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Q9LCB9

- 3XYN2_VIBSX

UniProt

Q9LCB9 - 3XYN2_VIBSX

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Protein

Beta-1,3-xylanase TXYA

Gene

txyA

Organism
Vibrio 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. 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
Complete GO annotation...

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

        10         20         30         40         50
MKKLAKMISV ATLGACAFQA HALDGKLVPD QGILVSVGQD VDSVNDYSSA
60 70 80 90 100
MGTTPAGVTN YVGIVNLDGL STDADAGAGR NNIVELANQY PTSALIVGVS
110 120 130 140 150
MNGEVQNVAN GQYNANIDTL IRTLGEFDRP VYLRWAYEVD GPWNGHNTED
160 170 180 190 200
LKQSFRHVYQ RIRELGYADN ISMVWQVASY CPTAPGQLGT WWPGDDVVDW
210 220 230 240 250
VGLSYFAPQD CNWDRVNEAA QWARSHNKPL FINESSPQRY QLADLTYSTD
260 270 280 290 300
PAKGTNRQAK TDQQIWSEWF EPFFQFMVDN QDILKGFTYI NADWDSQWRW
310 320 330 340 350
AAPYNEGYWG DSRVQVIPYI KQKWQETLSD PKFIRHSDEL FAQLGYGNSD
360 370 380 390 400
GGNGGDNGGD NGGDNGGETP ENCTDDFNFN YVSDNEIEVY HVDKGWSAGW
410 420 430 440 450
NYLCLDDYCL SGTKSNGAFS RSFSAQLGQT YKMTFKVEDI TGQGQQIIDK
460
TVTFTNQVCN
Length:460
Mass (Da):51,324
Last modified:October 1, 2000 - v1
Checksum:i6EFA748496BA092A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029043 Genomic DNA. Translation: BAA94698.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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