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P26204 (BGLS_TRIRP) 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:
Non-cyanogenic beta-glucosidase

EC=3.2.1.21
OrganismTrifolium repens (Creeping white clover)
Taxonomic identifier3899 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeTrifolium

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Tissue specificity

Leaves.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termDirect 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 peptide1 – 1818 Potential
Chain19 – 493475Non-cyanogenic beta-glucosidase
PRO_0000011764

Regions

Region478 – 4792Substrate binding By similarity

Sites

Active site2041Proton donor Potential
Active site4221Nucleophile By similarity
Binding site541Substrate By similarity
Binding site1581Substrate By similarity
Binding site2031Substrate By similarity
Binding site3461Substrate By similarity
Binding site4711Substrate By similarity

Amino acid modifications

Glycosylation341N-linked (GlcNAc...) Potential
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential
Glycosylation4121N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P26204 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: B6B3BAA5BBFFCB8F

FASTA49355,960
        10         20         30         40         50         60 
MDFIVAIFAL FVISSFTITS TNAVEASTLL DIGNLSRSSF PRGFIFGAGS SAYQFEGAVN 

        70         80         90        100        110        120 
EGGRGPSIWD TFTHKYPEKI RDGSNADITV DQYHRYKEDV GIMKDQNMDS YRFSISWPRI 

       130        140        150        160        170        180 
LPKGKLSGGI NHEGIKYYNN LINELLANGI QPFVTLFHWD LPQVLEDEYG GFLNSGVIND 

       190        200        210        220        230        240 
FRDYTDLCFK EFGDRVRYWS TLNEPWVFSN SGYALGTNAP GRCSASNVAK PGDSGTGPYI 

       250        260        270        280        290        300 
VTHNQILAHA EAVHVYKTKY QAYQKGKIGI TLVSNWLMPL DDNSIPDIKA AERSLDFQFG 

       310        320        330        340        350        360 
LFMEQLTTGD YSKSMRRIVK NRLPKFSKFE SSLVNGSFDF IGINYYSSSY ISNAPSHGNA 

       370        380        390        400        410        420 
KPSYSTNPMT NISFEKHGIP LGPRAASIWI YVYPYMFIQE DFEIFCYILK INITILQFSI 

       430        440        450        460        470        480 
TENGMNEFND ATLPVEEALL NTYRIDYYYR HLYYIRSAIR AGSNVKGFYA WSFLDCNEWF 

       490 
AGFTVRFGLN FVD 

« 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 135-157.
Strain: S100 (EG).
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56734 mRNA. Translation: CAA40058.1.
PIRGLJY31. S16581.

3D structure databases

ProteinModelPortalP26204.
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]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGLS_TRIRP
AccessionPrimary (citable) accession number: P26204
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
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