Beta-1,3-xylanase precursor

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

Last modified May 1, 2013. Version 42. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Beta-1,3-xylanase
EC=3.2.1.32

Gene names

Name:	txyA
Synonyms:	3xynAlc

Organism

Alcaligenes sp.

Taxonomic identifier

512 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Alcaligenes

Protein attributes

Sequence length	469 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation Xylan degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW xylan catabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	polysaccharide binding Inferred from direct assay Ref.1. Source: UniProtKB xylan 1,3-beta-xylosidase activity Inferred from direct assay Ref.1. Source: UniProtKB xylan endo-1,3-beta-xylosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

Ref.2

Chain

23 – 469

447

Beta-1,3-xylanase Ref.2

PRO_0000403219

Regions

Region

377 – 469

Carbohydrate binding module (CBM)

Compositional bias

345 – 375

Gly-rich

Amino acid modifications

Disulfide bond

Disulfide bond

Secondary structure

469

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q8RS40 [UniParc].

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

FASTA

469

52,257

        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

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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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2COV	X-ray	1.25	D/E/F/G/H/I	375-469	[»]

ProteinModelPortal

Q8RS40.

SMR

Q8RS40. Positions 23-346, 378-469.

ModBase

Search...

Protein family/group databases

CAZy

CBM31. Carbohydrate-Binding Module Family 31.
GH26. Glycoside Hydrolase Family 26.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

3.2.1.32. 236.

Family and domain databases

Gene3D

3.20.20.80. 1 hit.

InterPro

IPR021016. Beta-xylanase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF11606. AlcCBM31. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q8RS40.

Entry information

Entry name

3XYN_ALCSP

Accession

Primary (citable) accession number: Q8RS40

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2011
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents