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Q4WR62 (BGLM_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:AFUA_1G17410
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length769 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-galactosidase activity

Inferred from direct assay PubMed 18020405. Source: ASPGD

beta-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 – 2222 Potential
Chain23 – 769747Probable beta-glucosidase M
PRO_0000394906

Sites

Active site2901 By similarity

Amino acid modifications

Glycosylation281N-linked (GlcNAc...) Potential
Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation2621N-linked (GlcNAc...) Potential
Glycosylation3181N-linked (GlcNAc...) Potential
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation3961N-linked (GlcNAc...) Potential
Glycosylation4371N-linked (GlcNAc...) Potential
Glycosylation5101N-linked (GlcNAc...) Potential
Glycosylation5461N-linked (GlcNAc...) Potential
Glycosylation6251N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4WR62 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 79C92A56D4325D19

FASTA76982,681
        10         20         30         40         50         60 
MHSNVGLAGL AGLLATASVC LSAPADQNIT SDTYFYGQSP PVYPSPEGTG TGSWAAAYAK 

        70         80         90        100        110        120 
AKKFVAQLTP EEKVNLTAGT DANNGCSGNI AAIPRLNFPG LCVSDAGNGL RGTDYVSSWP 

       130        140        150        160        170        180 
SGLHVGASWN KALARQRAVQ MATEFRKKGV NVLLGPVVGP LGRVAEAGRN WEGFSNDPYL 

       190        200        210        220        230        240 
SGALVYETVD GAQSVGVATC TKHYILNEQE TNRNPGMEDG VEVAAVSSNI DDKTMHELYL 

       250        260        270        280        290        300 
WPFQDAVLAG SASIMCSYNR VNNSYGCQNS KTLNGLLKTE LGFQGYVMTD WGAQHAGIAG 

       310        320        330        340        350        360 
ANAGLDMVMP STETWGANLT TAISNGTMDA SRLDDMATRI IASWYQMNQD SDFPSPGAGM 

       370        380        390        400        410        420 
PSDMYAPHQR VIGRDASSKQ TLLRGAIEGH VLVKNNHSAL PLKSPQLLSV FGYDAKGPNA 

       430        440        450        460        470        480 
LKQNFNWLSY SPAIQENHTL WVGGGSGANN AAYIDAPIDA IQRQAYEDGT SVLYDISSED 

       490        500        510        520        530        540 
PEVDPTTDAC LVFINSYATE GWDRPGLADN SSDTLVKNVA RKCANTIVTI HNAGIRVVGE 

       550        560        570        580        590        600 
WIDHENVTAV IFAHLPGQDS GRALVELLYG RANPSGKLPY TVAKKVEDYG SLLHPSLPET 

       610        620        630        640        650        660 
PYGLFPQSDF DEGVYIDYRA FDRANITAQF EFGFGLSYTS FDYSGLQISN PKQSPQYPPS 

       670        680        690        700        710        720 
AAIQQGGNPH LWDNIVTVSA EIKNTGRVAG AEVAQLYIGI PNGPVRQLRG FEKVDVSAGE 

       730        740        750        760 
TTQVQFALNR RDLSTWDVEA QQWSLQRGTY RVYVGRSSRD LPLTGSFTL 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000004 Genomic DNA. Translation: EAL91070.1.
RefSeqXP_753108.1. XM_748015.1.

3D structure databases

ProteinModelPortalQ4WR62.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00007078.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00007078; CADAFUAP00007078; CADAFUAG00007078.
GeneID3510140.
KEGGafm:AFUA_1G17410.

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_ASPFU
AccessionPrimary (citable) accession number: Q4WR62
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: February 19, 2014
This is version 52 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