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B8NXJ2 (XYNF3_ASPFN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 32. 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 endo-1,4-beta-xylanase F3

Short name=Xylanase F3
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase F3
Gene names
Name:xynF3
Synonyms:xlnF3
ORF Names:AFLA_008110
OrganismAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167) [Complete proteome]
Taxonomic identifier332952 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose By similarity.

Catalytic activity

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted By similarity.

Induction

Expressed in presence of xylan and repressed by glucose.

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 324305Probable endo-1,4-beta-xylanase F3
PRO_0000393187

Sites

Active site1551Proton donor By similarity
Active site2601Nucleophile By similarity

Amino acid modifications

Disulfide bond278 ↔ 284 By similarity

Sequences

Sequence LengthMass (Da)Tools
B8NXJ2 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: AD8AEFAF8EDB4496

FASTA32435,239
        10         20         30         40         50         60 
MVHLKALASG TLFASLASSA VISRQAAASI NDAFVAHGKK YFGTCSDQAL LQNSQNEAIV 

        70         80         90        100        110        120 
RADFGQLTPE NSMKWDALEP SQGSFSFAGA DFLADYAKTN NKLVRGHTLV WHSQLPSWVQ 

       130        140        150        160        170        180 
GITDKDTLTE VIKNHITTIM QRYKGQIYAW DVVNEIFDED GTLRDSVFSQ VLGEDFVRIA 

       190        200        210        220        230        240 
FETAREADPN AKLYINDYNL DSADYAKTKG MVSYVKKWLD AGVPIDGIVS LLPPRDEGLT 

       250        260        270        280        290        300 
SCTALTALAS TGVSEVAVTE LDIEGASSES YLEVVNACLD VSSCVGITVW GVSDKDSWRS 

       310        320 
STSPLLFDSN YQAKDAYNAI IDAL 

« 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
EQ963486 Genomic DNA. Translation: EED44928.1.
RefSeqXP_002385057.1. XM_002385016.1.

3D structure databases

ProteinModelPortalB8NXJ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5059.CADAFLAP00012922.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFLAT00012922; CADAFLAP00012922; CADAFLAG00012922.
GeneID7920217.
KEGGafv:AFLA_008110.

Phylogenomic databases

eggNOGCOG3693.
HOGENOMHOG000019847.
KOK01181.
OMAWRSSESP.
OrthoDBEOG7GJ6PM.

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameXYNF3_ASPFN
AccessionPrimary (citable) accession number: B8NXJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 32 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