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Q4WGT3 (BGLL_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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 L

EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase L
Cellobiase L
Gentiobiase L
Gene names
Name:bglL
ORF Names:AFUA_7G06140
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length739 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   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

Signal peptide1 – 1717 Potential
Chain18 – 739722Probable beta-glucosidase L
PRO_0000394900

Sites

Active site2521 By similarity

Amino acid modifications

Glycosylation401N-linked (GlcNAc...) Potential
Glycosylation2241N-linked (GlcNAc...) Potential
Glycosylation3981N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4WGT3 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: DCDFA27EB664D341

FASTA73978,381
        10         20         30         40         50         60 
MQTLFLSLLA AAVTVHAYGS GGSNWDQAYS RAKDALQKLN QTEKVGLVTG VKWMGGPCVG 

        70         80         90        100        110        120 
NTYKPESIDY PSLCLQDSPL GIRFANPVTA FPAGINAGAT WDTQLLYARG AAMGAEAKGL 

       130        140        150        160        170        180 
GIHVQLGPVA GPLGKNPNGG RNWEGFSVDP YLSGVAMEKT IRGMQDSGVQ ACAKHWLGNE 

       190        200        210        220        230        240 
QEHYRDTISS NIGDRAAHEL YVWPFMDAVK AGVASVMCSY NKVNGTWACE SDALNNKLMK 

       250        260        270        280        290        300 
EELGFPGYIM SDWNAQHSTV NSAVSGLDMT MPGSDFSNPP GSIFWGSNLE AAVADGSVPQ 

       310        320        330        340        350        360 
SRLDDMVTRI LAAWYLVGQD QGYPPVAFSS WNGGKANVDV TADHGTVARA VARDSIVLLK 

       370        380        390        400        410        420 
NGHGTLPLRK PKSLAIVGSD AIVNPAGPNA CSDRGCNNGT LAMGWGSGTA EFPYLVGPLD 

       430        440        450        460        470        480 
AIQKRAAADG TKIVPSATDD PTAGASAAAA AETAIVFINS DSGEGYITVE GNLGDRNNLD 

       490        500        510        520        530        540 
PWHNGNELVK AVAAASKNVI VVIHSVGPII LETILAQPSV KAIVWAGLPG QESGNALVDV 

       550        560        570        580        590        600 
IYGDTTPSGK LPYTIAKQAA DYGASWINAE TDDFPEGLYV DYRHFDAKGI APRYEFGYGL 

       610        620        630        640        650        660 
SYTTFKYSGL WVNMDASAGA ANGQVVPGGP ADLFEVVGQV SVSVRNNGRV AGAEVAQLYL 

       670        680        690        700        710        720 
GLPDSAPATP PKQLRGFQKL MLQPGQTGRA TFKLTRRDLS YWDVQQQKWV VPSGTFKVYV 

       730 
GSSSRDIREE GSFRVRRGW 

« 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
AAHF01000009 Genomic DNA. Translation: EAL86858.1.
RefSeqXP_748896.1. XM_743803.1.

3D structure databases

ProteinModelPortalQ4WGT3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00009601.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00009601; CADAFUAP00009601; CADAFUAG00009601.
GeneID3506305.
KEGGafm:AFUA_7G06140.

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000031215.
KOK05349.
OMAWACESDA.
OrthoDBEOG7HMS8F.

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
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. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBGLL_ASPFU
AccessionPrimary (citable) accession number: Q4WGT3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: February 19, 2014
This is version 54 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