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Q5B6Q3 (EXGB_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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:
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:AN3777
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 length409 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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. Ref.1

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
Reference proteome
Gene Ontology (GO)
   Biological_processglucan catabolic process

Inferred from direct assay Ref.1. Source: ASPGD

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucan endo-1,6-beta-glucosidase activity

Inferred from direct assay Ref.1. Source: ASPGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 409393Glucan endo-1,6-beta-glucosidase B
PRO_0000394710

Sites

Active site2281Proton donor By similarity
Active site3301Nucleophile By similarity

Amino acid modifications

Glycosylation351N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5B6Q3 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 83704098EDC15087

FASTA40946,267
        10         20         30         40         50         60 
MKFILPLFTS LPVALAWLPG IDKDIYSAAG TNIFNVTSAS SKRWLPASKK IRGVNLGSHF 

        70         80         90        100        110        120 
VIEPWMASMA WSNMGCSGQR SEFDCVMALG QETADQAFAD HWGSWITQDD INQMVQYGLN 

       130        140        150        160        170        180 
TIRIPVGYWL KEDLVYADSE HFPKGGIGYL EDVCGWASDA GMYIIIDLHG APGAQQPKQP 

       190        200        210        220        230        240 
FTGQYAPNPG FYQDYQYDRA LEFLEWMTTS IHQNNKFRNV GMLEIVNEPV QNADQASSMI 

       250        260        270        280        290        300 
NSYYPSAFTR IRNTESSLGI TSNNYLHIQM MNEKWGSGDP TQSLTDNYFA AYDDHRYVKW 

       310        320        330        340        350        360 
DSSVAVDKES YISASCVDDR GGNWPTIVGE WSLSVPDNVE HTADWEPSSN TDFYARWFAA 

       370        380        390        400 
QAIAYEKQEG WVFWSWKAQL GDYRWSYKDA VDAGVIPKDL DSIYDYSPC 

« 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], FUNCTION.
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
DQ490491 mRNA. Translation: ABF50867.1.
AACD01000061 Genomic DNA. Translation: EAA59985.1.
BN001302 Genomic DNA. Translation: CBF75405.1.
RefSeqXP_661381.1. XM_656289.1.

3D structure databases

ProteinModelPortalQ5B6Q3.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00004938; CADANIAP00004938; CADANIAG00004938.
GeneID2873201.
KEGGani:AN3777.2.

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_EMENI
AccessionPrimary (citable) accession number: Q5B6Q3
Secondary accession number(s): C8V716, Q1HFT3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: February 19, 2014
This is version 62 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