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Q5BCC6 (BGLC_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-glucosidase C
EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase C
Cellobiase C
Gentiobiase C
Gene names
Name:bglC
ORF Names:AN1804
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella ›

Protein attributes

Sequence length618 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. Ref.3

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 Probable.

Sequence similarities

Belongs to the glycosyl hydrolase 3 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.0. Ref.3

Temperature dependence:

Optimum temperature is 52 degrees Celsius.

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

glucan catabolic process

Inferred from direct assay Ref.3. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-glucosidase activity

Inferred from direct assay Ref.3. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 618599Beta-glucosidase C
PRO_0000394105

Sites

Active site3301 By similarity

Amino acid modifications

Glycosylation401N-linked (GlcNAc...) Potential
Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation2111N-linked (GlcNAc...) Potential
Glycosylation2631N-linked (GlcNAc...) Potential
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation4481N-linked (GlcNAc...) Potential
Glycosylation4771N-linked (GlcNAc...) Potential
Glycosylation4821N-linked (GlcNAc...) Potential
Glycosylation5021N-linked (GlcNAc...) Potential
Glycosylation5171N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5BCC6 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 478BEDD19CF97756

FASTA61868,420
        10         20         30         40         50         60 
MRVDSTVLAL VALATDCLGL AIKSNEPELL RRDALPIYKN ASYCVDERVR DLLSRMTLEE 

        70         80         90        100        110        120 
KAGQLFHKQL SEGPLDDDSS GNSTETMIGK KHMTHFNLAS DITNATQTAE FINLIQKRAL 

       130        140        150        160        170        180 
QTRLGIPITI STDPRHSFTE NVGTGFQAGV FSQWPESLGL AALRDPQLVR EFAEVAREEY 

       190        200        210        220        230        240 
LAVGIRAALH PQVDLSTEPR WARISGTWGE NSTLTSELIV EYIKGFQGEG KLGPKSVKTV 

       250        260        270        280        290        300 
TKHFPGGGPM ENGEDSHFYY GKNQTYPGNN IDEHLIPFKA ALAAGATEIM PYYSRPIGTN 

       310        320        330        340        350        360 
WEAVGFSFNK EIVTDLLRGE LGFDGIVLTD WGLITDTYIG NQYMPARAWG VEYLSELQRA 

       370        380        390        400        410        420 
ARILDAGCDQ FGGEERPELI VQLVREGTIS EDRIDVSVAR LLKEKFLLGL FDNPFVNASA 

       430        440        450        460        470        480 
ANNIVGNEHF VNLGRDAQRR SYTLLTNNQT ILPLAKPGEG TRFYIEGFDS AFMSARNYTV 

       490        500        510        520        530        540 
VNTTEEADFA LLRYNAPYEP RNGTFEANFH AGSLAFNATE KARQAKIYSS LPTIVDIILD 

       550        560        570        580        590        600 
RPAVIPEVVE QAQAVLASYG SDSEAFLDVV FGVSKPEGKL PFDLPRSMDA VEAQAEDLPF 

       610 
DTENPVFRYG HGLEYEDN

« 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.
[3]"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: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACD01000029 Genomic DNA. Translation: EAA64969.1.
BN001307 Genomic DNA. Translation: CBF85593.1.
RefSeqXP_659408.1. XM_654316.1.

3D structure databases

ProteinModelPortalQ5BCC6.
ModBaseSearch...

Protein family/group databases

mycoCLAPBGL3C_EMENI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00008452; CADANIAP00008452; CADANIAG00008452.
GeneID2874927.
KEGGani:AN1804.2.

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000285275.
OMAMPTYSIL.
OrthoDBEOG4RZ27G.

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProIPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR30620. PTHR30620. 1 hit.
PfamPF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSPR00133. GLHYDRLASE3.
SUPFAMSSF52279. Glyco_hydro_3_C. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00775. GLYCOSYL_HYDROL_F3. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGLC_EMENI
AccessionPrimary (citable) accession number: Q5BCC6
Secondary accession number(s): C8VPG3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: April 26, 2005
Last modified: March 6, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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