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P56588 (XYNA_PENSI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

Short name=Xylanase
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
OrganismPenicillium simplicissimum
Taxonomic identifier69488 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
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.

Subunit structure

Monomer.

Subcellular location

Secreted.

Sequence similarities

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical term3D-structure
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

Chain1 – 302302Endo-1,4-beta-xylanase
PRO_0000184067

Sites

Active site1321Proton donor
Active site2381Nucleophile

Amino acid modifications

Modified residue11Pyrrolidone carboxylic acid
Disulfide bond256 ↔ 262

Secondary structure

........................................................ 302
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56588 [UniParc].

Last modified December 15, 1998. Version 1.
Checksum: EE7821FA58687FFC

FASTA30232,551
        10         20         30         40         50         60 
QASVSIDAKF KAHGKKYLGT IGDQYTLTKN TKNPAIIKAD FGQLTPENSM KWDATEPNRG 

        70         80         90        100        110        120 
QFTFSGSDYL VNFAQSNGKL IRGHTLVWHS QLPGWVSSIT DKNTLISVLK NHITTVMTRY 

       130        140        150        160        170        180 
KGKIYAWDVL NEIFNEDGSL RNSVFYNVIG EDYVRIAFET ARSVDPNAKL YINDYNLDSA 

       190        200        210        220        230        240 
GYSKVNGMVS HVKKWLAAGI PIDGIGSQTH LGAGAGSAVA GALNALASAG TKEIAITELD 

       250        260        270        280        290        300 
IAGASSTDYV NVVNACLNQA KCVGITVWGV ADPDSWRSSS SPLLFDGNYN PKAAYNAIAN 


AL 

« Hide

References

[1]"Structure of the xylanase from Penicillium simplicissimum."
Schmidt A., Schlacher A., Steiner W., Schwab H., Kratky C.
Protein Sci. 7:2081-2088(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
Strain: BT 2246.
[2]"Xylan binding subsite mapping in the xylanase from Penicillium simplicissimum using xylooligosaccharides as cryo-protectant."
Schmidt A., Gubitz G.M., Kratky C.
Biochemistry 38:2403-2412(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF070417 Genomic DNA. Translation: AAC23574.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B30X-ray2.25A2-302[»]
1B31X-ray1.75A1-302[»]
1B3VX-ray2.40A1-302[»]
1B3WX-ray2.60A2-302[»]
1B3XX-ray2.20A2-302[»]
1B3YX-ray2.45A2-302[»]
1B3ZX-ray2.30A2-302[»]
1BG4X-ray1.75A2-302[»]
ProteinModelPortalP56588.
SMRP56588. Positions 1-302.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16225.
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.
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP56588.

Entry information

Entry nameXYNA_PENSI
AccessionPrimary (citable) accession number: P56588
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: July 9, 2014
This is version 74 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries