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Q4X1N4 (EXGB_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:AFUA_2G09350
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length396 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
Reference 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 – 1717 Potential
Chain18 – 396379Probable glucan endo-1,6-beta-glucosidase B
PRO_0000394707

Sites

Active site2191Proton donor By similarity
Active site3201Nucleophile By similarity

Amino acid modifications

Glycosylation301N-linked (GlcNAc...) Potential
Glycosylation2721N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4X1N4 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: D53B00929BC0E598

FASTA39644,795
        10         20         30         40         50         60 
MIRRLAAFSA LSGLATAWLP EVNKKITSTN GTNLFTSSNG KIRGVNLGSQ FVFEPWIAEK 

        70         80         90        100        110        120 
AWSDMGCGGQ KSEFDCVSRL GQANANSAFA SHWGSWITQD DIAEMVSYGL NTIRVPVGYW 

       130        140        150        160        170        180 
MREDLVYSDS EHFPQGGLQY LENLCEWASD AGLYIIIDLH GAPGAQTPQN PFTGQYAPIA 

       190        200        210        220        230        240 
GFYQDYQFEG ALKFLEWMTT NIHQNDKFRN VGMLEVVNEP VQDAGKVGSM RSSYYPNAFK 

       250        260        270        280        290        300 
RIRAAEQSLN IDRNNYLHIQ MMDRLWGSGD PNESLTDTYY AAYDDHRYLK WASVAVSKDS 

       310        320        330        340        350        360 
YISTSCSDQL NSNTPTIVGE WSLSVPDNVQ WNSDWSPDSN KDFYKKWFAA QVTAYERQQG 

       370        380        390 
WIFWTWKAQL GDYRWSYQGG LLLTRPGIGD QQVLTL 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000001 Genomic DNA. Translation: EAL93231.1.
RefSeqXP_755269.1. XM_750176.1.

3D structure databases

ProteinModelPortalQ4X1N4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00004063; CADAFUAP00004063; CADAFUAG00004063.
GeneID3513261.
KEGGafm:AFUA_2G09350.

Phylogenomic databases

eggNOGCOG2730.
HOGENOMHOG000217590.
KOK01238.
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_ASPFU
AccessionPrimary (citable) accession number: Q4X1N4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: February 19, 2014
This is version 54 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