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P40943 (XYN1_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 86. 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
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length407 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.

Induction

By xylose.

Sequence similarities

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

Sequence caution

The sequence ABI49951.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
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 – 2828 Ref.2
Chain29 – 407379Endo-1,4-beta-xylanase
PRO_0000007968

Sites

Active site1871Proton donor By similarity
Active site2931Nucleophile By similarity

Secondary structure

........................................................................ 407
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40943 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: AD385C90B252B82A

FASTA40746,763
        10         20         30         40         50         60 
MRNVVRKPLT IGLALTLLLP MGMTATSAKN ADSYAKKPHI SALNAPQLDQ RYKNEFTIGA 

        70         80         90        100        110        120 
AVEPYQLQNE KDVQMLKRHF NSIVAENVMK PISIQPEEGK FNFEQADRIV KFAKANGMDI 

       130        140        150        160        170        180 
RFHTLVWHSQ VPQWFFLDKE GKPMVNETDP VKREQNKQLL LKRLETHIKT IVERYKDDIK 

       190        200        210        220        230        240 
YWDVVNEVVG DDGKLRNSPW YQIAGIDYIK VAFQAARKYG GDNIKLYMND YNTEVEPKRT 

       250        260        270        280        290        300 
ALYNLVKQLK EEGVPIDGIG HQSHIQIGWP SEAEIEKTIN MFAALGLDNQ ITELDVSMYG 

       310        320        330        340        350        360 
WPPRAYPTYD AIPKQKFLDQ AARYDRLFKL YEKLSDKISN VTFWGIADNH TWLDSRADVY 

       370        380        390        400 
YDANGNVVVD PNAPYAKVEK GKGKDAPFVF GPDYKVKPAY WAIIDHK 

« Hide

References

[1]"Cloning and DNA sequence of the gene coding for Bacillus stearothermophilus T-6 xylanase."
Gat O., Lapidot A., Alchanati I., Regueros C., Shoham Y.
Appl. Environ. Microbiol. 60:1889-1896(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: T-6 / NCIMB 40221.
[2]"Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6."
Khasin A., Alchanati I., Shoham Y.
Appl. Environ. Microbiol. 59:1725-1730(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-73.
Strain: T-6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ868502 Genomic DNA. Translation: ABI49951.1. Different initiation.
PIRI40570.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HIZX-ray2.40A29-407[»]
1R85X-ray1.45A29-407[»]
1R86X-ray1.80A29-407[»]
1R87X-ray1.67A29-407[»]
3MMDX-ray1.70A29-407[»]
ProteinModelPortalP40943.
SMRP40943. Positions 33-407.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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

EvolutionaryTraceP40943.

Entry information

Entry nameXYN1_GEOSE
AccessionPrimary (citable) accession number: P40943
Secondary accession number(s): Q09LX3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 13, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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