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Q4WU49 (BGLI_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 56. 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 I

EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase I
Cellobiase I
Gentiobiase I
Gene names
Name:bglI
ORF Names:AFUA_5G07190
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length838 AA.
Sequence statusComplete.
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.

Contains 1 PA14 domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   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

Chain1 – 838838Probable beta-glucosidase I
PRO_0000394886

Regions

Domain396 – 542147PA14

Sites

Active site2251 By similarity

Amino acid modifications

Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation4931N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4WU49 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 778CBDF5A0B2C14B

FASTA83892,208
        10         20         30         40         50         60 
MVQLDVEKTI EELTLGEKVA LTAGIDFWHT AAVPRLNIPS LRMSDGPNGV RGTRFFNGVP 

        70         80         90        100        110        120 
AACFPCATAL GATWDTKLLY EVGRLMGEES IAKGAHVVLG PTINTQRSPL GGRGFESFAE 

       130        140        150        160        170        180 
DGVLSGILAG HYCKGLQETG VAATLKHFVC NDQEHERLAV DSIVTMRAMR EIYLLPFQLA 

       190        200        210        220        230        240 
MRICKTACVM TAYNKVNGTH VSENKQIITD ILRKEWGWDG LVMSDWFGTY STCDAINAGL 

       250        260        270        280        290        300 
DLEMPGPTRW RGTALAHAVS SNKAFEFVMD ERVRNILNLH NFVEPLGIPE NAPEKALNRP 

       310        320        330        340        350        360 
EDQALLRRAA AESVVLIKNQ DNILPLKKEK PILVIGPNAK TAAYCGGGSA SLDAYYTVTP 

       370        380        390        400        410        420 
FEGVAAQSQG EVTFSQGVYS YKELPLLGPL LKTDDGKKGF KFRVYNEPPS EPNRQLIDEL 

       430        440        450        460        470        480 
HLESSSGFLM DYKHPKIKTF TFYVDMEGYF TPEEDGIYDF GVTVVGTGKL FVDDELVVDN 

       490        500        510        520        530        540 
SKNQRQGTAM FGNATVEEKG SKELKAGQTY KVVLQFGTAP TSDLDMRGVV IFGPGGFRFG 

       550        560        570        580        590        600 
AARRVSQEEL ISKAAELASQ TSQVVIFAGL TSEWETEGYD RDHMDLPPGS DEMISRVLDA 

       610        620        630        640        650        660 
NPDTVVVIQS GTPVTMPWAH KAKALLQAWF GGNECGNGIA DVLYGNVNPA AKLPLSFPVR 

       670        680        690        700        710        720 
LQDNPSYLNF RSERGRVLYG EDIYVGYRYY EKVDLAPLFP FGHGLSYTTF SRSDLSLATT 

       730        740        750        760        770        780 
PEKPQLEDGE PITVTVSVTN TGSVAGAEIV QLWVAPPPTG VNRPVRELKG FTKVFLQPGE 

       790        800        810        820        830 
TKKVEIVVEK KLATSWWDEQ REKWASEKGT YEVLVTGTGD EVLKSSFEVE KTRYWLGL 

« 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
AAHF01000003 Genomic DNA. Translation: EAL91877.1.
RefSeqXP_753915.1. XM_748822.1.

3D structure databases

ProteinModelPortalQ4WU49.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00006281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00006281; CADAFUAP00006281; CADAFUAG00006281.
GeneID3511295.
KEGGafm:AFUA_5G07190.

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000031215.
KOK05349.
OMAVNIHRSG.
OrthoDBEOG7H799Q.

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D3.20.20.300. 1 hit.
3.40.50.1700. 2 hits.
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.
IPR011658. PA14.
[Graphical view]
PANTHERPTHR30620. PTHR30620. 1 hit.
PfamPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
PF07691. PA14. 1 hit.
[Graphical view]
PRINTSPR00133. GLHYDRLASE3.
SMARTSM00758. PA14. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 2 hits.
PROSITEPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGLI_ASPFU
AccessionPrimary (citable) accession number: Q4WU49
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: November 13, 2013
This is version 56 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