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Q5BB53 (BGLI_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 55. 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:AN2227
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 length839 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Beta-glucosidases are one of a number of cellulolytic enzymes, and catalyze 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.

Sequence caution

The sequence CBF86422.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAA63912.1 differs from that shown. Reason: Erroneous gene model prediction.

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 – 839839Probable beta-glucosidase I
PRO_0000394890

Regions

Domain399 – 522124PA14

Sites

Active site2251 By similarity

Amino acid modifications

Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation4941N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5BB53 [UniParc].

Last modified June 15, 2010. Version 2.
Checksum: 8790901E0381A819

FASTA83992,621
        10         20         30         40         50         60 
MPQLDVDKTI EELRLGEKID LVSGIDFWHT ASVPRLNIPS LRMSDGPNGV RGTRFFNGVP 

        70         80         90        100        110        120 
AACFPCATAL GATWDTELLH KVGHLMGEEA IAKGAHVILG PTINTQRSPL GGRGFESFAE 

       130        140        150        160        170        180 
DGVLAGHLAG YCSKGIQEKG VAACLKHFVC NDQEHERLAV DSIVTDRATR EIYLLPFQIA 

       190        200        210        220        230        240 
MRICKTATVM TAYNKINGTH VSENKKYITD ILRKEWGWDG LVMSDWFGTY SCTSESIIAG 

       250        260        270        280        290        300 
LDIEMPGKTR WRGDALAHAV SSNKVHEFVL DERVRNVLNL VNYVEPLGIP ENAEEKVLNR 

       310        320        330        340        350        360 
PEDQALLRRA AAESIVLLKN EDNILPFNKE KSIAVIGPNA KIAAYCGGGS ASLDAYYTIT 

       370        380        390        400        410        420 
PFEGVSAQSK GEVHFAQGSY SYKDLPLIGH LLKTDDGKTG FKFRVYDEPA SSSNRELLHE 

       430        440        450        460        470        480 
LHLVSSQGFL MDYRHPKIKS YLYYVDMEGY FTPEESGVYD FGVVVVGTGK LLVDDEVVVD 

       490        500        510        520        530        540 
NTKNQRLGSA FFGNGTVEEK GSKELMAGQK YKITFQFGTA PTSDIDTRGV VIFGPGGFRF 

       550        560        570        580        590        600 
GAARRQTQEE LISKAVEVAS KADQVVVFAG LTSEWETEGY DRPDMDLPPG SDELISKILE 

       610        620        630        640        650        660 
VKPNAAIVIQ SGTPVTMPWA PKAKALLQAW FGGNECGNGI ADVLYGNVNP SGKLPLTFPV 

       670        680        690        700        710        720 
RLQDNPSYLN FRSERGRVLY GEDIYVGYRY YEKAQLPPLF PFGHGLSYTT FTREKLELNT 

       730        740        750        760        770        780 
SPEKDKLQDG EPITARVTVT NTGKVAGAET VQLWVVPPPT EVNRPVRELK GFAKVHLEPG 

       790        800        810        820        830 
ESKDVEIVVE KKLATSWWDE KREAWASEKG VYWVQVTGTG EGVLTAEFEV KKTRFWTGL 

« Hide

References

« Hide 'large scale' references
[1]"Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"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.
[3]"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
DQ490477 mRNA. Translation: ABF50853.1.
AACD01000036 Genomic DNA. Translation: EAA63912.1. Sequence problems.
BN001307 Genomic DNA. Translation: CBF86422.1. Sequence problems.
RefSeqXP_659831.1. XM_654739.1.

3D structure databases

ProteinModelPortalQ5BB53.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00008912.

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00008912; CADANIAP00008912; CADANIAG00008912.
GeneID2875705.
KEGGani:AN2227.2.

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000031215.
KOK05349.
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_EMENI
AccessionPrimary (citable) accession number: Q5BB53
Secondary accession number(s): C8VML9, Q1HFU7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: March 19, 2014
This is version 55 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