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Q5B0F4 (BGLG_EMENI) 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 G

EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase G
Cellobiase G
Gentiobiase G
Gene names
Name:bglG
ORF Names:AN5976
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 length819 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 CBF70434.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence EAA57725.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 – 819799Probable beta-glucosidase G
PRO_0000394119

Sites

Active site3051 By similarity

Amino acid modifications

Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation591N-linked (GlcNAc...) Potential
Glycosylation1071N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) Potential
Glycosylation2771N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation3441N-linked (GlcNAc...) Potential
Glycosylation3511N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential
Glycosylation5001N-linked (GlcNAc...) Potential
Glycosylation5091N-linked (GlcNAc...) Potential
Glycosylation5541N-linked (GlcNAc...) Potential
Glycosylation5671N-linked (GlcNAc...) Potential
Glycosylation5881N-linked (GlcNAc...) Potential
Glycosylation6271N-linked (GlcNAc...) Potential
Glycosylation6831N-linked (GlcNAc...) Potential
Glycosylation7191N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5B0F4 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 932C81818E1B7F6B

FASTA81988,639
        10         20         30         40         50         60 
MTSASQILVW GLLAASGAQA QNYGGGSSRS DDAFSYVQPK NTTILGAYGH SPAVYPSPNT 

        70         80         90        100        110        120 
TGSGGWETAL AQAQDFVAQL TLEEKANMVT GQPGPCVGNI IAIPRLNFSG LCLQDGPLAI 

       130        140        150        160        170        180 
RVTDMASVFS AGVTAAASWD RKILYERGYA MGQEFKAKGA HVALGPVAGP LGRSAYSGRN 

       190        200        210        220        230        240 
WEGFAADPYL TGVAMEETIQ GYQDAGVQAC PKHFIGNEQE TMRNPTFNDS APLGTVIQEA 

       250        260        270        280        290        300 
VSSNIDDRTM HELYLWPFAN AVHAKAASIM CSYQRINGSY GCENSKTLNG LLKGELGFQG 

       310        320        330        340        350        360 
YVMSDWGATH SGVAGIKSGQ DMDMPGGLGA YGQTFINRSF FGGNVTAAVN NGTLEESRID 

       370        380        390        400        410        420 
DMILRIMTPY FWLGQDQDYP TVDPSTADYN TFSPRNTWYQ DFNLTGERSR DVRGNHAALI 

       430        440        450        460        470        480 
RKQAAEATVL LKNKNNALPL KAPKTLAVFG NDASDITNGP YNDATYEYGT LAAGGGSGTG 

       490        500        510        520        530        540 
RFTYLVSPLT AINARAQKDN TSLVQFWLNN TQIATSDVQA DLLRVPTPPT ACLVFVKTWA 

       550        560        570        580        590        600 
EEGADREHLR LDYNGTEVVE AVAAACNNTI VVTHSSGINE LPFANHPNVT AILAAHFPGQ 

       610        620        630        640        650        660 
ESGNSIVDVL YGDVNPSGRL PYTIARNGSD YNAPPTTAVT TSGREDWQSW FDEKLEIDYR 

       670        680        690        700        710        720 
YFDAHNIPVL YEFGFGLSYT TFNISDIYAT RVVDSITSAP EDRAIQPGGN PELWETIYNV 

       730        740        750        760        770        780 
TVSVTNTGDV EGATVPQLYV TFPDSTPEGT PPKQLRGFDK VSLQPGESTK VIFELMRRDL 

       790        800        810 
SYWDTVSQQW LIPEGDFTIR VGFSSRNLKE VTTITPVSE 

« 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
AACD01000102 Genomic DNA. Translation: EAA57725.1. Different initiation.
BN001301 Genomic DNA. Translation: CBF70434.1. Different initiation.
RefSeqXP_663580.1. XM_658488.1.

3D structure databases

ProteinModelPortalQ5B0F4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00007042; CADANIAP00007042; CADANIAG00007042.
GeneID2870885.
KEGGani:AN5976.2.

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000031215.
KOK05349.
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 nameBGLG_EMENI
AccessionPrimary (citable) accession number: Q5B0F4
Secondary accession number(s): C8V3B8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: May 18, 2010
Last modified: February 19, 2014
This is version 52 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