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Q0GC07 (Q0GC07_THENN) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 36. Feed History...

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

Protein attributes

Sequence length721 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Ontologies

Keywords
   Molecular functionGlycosidase EMBL ABI29899.1
Hydrolase
   Technical term3D-structure PDB 2X42 PDB 2X40 PDB 2X41
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region163 – 1642Glucose binding PDB 2X42

Sites

Binding site581Glucose PDB 2X42
Binding site1301Glucose PDB 2X42
Binding site2101Glucose PDB 2X42
Binding site2431Glucose PDB 2X42

Sequences

Sequence LengthMass (Da)Tools
Q0GC07 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 78D048F6F9F3AFEA

FASTA72181,160
        10         20         30         40         50         60 
MEKVNEILSQ LTLEEKVKLV VGVGLPGLFG NPHSRVAGAA GETHPVPRVG LPAFVLADGP 

        70         80         90        100        110        120 
AGLRINPTRE NDENTYYTTA FPVEIMLAST WNRELLEEVG KAMGEEVREY GVDVLLAPAM 

       130        140        150        160        170        180 
NIHRNPLCGR NFEYYSEDPV LSGEMASSFV KGVQSQGVGA CIKHFVANNQ ETNRMVVDTI 

       190        200        210        220        230        240 
VSERALREIY LRGFEIAVKK SKPWSVMSAY NKLNGKYCSQ NEWLLKKVLR EEWGFEGFVM 

       250        260        270        280        290        300 
SDWYAGDNPV EQLKAGNDLI MPGKAYQVNT ERRDEIEEIM EALKEGKLSE EVLDECVRNI 

       310        320        330        340        350        360 
LKVLVNAPSF KNYRYSNKPD LEKHAKVAYE AGAEGVVLLR NEEALPLSEN SKIALFGTGQ 

       370        380        390        400        410        420 
IETIKGGTGS GDTHPRYAIS ILEGIKERGL NFDEELAKTY EDYIKKMRET EEYKPRRDSW 

       430        440        450        460        470        480 
GTIIKPKLPE NFLSEKEIHK LAKKNDVAVI VISRISGEGY DRKPVKGDFY LSDDETDLIK 

       490        500        510        520        530        540 
TVSREFHEQG KKVIVLLNIG SPVEVVSWRD LVDGILLVWQ AGQETGRIVA DVLTGRINPS 

       550        560        570        580        590        600 
GKLPTTFPRD YSDVPSWTFP GEPKDNPQKV VYEEDIYVGY RYYDTFGVEP AYEFGYGLSY 

       610        620        630        640        650        660 
TTFEYSDLNV SFDGETLRVQ YRIENTGGRA GKEVSQVYIK APKGKIDKPF QELKAFHKTR 

       670        680        690        700        710        720 
LLNPGESEEV VLEIPVRDLA SFNGEEWVVE AGEYEVRVGA SSRNIKLKGT FSVGEERRFK 


P 

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References

[1]"Subcritical water extraction and beta-glucosidase-catalyzed hydrolysis of quercetin glycosides in onion waste."
Turner C., Turner P., Jacobson G., Almgren K., Waldeback M., Sjoberg P., Nordberg Karlsson E., Markides K.E.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DSM 4359 EMBL ABI29899.1.
[2]"A novel variant of Thermotoga neapolitana beta-glucosidase B is an efficient catalyst for the synthesis of alkyl glucosides by transglycosylation."
Turner P., Svensson D., Adlercreutz P., Nordberg Karlsson E.
J. Biotechnol. 130:67-74(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DSM 4359 EMBL ABI29899.1.
[3]"Structural and functional analyses of beta-glucosidase 3B from Thermotoga neapolitana: a thermostable three-domain representative of glycoside hydrolase 3."
Pozzo T., Pasten J.L., Karlsson E.N., Logan D.T.
J. Mol. Biol. 397:724-739(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH GLUCOSE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ873691 Genomic DNA. Translation: ABI29899.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2X40X-ray2.31A1-721[»]
2X41X-ray2.05A1-721[»]
2X42X-ray2.10A1-721[»]
ProteinModelPortalQ0GC07.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1472.

Family and domain databases

Gene3D3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR019800. Glyco_hydro_3_AS.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR30620. PTHR30620. 1 hit.
PfamPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSPR00133. GLHYDRLASE3.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 2 hits.
PROSITEPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ0GC07.

Entry information

Entry nameQ0GC07_THENN
AccessionPrimary (citable) accession number: Q0GC07
Entry history
Integrated into UniProtKB/TrEMBL: October 3, 2006
Last sequence update: October 3, 2006
Last modified: June 11, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)