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Reviewed, UniProtKB/Swiss-Prot O43097 (XYNA_THELA)

Last modified November 24, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
Gene names
Name: XYNA
OrganismThermomyces lanuginosus (Humicola lanuginosa)
Taxonomic identifier5541 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › mitosporic Ascomycota › Thermomyces

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Protein attributes

Sequence length225 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Ref.2

Pathway

Glycan degradation; xylan degradation.

Induction

By xylan. Ref.2

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

Vmax=2223.3 µmol/min/mg enzyme

pH dependence:

Optimum pH is 6.0.

Temperature dependence:

Optimum temperature is 60 degrees Celsius. Thermostable.

Mass spectrometry

Molecular mass is 21300 Da from positions 32 - 225. Determined by MALDI. Ref.2

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Ontologies

Keywords
   Biological processXylan degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionendo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131
Chain32 – 225194Endo-1,4-beta-xylanase
PRO_0000008012

Sites

Active site1171Nucleophile
Active site2091Proton donor

Amino acid modifications

Modified residue321Pyrrolidone carboxylic acid
Disulfide bond141 ↔ 185

Secondary structure

1 ................................ 225
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O43097-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: FAA79A914C5C676C

FASTA22524,356
        10         20         30         40         50         60 
MVGFTPVALA ALAATGALAF PAGNATELEK RQTTPNSEGW HDGYYYSWWS DGGAQATYTN 

        70         80         90        100        110        120 
LEGGTYEISW GDGGNLVGGK GWNPGLNARA IHFEGVYQPN GNSYLAVYGW TRNPLVEYYI 

       130        140        150        160        170        180 
VENFGTYDPS SGATDLGTVE CDGSIYRLGK TTRVNAPSID GTQTFDQYWS VRQDKRTSGT 

       190        200        210        220 
VQTGCHFDAW ARAGLNVNGD HYYQIVATEG YFSSGYARIT VADVG

« Hide

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References

[1]"Cloning and characterization of the gene for the thermostable xylanase XynA from Thermomyces lanuginosus."
Schlacher A., Holzmann K., Hayn M., Steiner W., Schwab H.
J. Biotechnol. 49:211-218(1996) [PubMed: 8879171] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 5826 / Tsiklinsky.
[2]"Thermomyces lanuginosus SS-8 endo-beta-1,4-D-xylanase precursor."
Shrivastava S., Deepalakshmi P.D., Shukla P., Mukhopadhyay K.
Submitted (AUG-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 193-218, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, MASS SPECTROMETRY.
Strain: SS-8.
[3]"Thermophilic xylanase from Thermomyces lanuginosus: high-resolution X-ray structure and modeling studies."
Gruber K., Klintschar G., Hayn M., Schlacher A., Steiner W., Kratky C.
Biochemistry 37:13475-13485(1998) [PubMed: 9753433] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
Strain: DSM 5826 / Tsiklinsky.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U35436 Genomic DNA. Translation: AAB94633.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YNAX-ray1.55A33-225[»]
ModBaseSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.

Enzyme and pathway databases

BRENDA3.2.1.8. 74338.

Family and domain databases

InterProIPR008985. ConA-like_lec_gl.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12_cat.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
Gene3DG3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit.
PfamPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameXYNA_THELA
AccessionPrimary (citable) accession number: O43097
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: November 24, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents