| IED ID | IndEnz0004000189 |
| Enzyme Type ID | xylanase000189 |
| 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; |