Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P23556 (XYNA_CALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 73. 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
OrganismCaldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Taxonomic identifier44001 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length342 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.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5-6.0.

Temperature dependence:

Optimum temperature is 70 degrees Celsius.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

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 – 342342Endo-1,4-beta-xylanase A
PRO_0000007984

Sites

Active site1441Proton donor By similarity
Active site2521Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
P23556 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: C5380F2AB0CC0271

FASTA34240,455
        10         20         30         40         50         60 
MRCLIVCENL EMLNLSLAKT YKDYFKIGAA VTAKDLEGVH RDILLKHFNS LTPENAMKFE 

        70         80         90        100        110        120 
NIHPEEQRYN FEEVARIKEF AIKNDMKLRG HTFVWHNQTP GWVFLDKNGE EASKELVIER 

       130        140        150        160        170        180 
LREHIKTLCE RYKDVVYAWD VVNEAVEDKT EKLLRESNWR KIIGDDYIKI AFEIAREYAG 

       190        200        210        220        230        240 
DAKLFYNDYN NEMPYKLEKT YKVLKELLER GTPIDGIGIQ AHWNIWDKNL VSNLKKAIEV 

       250        260        270        280        290        300 
YASLGLEIHI TELDISVFEF EDKRTDLFEP TPEMLELQAK VYEDVFAVFR EYKDVITSVT 

       310        320        330        340 
LWGISDRHTW KDNFPVKGRK DWPLLFDVNG KPKEALYRIL RF 

« Hide

References

[1]"Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile 'Caldocellum saccharolyticum'."
Luethi E., Love D.R., McAnulty J., Wallace C., Caughey P.A., Saul D.J., Bergquist P.L.
Appl. Environ. Microbiol. 56:1017-1024(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A cluster of genes involved in xylan degradation cloned from the extreme thermophile Caldicellulosiruptor saccharolyticus."
Te'O V.S. Jr., Gibbs M.D., Saul D.J., Bergquist P.L.
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Xylanase from the extremely thermophilic bacterium 'Caldocellum saccharolyticum': overexpression of the gene in Escherichia coli and characterization of the gene product."
Luethi E., Jasmat N.B., Bergquist P.L.
Appl. Environ. Microbiol. 56:2677-2683(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34459 Genomic DNA. Translation: AAA23059.1.
AF005383 Genomic DNA. Translation: AAB87374.1.
PIRA60154. A37202.

3D structure databases

ProteinModelPortalP23556.
SMRP23556. Positions 16-341.
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...

Entry information

Entry nameXYNA_CALSA
AccessionPrimary (citable) accession number: P23556
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: December 11, 2013
This is version 73 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries