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P55331 (XYNA_ASPTU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 70. 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 A

Short name=Xylanase A
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Endo-1,4-beta-xylanase I
Short name=Xylanase I
Gene names
Name:xynA
Synonyms:xlnA
OrganismAspergillus tubingensis
Taxonomic identifier5068 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length211 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.

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.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 By similarity
Chain28 – 211184Endo-1,4-beta-xylanase A
PRO_0000007995

Sites

Active site1061Nucleophile By similarity
Active site1971Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P55331 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 1A88D060C67080D4

FASTA21122,576
        10         20         30         40         50         60 
MKVTAAFAGL LVTAFAAPAP EPDLVSRSAG INYVQNYNGN LGDFTYDESA GTFSMYWEDG 

        70         80         90        100        110        120 
VSSDFVVGLG WTTGSSNAIT YSAEYSASGS ASYLAVYGWV NYPQAEYYIV EDYGDYNPCS 

       130        140        150        160        170        180 
SATSLGTVYS DGSTYQVCTD TRTNEPSITG TSTFTQYFSV RESTRTSGTV TVANHFNFWA 

       190        200        210 
HHGFGNSDFN YQVVAVEAWS GAGSASVTIS S 

« Hide

References

[1]"Regulation of the xylanase-encoding xlnA gene of Aspergillus tubigensis."
de Graaff L.H., van den Broeck H.C., van Ooijen A.J.J., Visser J.
Mol. Microbiol. 12:479-490(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NW756.
[2]de Graaff L.H., van den Broeck H.C., van Ooijen A.J.J., Visser J.
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L26988 Genomic DNA. Translation: AAB05996.1.
PIRS49542.

3D structure databases

ProteinModelPortalP55331.
SMRP55331. Positions 30-210.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.
mycoCLAPXYN11A_ASPTU.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_ASPTU
AccessionPrimary (citable) accession number: P55331
Secondary accession number(s): Q12568
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1998
Last modified: November 13, 2013
This is version 70 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