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Q9LCB9 (3XYN2_VIBSX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 TXYA

EC=3.2.1.32
Alternative name(s):
Endo-1,3-beta-xylanase
Gene names
Name:txyA
OrganismVibrio sp.
Taxonomic identifier678 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length460 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. Weakly active toward beta-1,3-xylotriose, yielding xylose and xylobiose. Converts beta-1,3-xylotetraose into xylotriose, xylobiose and xylose. Converts beta-1,3-xylopentaose into xylotetraose, xylotriose, xylobiose and xylose. Does not hydrolyze xylobiose, p-nitrophenyl-beta-xyloside, beta-1,4-xylan, curdlan or carboxymethylcellulose. 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 Cu2+, Hg2+ and N-bromosuccinimide. Strongly inhibited by Ag+, Zn2+ and Pb2+. Moderately inhibited by Fe3+, Al3+, Mn2+, dithiothreitol and p-chloromercuribenzoic acid. Slightly activated by Mg2+ and Ca2+. Unaffected by Na+, K+, Ba2+, EDTA, iodoacetic acid and N-ethylmalaimide. 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 By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 26 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0. Stable between pH 5.0 and 8.0. Ref.2

Temperature dependence:

Optimum temperature is 37 degrees Celsius. Stable below 30 degrees Celsius. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.1 Ref.2
Chain23 – 460438Beta-1,3-xylanase TXYA Ref.1 Ref.2
PRO_0000403221

Regions

Region368 – 46093Carbohydrate binding module (CBM)

Amino acid modifications

Disulfide bond373 ↔ 459 By similarity UniProtKB Q8RS40
Disulfide bond404 ↔ 409 By similarity UniProtKB Q8RS40

Sequences

Sequence LengthMass (Da)Tools
Q9LCB9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 6EFA748496BA092A

FASTA46051,324
        10         20         30         40         50         60 
MKKLAKMISV ATLGACAFQA HALDGKLVPD QGILVSVGQD VDSVNDYSSA MGTTPAGVTN 

        70         80         90        100        110        120 
YVGIVNLDGL STDADAGAGR NNIVELANQY PTSALIVGVS MNGEVQNVAN GQYNANIDTL 

       130        140        150        160        170        180 
IRTLGEFDRP VYLRWAYEVD GPWNGHNTED LKQSFRHVYQ RIRELGYADN ISMVWQVASY 

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

       250        260        270        280        290        300 
QLADLTYSTD PAKGTNRQAK TDQQIWSEWF EPFFQFMVDN QDILKGFTYI NADWDSQWRW 

       310        320        330        340        350        360 
AAPYNEGYWG DSRVQVIPYI KQKWQETLSD PKFIRHSDEL FAQLGYGNSD GGNGGDNGGD 

       370        380        390        400        410        420 
NGGDNGGETP ENCTDDFNFN YVSDNEIEVY HVDKGWSAGW NYLCLDDYCL SGTKSNGAFS 

       430        440        450        460 
RSFSAQLGQT YKMTFKVEDI TGQGQQIIDK TVTFTNQVCN 

« Hide

References

[1]"Cloning, sequencing, and expression in Escherichia coli of the new gene encoding beta-1,3-xylanase from a marine bacterium, Vibrio sp. strain XY-214."
Araki T., Hashikawa S., Morishita T.
Appl. Environ. Microbiol. 66:1741-1743(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-41 AND 300-313, FUNCTION, CATALYTIC ACTIVITY.
Strain: XY-214.
[2]"Purification and characterization of beta-1,3-xylanase from a marine bacterium, Vibrio sp. XY-214."
Araki T., Tani S., Maeda K., Hashikawa S., Nakagawa H., Morishita T.
Biosci. Biotechnol. Biochem. 63:2017-2019(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-38, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
Strain: XY-214.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB029043 Genomic DNA. Translation: BAA94698.1.

3D structure databases

ProteinModelPortalQ9LCB9.
SMRQ9LCB9. Positions 23-346, 370-460.
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

BioCycMetaCyc:MONOMER-16528.

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...

Entry information

Entry name3XYN2_VIBSX
AccessionPrimary (citable) accession number: Q9LCB9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: October 1, 2000
Last modified: October 16, 2013
This is version 44 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries