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

Q8RS40 (3XYN_ALCSP) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 43. 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:
Beta-1,3-xylanase

EC=3.2.1.32
Gene names
Name:txyA
Synonyms:3xynAlc
OrganismAlcaligenes sp.
Taxonomic identifier512 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeAlcaligenes

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylotriose and xylobiose with smaller amounts of xylotetraose, xylose, xylopentaose and xylohexaose. Does not hydrolyze xylobiose, p-nitrophenyl-beta-xyloside, beta-1,4-xylan, carboxymethylcellulose, curdlan, glucomannan or beta-1,4-mannan. Ref.1 Ref.2

Catalytic activity

Random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans. Ref.1 Ref.2

Enzyme regulation

Completely inhibited by CuCl2, FeCl3, HgCl2 and N-bromosuccinimide. Moderately inhibited by AgCl, AlCl3, Pb(CH3COO)2 and dithiothreitol. BaCl2, CaCl2, KCl, MgCl2, MnCl2, NaCl, ZnCl2, ethylenediaminetetraacetic acid, N-ethylmaleimide, iodoacetic acid and p-chloromercuribenzoic acid have little or no effect on activity. Ref.2

Induction

By beta-1,3-xylan. Ref.2

Domain

The carbohydrate binding module (CBM) binds to insoluble beta-1,3-xylan, but not to insoluble beta-1,4-xylan, beta-1,4-glucan, beta-1,4-mannan, curdlan, chitin, or soluble polysaccharides. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 26 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0-7.5. Stable from pH 5.0-11.0. Retains 65% and 70% of activity respectively when incubated at pH 4.0 and 12.0 for 24 hours. Ref.1 Ref.2

Temperature dependence:

Optimum temperature is 40 degrees Celsius. Stable below 40 degrees Celsius. Loses 70% and 99% of activity respectively when incubated for 10 minutes at 50 and 60 degrees Celsius. Ref.1 Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.2
Chain23 – 469447Beta-1,3-xylanase Ref.2
PRO_0000403219

Regions

Region377 – 46993Carbohydrate binding module (CBM)
Compositional bias345 – 37531Gly-rich

Amino acid modifications

Disulfide bond382 ↔ 468 Ref.3
Disulfide bond413 ↔ 418 Ref.3

Secondary structure

................... 469
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8RS40 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: B61058CE40353F58

FASTA46952,257
        10         20         30         40         50         60 
MKKLAKMISI ATLGACAFSA HALDGKLVPN EGVLVSVGQD VDSVNDYSSA MSTTPAGVTN 

        70         80         90        100        110        120 
YVGIVNLDGL ASNADAGAGR NNVVELANLY PTSALIVGVS MNGQIQNVAQ GQYNANIDTL 

       130        140        150        160        170        180 
IQTLGELDRP VYLRWAYEVD GPWNGHNTED LKQSFRNVYQ RIRELGYGDN ISMIWQVASY 

       190        200        210        220        230        240 
CPTAPGQLSS WWPGDDVVDW VGLSYFAPQD CNWDRVNEAA QWARSHNKPL FINESSPQRY 

       250        260        270        280        290        300 
QLADRTYSSD PAKGTNRQSK TEQQIWSEWF APYFQFMEDN KDILKGFTYI NADWDSQWRW 

       310        320        330        340        350        360 
AAPYNEGYWG DSRVQVLPYI KQQWQDTLEN PKFINHSSDL FAKLGYVADG GDNGGDNGGD 

       370        380        390        400        410        420 
NGGDNGGDNG GDNGGTEPPE NCQDDFNFNY VSDQEIEVYH VDKGWSAGWN YVCLNDYCLP 

       430        440        450        460 
GNKSNGAFRK TFNAVLGQDY KLTFKVEDRY GQGQQILDRN ITFTTQVCN 

« Hide

References

[1]"Novel carbohydrate-binding module of beta-1,3-xylanase from a marine bacterium, Alcaligenes sp. strain XY-234."
Okazaki F., Tamaru Y., Hashikawa S., Li Y.T., Araki T.
J. Bacteriol. 184:2399-2403(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CBM31 DOMAIN.
Strain: XY-234.
[2]"Purification and characterization of beta-1,3-xylanase from a marine bacterium, Alcaligenes sp. XY-234."
Araki T., Inoue N., Morishita T.
J. Gen. Appl. Microbiol. 44:269-274(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-35, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
Strain: XY-234.
[3]"The first crystal structure of a family 31 carbohydrate-binding module with affinity to beta-1,3-xylan."
Hashimoto H., Tamai Y., Okazaki F., Tamaru Y., Shimizu T., Araki T., Sato M.
FEBS Lett. 579:4324-4328(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 375-469, DISULFIDE BONDS.
Strain: XY-234.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB039953 Genomic DNA. Translation: BAB88993.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2COVX-ray1.25D/E/F/G/H/I375-469[»]
ProteinModelPortalQ8RS40.
SMRQ8RS40. Positions 23-346, 378-469.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM31. Carbohydrate-Binding Module Family 31.
GH26. Glycoside Hydrolase Family 26.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.32. 236.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR021016. Beta-xylanase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF11606. AlcCBM31. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ8RS40.

Entry information

Entry name3XYN_ALCSP
AccessionPrimary (citable) accession number: Q8RS40
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: June 1, 2002
Last modified: October 16, 2013
This is version 43 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries