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Q4WG11 (XYNA_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 64. 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:
Endo-1,4-beta-xylanase xynf11a

Short name=Xylanase xynf11a
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase xynf11a
Gene names
Name:xlnA
Synonyms:xynf11a
ORF Names:AFUA_3G00320
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.2

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.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.0. Stable in the pH range from 4.0 to 8.0. Ref.2

Temperature dependence:

Optimum temperature is 60 degrees Celsius. Around 53 percent activity is retained at 70 degrees Celsius. Stable from 30 to 60 degrees Celsius with maximum stability at 30 degrees Celsius.

Ontologies

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

Inferred from direct assay Ref.2. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 228210Endo-1,4-beta-xylanase xynf11a
PRO_0000393161

Sites

Active site1241Nucleophile By similarity
Active site2151Proton donor By similarity

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4WG11 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 7DBED47138DA238F

FASTA22824,494
        10         20         30         40         50         60 
MVSFSYLLLA CSAIGALAAP VEPETTSFNE TALHEFAERA GTPSSTGWNN GYYYSFWTDG 

        70         80         90        100        110        120 
GGDVTYTNGA GGSYSVNWRN VGNFVGGKGW NPGSARTINY GGSFNPSGNG YLAVYGWTTN 

       130        140        150        160        170        180 
PLIEYYVVES YGTYNPGSGG TFRGTVNTDG GTYNIYTAVR YNAPSIEGTK TFTQYWSVRT 

       190        200        210        220 
SKRTGGTVTM ANHFNAWSRL GMNLGTHNYQ IVATEGYQSS GSASITVY 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of recombinant xylan degrading enzymes from Aspergillus fumigatus isolate SL1."
Dabrowski S., Ahring B.K.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: SL1.
[2]"Cloning and expression of GH11 xylanase gene from Aspergillus fumigatus MKU1 in Pichia pastoris."
Jeya M., Thiagarajan S., Lee J.K., Gunasekaran P.
J. Biosci. Bioeng. 108:24-29(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: MKU1.
[3]"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
DQ156553 mRNA. Translation: ABA40419.1.
EF375873 Genomic DNA. Translation: ABN48478.1.
AAHF01000010 Genomic DNA. Translation: EAL86316.1.
RefSeqXP_748354.1. XM_743261.1.

3D structure databases

ProteinModelPortalQ4WG11.
SMRQ4WG11. Positions 42-227.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00000232.

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.
mycoCLAPXYN11A_ASPFU.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00000232; CADAFUAP00000232; CADAFUAG00000232.
GeneID3505821.
KEGGafm:AFUA_3G00320.

Phylogenomic databases

eggNOGNOG05353.
HOGENOMHOG000179135.
KOK01181.
OMASEGYHNG.
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_ASPFU
AccessionPrimary (citable) accession number: Q4WG11
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: July 5, 2005
Last modified: March 19, 2014
This is version 64 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