IED ID | IndEnz0008000602 |
Enzyme Type ID | cellulase000602 |
Protein Name |
Endo-1,4-beta-xylanase Z Xylanase Z EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase Z |
Gene Name | xynZ Cthe_1963 |
Organism | Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Oscillospiraceae Acetivibrio Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum) Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum) |
Enzyme Sequence | MSRKLFSVLLVGLMLMTSLLVTISSTSAASLPTMPPSGYDQVRNGVPRGQVVNISYFSTATNSTRPARVYLPPGYSKDKKYSVLYLLHGIGGSENDWFEGGGRANVIADNLIAEGKIKPLIIVTPNTNAAGPGIADGYENFTKDLLNSLIPYIESNYSVYTDREHRAIAGLSMGGGQSFNIGLTNLDKFAYIGPISAAPNTYPNERLFPDGGKAAREKLKLLFIACGTNDSLIGFGQRVHEYCVANNINHVYWLIQGGGHDFNVWKPGLWNFLQMADEAGLTRDGNTPVPTPSPKPANTRIEAEDYDGINSSSIEIIGVPPEGGRGIGYITSGDYLVYKSIDFGNGATSFKAKVANANTSNIELRLNGPNGTLIGTLSVKSTGDWNTYEEQTCSISKVTGINDLYLVFKGPVNIDWFTFGVESSSTGLGDLNGDGNINSSDLQALKRHLLGISPLTGEALLRADVNRSGKVDSTDYSVLKRYILRIITEFPGQGDVQTPNPSVTPTQTPIPTISGNALRDYAEARGIKIGTCVNYPFYNNSDPTYNSILQREFSMVVCENEMKFDALQPRQNVFDFSKGDQLLAFAERNGMQMRGHTLIWHNQNPSWLTNGNWNRDSLLAVMKNHITTVMTHYKGKIVEWDVANECMDDSGNGLRSSIWRNVIGQDYLDYAFRYAREADPDALLFYNDYNIEDLGPKSNAVFNMIKSMKERGVPIDGVGFQCHFINGMSPEYLASIDQNIKRYAEIGVIVSFTEIDIRIPQSENPATAFQVQANNYKELMKICLANPNCNTFVMWGFTDKYTWIPGTFPGYGNPLIYDSNYNPKPAYNAIKEALMGY |
Enzyme Length | 837 |
Uniprot Accession Number | P10478 |
Absorption | |
Active Site | ACT_SITE 645; /note=Proton donor; ACT_SITE 754; /note=Nucleophile |
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 |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (21); Chain (1); Disulfide bond (1); Domain (3); Helix (23); Signal peptide (1); Turn (7) |
Keywords | 3D-structure;Carbohydrate metabolism;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Signal;Xylan degradation |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (3) |
Cross Reference PDB | 1JJF; 1JT2; 1XYZ; |
Mapped Pubmed ID | 11601976; 16127726; |
Motif | |
Gene Encoded By | |
Mass | 92,263 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.1.1.73;3.2.1.73;3.2.1.8; |