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P26205

- BGLT_TRIRP

UniProt

P26205 - BGLT_TRIRP

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Protein

Cyanogenic beta-glucosidase

Gene
LI
Organism
Trifolium repens (Creeping white clover)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441Substrate By similarity
Binding sitei148 – 1481Substrate By similarity
Binding sitei193 – 1931Substrate By similarity
Active sitei194 – 1941Proton donor
Binding sitei337 – 3371Substrate By similarity
Active sitei408 – 4081Nucleophile

GO - Molecular functioni

  1. beta-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyanogenic beta-glucosidase (EC:3.2.1.21)
Alternative name(s):
Linamarase
Gene namesi
Name:LI
OrganismiTrifolium repens (Creeping white clover)
Taxonomic identifieri3899 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeTrifolium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 11›111 PublicationAdd
BLAST
Chaini12 – 425414Cyanogenic beta-glucosidasePRO_0000011765Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi213 ↔ 221
Glycosylationi220 – 2201N-linked (GlcNAc...) Reviewed prediction
Glycosylationi412 – 4121N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Leaves.

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
425
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 243
Helixi27 – 293
Beta strandi35 – 395
Helixi42 – 454
Beta strandi49 – 513
Helixi58 – 658
Helixi67 – 693
Beta strandi76 – 783
Helixi82 – 9514
Beta strandi100 – 1045
Helixi107 – 1104
Helixi116 – 1183
Helixi122 – 13716
Beta strandi141 – 1499
Helixi153 – 1597
Helixi161 – 1633
Helixi167 – 18216
Turni183 – 1853
Beta strandi188 – 1936
Helixi195 – 2039
Helixi215 – 2173
Turni226 – 2283
Helixi229 – 25123
Helixi253 – 2564
Beta strandi259 – 2657
Beta strandi268 – 2758
Helixi276 – 28914
Helixi291 – 2999
Helixi304 – 3107
Helixi311 – 3133
Helixi319 – 3257
Beta strandi330 – 3356
Beta strandi339 – 3446
Helixi355 – 3584
Beta strandi361 – 3677
Beta strandi370 – 3734
Helixi386 – 39813
Beta strandi404 – 4085

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CBGX-ray2.15A12-412[»]
ProteinModelPortaliP26205.
SMRiP26205. Positions 12-412.

Miscellaneous databases

EvolutionaryTraceiP26205.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26205-1 [UniParc]FASTAAdd to Basket

« Hide

LLSITTTHIH AFKPLPISFD DFSDLNRSCF APGFVFGTAS SAFQYEGAAF    50
EDGKGPSIWD TFTHKYPEKI KDRTNGDVAI DEYHRYKEDI GIMKDMNLDA 100
YRFSISWPRV LPKGKLSGGV NREGINYYNN LINEVLANGM QPYVTLFHWD 150
VPQALEDEYR GFLGRNIVDD FRDYAELCFK EFGDRVKHWI TLNEPWGVSM 200
NAYAYGTFAP GRCSDWLKLN CTGGDSGREP YLAAHYQLLA HAAAARLYKT 250
KYQASQNGII GITLVSHWFE PASKEKADVD AAKRGLDFML GWFMHPLTKG 300
RYPESMRYLV RKRLPKFSTE ESKELTGSFD FLGLNYYSSY YAAKAPRIPN 350
ARPAIQTDSL INATFEHNGK PLGPMAASSW LCIYPQGIRK LLLYVKNHYN 400
NPVIYITENG RNSSTINTVT SRIPF 425
Length:425
Mass (Da):48,325
Last modified:May 1, 1992 - v1
Checksum:i20B983B65C47A678
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56733 mRNA. Translation: CAA40057.1.
PIRiS16580. GLJY14.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56733 mRNA. Translation: CAA40057.1 .
PIRi S16580. GLJY14.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CBG X-ray 2.15 A 12-412 [» ]
ProteinModelPortali P26205.
SMRi P26205. Positions 12-412.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P26205.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR10353. PTHR10353. 1 hit.
Pfami PF00232. Glyco_hydro_1. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiBGLT_TRIRP
AccessioniPrimary (citable) accession number: P26205
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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