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Q02126 (E13C_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 GIII

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

Protein attributes

Sequence length330 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.

Developmental stage

Accumulates in developing leaves.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Ontologies

Keywords
   Biological processPlant defense
   DomainSignal
   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

Signal peptide1 – 2525 Ref.3
Chain26 – 330305Glucan endo-1,3-beta-glucosidase GIII
PRO_0000011849

Sites

Active site2551Nucleophile By similarity
Active site3121Proton donor By similarity

Experimental info

Sequence conflict1691D → S Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q02126 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: B8A262CF345A79E7

FASTA33034,887
        10         20         30         40         50         60 
MARKGVDVAV ALVLVALAAF PAVHSIGVCN GVLGNNLPAP SDVVTLYRSK RIDAMRIYEP 

        70         80         90        100        110        120 
ESKVLTALSG TGIAVLMDVG PALPSLASSP SAAAAWVKAN VSSFPGVSFR YIAVRNEVMD 

       130        140        150        160        170        180 
SAGQSTILPA MRNVQRALAA AGSPIKVSTS VRFDVFNNTS PPSNGVLADK SGFLRPILNF 

       190        200        210        220        230        240 
LARPARPLLA NVYPYFAYKG NPRDIQLTFA TFVPGSTTVN DNGLTYTNLF DAMVDSIYAA 

       250        260        270        280        290        300 
LEKAGTPGVK VVISESGWPS DQGFGATAQN ARAYNQGLIN HVGNGSPKKA GALESYIFAM 

       310        320        330 
FNENLKDGDE LEKNFGLFKP NMSPAYAITF 

« Hide

References

[1]"Purification, characterization and gene structure of (1-->3)-beta-glucanase isoenzyme GIII from barley (Hordeum vulgare)."
Wang J., Xu P., Fincher G.B.
Eur. J. Biochem. 209:103-109(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: cv. Clipper and cv. NK 1558.
[2]"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 [GENOMIC DNA] OF 26-330.
[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 26-37.
Strain: cv. Clipper.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X67099 Genomic DNA. Translation: CAA47473.1.
PIRS29311.

3D structure databases

ProteinModelPortalQ02126.
SMRQ02126. Positions 26-330.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneQ02126.

Enzyme and pathway databases

SABIO-RKQ02126.

Gene expression databases

GenevestigatorQ02126.

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 nameE13C_HORVU
AccessionPrimary (citable) accession number: Q02126
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 16, 2013
This is version 66 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