Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9LCB9

- 3XYN2_VIBSX

UniProt

Q9LCB9 - 3XYN2_VIBSX

Protein

Beta-1,3-xylanase TXYA

Gene

txyA

Organism
Vibrio sp.
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.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 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.1 Publication

    pH dependencei

    Optimum pH is 7.0. Stable between pH 5.0 and 8.0.1 Publication

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius. Stable below 30 degrees Celsius.1 Publication

    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

    BioCyciMetaCyc:MONOMER-16528.

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-1,3-xylanase TXYA (EC:3.2.1.32)
    Alternative name(s):
    Endo-1,3-beta-xylanaseImported
    Gene namesi
    Name:txyAImported
    OrganismiVibrio sp.
    Taxonomic identifieri678 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22222 PublicationsAdd
    BLAST
    Chaini23 – 460438Beta-1,3-xylanase TXYA2 PublicationsPRO_0000403221Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi373 ↔ 459By similarity
    Disulfide bondi404 ↔ 409By similarity

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Inductioni

    By beta-1,3-xylan.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LCB9.
    SMRiQ9LCB9. Positions 23-346, 370-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni368 – 46093Carbohydrate binding module (CBM)Add
    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.By similarity

    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.

    Q9LCB9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKLAKMISV ATLGACAFQA HALDGKLVPD QGILVSVGQD VDSVNDYSSA    50
    MGTTPAGVTN YVGIVNLDGL STDADAGAGR NNIVELANQY PTSALIVGVS 100
    MNGEVQNVAN GQYNANIDTL IRTLGEFDRP VYLRWAYEVD GPWNGHNTED 150
    LKQSFRHVYQ RIRELGYADN ISMVWQVASY CPTAPGQLGT WWPGDDVVDW 200
    VGLSYFAPQD CNWDRVNEAA QWARSHNKPL FINESSPQRY QLADLTYSTD 250
    PAKGTNRQAK TDQQIWSEWF EPFFQFMVDN QDILKGFTYI NADWDSQWRW 300
    AAPYNEGYWG DSRVQVIPYI KQKWQETLSD PKFIRHSDEL FAQLGYGNSD 350
    GGNGGDNGGD NGGDNGGETP ENCTDDFNFN YVSDNEIEVY HVDKGWSAGW 400
    NYLCLDDYCL SGTKSNGAFS RSFSAQLGQT YKMTFKVEDI TGQGQQIIDK 450
    TVTFTNQVCN 460
    Length:460
    Mass (Da):51,324
    Last modified:October 1, 2000 - v1
    Checksum:i6EFA748496BA092A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB029043 Genomic DNA. Translation: BAA94698.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB029043 Genomic DNA. Translation: BAA94698.1 .

    3D structure databases

    ProteinModelPortali Q9LCB9.
    SMRi Q9LCB9. Positions 23-346, 370-460.
    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

    BioCyci MetaCyc:MONOMER-16528.

    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. "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-214Imported.
    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-2141 Publication.

    Entry informationi

    Entry namei3XYN2_VIBSX
    AccessioniPrimary (citable) accession number: Q9LCB9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2011
    Last sequence update: October 1, 2000
    Last modified: October 1, 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

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3