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Q5AWD4 (BGLM_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 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 M

EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase M
Cellobiase M
Gentiobiase M
Gene names
Name:bglM
ORF Names:AN7396
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 length772 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 – 2020 Potential
Chain21 – 772752Probable beta-glucosidase M
PRO_0000394909

Sites

Active site2871 By similarity

Amino acid modifications

Glycosylation2591N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation3221N-linked (GlcNAc...) Potential
Glycosylation4381N-linked (GlcNAc...) Potential
Glycosylation5231N-linked (GlcNAc...) Potential
Glycosylation5471N-linked (GlcNAc...) Potential
Glycosylation5741N-linked (GlcNAc...) Potential
Glycosylation5861N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5AWD4 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 5EDBC03088B10ED2

FASTA77283,526
        10         20         30         40         50         60 
MLTSWGKTGF VLALALGGRA AENVITSDTF FYGESPPVYP SPEGTGAGDW ASAYTKARAF 

        70         80         90        100        110        120 
VAQLSDDEKI QLTAGVSSNT ACSGFIQPID RLGFPGICMS DAGNGLRGTD YVNGWSSGIS 

       130        140        150        160        170        180 
VGASWNRDLA HSRGAYMGQE YRKKGVNMIL GPVVGPLGRV ALGGRNWEGY AADPYLSGVL 

       190        200        210        220        230        240 
VSESVKGLQS QKVATSVKHF IANEQETNRN PTTDSERNVV QSVSSNIDDK TMHELYLWPF 

       250        260        270        280        290        300 
QDAVLAGATN LMCSYNRVNN SYACQNSKLL NGVLKTELGF QGYVVTDWGA QHAGIASANA 

       310        320        330        340        350        360 
GLDVVMPRSS TWNSNLTTAI ANGTMEASRL DDMITRLMAT WYYLDQDTEF PSPGVGMPSS 

       370        380        390        400        410        420 
PSAAHQAVIA TSPEAKPILL QSAIESHVLV KNTDGALPLK SPKLISVFGY DAYAPLTYDL 

       430        440        450        460        470        480 
GNNFDFSSTR VRSDLYKNGT LYVGGGSGLN SPAYIDAPID AIKRRAYEDG SSVLWDFTSE 

       490        500        510        520        530        540 
NPSVDYTSDV CLVFINAYAT EGYDRQALSD THSDSVVENI AGNCSNTIVV VHNAGIRTAE 

       550        560        570        580        590        600 
AWVDHANVTA IIYAHLPGQD IGRALVRLLY GESNFSGRLP YTVAKNSSDY GSLLEPSQPE 

       610        620        630        640        650        660 
GKYQYFPQSD FSEGVYIDYR AFDKDGIVPQ YAFGYGLSYT TFEYSDLKIS KNSDGVPSIY 

       670        680        690        700        710        720 
PAKASILPGG NPHLFDELVT VTAKIRNTGN VDGQEVAQLY VGIPDGPVRQ LRGFDKVLIE 

       730        740        750        760        770 
SGSSATVTFS LTRRDLSTWD ANAQEWSLQR GTYKIFVGRD SRDLPLEETL VF 

« 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
AACD01000128 Genomic DNA. Translation: EAA61767.1.
BN001304 Genomic DNA. Translation: CBF78465.1.
RefSeqXP_680665.1. XM_675573.1.

3D structure databases

ProteinModelPortalQ5AWD4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00000031.

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00000031; CADANIAP00000031; CADANIAG00000031.
GeneID2869858.
KEGGani:AN7396.2.

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000031215.
KOK05349.
OMARANPSGK.
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. 2 hits.
ProtoNetSearch...

Entry information

Entry nameBGLM_EMENI
AccessionPrimary (citable) accession number: Q5AWD4
Secondary accession number(s): C8VCE8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: March 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