Detail Information for IndEnz0004000212
IED ID IndEnz0004000212
Enzyme Type ID xylanase000212
Protein Name Bifunctional xylanase/deacetylase
Includes: Endo-1,4-beta-xylanase D
XYLD
Xylanase D
EC 3.2.1.8
; Acetylated xylan deacetylase
EC 3.5.1.-
Gene Name xynD
Organism Cellulomonas fimi
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Micrococcales Cellulomonadaceae Cellulomonas Cellulomonas fimi
Enzyme Sequence MSDSFEATRTTRRRRPLQALTGLLAAGALVAGALAAASPAAAAVTSNTTGTHDGYFYSFWTDSPGSVSMDLNSGGGYTRWSNTGNFVAGKGWSTGGRKTVSYSGQFNPSRNAYLTLYGWTQSPLVEYYIVDSWGTYRPTGTFMGTVTSDGGTYDIYRTQRVNKPSIEGDSSTFYQYWSVRQQKRTGGTITSGNHFDAWASKGMNLGRHNYMIMATEGYQSSGSSSITVSEGSGGGGGGDTGGGGGSTGCSVTATRAEEWSDRFNVTYSVSGSSAWTVNLALNGSQTIQASWNANVTGSGSTRTVTPNGSGNTFGVTVMKNGSSTTPAATCAGSGGGTATPTPTPTPTPTPQSCSAGYVGLTFDDGPNTGTTNQILSTLTQYGATATVFPTGQNAQGNPSLMQAYKNAGVQIGNHSWDHPHLVNMSQSDMQSQLTRTQQAIQQTAGVTPTLFRPPYGESNATLRQVESSLGLREIIWDVDSQDWNNASASQIRQAASRLTNGQIILMHDWPAATVQALPGILQDLRSRNLCTGHISSSTGRAVAPSSAGGGGGGGGGTGSCSVSAVRGEEWADRFNVTYSVSGSSSWVVTLGLNGGQSVQSSWNAALTGSSGTVTARPNGSGNSFGVTFYKNGSSATPGATCATG
Enzyme Length 644
Uniprot Accession Number P54865
Absorption
Active Site ACT_SITE 126; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 216; /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; 3.5.1.-
Enzyme Function FUNCTION: Endo-acting xylanase which displays no detectable activity against polysaccharides other than xylan. Hydrolyzes glucosidic bonds with retention of anomeric configuration.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan degradation; xylan degradation.
nucleotide Binding
Features Active site (2); Beta strand (16); Chain (1); Domain (4); Region (6); Signal peptide (1)
Keywords 3D-structure;Carbohydrate metabolism;Glycosidase;Hydrolase;Multifunctional enzyme;Polysaccharide degradation;Repeat;Signal;Xylan degradation
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..43; /evidence=ECO:0000255
Structure 3D NMR spectroscopy (6)
Cross Reference PDB 1E5B; 1E5C; 1HEH; 1HEJ; 1XBD; 2XBD;
Mapped Pubmed ID 10425686; 10973978; 11327868;
Motif
Gene Encoded By
Mass 66,582
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.8;