IED ID | IndEnz0008000440 |
Enzyme Type ID | cellulase000440 |
Protein Name |
Bifunctional xylanase/xylan deacetylase XYLE Includes: Endo-1,4-beta-xylanase Xyn11A Xylanase 11A EC 3.2.1.8 ; Acetylxylan deacetylase EC 3.1.1.72 |
Gene Name | xyn11A xynE |
Organism | Cellvibrio japonicus (Pseudomonas fluorescens subsp. cellulosa) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Cellvibrionales Cellvibrionaceae Cellvibrio Cellvibrio japonicus (Pseudomonas fluorescens subsp. cellulosa) |
Enzyme Sequence | MKLPTLGKCVVRTLMGAVALGAISVNAQTLSSNSTGTNNGFYYTFWKDSGDASMTLLSGGRYQSSWGNSTNNWVGGKGWNPGNNSRVISYSGSYGVDSSQNSYLALYGWTRSPLIEYYVIESYGSYNPASCSGGTDYGSFQSDGATYNVRRCQRVNQPSIDGTQTFYQYFSVRNPKKGFGNISGTITFANHVNFWASKGLNLGNHNYQVLATEGYQSRGSSDITVSEGTSGGGTSSVGGASSSVNSSTGGGSSGGITVRARGANGSEHINLRVGGAVVANWTLGTSFQNYLYSGNASGDIQVQFDNDASGRDVVVDYIIVNGETRQAEDMEHNSAVYANGRCGGGSYSENMHCNGEIGFGYTYDCFSGNCSGGNGGSNSSAGNSSSGNTGGGGSNCSGYVGITFDDGPNSNTATLVNLLRQNNLTPVTWFNQGNNVASNAHLMSQQLSVGEVHNHSYTHPHMTSWTYQQVYDELNRTNQAIQNAGAPKPTLFRPPYGELNSTIQQAAQALGLRVVTWDVDSQDWNGASAAAIANAANQLQNGQVILMHDGSYTNTNSAIAQIATNLRAKGLCPGRIDPNTGRAVAPSSSGGSSSVALSSSSRSSSSAGGNTGGNCQCNWWGTFYPLCQTQTSGWGWENSRSCISTSTCNSQGTGGGGVVCN |
Enzyme Length | 661 |
Uniprot Accession Number | Q59674 |
Absorption | |
Active Site | ACT_SITE 116; /note=Nucleophile; for endoxylanase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 213; /note=Proton donor; for endoxylanase activity; /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; Evidence={ECO:0000269|PubMed:7492333}; CATALYTIC ACTIVITY: Reaction=Deacetylation of xylans and xylo-oligosaccharides.; EC=3.1.1.72; Evidence={ECO:0000269|PubMed:7492333}; |
DNA Binding | |
EC Number | 3.2.1.8; 3.1.1.72 |
Enzyme Function | FUNCTION: Endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides. Is able to hydrolyze oat spelt xylan and the arabinoxylans from wheat and rye, releasing xylobiose as the major product. Also likely catalyzes, via its C-terminal domain, the removal of acetyl groups from acetylated xylan. Thus, has the capability of hydrolyzing acetylated xylan. Does not attack mannan, galactan, arabinan or any cellulosic substrates. {ECO:0000269|PubMed:12107129, ECO:0000269|PubMed:7492333}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Glycan degradation; xylan degradation. |
nucleotide Binding | |
Features | Active site (2); Chain (1); Compositional bias (2); Domain (3); Region (3); Signal peptide (1) |
Keywords | Carbohydrate metabolism;Glycosidase;Hydrolase;Multifunctional enzyme;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
Interact With | |
Induction | INDUCTION: Induced when the bacterium is cultured on xylan or beta-glucan but not on medium containing mannan. Is repressed by glucose. Transcription of xyn11A occurs in early exponential phase, and thus earlier than transcription of xyn11B. {ECO:0000269|PubMed:12107129}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12107129}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 69,193 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |