Detail Information for IndEnz0008000448
IED ID IndEnz0008000448
Enzyme Type ID cellulase000448
Protein Name Endo-1,4-beta-xylanase A
Xylanase A
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase A
22 kDa xylanase
Xylanase X22
Gene Name xlnA AN3613
Organism Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Enzyme Sequence MVSFKSLLVLCCAALGAFATPVGSEDLAAREASLLERSTPSSTGWSNGYYYSFWTDGGGDVTYTNGAGGSYTVQWSNVGNFVGGKGWNPGSTRTINYGGSFNPSGNGYLAVYGWTQNPLIEYYIVESYGTYNPGSGGQHRGTVYSDGATYDIYTATRYNAPSIEGTATFEQFWSVRQSKRTGGTVTTANHFNAWAALGMRLGTHNYQIVATEGYQSSGSASITVY
Enzyme Length 225
Uniprot Accession Number P55332
Absorption
Active Site ACT_SITE 121; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 212; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10063
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 FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. {ECO:0000269|PubMed:16844780, ECO:0000269|PubMed:8787417}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 52 degrees Celsius. {ECO:0000269|PubMed:16844780};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.4. {ECO:0000269|PubMed:16844780};
Pathway PATHWAY: Glycan degradation; xylan degradation.
nucleotide Binding
Features Active site (2); Chain (1); Domain (1); Signal peptide (1)
Keywords Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Signal;Xylan degradation
Interact With
Induction INDUCTION: Expressed in the presence of D-xylose under conditions of alkaline ambient pH, probably under the regulation of the pacC transcription factor. Repressed in presence of glucose through the action of the creA transcription repressor. {ECO:0000269|PubMed:18420433, ECO:0000269|PubMed:9495775, ECO:0000269|PubMed:9987120}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25043916, ECO:0000269|PubMed:8787417}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 24,070
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda