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Q03467 (E13B_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. 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
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Implicated in the defense of plants against pathogens.

Catalytic activity

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

Tissue specificity

Constitutively expressed in seedling roots.

Induction

By fungal elicitors.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Ontologies

Keywords
   Biological processPlant defense
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Pyrrolidone carboxylic acid
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 – 3232 Potential
Chain33 – 347315Glucan endo-1,3-beta-glucosidase
PRO_0000011855
Propeptide348 – 37023Removed in mature form By similarity
PRO_0000011856

Sites

Active site2721Nucleophile By similarity
Active site3281Proton donor By similarity

Amino acid modifications

Modified residue331Pyrrolidone carboxylic acid Probable
Glycosylation3611N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q03467 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 93847A4CF99B6186

FASTA37041,050
        10         20         30         40         50         60 
MASFFARTRR FSLVSLFLLE LFTINLIPTT DAQIGICYGM MGNNLPPANE VIALYKANNI 

        70         80         90        100        110        120 
KRMRLYDPNQ PALNALRDSG IELILGIPNS DLQTLATNQD SARQWVQRNV LNFYPSVKIK 

       130        140        150        160        170        180 
YIAVGNEVSP VGGSSWLAQY VLPATQNVYQ AIRAQGLHDQ IKVTTAIDMT LIGNSFPPSK 

       190        200        210        220        230        240 
GSFRSDVRSY LDPFIGYLVY AGAPLLVNVY PYFSHIGNPR DISLPYALFT SPGVMVQDGP 

       250        260        270        280        290        300 
NGYQNLFDAM LDSVHAALDN TGIGWVNVVV SESGWPSDGG SATSYDNARI YLDNLIRHVG 

       310        320        330        340        350        360 
KGTPRRPWAT EAYLFAMFDE NQKSPELEKH FGVFYPNKQK KYPFGFGGER RDGEIVEGDF 

       370 
NGTVSLKSDM 

« Hide

References

[1]"Nucleotide sequence of a pea (Pisum sativum L.) beta-1,3-glucanase gene."
Chang M.-M., Culley D.E., Hadwiger L.A.
Plant Physiol. 101:1121-1122(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Alcan.
Tissue: Leaf.
[2]"Molecular characterization of a pea beta-1,3-glucanase induced by Fusarium solani and chitosan challenge."
Chang M.-M., Hadwiger L.A., Horovitz D.
Plant Mol. Biol. 20:609-618(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-370.
Strain: cv. Alcan.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S51479 Genomic DNA. Translation: AAB24398.1.
L02212 Genomic DNA. Translation: AAA33648.1.
S69419 Genomic DNA. No translation available.
PIRT06552.

3D structure databases

ProteinModelPortalQ03467.
SMRQ03467. Positions 34-346.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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 nameE13B_PEA
AccessionPrimary (citable) accession number: Q03467
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 67 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