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Q5B6C6 (BGLF_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 53. 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 F

EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase F
Cellobiase F
Gentiobiase F
Gene names
Name:bglF
ORF Names:AN10482
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 length868 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.

Sequence caution

The sequence EAA58835.1 differs from that shown. Reason: Erroneous gene model prediction.

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 – 2020 Potential
Chain21 – 868848Probable beta-glucosidase F
PRO_0000394114

Sites

Active site2851 By similarity

Amino acid modifications

Glycosylation651N-linked (GlcNAc...) Potential
Glycosylation731N-linked (GlcNAc...) Potential
Glycosylation2571N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) Potential
Glycosylation3601N-linked (GlcNAc...) Potential
Glycosylation3951N-linked (GlcNAc...) Potential
Glycosylation4211N-linked (GlcNAc...) Potential
Glycosylation7261N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5B6C6 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 2CBEC9AF65A2E6F2

FASTA86893,918
        10         20         30         40         50         60 
MAHRWLILAL VAAAAPRALA SPGPSLNERQ SDDEPFSPPY YPAPNGGWVS TWAEAYEKAH 

        70         80         90        100        110        120 
SIVSNLTLAE KVNLTTGTGI FMGPCAGQTG SVPRLGIPNL CLHDSPLGVR NTDHNTAFPP 

       130        140        150        160        170        180 
GITVGATFDK SLMYERGVGL GEEARGKGVN VLLGPSVGPL GRKPRGGRNW EGFGFDPVLQ 

       190        200        210        220        230        240 
GIGGAETIKG MQSTGLIACI KHFVGNEQEM HRMSSVVTQG YSSNIDDRTL HELYIWPFAE 

       250        260        270        280        290        300 
GVRAEVGSVM IAYNDVNKSS CSQNSKLING VLKDELGFQG FVVTDWLAHY GGVSSALAGL 

       310        320        330        340        350        360 
DMDMPGDGAV PLFGNSYWGP ELSRSILNGT VPVERLNDMV TRILATWYKM GQDQDYPLPN 

       370        380        390        400        410        420 
FSSNTEDEKG LLYPGAVISP IGVVNQYVNV QGNHNITARA IARDAITLLK NEGDLLPLRR 

       430        440        450        460        470        480 
NDSLKVFGTD AGPDPQGLNS CADKGCNRGV LTMGWGSGTS KLPYLITPQE AIANITPTAE 

       490        500        510        520        530        540 
FFITDSFPSS VDANDEDIAI VFINSDSGEN YITVDGNPGD RKTSGLHAWH NGDELVKAAA 

       550        560        570        580        590        600 
ERFSQVVVVI HTVGPIILEE WIDLDSVKAV LIAHLPGQEA GYSLTDVLFG DYSPSGHLPY 

       610        620        630        640        650        660 
TIPYQESNYP SSVGLLQQPF GQIQDYYTEG LYIDYRHFLK EDITPRYAFG HGLSYTTFEF 

       670        680        690        700        710        720 
SEPALSVVTP LDSAYPPSRP AKGPTPTYPN TIPPASEAAW PAKFNRIWRY IYPYLNNPQA 

       730        740        750        760        770        780 
DAAVANSSKT YPYPDGYSTD PQPPPRAGGA EGGNPALWDV AFSVQVTVTN TGQHSGRAVA 

       790        800        810        820        830        840 
QLYVELPDSL GLDTPSRQLR QFEKTKVLET GQSETLTLEV TRKDVSVWDV EVQDWKTVVG 

       850        860 
GEGVKIHIGE SVLDIRTECE VGGRCVTL 

« 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
AACD01000063 Genomic DNA. Translation: EAA58835.1. Sequence problems.
BN001302 Genomic DNA. Translation: CBF75129.1.
RefSeqXP_661508.1. XM_656416.1.

3D structure databases

ProteinModelPortalQ5B6C6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00004795; CADANIAP00004795; CADANIAG00004795.
GeneID2873326.
KEGGani:AN3904.2.

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000031215.
OMAENYITVE.
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.
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. 1 hit.
PROSITEPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGLF_EMENI
AccessionPrimary (citable) accession number: Q5B6C6
Secondary accession number(s): C8V6A2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 53 of the entry and version 2 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