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P26205 (BGLT_TRIRP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Cyanogenic beta-glucosidase

EC=3.2.1.21
Alternative name(s):
Linamarase
Gene names
Name:LI
OrganismTrifolium repens (Creeping white clover)
Taxonomic identifier3899 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeTrifolium

Protein attributes

Sequence length425 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes cyanoglucosides, contributing to the release of hydrocyanic acid, which functions as a defense mechanism against small predators, when the leaf tissue is damaged.

Catalytic activity

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

Subunit structure

Homodimer.

Tissue specificity

Leaves.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide‹1 – 11›11 Ref.1
Chain12 – 425414Cyanogenic beta-glucosidase
PRO_0000011765

Sites

Active site1941Proton donor
Active site4081Nucleophile
Binding site441Substrate By similarity
Binding site1481Substrate By similarity
Binding site1931Substrate By similarity
Binding site3371Substrate By similarity

Amino acid modifications

Glycosylation2201N-linked (GlcNAc...) Potential
Glycosylation4121N-linked (GlcNAc...) Potential
Disulfide bond213 ↔ 221

Experimental info

Non-terminal residue11

Secondary structure

......................................................................... 425
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26205 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 20B983B65C47A678

FASTA42548,325
        10         20         30         40         50         60 
LLSITTTHIH AFKPLPISFD DFSDLNRSCF APGFVFGTAS SAFQYEGAAF EDGKGPSIWD 

        70         80         90        100        110        120 
TFTHKYPEKI KDRTNGDVAI DEYHRYKEDI GIMKDMNLDA YRFSISWPRV LPKGKLSGGV 

       130        140        150        160        170        180 
NREGINYYNN LINEVLANGM QPYVTLFHWD VPQALEDEYR GFLGRNIVDD FRDYAELCFK 

       190        200        210        220        230        240 
EFGDRVKHWI TLNEPWGVSM NAYAYGTFAP GRCSDWLKLN CTGGDSGREP YLAAHYQLLA 

       250        260        270        280        290        300 
HAAAARLYKT KYQASQNGII GITLVSHWFE PASKEKADVD AAKRGLDFML GWFMHPLTKG 

       310        320        330        340        350        360 
RYPESMRYLV RKRLPKFSTE ESKELTGSFD FLGLNYYSSY YAAKAPRIPN ARPAIQTDSL 

       370        380        390        400        410        420 
INATFEHNGK PLGPMAASSW LCIYPQGIRK LLLYVKNHYN NPVIYITENG RNSSTINTVT 


SRIPF 

« Hide

References

[1]"Nucleotide and derived amino acid sequence of the cyanogenic beta-glucosidase (linamarase) from white clover (Trifolium repens L.)."
Oxtoby E., Dunn M.A., Pancoro A., Hughes M.A.
Plant Mol. Biol. 17:209-219(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 12-25 AND 125-147.
Strain: S100 (EG).
Tissue: Leaf.
[2]"The crystal structure of a cyanogenic beta-glucosidase from white clover, a family 1 glycosyl hydrolase."
Barrett T., Suresh C.G., Tolley S.P., Dodson E.J., Hughes M.A.
Structure 3:951-960(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56733 mRNA. Translation: CAA40057.1.
PIRGLJY14. S16580.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CBGX-ray2.15A12-412[»]
ProteinModelPortalP26205.
SMRP26205. Positions 12-412.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26205.

Entry information

Entry nameBGLT_TRIRP
AccessionPrimary (citable) accession number: P26205
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: February 19, 2014
This is version 85 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries