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Q5B5S8 (BGLA_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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 A

EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase A
Cellobiase A
Gentiobiase A
Gene names
Name:bglA
Synonyms:bgl1
ORF Names:AN4102
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 length863 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 CBF74704.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CBF74704.1 differs from that shown. Reason: Frameshift at position 844.

The sequence EAA59363.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAA59363.1 differs from that shown. Reason: Frameshift at position 844.

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 – 863844Probable beta-glucosidase A
PRO_0000394100

Sites

Active site2831 By similarity

Amino acid modifications

Glycosylation651N-linked (GlcNAc...) Potential
Glycosylation2141N-linked (GlcNAc...) Potential
Glycosylation2551N-linked (GlcNAc...) Potential
Glycosylation3181N-linked (GlcNAc...) Potential
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation3571N-linked (GlcNAc...) Potential
Glycosylation4931N-linked (GlcNAc...) Potential
Glycosylation5261N-linked (GlcNAc...) Potential
Glycosylation5451N-linked (GlcNAc...) Potential
Glycosylation5671N-linked (GlcNAc...) Potential
Glycosylation6641N-linked (GlcNAc...) Potential
Glycosylation7151N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5B5S8 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 3C46FE9E7731E2A2

FASTA86393,242
        10         20         30         40         50         60 
MKLGWLEAAA LTAASVASAQ VKQDDLPVSP PYYPSPWSNG EGEWAEAYNR AVQIVSQMTL 

        70         80         90        100        110        120 
DEKVNLTTGT GMSEKCVGQT GSVPRLGINS ICLQDGPLGI RFTDYNSAFP AGVNVAATWD 

       130        140        150        160        170        180 
RQLAYIRGHA MGQEFSDKGI DVQLGPAAGP LGRFPDGGRN WEGFSPDPVL SGVLFAETIK 

       190        200        210        220        230        240 
GIQDAGVIAT AKHYLLNEQE HFRQVPEANG YGYNITETLS ENVDDKTLHE LYLWPFADAV 

       250        260        270        280        290        300 
RAGVGAIMCS YQHLNNTQAC QNSHLLNKLL KAELGFQGFV MSDWSATHSG VGSALAGMDM 

       310        320        330        340        350        360 
TMPGDIAFND GLSYYGPNLT ISVLNGTVPQ WRVDDMAVRV MAAFYKVGRD RLATPPNFSS 

       370        380        390        400        410        420 
WTRAEKGYEH ASIDGGAYGT VNEFVDVQQD HASLIRRVGA DSIVLLKNEG SLPLTGKERN 

       430        440        450        460        470        480 
VAILGEDAGS NPYGANGCDD RGCAQGTLAM GWGSGTANFP YLVTPEQAIQ QEVLKGRGNV 

       490        500        510        520        530        540 
FAVTDNWALD KVNKTASEST VSLVFVNAGA GEGFISVDGN EGDRKNLTLW KNGENLIKAA 

       550        560        570        580        590        600 
ASNCNNTIVV IHSVGAVLVD QFYEHPNVTA ILWAGLPGQE SGNSLVDVLY GRVNPNGKSP 

       610        620        630        640        650        660 
FTWGKTREAY GAPLLTEANN GNGAPQTDHT EGVFIDYRHF DRTNQTPIYE FGHGLSYTTF 

       670        680        690        700        710        720 
KYSNLTVQKL NAPAYSPASG QTKAAPTFGT IGEAEDYVFP DSITRVREFI YPWINSTDLK 

       730        740        750        760        770        780 
ESSGDPNYGW DDEDYIPEGA KDGSPQDVLP SGGGAGGNPR LYDDLFRITA IIKNTGPVAG 

       790        800        810        820        830        840 
TEVPQLYVSL GGPNEPKVVL RGFDKLVIQP GEERVFTTTL TRRDLSNWDM EKDDWVITSY 

       850        860 
PKKVFVGSSS RKLPLRASLP AVQ 

« 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
AACD01000067 Genomic DNA. Translation: EAA59363.1. Sequence problems.
BN001302 Genomic DNA. Translation: CBF74704.1. Sequence problems.
RefSeqXP_661706.1. XM_656614.1.

3D structure databases

ProteinModelPortalQ5B5S8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00004577.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00004577; CADANIAP00004577; CADANIAG00004577.
GeneID2873521.
KEGGani:AN4102.2.

Phylogenomic databases

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

Entry information

Entry nameBGLA_EMENI
AccessionPrimary (citable) accession number: Q5B5S8
Secondary accession number(s): C8V5A6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 51 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