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Q8RS40

- 3XYN_ALCSP

UniProt

Q8RS40 - 3XYN_ALCSP

Protein

Beta-1,3-xylanase

Gene

txyA

Organism
Alcaligenes sp.
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    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

    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 – 3823
    Beta strandi384 – 3929
    Beta strandi395 – 4017
    Beta strandi408 – 4147
    Beta strandi417 – 4204
    Beta strandi422 – 4243
    Beta strandi427 – 4337
    Beta strandi439 – 44810
    Turni449 – 4524
    Beta strandi453 – 46210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MKKLAKMISI ATLGACAFSA HALDGKLVPN EGVLVSVGQD VDSVNDYSSA    50
    MSTTPAGVTN YVGIVNLDGL ASNADAGAGR NNVVELANLY PTSALIVGVS 100
    MNGQIQNVAQ GQYNANIDTL IQTLGELDRP VYLRWAYEVD GPWNGHNTED 150
    LKQSFRNVYQ RIRELGYGDN ISMIWQVASY CPTAPGQLSS WWPGDDVVDW 200
    VGLSYFAPQD CNWDRVNEAA QWARSHNKPL FINESSPQRY QLADRTYSSD 250
    PAKGTNRQSK TEQQIWSEWF APYFQFMEDN KDILKGFTYI NADWDSQWRW 300
    AAPYNEGYWG DSRVQVLPYI KQQWQDTLEN PKFINHSSDL FAKLGYVADG 350
    GDNGGDNGGD NGGDNGGDNG GDNGGTEPPE NCQDDFNFNY VSDQEIEVYH 400
    VDKGWSAGWN YVCLNDYCLP GNKSNGAFRK TFNAVLGQDY KLTFKVEDRY 450
    GQGQQILDRN ITFTTQVCN 469
    Length:469
    Mass (Da):52,257
    Last modified:June 1, 2002 - v1
    Checksum:iB61058CE40353F58
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB039953 Genomic DNA. Translation: BAB88993.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB039953 Genomic DNA. Translation: BAB88993.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 44 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