Detail Information for IndEnz0004000124
IED ID IndEnz0004000124
Enzyme Type ID xylanase000124
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
Organism Aureobasidium pullulans (Black yeast) (Pullularia pullulans)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Dothideomycetidae Dothideales Saccotheciaceae Aureobasidium Aureobasidium pullulans (Black yeast) (Pullularia pullulans)
Enzyme Sequence MKFFATIAALVVGAVAAPVAEAEAEASSPMLIERAGPGGINYVQNYNGNLGQFTYNENAGTYSMYWNNGVNGDFVVGLGWSTGAARSITYSSNYQASGGSYLSVYGWINSPQAEYYIVESYGSYNPCGAGQSGVTQLGTVCSDGATYTVYTDTRTNQPSITGTSTFKQYWSVRQTKRTSGTVTTGNHFAYWAKYGFGNSYNFQVMPVEAFSGTGSASVTVS
Enzyme Length 221
Uniprot Accession Number Q12562
Absorption
Active Site ACT_SITE 114; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 208; /note=Proton donor; /evidence=ECO:0000250
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; Evidence={ECO:0000269|PubMed:8572698};
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.
Temperature Dependency
PH Dependency
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;Secreted;Signal;Xylan degradation
Interact With
Induction INDUCTION: Expressed in cultures grown in medium containing D-xylose or oat spelt xylan. Transcription is completely repressed in the presence of glucose. {ECO:0000269|PubMed:10585539, ECO:0000269|PubMed:7944361}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8572698}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..16; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 23,531
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda