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Q5BD29 (BTGE_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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 btgE

EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase btgE
Cellobiase btgE
Gentiobiase btgE
Gene names
Name:btgE
ORF Names:AN1551
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 length555 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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

Secretedcell wall. Note: Covalently-linked to the cell wall. Ref.4

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentCell wall
Secreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 1818 Potential
Chain19 – 555537Probable beta-glucosidase btgE
PRO_0000395136

Regions

Compositional bias49 – 288240Thr-rich

Sites

Active site4881Nucleophile By similarity
Active site5461Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5BD29 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: B8F0DF0153079DCA

FASTA55557,672
        10         20         30         40         50         60 
MRGAILATAA AFAGTAVADM HMRRHAHEGL HHRALHASSA VPEEECGCTT EVITYWGEPT 

        70         80         90        100        110        120 
TIPLSVPTST VTSETTETVH STSYSTVTVT ATSSAAPVET PSETPSPTPE VTLPTAGVTS 

       130        140        150        160        170        180 
YSETGTYTIP ATTITVTDTT TVCGATTTEL PSGTHTYGGV TTIVETATTI TCPYATVKPT 

       190        200        210        220        230        240 
GSTVTSVIET TTYVCPSAGT YTIAPTTTFV PTSTVVVYPT PETVTPGTYT NPGTTITVTR 

       250        260        270        280        290        300 
TEDVYVCPYT NGNVPTSVPA LPTTSAASTT TAVPSSSTTT SSATSVPTGA SGNKMGMTFT 

       310        320        330        340        350        360 
PYNNDGSCMA KNDVLEQVGL IKGKGFSHVR VYGTDCHTLE YVGAACSTHG LKMILGVNVE 

       370        380        390        400        410        420 
GSTGFDGARS QFKDITNWGQ WDLVSLIVVG NEVVTSNIAS AAQLASFVSE GASAFSAAGY 

       430        440        450        460        470        480 
TGQVTTAEPI DVWLSNGATL CPVVDILGAN LHPFFNPEFT AAEAGTLVSN QIKDLKQVCT 

       490        500        510        520        530        540 
GKDVINLETG WPNAGSANGK AIPGQSQQTT AIKSLVEKVG DVSVFFSYAD DGWKSKFATS 

       550 
DKYNVEQHWG CIDQF 

« 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.
[4]"Comprehensive genomic analysis of cell wall genes in Aspergillus nidulans."
de Groot P.W., Brandt B.W., Horiuchi H., Ram A.F., de Koster C.G., Klis F.M.
Fungal Genet. Biol. 46:S72-S81(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ490473 mRNA. Translation: ABF50849.1.
AACD01000025 Genomic DNA. Translation: EAA64258.1.
BN001307 Genomic DNA. Translation: CBF85093.1.
RefSeqXP_659155.1. XM_654063.1.

3D structure databases

ProteinModelPortalQ5BD29.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00008179; CADANIAP00008179; CADANIAG00008179.
GeneID2874885.
KEGGani:AN1551.2.

Phylogenomic databases

eggNOGCOG5309.
HOGENOMHOG000158427.
OMAYSTDCDT.
OrthoDBEOG73FQWG.

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBTGE_EMENI
AccessionPrimary (citable) accession number: Q5BD29
Secondary accession number(s): C8VMY9, Q1HFV1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: February 19, 2014
This is version 57 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