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Q5B9F2 (BGLL_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 51. 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:AN2828
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length737 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 – 1919 Potential
Chain20 – 737718Probable beta-glucosidase L
PRO_0000394902

Sites

Active site2531 By similarity

Amino acid modifications

Glycosylation2251N-linked (GlcNAc...) Potential
Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation3651N-linked (GlcNAc...) Potential
Glycosylation6081N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5B9F2 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: CA6A418D21C1F829

FASTA73777,815
        10         20         30         40         50         60 
MRSLIRSGAL NAFLAASLAT GQVLTWDEAY TKATSDLSLL SQEEKVGIVT GVTWQGGPCV 

        70         80         90        100        110        120 
GNTYEPTSIP YPSLCLQDGP LSVRFANPVT VFPAGINAGA TWDRELIRAR GVAMGAESRG 

       130        140        150        160        170        180 
LGVHVQLGPV AGALGKIPSA GRNWEGFSND PYLAGIAMAE AIQGMQSSGV QACAKHYLLN 

       190        200        210        220        230        240 
EQEYNRDTIS SNADDRTIHE LYLWPFYDAV KANVASVMCS YNKINGTWAC EHDALLNGLL 

       250        260        270        280        290        300 
KGELGFKGHV LSDWNAQHST VQSANTGLDM TMPGSDFSTP PGSIYWGDNL AAAIADGSVP 

       310        320        330        340        350        360 
QERLDDMVTR ILAAWYLVGQ DQGHPPVAFS SWDGGAASVN VTTPEHGELA RTIARDSIVL 

       370        380        390        400        410        420 
LKNTNGSLPL AKPASLAVIG SDAIVNPDGA NACADRGCNK GTLAQGWGSG TAEFPYLVAP 

       430        440        450        460        470        480 
LDAIEEKLAG AGTAIITSTT DDATSGAEAA AAAETAIVFI TSDSGEGYIT VEGHEGDRNN 

       490        500        510        520        530        540 
LDPWHNGNLL VQAVARTNTP TIVVLHSVGP VTLETILAEP NVVAVVWAGL PGQESGHALT 

       550        560        570        580        590        600 
DVLFGDYAPS GKLPFTIGKS EEDYGADWTT SQVDDFAEGL FIDYRHFDQY GIEPRYEFGF 

       610        620        630        640        650        660 
GLSYTSFNYS TLSTSISTTP GPTTGETIVG GPSDLFAPIG TVSAYVANTG HVAGAEVVQL 

       670        680        690        700        710        720 
YIGYPDSAPS IPPKQLRGFD KLHLVPGESG IATFELTRRD ISYWDVGLQK WVVASGTFEV 

       730 
FVGASSRDIR LTGSFTV 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACD01000051 Genomic DNA. Translation: EAA63399.1.
BN001306 Genomic DNA. Translation: CBF83924.1.
RefSeqXP_660432.1. XM_655340.1.

3D structure databases

ProteinModelPortalQ5B9F2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00010267.

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00010267; CADANIAP00010267; CADANIAG00010267.
GeneID2873975.
KEGGani:AN2828.2.

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000031215.
KOK05349.
OMANAWHNGN.
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_EMENI
AccessionPrimary (citable) accession number: Q5B9F2
Secondary accession number(s): C8VJG1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: March 19, 2014
This is version 51 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