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Protein

Beta-glucosidase

Gene

bglT

Organism
Thermus thermophilus
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

GO - Molecular functioni

  1. beta-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucosidaseUniRule annotation (EC:3.2.1.21UniRule annotation)
Gene namesi
Name:bglTImported
Synonyms:b-glyImported
OrganismiThermus thermophilusImported
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZJKX-ray2.20A/B/C1-431[»]
ProteinModelPortaliQ9RA61.
SMRiQ9RA61. Positions 4-429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.UniRule annotation

Phylogenomic databases

KOiK05350.
OrthoDBiEOG60658J.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR017736. Glyco_hydro_1_beta-glucosidase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
TIGRFAMsiTIGR03356. BGL. 1 hit.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9RA61-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTENAEKFLW GVATSAYQIE GATQEDGRGP SIWDAFAQRP GAIRDGSTGE
60 70 80 90 100
PACDHYRRYE EDIALMQSLG VRAYRFSVAW PRILPEGRGR INPKGLAFYD
110 120 130 140 150
RLVDRLLASG ITPFLTLYHW DLPLALEERG GWRSRETAFA FAEYAEAVAR
160 170 180 190 200
ALADRVPFFA TLNEPWCSAF LGHWTGEHAP GLRNLEAALR AAHHLLLGHG
210 220 230 240 250
LAVEALRAAG ARRVGIVLNF APAYGEDPEA VDVADRYHNR FFLDPILGKG
260 270 280 290 300
YPESPFRDPP PVPILSRDLE LVARPLDFLG VNYYAPVRVA PGTGTLPVRY
310 320 330 340 350
LPPEGPATAM GWEVYPEGLH HLLKRLGREV PWPLYVTENG AAYPDLWTGE
360 370 380 390 400
AVVEDPERVA YLEAHVEAAL RAREEGVDLR GYFVWSLMDN FEWAFGYTRR
410 420 430
FGLYYVDFPS QRRIPKRSAL WYRERIARAQ T
Length:431
Mass (Da):48,612
Last modified:May 1, 2000 - v1
Checksum:iD6F7993D61D985E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF135400 Genomic DNA. Translation: AAD32630.2.
Y16753 Genomic DNA. Translation: CAB42553.3.
RefSeqiYP_006025.1. NC_005838.1.

Genome annotation databases

KEGGitth:TT_P0042.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF135400 Genomic DNA. Translation: AAD32630.2.
Y16753 Genomic DNA. Translation: CAB42553.3.
RefSeqiYP_006025.1. NC_005838.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZJKX-ray2.20A/B/C1-431[»]
ProteinModelPortaliQ9RA61.
SMRiQ9RA61. Positions 4-429.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGitth:TT_P0042.

Phylogenomic databases

KOiK05350.
OrthoDBiEOG60658J.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR017736. Glyco_hydro_1_beta-glucosidase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
TIGRFAMsiTIGR03356. BGL. 1 hit.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and expression of a beta-glycosidase gene from Thermus thermophilus. Sequence and biochemical characterization of the encoded enzyme."
    Dion M.P., Fourage L., Colas B., Hallet J.H.
    Glycoconj. J. 16:27-37(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: HB27Imported.
  2. "The structure of the alpha-galactosidase gene loci in Thermus brockianus ITI360 and Thermus thermophilus TH125."
    Fridjonsson O., Watzlawick H., Mattes R.
    Extremophiles 4:23-33(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: TH125Imported.
  3. Dion M.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: HB27Imported.
  4. "Semi-rational approach for converting a GH1 beta-glycosidase into a beta-transglycosidase."
    Teze D., Hendrickx J., Czjzek M., Ropartz D., Sanejouand Y.H., Tran V., Tellier C., Dion M.
    Protein Eng. Des. Sel. 27:13-19(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).

Entry informationi

Entry nameiQ9RA61_THETH
AccessioniPrimary (citable) accession number: Q9RA61
Secondary accession number(s): Q9X9D4
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: April 29, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.