Detail Information for IndEnz0004000076
IED ID IndEnz0004000076
Enzyme Type ID xylanase000076
Protein Name Endo-1,4-beta-xylanase A
Xylanase A
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase A
Gene Name xynA BH2120
Organism Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) (Bacillus halodurans)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Alkalihalobacillus Alkalihalobacillus halodurans (Bacillus halodurans) Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) (Bacillus halodurans)
Enzyme Sequence MITLFRKPFVAGLAISLLVGGGIGNVAAAQGGPPKSGVFGENEKRNDQPFAWQVASLSERYQEQFDIGAAVEPYQLEGRQAQILKHHYNSLVAENAMKPESLQPREGEWNWEGADKIVEFARKHNMELRFHTLVWHSQVPEWFFIDEDGNRMVDETDPDKREANKQLLLERMENHIKTVVERYKDDVTSWDVVNEVIDDGGGLRESEWYQITGTDYIKVAFETARKYGGEEAKLYINDYNTEVPSKRDDLYNLVKDLLEQGVPIDGVGHQSHIQIGWPSIEDTRASFEKFTSLGLDNQVTELDMSLYGWPPTGAYTSYDDIPAELLQAQADRYDQLFELYEELAADISSVTFWGIADNHTWLDGRAREYNNGVGIDAPFVFDHNYRVKPAYWRIID
Enzyme Length 396
Uniprot Accession Number P07528
Absorption
Active Site ACT_SITE 195; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 301; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10061
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8;
DNA Binding
EC Number 3.2.1.8
Enzyme Function
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Active over a very broad pH range.;
Pathway PATHWAY: Glycan degradation; xylan degradation.
nucleotide Binding
Features Active site (2); Beta strand (13); Chain (1); Domain (1); Helix (18); Signal peptide (1); Turn (4)
Keywords 3D-structure;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Signal;Xylan degradation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..28; /evidence=ECO:0000269|Ref.1
Structure 3D X-ray crystallography (3)
Cross Reference PDB 2UWF; 7CPK; 7CPL;
Mapped Pubmed ID 19567261; 33604642;
Motif
Gene Encoded By
Mass 45,294
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda