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B8NBJ4 (EXGB_ASPFN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 glucan endo-1,6-beta-glucosidase B

EC=3.2.1.75
Alternative name(s):
Beta-1,6-glucanase B
Endo-1,6-beta-D-glucanase B
Endo-1,6-beta-glucanase B
Gene names
Name:exgB
ORF Names:AFLA_045690
OrganismAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167) [Complete proteome]
Taxonomic identifier332952 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. Acts on lutean, pustulan and 1,6-oligo-beta-D-glucosides By similarity.

Catalytic activity

Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-glucans.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cell wall biogenesis/degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpolysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucan endo-1,6-beta-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 – 392374Probable glucan endo-1,6-beta-glucosidase B
PRO_0000394706

Sites

Active site2201Proton donor By similarity
Active site3221Nucleophile By similarity

Amino acid modifications

Glycosylation311N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
B8NBJ4 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: BD96C170AF70A32C

FASTA39245,214
        10         20         30         40         50         60 
MKVTRLAVLN TLATLTVAWL PTTDKTITSS NGTDLFKASH GKIRGVNLGS QFVFEPWIAT 

        70         80         90        100        110        120 
KAWSELGCEG QESEFDCVMK LGQDAANKAF AKHWDSWITK EDIKEIRSYG LNTIRIPVGY 

       130        140        150        160        170        180 
WMNEDLIYHD SEYFPHGGFA YLEKLCGWAS DAGLYIIIDL HGAPGAQVAK NAFTGQFADT 

       190        200        210        220        230        240 
PGFYVDFQYQ RALEFLEWMT IKVHTLHNFR NVGMLEVVNE PVQNPQVTTT LRSNYYPNAF 

       250        260        270        280        290        300 
HSIRKVEGAL SIDRKDYLHI QMMDGAWGAG DPHEHLTDDY YAAYDNHRYL KWDPRVEVSK 

       310        320        330        340        350        360 
DSYIKTSCND NVATNWPAII GEWSLGVPDN VQETADWKPY SNLDFYQKWF AAQVQNYEQH 

       370        380        390 
QGWIFWTWKT QLDEYRWSYR GTYLSGFWQT SS 

« Hide

References

[1]"Genome sequence of Aspergillus flavus strain NRRL 3357."
Payne W.G.A., Dean R.A., Nierman W.C., Amedeo P., Caler E.G.A., Fedorova N.D., Maiti R., Joardar V., Inman J., Galinsky K.J., Yu J., Bhatnagar D., Cleveland T.E.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EQ963476 Genomic DNA. Translation: EED52867.1.
RefSeqXP_002378031.1. XM_002377990.1.

3D structure databases

ProteinModelPortalB8NBJ4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFLAT00005896; CADAFLAP00005896; CADAFLAG00005896.
GeneID7912453.
KEGGafv:AFLA_045690.

Phylogenomic databases

eggNOGCOG2730.
HOGENOMHOG000217590.
OMASEHFPQG.
OrthoDBEOG776T0C.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameEXGB_ASPFN
AccessionPrimary (citable) accession number: B8NBJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 31 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries