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P23535 (E13B_PHAVU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. 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, basic isoform

EC=3.2.1.39
Alternative name(s):
(1->3)-beta-glucan endohydrolase
Short name=(1->3)-beta-glucanase
Beta-1,3-endoglucanase
OrganismPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifier3885 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

Protein attributes

Sequence length348 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.

Subcellular location

Vacuole By similarity.

Induction

By fungal elicitor.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Ontologies

Keywords
   Biological processPlant defense
   Cellular componentVacuole
   Molecular functionGlycosidase
Hydrolase
   PTMPyrrolidone carboxylic acid
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

defense response

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentvacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 316316Glucan endo-1,3-beta-glucosidase, basic isoform
PRO_0000011857
Propeptide317 – 34832Removed in mature form By similarity
PRO_0000011858

Sites

Active site2401Nucleophile By similarity
Active site2971Proton donor By similarity

Amino acid modifications

Modified residue11Pyrrolidone carboxylic acid Probable

Sequences

Sequence LengthMass (Da)Tools
P23535 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 83177308F77429D6

FASTA34838,869
        10         20         30         40         50         60 
QIGVCYGMMG NNLPSANEVI NLYRSNNIRR MRLYDPNQAA LQALRNSGIE LILGVPNSDL 

        70         80         90        100        110        120 
QGLATNADTA RQWVQRNVLN FWPSVKIKYI AVGNEVSPVG GSSWYAQYVL PAVQNVYQAV 

       130        140        150        160        170        180 
RAQGLHDQIK VSTAIDMTLI GNSYPPSQGS FRGDVRSYLD PIIGYLLYAS APLHVNVYPY 

       190        200        210        220        230        240 
FSYSGNPRDI SLPYALFTSP NVVVRDGQYG YQNLFDAMLD SVHAAIDNTR IGYVEVVVSE 

       250        260        270        280        290        300 
SGWPSDGGFG ATYDNARVYL DNLVRRAGRG SPRRPSKPTE TYIFAMFDEN QKSPEIEKHF 

       310        320        330        340 
GLFKPSKEKK YPFGFGAQRM QRLLLMSSMQ HIPLRVTCKL EPSSQSLL 

« Hide

References

[1]"cDNA cloning and characterization of a putative 1,3-beta-D-glucanase transcript induced by fungal elicitor in bean cell suspension cultures."
Edington B.V., Lamb C.J., Dixon R.A.
Plant Mol. Biol. 16:81-94(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53129 mRNA. Translation: CAA37289.1.
PIRS13323.

3D structure databases

ProteinModelPortalP23535.
SMRP23535. Positions 2-315.
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_PHAVU
AccessionPrimary (citable) accession number: P23535
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: February 19, 2014
This is version 70 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