Detail Information for IndEnz0008000532
IED ID IndEnz0008000532
Enzyme Type ID cellulase000532
Protein Name Probable endo-1,4-beta-xylanase B
Xylanase B
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase B
Endo-1,4-beta-xylanase G1
Xylanase G1
Gene Name xlnB xynB xynG1 ACLA_085410
Organism Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus clavatus Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
Enzyme Sequence MVSFSSLALALSTVVGVLAAPGSEKYVELAKHQLTHSQTGTKNGYYYSFWTDNRGQVSYTNGKGGQYSVNWKDCGNFVAGKGWNPASAKTVTYSGNWKPSGNSYVSVYGWTQNPLIEFYIVESFGSYNPSTGATELGTVESDGGTYKIYKTKRVDAPSIEGKKTFDQFWSVRTSHRVGGTVTTKNHFNAWAKSGLKLGTFNYMILATEGYHSSGSATMTVS
Enzyme Length 221
Uniprot Accession Number A1CU59
Absorption
Active Site ACT_SITE 117; /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;
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:0000250}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan degradation; xylan degradation.
nucleotide Binding
Features Active site (2); Chain (1); Domain (1); Erroneous initiation (1); Signal peptide (1)
Keywords Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Signal;Xylan degradation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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 24,058
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda