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Q8RS40

- 3XYN_ALCSP

UniProt

Q8RS40 - 3XYN_ALCSP

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Protein

Beta-1,3-xylanase

Gene

txyA

Organism
Alcaligenes sp.
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Enzyme regulationi

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.1 Publication

pH dependencei

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.2 Publications

Temperature dependencei

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.2 Publications

GO - Molecular functioni

  1. polysaccharide binding Source: UniProtKB
  2. xylan 1,3-beta-xylosidase activity Source: UniProtKB
  3. xylan endo-1,3-beta-xylosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
  2. xylan catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

BRENDAi3.2.1.32. 236.

Protein family/group databases

CAZyiCBM31. Carbohydrate-Binding Module Family 31.
GH26. Glycoside Hydrolase Family 26.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,3-xylanaseImported (EC:3.2.1.32)
Gene namesi
Name:txyA1 Publication
Synonyms:3xynAlcImported
OrganismiAlcaligenes sp.
Taxonomic identifieri512 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeAlcaligenes

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 469447Beta-1,3-xylanase1 PublicationPRO_0000403219Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi382 ↔ 4681 Publication
Disulfide bondi413 ↔ 4181 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

By beta-1,3-xylan.1 Publication

Structurei

Secondary structure

1
469
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi380 – 3823Combined sources
Beta strandi384 – 3929Combined sources
Beta strandi395 – 4017Combined sources
Beta strandi408 – 4147Combined sources
Beta strandi417 – 4204Combined sources
Beta strandi422 – 4243Combined sources
Beta strandi427 – 4337Combined sources
Beta strandi439 – 44810Combined sources
Turni449 – 4524Combined sources
Beta strandi453 – 46210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2COVX-ray1.25D/E/F/G/H/I375-469[»]
ProteinModelPortaliQ8RS40.
SMRiQ8RS40. Positions 23-346, 378-469.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8RS40.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni377 – 46993Carbohydrate binding module (CBM)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi345 – 37531Gly-richSequence AnalysisAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the glycosyl hydrolase 26 family.Sequence Analysis

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR021016. Beta-xylanase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF11606. AlcCBM31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8RS40-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKLAKMISI ATLGACAFSA HALDGKLVPN EGVLVSVGQD VDSVNDYSSA
60 70 80 90 100
MSTTPAGVTN YVGIVNLDGL ASNADAGAGR NNVVELANLY PTSALIVGVS
110 120 130 140 150
MNGQIQNVAQ GQYNANIDTL IQTLGELDRP VYLRWAYEVD GPWNGHNTED
160 170 180 190 200
LKQSFRNVYQ RIRELGYGDN ISMIWQVASY CPTAPGQLSS WWPGDDVVDW
210 220 230 240 250
VGLSYFAPQD CNWDRVNEAA QWARSHNKPL FINESSPQRY QLADRTYSSD
260 270 280 290 300
PAKGTNRQSK TEQQIWSEWF APYFQFMEDN KDILKGFTYI NADWDSQWRW
310 320 330 340 350
AAPYNEGYWG DSRVQVLPYI KQQWQDTLEN PKFINHSSDL FAKLGYVADG
360 370 380 390 400
GDNGGDNGGD NGGDNGGDNG GDNGGTEPPE NCQDDFNFNY VSDQEIEVYH
410 420 430 440 450
VDKGWSAGWN YVCLNDYCLP GNKSNGAFRK TFNAVLGQDY KLTFKVEDRY
460
GQGQQILDRN ITFTTQVCN
Length:469
Mass (Da):52,257
Last modified:June 1, 2002 - v1
Checksum:iB61058CE40353F58
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB039953 Genomic DNA. Translation: BAB88993.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB039953 Genomic DNA. Translation: BAB88993.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2COV X-ray 1.25 D/E/F/G/H/I 375-469 [» ]
ProteinModelPortali Q8RS40.
SMRi Q8RS40. Positions 23-346, 378-469.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

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

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 3.2.1.32. 236.

Miscellaneous databases

EvolutionaryTracei Q8RS40.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR021016. Beta-xylanase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF11606. AlcCBM31. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  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-234Imported.
  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-2341 Publication.
  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-2341 Publication.

Entry informationi

Entry namei3XYN_ALCSP
AccessioniPrimary (citable) accession number: Q8RS40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: June 1, 2002
Last modified: November 26, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3