves of barley (Hordeum vulgare)."
Hrmova M., Fincher G.B.
Biochem. J. 289:453-461(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-13, CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96938 mRNA. Translation: AAA32960.1.
PIRJC1434.

3D structure databases

ProteinModelPortalP34742.
SMRP34742. Positions 2-309.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP34742.

Enzyme and pathway databases

SABIO-RKP34742.

Gene expression databases

GenevestigatorP34742.

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...

Entry information

Entry nameE13A_HORVU
AccessionPrimary (citable) accession number: P34742
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 1, 1994
Last modified: October 16, 2013
This is version 66 of the entry and version 2 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