|Protein name||Bifunctional xylanase/deacetylase||endo-1,4-beta-xylanase (EC 184.108.40.206)endo-(1->4)-beta-xylan 4-xylanohydrolase (EC 220.127.116.11)endo-1,4-xylanase (EC 18.104.22.168)xylanase (EC 22.214.171.124)beta-1,4-xylanase (EC 126.96.36.199)endo-1,4-xylanase (EC 188.8.131.52)endo-beta-1,4-xylanase (EC 184.108.40.206)endo-1,4-beta-D-xylanase (EC 220.127.116.11)1,4-beta-xylan xylanohydrolase (EC 18.104.22.168)beta-xylanase (EC 22.214.171.124)beta-1,4-xylan xylanohydrolase (EC 126.96.36.199)endo-1,4-beta-xylanase (EC 188.8.131.52)beta-D-xylanase (EC 184.108.40.206)|
|Includes||Endo-1,4-beta-xylanase D(Xylanase D)(XYLD) EC 220.127.116.11Acetylated xylan deacetylase EC 3.5.1.-|
|CAZy||GH11 (Glycoside Hydrolase Family)|
|Activity||Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.|
|Authors||Gilkes NR, Henrissat B, Kilburn DG, Miller RC Jr, Warren RA|
|Title||Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.|
|Authors||Millward-Sadler SJ, Poole DM, Henrissat B, Hazlewood GP, Clarke JH, Gilbert HJ|
|Title||Evidence for a general role for high-affinity non-catalytic cellulose binding domains in microbial plant cell wall hydrolases.|
|Authors||Black GW, Hazlewood GP, Millward-Sadler SJ, Laurie JI, Gilbert HJ|
|Title||A modular xylanase containing a novel non-catalytic xylan-specific binding domain.|
|Journal||Structure Fold Des|
|Authors||Simpson PJ, Bolam DN, Cooper A, Ciruela A, Hazlewood GP, Gilbert HJ, Williamson MP|
|Title||A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity.|
|Authors||Bolam DN, Xie H, White P, Simpson PJ, Hancock SM, Williamson MP, Gilbert HJ|
|Title||Evidence for synergy between family 2b carbohydrate binding modules in Cellulomonas fimi xylanase 11A.|
|Authors||Xie H, Bolam DN, Nagy T, Szabo L, Cooper A, Simpson PJ, Lakey JH, Williamson MP, Gilbert HJ|
|Title||Role of hydrogen bonding in the interaction between a xylan binding module and xylan.|
|This enzyme belongs to glycosidase family-11.|
This enzyme is composed of four domains: the N-terminal catalytic domain, another catalytic domain, which is located between two xylan domains. However, the structures of the catalytic domains have not been determined yet, although those of its homologous enzymes have been solved.
Moreover, this enzyme is a bifunctional enzyme with deacetylase activity for acetylated xylan (E.C. 3.5.1.-), according to the Uniprot information. However, the E.C. number seems to be for amide hydrolysis, although it is for ester bonds.
The N-terminal catalytic domain is for endo-1,4-beta-xylanase (18.104.22.168), whereas the other catalytic domain seems to be for deacetylase (3.5.1.-).