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Q5AUW5 (BGLD_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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 D

EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase D
Cellobiase D
Gentiobiase D
Gene names
Name:bglD
ORF Names:AN7915
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 length812 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 EAA59569.1 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

secondary metabolic process

Inferred from expression pattern PubMed 19448638. Source: ASPGD

   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 – 1818 Potential
Chain19 – 812794Probable beta-glucosidase D
PRO_0000394108

Regions

Compositional bias191 – 24656Gly-rich
Compositional bias212 – 26251Ser-rich

Sites

Active site3241 By similarity

Amino acid modifications

Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Potential
Glycosylation3601N-linked (GlcNAc...) Potential
Glycosylation3841N-linked (GlcNAc...) Potential
Glycosylation4221N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential
Glycosylation5921N-linked (GlcNAc...) Potential
Glycosylation6461N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5AUW5 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: A70CFB5FF35CBD1B

FASTA81286,383
        10         20         30         40         50         60 
MRVPSLSVLS FLLGTALAAA SNFEAGLLSS GKVSLGDWKS AHEKASQFVA KLNTTEKIKL 

        70         80         90        100        110        120 
ITGSSVTTTN GETFTALDIL DGDMGAQAYY YVSAFSLSSA LAMTWDKEAM YEQGRAIAAE 

       130        140        150        160        170        180 
FYGKGIQMVA GPTSQPLGRT PWGGRLVESF GPDPYLNGIA TGLETRAYAD VGVIAGAKHF 

       190        200        210        220        230        240 
ILNEQETNRT GGMGGGGGAP GGGGMGRGAE FSSSVPGGMS PTSSAGAIPS STSTPGGSGM 

       250        260        270        280        290        300 
GGGMAGSSAF SSSSSSGAPY SSNADDKTLH ETYLWSFYDA VHSGLGGVMC AMTKVNGTLS 

       310        320        330        340        350        360 
CQSSSLLLDI LKTELGFPGM VWPDTNGQQD ALASAANGLD YGSSSLWSES TIEGYLESNN 

       370        380        390        400        410        420 
ITEARLNDMA IRNLMGYYYV NLDNGTQPST AAQDDYVDVR ANHAKLIRSH GSKSMVLLKN 

       430        440        450        460        470        480 
KNNTLPLYKP HKMAIFGSHA RAAVAGPNMQ FSVEGSGPTY DGHIATDSGS GQASLPYLIT 

       490        500        510        520        530        540 
PENALNIKAS QDGTMLRWIA NDTYSSSTGS ALVMQGSSST SVTPSVSAYS ENMDVCLVFI 

       550        560        570        580        590        600 
NALAGEGADR TELRNTDQDN LINEVADNCD NTVVVINTVG ARILDSWIEH ENVTAVLYGS 

       610        620        630        640        650        660 
LLGQESGNSI VDVLYGDVNP SGRLTYTIAK TESDYNVDIC YTAQCNFTEG NYIDYRYFDA 

       670        680        690        700        710        720 
YNVTPRYEFG YGLSYTDFAY SNLHIQGPSA LSTYPTGQLA VGGYEDLWDT VAKVTVTIRN 

       730        740        750        760        770        780 
AGSLDGAEVP QLYISYPDVA KQPVRQLRGF HNVYIKKGQS TKVTFELRRR DISYWDVQHQ 

       790        800        810 
KWAVAPGTYE AWVGASSRDL RTHGSFVVKT KA 

« 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
AACD01000135 Genomic DNA. Translation: EAA59569.1. Sequence problems.
BN001302 Genomic DNA. Translation: CBF73514.1.
RefSeqXP_681184.1. XM_676092.1.

3D structure databases

ProteinModelPortalQ5AUW5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00003933; CADANIAP00003933; CADANIAG00003933.
GeneID2869248.
KEGGani:AN7915.2.

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000031215.
OMATYQGHLA.
OrthoDBEOG7XH6ZD.

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D3.20.20.300. 2 hits.
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. 2 hits.
SSF52279. SSF52279. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBGLD_EMENI
AccessionPrimary (citable) accession number: Q5AUW5
Secondary accession number(s): C8V4V5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 54 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