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P33559 (XYNA_ASPKA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. 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
Gene names
Name:xynA
OrganismAspergillus kawachii (White koji mold) (Aspergillus awamori var. kawachi)
Taxonomic identifier40384 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted.

Sequence similarities

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

Ontologies

Keywords
   Biological processXylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

endo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.1
Chain26 – 327302Endo-1,4-beta-xylanase A
PRO_0000007965

Sites

Active site1571Proton donor By similarity
Active site2631Nucleophile By similarity

Amino acid modifications

Modified residue261Pyrrolidone carboxylic acid
Disulfide bond281 ↔ 287 By similarity

Sequences

Sequence LengthMass (Da)Tools
P33559 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: ECD572EA169A9B20

FASTA32735,438
        10         20         30         40         50         60 
MVQIKAAALA MLFASHVLSE PIEPRQASVS IDSKFKAHGK KYLGNIGDQY TLTKNSKTPA 

        70         80         90        100        110        120 
VIKADFGALT PENSMKWDAT EPSRGQFSFS GSDYLVNFAQ SNNKLIRGHT LVWHSQLPSW 

       130        140        150        160        170        180 
VQAITDKNTL IEVMKNHITT VMQHYKGKIY AWDVVNEIFN EDGSLRDSVF YKVIGDDYVR 

       190        200        210        220        230        240 
IAFETARAAD PNAKLYINDY NLDSASYPKL AGMVSHVKKW IEAGIPIDGI GSQTHLSAGG 

       250        260        270        280        290        300 
GAGISGALNA LAGAGTKEIA VTELDIAGAS STDYVEVVEA CLDQPKCIGI TVWGVADPDS 

       310        320 
WRSSSTPLLF DSNYNPKPAY TAIANAL 

« Hide

References

[1]"Cloning and sequencing of the xynA gene encoding xylanase A of Aspergillus kawachii."
Ito K., Ikemasu T., Ishikawa T.
Biosci. Biotechnol. Biochem. 56:906-912(1992) [PubMed: 1368254] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-33; 41-54; 63-76 AND 76-100.
Strain: NBRC 4308.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D14847 Genomic DNA. Translation: BAA03575.1.

3D structure databases

ProteinModelPortalP33559.
SMRP33559. Positions 26-327.
ModBaseSearch...

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNA_ASPKA
AccessionPrimary (citable) accession number: P33559
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families