Detail Information for IndEnz0004000008
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;