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Q4WA69 (BGLK_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 55. 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:
Probable beta-glucosidase K

EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase K
Cellobiase K
Gentiobiase K
Gene names
Name:bglK
ORF Names:AFUA_7G00240
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length767 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose By similarity.

Catalytic activity

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

Pathway

Glycan metabolism; cellulose degradation.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 3 family.

Contains 1 PA14 domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 767767Probable beta-glucosidase K
PRO_0000394897

Regions

Domain406 – 541136PA14

Sites

Active site2321 By similarity

Amino acid modifications

Glycosylation191N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation4771N-linked (GlcNAc...) Potential
Glycosylation7491N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4WA69 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: BF4924E3FE58BC4E

FASTA76783,358
        10         20         30         40         50         60 
MGEICPRRED FDIDYILKNA SLLEKVSLLA GYDFWHTAPL PRFNVPSVRV SDGPNGVRGT 

        70         80         90        100        110        120 
KFFDGVRAAC LPCGTGLAAT WDQSLLYDAG VLIGQECLAK GAHCWLVPTV CIQRSPLGGR 

       130        140        150        160        170        180 
GFESFAEDPY ATGKLAAAYI RGAQSTGVIS TIKHFAANDQ EHERISVNAV MSERALREVH 

       190        200        210        220        230        240 
LLPFQIAIAD SAPGAVMTCY NKVNGQHLSE SKEMLDGLLR REWGWKGLIM SDWFGTYSTA 

       250        260        270        280        290        300 
EALNAGLGLE MPGTTRLRGP LLELAISSRK VSRATLDERA RTVLEFVQRA RKAEVSAVES 

       310        320        330        340        350        360 
TRDFPEDRRL NRKLAADSIV LLKNESGLLP LNPQTLTSVA LIGPNMKTAA FCGGGSASLQ 

       370        380        390        400        410        420 
PYYSTSPYQG ITSQLPPGVE VLYETGATSY AFIPELEASE VRTPEGQPGL RMRFYRDPPS 

       430        440        450        460        470        480 
VQERRVLMGF SNPELDRLFY ADIEAELIAP ATGPFQFGLA VYGSASLFLN DQLIIDNTTV 

       490        500        510        520        530        540 
QRGGTFFFGK GTLEETATVD LVQGQSYQIK VQFASGPSSK LVKPGVVNFG GGAGRLGMVQ 

       550        560        570        580        590        600 
VVDPERAIAR AVEAAKRADI TILGVGLTRD HESEGFDRSH MDLPPAVASL VTAVLDVAPD 

       610        620        630        640        650        660 
AILLTQSGTP FSMLPWADLV KTHLHAWFGG NELGNGIADV LFGVVNPSGK LPLSFPRRIE 

       670        680        690        700        710        720 
DTPTYLNFGS ERGQVTYGEG IYVGYKLLRK SPTSCALSIR ARFVVHLLCV LRFDGRHRVR 

       730        740        750        760 
YTECSKLGRR GRSGSSPAVY RGRSNNVVNR TSHQGAQRIS KGGFAAR 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000015 Genomic DNA. Translation: EAL84867.1.
RefSeqXP_746905.1. XM_741812.1.

3D structure databases

ProteinModelPortalQ4WA69.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00001243; CADAFUAP00001243; CADAFUAG00001243.
GeneID3504260.
KEGGafm:AFUA_7G00240.

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000031215.
KOK01238.
OMAQRGGTFF.
OrthoDBEOG7H799Q.

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D3.20.20.300. 1 hit.
3.40.50.1700. 2 hits.
InterProIPR026892. Glyco_hydro_3.
IPR019800. Glyco_hydro_3_AS.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
IPR011658. PA14.
[Graphical view]
PANTHERPTHR30620. PTHR30620. 1 hit.
PfamPF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
PF07691. PA14. 1 hit.
[Graphical view]
PRINTSPR00133. GLHYDRLASE3.
SMARTSM00758. PA14. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 2 hits.
PROSITEPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGLK_ASPFU
AccessionPrimary (citable) accession number: Q4WA69
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: November 13, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries