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Protein

Beta-glucosidase A

Gene

bglA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 3 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.

Pathwayi: cellulose degradation

This protein is involved in the pathway cellulose degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway cellulose degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei166Proton donorSequence analysis1
Active sitei351NucleophilePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00696.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucosidase A (EC:3.2.1.21)
Alternative name(s):
Beta-D-glucoside glucohydrolase
Cellobiase
Gentiobiase
Gene namesi
Name:bglA
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000638791 – 446Beta-glucosidase AAdd BLAST446

Structurei

Secondary structure

1446
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 15Combined sources5
Helixi18 – 21Combined sources4
Helixi27 – 29Combined sources3
Helixi34 – 39Combined sources6
Helixi46 – 48Combined sources3
Beta strandi51 – 53Combined sources3
Helixi57 – 70Combined sources14
Beta strandi75 – 79Combined sources5
Helixi82 – 85Combined sources4
Beta strandi89 – 91Combined sources3
Helixi95 – 110Combined sources16
Beta strandi114 – 122Combined sources9
Helixi126 – 129Combined sources4
Turni130 – 132Combined sources3
Helixi133 – 135Combined sources3
Helixi139 – 154Combined sources16
Turni155 – 157Combined sources3
Beta strandi160 – 165Combined sources6
Helixi167 – 175Combined sources9
Helixi187 – 211Combined sources25
Beta strandi216 – 231Combined sources16
Helixi233 – 246Combined sources14
Helixi249 – 257Combined sources9
Helixi262 – 268Combined sources7
Helixi269 – 271Combined sources3
Helixi276 – 279Combined sources4
Helixi280 – 283Combined sources4
Beta strandi288 – 302Combined sources15
Helixi307 – 309Combined sources3
Beta strandi310 – 313Combined sources4
Helixi329 – 342Combined sources14
Beta strandi347 – 352Combined sources6
Helixi369 – 387Combined sources19
Beta strandi392 – 398Combined sources7
Helixi406 – 411Combined sources6
Beta strandi416 – 419Combined sources4
Turni421 – 423Combined sources3
Beta strandi426 – 428Combined sources3
Helixi430 – 441Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OD0X-ray2.11A/B2-446[»]
1OIFX-ray2.12A/B2-446[»]
1OIMX-ray2.15A/B2-446[»]
1OINX-ray2.15A/B2-446[»]
1UZ1X-ray2.00A/B2-446[»]
1W3JX-ray2.00A/B2-446[»]
2CBUX-ray1.85A/B2-446[»]
2CBVX-ray1.95A/B2-446[»]
2CESX-ray2.15A/B2-446[»]
2CETX-ray1.97A/B2-446[»]
2J75X-ray1.85A/B2-446[»]
2J77X-ray2.10A/B2-446[»]
2J78X-ray1.65A/B2-446[»]
2J79X-ray1.94A/B2-446[»]
2J7BX-ray1.87A/B2-446[»]
2J7CX-ray2.09A/B2-446[»]
2J7DX-ray2.24A/B2-446[»]
2J7EX-ray2.19A/B2-446[»]
2J7FX-ray2.28A/B2-446[»]
2J7GX-ray1.91A/B2-446[»]
2J7HX-ray1.95A/B2-446[»]
2JALX-ray1.90A/B2-446[»]
2VRJX-ray1.90A/B2-446[»]
2WBGX-ray1.85A/B/C/D2-446[»]
2WC3X-ray2.00A/B/C/D2-446[»]
2WC4X-ray1.70A/B/C/D2-446[»]
4GXPX-ray3.00A/B/C1-160[»]
A/B/C204-217[»]
A/B/C352-380[»]
A/B/C395-446[»]
ProteinModelPortaliQ08638.
SMRiQ08638.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08638.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.Curated

Phylogenomic databases

KOiK05350.

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.
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]
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.

Q08638-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVKKFPEGF LWGVATASYQ IEGSPLADGA GMSIWHTFSH TPGNVKNGDT
60 70 80 90 100
GDVACDHYNR WKEDIEIIEK LGVKAYRFSI SWPRILPEGT GRVNQKGLDF
110 120 130 140 150
YNRIIDTLLE KGITPFVTIY HWDLPFALQL KGGWANREIA DWFAEYSRVL
160 170 180 190 200
FENFGDRVKN WITLNEPWVV AIVGHLYGVH APGMRDIYVA FRAVHNLLRA
210 220 230 240 250
HARAVKVFRE TVKDGKIGIV FNNGYFEPAS EKEEDIRAVR FMHQFNNYPL
260 270 280 290 300
FLNPIYRGDY PELVLEFARE YLPENYKDDM SEIQEKIDFV GLNYYSGHLV
310 320 330 340 350
KFDPDAPAKV SFVERDLPKT AMGWEIVPEG IYWILKKVKE EYNPPEVYIT
360 370 380 390 400
ENGAAFDDVV SEDGRVHDQN RIDYLKAHIG QAWKAIQEGV PLKGYFVWSL
410 420 430 440
LDNFEWAEGY SKRFGIVYVD YSTQKRIVKD SGYWYSNVVK NNGLED
Length:446
Mass (Da):51,548
Last modified:October 1, 1994 - v1
Checksum:i2E5B06E72BF84C01
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74163 Genomic DNA. Translation: CAA52276.1.
PIRiS41561. S34570.
RefSeqiWP_004082398.1. NZ_CP011107.1.

Genome annotation databases

KEGGitmi:THEMA_04935.
tmw:THMA_1897.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74163 Genomic DNA. Translation: CAA52276.1.
PIRiS41561. S34570.
RefSeqiWP_004082398.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OD0X-ray2.11A/B2-446[»]
1OIFX-ray2.12A/B2-446[»]
1OIMX-ray2.15A/B2-446[»]
1OINX-ray2.15A/B2-446[»]
1UZ1X-ray2.00A/B2-446[»]
1W3JX-ray2.00A/B2-446[»]
2CBUX-ray1.85A/B2-446[»]
2CBVX-ray1.95A/B2-446[»]
2CESX-ray2.15A/B2-446[»]
2CETX-ray1.97A/B2-446[»]
2J75X-ray1.85A/B2-446[»]
2J77X-ray2.10A/B2-446[»]
2J78X-ray1.65A/B2-446[»]
2J79X-ray1.94A/B2-446[»]
2J7BX-ray1.87A/B2-446[»]
2J7CX-ray2.09A/B2-446[»]
2J7DX-ray2.24A/B2-446[»]
2J7EX-ray2.19A/B2-446[»]
2J7FX-ray2.28A/B2-446[»]
2J7GX-ray1.91A/B2-446[»]
2J7HX-ray1.95A/B2-446[»]
2JALX-ray1.90A/B2-446[»]
2VRJX-ray1.90A/B2-446[»]
2WBGX-ray1.85A/B/C/D2-446[»]
2WC3X-ray2.00A/B/C/D2-446[»]
2WC4X-ray1.70A/B/C/D2-446[»]
4GXPX-ray3.00A/B/C1-160[»]
A/B/C204-217[»]
A/B/C352-380[»]
A/B/C395-446[»]
ProteinModelPortaliQ08638.
SMRiQ08638.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGitmi:THEMA_04935.
tmw:THMA_1897.

Phylogenomic databases

KOiK05350.

Enzyme and pathway databases

UniPathwayiUPA00696.

Miscellaneous databases

EvolutionaryTraceiQ08638.

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.
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]
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...

Entry informationi

Entry nameiBGLA_THEMA
AccessioniPrimary (citable) accession number: Q08638
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 2, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

As the DNA coding for this protein is not found in the complete genome of T.maritima. It could have originated from another bacterial species.Curated

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.