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Q9X108 (BGLT_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6-phospho-beta-glucosidase BglT

EC=3.2.1.86
Gene names
Name:bglT
Ordered Locus Names:TM_1281
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes cellobiose 6'-phosphate into glucose 6-phosphate (Glc6P) and glucose.

Catalytic activity

6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate.

Cofactor

Binds 1 NAD per subunit.

Binds 1 manganese ion per subunit.

Subunit structure

Homodimer or homotetramer. Exists in a homodimer/homotetramer equilibrium state in solution.

Miscellaneous

Is a retaining glucosidase as it hydrolyzes glycosidic bond with retention of anomeric configuration. Reaction mechanism includes redox steps involving NAD and stabilization of intermediates by Mn2+.

Sequence similarities

Belongs to the glycosyl hydrolase 4 family.

Biophysicochemical properties

Kinetic parameters:

KM=41 µM for p-nitrophenyl-beta-D-glucopyranoside 6-phosphate

pH dependence:

Optimum pH is 8.0. Active from pH 6.5 to 10.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4154156-phospho-beta-glucosidase BglT
PRO_0000169857

Regions

Nucleotide binding1 – 6464NAD

Sites

Active site2411Proton acceptor
Metal binding1621Manganese
Metal binding1921Manganese
Binding site871Substrate
Binding site1401Substrate
Binding site1631Substrate
Binding site2611Substrate
Site1031Increases basicity of active site Tyr By similarity

Secondary structure

..................................................................... 415
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X108 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: FB4E3B358245BFEE

FASTA41547,627
        10         20         30         40         50         60 
MRIAVIGGGS SYTPELVKGL LDISEDVRID EVIFYDIDEE KQKIVVDFVK RLVKDRFKVL 

        70         80         90        100        110        120 
ISDTFEGAVV DAKYVIFQFR PGGLKGREND EGIPLKYGLI GQETTGVGGF SAALRAFPIV 

       130        140        150        160        170        180 
EEYVDTVRKT SNATIVNFTN PSGHITEFVR NYLEYEKFIG LCNVPINFIR EIAEMFSARL 

       190        200        210        220        230        240 
EDVFLKYYGL NHLSFIEKVF VKGEDVTEKV FENLKLKLSN IPDEDFPTWF YDSVRLIVNP 

       250        260        270        280        290        300 
YLRYYLMEKK MFKKISTHEL RAREVMKIEK ELFEKYRTAV EIPEELTKRG GSMYSTAAAH 

       310        320        330        340        350        360 
LIRDLETDEG KIHIVNTRNN GSIENLPDDY VLEIPCYVRS GRVHTLSQGK GDHFALSFIH 

       370        380        390        400        410 
AVKMYERLTI EAYLKRSKKL ALKALLSHPL GPDVEDAKDL LEEILEANRE YVKLG 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 beta-glycosidase from Thermotoga maritima."
Yip V.L.Y., Varrot A., Davies G.J., Rajan S.S., Yang X., Thompson J., Anderson W.F., Withers S.G.
J. Am. Chem. Soc. 126:8354-8355(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, REACTION MECHANISM.
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[3]"NAD(+) and metal-ion dependent hydrolysis by family 4 glycosidases: structural insight into specificity for phospho-beta-D-glucosides."
Varrot A., Yip V.L.Y., Li Y., Rajan S.S., Yang X., Anderson W.F., Thompson J., Withers S.G., Davies G.J.
J. Mol. Biol. 346:423-435(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH NAD(+) AND GLUCOSE-6-PHOSPHATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD36356.1.
PIRE72273.
RefSeqNP_229086.1. NC_000853.1.
YP_007977635.1. NC_021214.1.
YP_008991622.1. NC_023151.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UP4X-ray2.85A/B/C/D/E/F/G/H1-415[»]
1UP6X-ray2.55A/B/C/D/E/F/G/H1-415[»]
1UP7X-ray2.40A/B/C/D/E/F/G/H1-415[»]
ProteinModelPortalQ9X108.
SMRQ9X108. Positions 1-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM1281.

Protein family/group databases

CAZyGH4. Glycoside Hydrolase Family 4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD36356; AAD36356; TM_1281.
GeneID898202.
KEGGtma:TM1281.
tmi:THEMA_07930.
tmm:Tmari_1286.
PATRIC23937500. VBITheMar51294_1296.

Phylogenomic databases

eggNOGCOG1486.
KOK01222.
OMAPSGHITE.
OrthoDBEOG6CP3SG.

Enzyme and pathway databases

SABIO-RKQ9X108.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProIPR019802. GlycHydrolase_4_CS.
IPR001088. Glyco_hydro_4.
IPR022616. Glyco_hydro_4_C.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF02056. Glyco_hydro_4. 1 hit.
PF11975. Glyco_hydro_4C. 1 hit.
[Graphical view]
PRINTSPR00732. GLHYDRLASE4.
SUPFAMSSF56327. SSF56327. 1 hit.
PROSITEPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9X108.

Entry information

Entry nameBGLT_THEMA
AccessionPrimary (citable) accession number: Q9X108
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries