Detail Information for IndEnz0008000180
IED ID IndEnz0008000180
Enzyme Type ID cellulase000180
Protein Name Reducing end xylose-releasing exo-oligoxylanase
RexA
EC 3.2.1.156
Gene Name xylA BAD_0300
Organism Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Bifidobacteriales Bifidobacteriaceae Bifidobacterium Bifidobacterium adolescentis Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a)
Enzyme Sequence MTNATDTNKTLGESMFAQCGYAQDAIDKRVSQVWHEIFEGPNKFYWENDEGLAYVMDTGNNDVRTEGMSYAMMIALQYDRKDVFDKLWGWVMRHMYMKDGHHAHYFAWSVAPDGTPNSNGPAPDGEEYFAMDLFLASRRWGDGEDIYEYSAWGREILRYCVHKGERYDGEPMWNPDNKLIKFIPETEWSDPSYHLPHFYEVFAEEADEEDRPFWHEAAAASRRYLQAACDERTGMNAEYADYDGKPHVDESNHWHFYSDAYRTAANIGLDAAWNGPQEVLCDRVAALQRFFLTHDRTSVYAIDGTAVDEVVLHPVGFLAATAQGALAAVHSAQPDAEHNAREWVRMLWNTPMRTGTRRYYDNFLYAFAMLALSGKYRYE
Enzyme Length 379
Uniprot Accession Number A1A048
Absorption
Active Site ACT_SITE 66; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:A0A0S2UQQ5; ACT_SITE 259; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:A0A0S2UQQ5
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-xylose residues from the reducing end of oligosaccharides.; EC=3.2.1.156; Evidence={ECO:0000269|PubMed:17586675};
DNA Binding
EC Number 3.2.1.156
Enzyme Function FUNCTION: Hydrolyzes xylooligosaccharides with a degree of polymerization of greater than or equal to 3, releasing xylose from the reducing end. Has low activity on birchwood xylan, oat spelt xylan and arabinoxylan. {ECO:0000269|PubMed:17586675}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. Stable up to 40 degrees Celsius. {ECO:0000269|PubMed:17586675};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. Stable between pH 4.0 and 10.0 for 120 minutes. {ECO:0000269|PubMed:17586675};
Pathway
nucleotide Binding
Features Active site (2); Chain (1)
Keywords Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Xylan degradation
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 43,785
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.156;