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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 – 441SubstrateBy similarity
Binding sitei148 – 1481SubstrateBy similarity
Binding sitei193 – 1931SubstrateBy similarity
Active sitei194 – 1941Proton donor
Binding sitei337 – 3371SubstrateBy 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...)Sequence Analysis
Glycosylationi412 – 4121N-linked (GlcNAc...)Sequence Analysis

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 – 243Combined sources
Helixi27 – 293Combined sources
Beta strandi35 – 395Combined sources
Helixi42 – 454Combined sources
Beta strandi49 – 513Combined sources
Helixi58 – 658Combined sources
Helixi67 – 693Combined sources
Beta strandi76 – 783Combined sources
Helixi82 – 9514Combined sources
Beta strandi100 – 1045Combined sources
Helixi107 – 1104Combined sources
Helixi116 – 1183Combined sources
Helixi122 – 13716Combined sources
Beta strandi141 – 1499Combined sources
Helixi153 – 1597Combined sources
Helixi161 – 1633Combined sources
Helixi167 – 18216Combined sources
Turni183 – 1853Combined sources
Beta strandi188 – 1936Combined sources
Helixi195 – 2039Combined sources
Helixi215 – 2173Combined sources
Turni226 – 2283Combined sources
Helixi229 – 25123Combined sources
Helixi253 – 2564Combined sources
Beta strandi259 – 2657Combined sources
Beta strandi268 – 2758Combined sources
Helixi276 – 28914Combined sources
Helixi291 – 2999Combined sources
Helixi304 – 3107Combined sources
Helixi311 – 3133Combined sources
Helixi319 – 3257Combined sources
Beta strandi330 – 3356Combined sources
Beta strandi339 – 3446Combined sources
Helixi355 – 3584Combined sources
Beta strandi361 – 3677Combined sources
Beta strandi370 – 3734Combined sources
Helixi386 – 39813Combined sources
Beta strandi404 – 4085Combined sources

3D structure databases

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

        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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

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 .
PIRi S16580. GLJY14.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 87 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