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B8NKE9 (XYNA_ASPFN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 29. 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 A

Short name=Xylanase A
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Gene names
Name:xlnA
ORF Names:AFLA_090240
OrganismAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167) [Complete proteome]
Taxonomic identifier332952 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Sequence similarities

Belongs to the glycosyl hydrolase 11 (cellulase G) family.

Sequence caution

The sequence EED48943.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 232213Probable endo-1,4-beta-xylanase A
PRO_0000393160

Sites

Active site1281Nucleophile By similarity
Active site2191Proton donor By similarity

Amino acid modifications

Glycosylation341N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
B8NKE9 [UniParc].

Last modified March 23, 2010. Version 2.
Checksum: 1F73104751EA561C

FASTA23224,605
        10         20         30         40         50         60 
MVSFSSILLA CSAAIGALAT PIEPLADHPN EAFNETAFND LVGRSTPSST GYNNGYYYSF 

        70         80         90        100        110        120 
WTDGGGDVTY TNGNGGSYSV QWSNVGNFVG GKGWNPGSSR AITYSGSFNP SGNGYLAVYG 

       130        140        150        160        170        180 
WTTDPLIEYY IVESYGTYNP GSGGTYKGQV TSDGGTYNIY TSVRTNAPSI IGTATFTQFW 

       190        200        210        220        230 
SVRTSKRVGG TVTTGNHFNA WAKYGLTLGT HNYQIVATEG YQSSGSSAIT VY 

« 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
EQ963480 Genomic DNA. Translation: EED48943.1. Different initiation.
RefSeqXP_002380844.1. XM_002380803.1.

3D structure databases

ProteinModelPortalB8NKE9.
SMRB8NKE9. Positions 46-231.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5059.CADAFLAP00008709.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7917023.
KEGGafv:AFLA_090240.

Phylogenomic databases

eggNOGNOG05353.
HOGENOMHOG000179135.
KOK01181.
OrthoDBEOG7VQJQX.

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.180. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNA_ASPFN
AccessionPrimary (citable) accession number: B8NKE9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 23, 2010
Last modified: March 19, 2014
This is version 29 of the entry and version 2 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