IED ID | IndEnz0004000008 |
Enzyme Type ID | xylanase000008 |
Protein Name |
Beta-1,3-xylanase TXYA EC 3.2.1.32 Endo-1,3-beta-xylanase |
Gene Name | txyA |
Organism | Vibrio sp. |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio unclassified Vibrio Vibrio sp. |
Enzyme Sequence | MKKLAKMISVATLGACAFQAHALDGKLVPDQGILVSVGQDVDSVNDYSSAMGTTPAGVTNYVGIVNLDGLSTDADAGAGRNNIVELANQYPTSALIVGVSMNGEVQNVANGQYNANIDTLIRTLGEFDRPVYLRWAYEVDGPWNGHNTEDLKQSFRHVYQRIRELGYADNISMVWQVASYCPTAPGQLGTWWPGDDVVDWVGLSYFAPQDCNWDRVNEAAQWARSHNKPLFINESSPQRYQLADLTYSTDPAKGTNRQAKTDQQIWSEWFEPFFQFMVDNQDILKGFTYINADWDSQWRWAAPYNEGYWGDSRVQVIPYIKQKWQETLSDPKFIRHSDELFAQLGYGNSDGGNGGDNGGDNGGDNGGETPENCTDDFNFNYVSDNEIEVYHVDKGWSAGWNYLCLDDYCLSGTKSNGAFSRSFSAQLGQTYKMTFKVEDITGQGQQIIDKTVTFTNQVCN |
Enzyme Length | 460 |
Uniprot Accession Number | Q9LCB9 |
Absorption | |
Active Site | ACT_SITE 138; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01100; ACT_SITE 234; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01100 |
Activity Regulation | ACTIVITY REGULATION: Completely inhibited by Cu(2+), Hg(2+) and N-bromosuccinimide. Strongly inhibited by Ag(+), Zn(2+) and Pb(2+). Moderately inhibited by Fe(3+), Al(3+), Mn(2+), dithiothreitol and p-chloromercuribenzoic acid. Slightly activated by Mg(2+) and Ca(2+). Unaffected by Na(+), K(+), Ba(2+), EDTA, iodoacetic acid and N-ethylmalaimide. {ECO:0000269|PubMed:10635569}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans.; EC=3.2.1.32; Evidence={ECO:0000269|PubMed:10635569, ECO:0000269|PubMed:10742274}; |
DNA Binding | |
EC Number | 3.2.1.32 |
Enzyme Function | FUNCTION: 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. {ECO:0000269|PubMed:10635569, ECO:0000269|PubMed:10742274}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. Stable below 30 degrees Celsius. {ECO:0000269|PubMed:10635569}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. Stable between pH 5.0 and 8.0. {ECO:0000269|PubMed:10635569}; |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Disulfide bond (2); Domain (1); Region (2); Signal peptide (1) |
Keywords | Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Signal;Xylan degradation |
Interact With | |
Induction | INDUCTION: By beta-1,3-xylan. {ECO:0000269|PubMed:10635569}. |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..22; /evidence="ECO:0000269|PubMed:10635569, ECO:0000269|PubMed:10742274" |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 51,324 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.2.1.32; |