Detail Information for IndEnz0011000496
IED ID IndEnz0011000496
Enzyme Type ID glucanase000496
Protein Name Arabinoxylan arabinofuranohydrolase
AXH
EC 3.2.1.55
AXH-m2,3
AXH-m23
Alpha-L-arabinofuranosidase
AF
Gene Name xynD
Organism Paenibacillus polymyxa (Bacillus polymyxa)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Paenibacillaceae Paenibacillus Paenibacillus polymyxa (Bacillus polymyxa)
Enzyme Sequence MIRKCLVLFLSFALLLSVFPMLNVDAANRPLAKIPGNSNPLMDHKLGADPYSLVYDGRVYIFMSSDTYVYNKDGSIKENDFSALDRIQVISSTDMVNWTDHGTIPVAGANNKNSGRGIAKWASNSWAPAVAHKKINGRDKFFLYFANGGAGIGVLTADTPIGPWTDPLGKALVTHSTPGMAGVTWLFDPAVLVDDDGTGYLYSGGGIPNESDPASIANPKTARVIKLGADMTSVIGSATTIDAPYLFEDSGIHKYNGKYYYSYCINFAGTHPQQYPAGEIGYMVSDNPMGPFTYKGHFLKNPYTFFGVGGNNHHAVFNFKNEWYVVYHAQTVSKAQIGAGKGYRSPHINKLVHKEDGSISEVQGNMTGIAQLSNMNPYTRVEAETIAWQAGVTTEPTQASGGPISNLNVTNIHNGDWIAVGKADFGSAGAKTFKANVATNVGGNIEVRLDSETGPLVGSLKVPSTGGMQTWREVETTINNATGVHNIYLVFTGSGSGNLLNLDAWQFTPNTGGNTITKVEAENMKIGGTYAGKISAPFDGVALYANADYVSYSQYFANSTHNISVRGASSNAGTAKVDLVIGGVTVGSFNFTGKTPTVQTLSNITHATGDQEIKLALTSDDGTWDAYVDFIEFSL
Enzyme Length 635
Uniprot Accession Number P45796
Absorption
Active Site ACT_SITE 49; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q45071; ACT_SITE 248; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q45071
Activity Regulation ACTIVITY REGULATION: Activated by calcium and magnesium. Inhibited by copper. {ECO:0000269|PubMed:8579824}.
Binding Site BINDING 311; /note=Substrate; /evidence=ECO:0000250
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.; EC=3.2.1.55;
DNA Binding
EC Number 3.2.1.55
Enzyme Function FUNCTION: Cleaves arabinose units from O-2- or O-3-monosubstituted xylose residues, thereby assisting in arabinoxylan (AX) and short-chain arabinoxylo-oligosaccharide (AXOS) degradation (By similarity). Preferres wheat flour xylan over oat spelt xylan as substrate. Does not display endoxylanase activity. {ECO:0000250, ECO:0000269|PubMed:8579824}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:8579824};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:8579824};
Pathway PATHWAY: Glycan degradation; xylan degradation.
nucleotide Binding
Features Active site (2); Beta strand (10); Binding site (1); Chain (1); Domain (2); Helix (1); Metal binding (15); Signal peptide (1); Site (1)
Keywords 3D-structure;Calcium;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding;Polysaccharide degradation;Repeat;Secreted;Signal;Xylan degradation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..26; /evidence=ECO:0000269|PubMed:8579824
Structure 3D X-ray crystallography (2)
Cross Reference PDB 1UX7; 1W0N;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 67,914
Kinetics
Metal Binding METAL 382; /note=Calcium 1; structural; /evidence=ECO:0000250; METAL 384; /note=Calcium 1; structural; /evidence=ECO:0000250; METAL 406; /note=Calcium 1; structural; /evidence=ECO:0000250; METAL 407; /note=Calcium 1; via carbonyl oxygen; structural; /evidence=ECO:0000250; METAL 503; /note=Calcium 1; structural; /evidence=ECO:0000250; METAL 503; /note=Calcium 1; via carbonyl oxygen; structural; /evidence=ECO:0000250; METAL 520; /note=Calcium 2; structural; METAL 522; /note=Calcium 2; structural; METAL 539; /note=Calcium 2; via carbonyl oxygen; structural; METAL 544; /note=Calcium 3; via carbonyl oxygen; structural; METAL 620; /note=Calcium 3; METAL 624; /note=Calcium 3; via carbonyl oxygen; structural; METAL 625; /note=Calcium 3; METAL 629; /note=Calcium 2; structural; METAL 629; /note=Calcium 2; via carbonyl oxygen; structural
Rhea ID
Cross Reference Brenda 3.2.1.8;