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Reviewed, UniProtKB/Swiss-Prot P34742 (E13A_HORVU)

Last modified October 13, 2009. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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.
Sequence processingThe displayed sequence is not processed.
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

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
P34742-1 [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: 1398132] [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: 8424790] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-13, CHARACTERIZATION.

Cross-references

Sequence databases

M96938 mRNA. Translation: AAA32960.1.
PIRJC1434.

3D structure databases

HSSPHSSP built from PDB template 1GHS based on UniProtKB P15737.
SMRP34742. Positions 2-309.
ModBaseSearch...

Protein family/group databases

CAZyGH17. Glycoside Hydrolase Family 17.

Organism-specific databases

GrameneP34742.

Enzyme and pathway databases

BRENDA3.2.1.39. 283.

Gene expression databases

GenevestigatorP34742.

Family and domain databases

InterProIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
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 13, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents