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Protein

Cyanogenic beta-glucosidase

Gene

LI

Organism
Trifolium repens (Creeping white clover)
Status
Reviewed-Annotation score: Annotation score: 5 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)DescriptionActionsGraphical viewLength
Binding sitei44SubstrateBy similarity1
Binding sitei148SubstrateBy similarity1
Binding sitei193SubstrateBy similarity1
Active sitei194Proton donor1
Binding sitei337SubstrateBy similarity1
Active sitei408Nucleophile1

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
Signal peptidei‹1 – 111 PublicationAdd BLAST›11
ChainiPRO_000001176512 – 425Cyanogenic beta-glucosidaseAdd BLAST414

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi213 ↔ 221
Glycosylationi220N-linked (GlcNAc...)Sequence analysis1
Glycosylationi412N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP26205.

Expressioni

Tissue specificityi

Leaves.

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1425
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi22 – 24Combined sources3
Helixi27 – 29Combined sources3
Beta strandi35 – 39Combined sources5
Helixi42 – 45Combined sources4
Beta strandi49 – 51Combined sources3
Helixi58 – 65Combined sources8
Helixi67 – 69Combined sources3
Beta strandi76 – 78Combined sources3
Helixi82 – 95Combined sources14
Beta strandi100 – 104Combined sources5
Helixi107 – 110Combined sources4
Helixi116 – 118Combined sources3
Helixi122 – 137Combined sources16
Beta strandi141 – 149Combined sources9
Helixi153 – 159Combined sources7
Helixi161 – 163Combined sources3
Helixi167 – 182Combined sources16
Turni183 – 185Combined sources3
Beta strandi188 – 193Combined sources6
Helixi195 – 203Combined sources9
Helixi215 – 217Combined sources3
Turni226 – 228Combined sources3
Helixi229 – 251Combined sources23
Helixi253 – 256Combined sources4
Beta strandi259 – 265Combined sources7
Beta strandi268 – 275Combined sources8
Helixi276 – 289Combined sources14
Helixi291 – 299Combined sources9
Helixi304 – 310Combined sources7
Helixi311 – 313Combined sources3
Helixi319 – 325Combined sources7
Beta strandi330 – 335Combined sources6
Beta strandi339 – 344Combined sources6
Helixi355 – 358Combined sources4
Beta strandi361 – 367Combined sources7
Beta strandi370 – 373Combined sources4
Helixi386 – 398Combined sources13
Beta strandi404 – 408Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CBGX-ray2.15A12-412[»]
ProteinModelPortaliP26205.
SMRiP26205.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26205.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR033132. Glyco_hydro_1_N_CS.
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

        10         20         30         40         50
LLSITTTHIH AFKPLPISFD DFSDLNRSCF APGFVFGTAS SAFQYEGAAF
60 70 80 90 100
EDGKGPSIWD TFTHKYPEKI KDRTNGDVAI DEYHRYKEDI GIMKDMNLDA
110 120 130 140 150
YRFSISWPRV LPKGKLSGGV NREGINYYNN LINEVLANGM QPYVTLFHWD
160 170 180 190 200
VPQALEDEYR GFLGRNIVDD FRDYAELCFK EFGDRVKHWI TLNEPWGVSM
210 220 230 240 250
NAYAYGTFAP GRCSDWLKLN CTGGDSGREP YLAAHYQLLA HAAAARLYKT
260 270 280 290 300
KYQASQNGII GITLVSHWFE PASKEKADVD AAKRGLDFML GWFMHPLTKG
310 320 330 340 350
RYPESMRYLV RKRLPKFSTE ESKELTGSFD FLGLNYYSSY YAAKAPRIPN
360 370 380 390 400
ARPAIQTDSL INATFEHNGK PLGPMAASSW LCIYPQGIRK LLLYVKNHYN
410 420
NPVIYITENG RNSSTINTVT SRIPF
Length:425
Mass (Da):48,325
Last modified:May 1, 1992 - v1
Checksum:i20B983B65C47A678
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56733 mRNA. Translation: CAA40057.1.
PIRiS16580. GLJY14.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56733 mRNA. Translation: CAA40057.1.
PIRiS16580. GLJY14.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CBGX-ray2.15A12-412[»]
ProteinModelPortaliP26205.
SMRiP26205.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PRIDEiP26205.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP26205.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR033132. Glyco_hydro_1_N_CS.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 93 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.