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Q08638 (BGLA_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Beta-glucosidase A
EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase
Cellobiase
Gentiobiase
Gene names
Name:bglA
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga ›

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Glycan metabolism; cellulose degradation.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

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.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionbeta-glucosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446Beta-glucosidase A
PRO_0000063879

Sites

Active site1661Proton donor Potential
Active site3511Nucleophile By similarity

Secondary structure

1 ......................................................................... 446
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08638 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 2E5B06E72BF84C01

FASTA44651,548
        10         20         30         40         50         60 
MNVKKFPEGF LWGVATASYQ IEGSPLADGA GMSIWHTFSH TPGNVKNGDT GDVACDHYNR 

        70         80         90        100        110        120 
WKEDIEIIEK LGVKAYRFSI SWPRILPEGT GRVNQKGLDF YNRIIDTLLE KGITPFVTIY 

       130        140        150        160        170        180 
HWDLPFALQL KGGWANREIA DWFAEYSRVL FENFGDRVKN WITLNEPWVV AIVGHLYGVH 

       190        200        210        220        230        240 
APGMRDIYVA FRAVHNLLRA HARAVKVFRE TVKDGKIGIV FNNGYFEPAS EKEEDIRAVR 

       250        260        270        280        290        300 
FMHQFNNYPL FLNPIYRGDY PELVLEFARE YLPENYKDDM SEIQEKIDFV GLNYYSGHLV 

       310        320        330        340        350        360 
KFDPDAPAKV SFVERDLPKT AMGWEIVPEG IYWILKKVKE EYNPPEVYIT ENGAAFDDVV 

       370        380        390        400        410        420 
SEDGRVHDQN RIDYLKAHIG QAWKAIQEGV PLKGYFVWSL LDNFEWAEGY SKRFGIVYVD 

       430        440 
YSTQKRIVKD SGYWYSNVVK NNGLED

« Hide

References

[1]"Comparative amino acid sequence analysis of Thermotoga maritima beta-glucosidase (BglA) deduced from the nucleotide sequence of the gene indicates distant relationship between beta-glucosidases of the BGA family and other families of beta-1,4-glycosyl hydrolases."
Liebl W., Gabelsberger J., Schleifer K.H.
Mol. Gen. Genet. 242:111-115(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X74163 Genomic DNA. Translation: CAA52276.1.
PIRS34570. S41561.

3D structure databases

PDBe
RCSB PDB
PDBj
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/C1-446[»]
ProteinModelPortalQ08638.
SMRQ08638. Positions 2-445.
ModBaseSearch...

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. 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]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
TIGRFAMsTIGR03356. BGL. 1 hit.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ08638.

Entry information

Entry nameBGLA_THEMA
AccessionPrimary (citable) accession number: Q08638
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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