{PDOC51659} {PS51659; GT23} {BEGIN} ******************************************************* * Glycosyltransferase family 23 (GT23) domain profile * ******************************************************* The fucosylation of glycoconjugates in mammalian organisms is related to a wide variety of biological preocesses, including cell adhesion, blood antigens, and some severe diseases including cancer metastasis, congenital disorders of glycosylation, and various microbial and virus infections. Fucosylation via alpha1,2-, alpha1,3- alpha1,4-, and alpha1,6-linkages, and protein O-fucosylation are accomplished by the cation of specific individual fucosyltransferases [1]. FUT8, a eukaryotic alpha1,6-fucosyltransferase, catalyzes the transfer of a fucosyl residue from guanine nucleotide diphosphate (GDP)-beta-L-fucose to the reducing terminal N-acetylglucosamine (GlcNAc) of asparagine-linked oligosaccharides (N-glycan). The catalytic domain of FUT8 is structurally similar to that of NodZ, a bacterial alpha1,6-fucosyltransferase. NodZ plays a role in the synthesis of the Nod factor, which is involved in the nodulation of legume roots for nitrogen fixing, and is known to catalyze the alpha1,6- fucosylation of lipo-chitooligosaccharides and variations thereof, including chitooligosaccharides. Both the eukaryotic and bacterial fucoslytransferase are classified into the GT23 family of Carbohydrate-Active enZYmes [E1] and share GDP-beta-L-fucose as the donor substrate. Although the acceptor substrates are different, a "common" chitobiose unit is contained in the reducing terminals of both substrates [2]. The GT23 domain is comprised of two structures, a N-terminal open sheet alpha/ beta structure and a C-terminal Rossmann fold which is frequently found in nucleotide binding proteins including glycosyltransferases (see ) [1,3,4]. The profile we developed covers the entire GT23 domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: October 2012 / First entry. [ 1] Ihara H., Ikeda Y., Toma S., Wang X., Suzuki T., Gu J., Miyoshi E., Tsukihara T., Honke K., Matsumoto A., Nakagawa A., Taniguchi N. "Crystal structure of mammalian alpha1,6-fucosyltransferase, FUT8." Glycobiology 17:455-466(2007). PubMed=17172260; DOI=10.1093/glycob/cwl079 [ 2] Ihara H., Hanashima S., Okada T., Ito R., Yamaguchi Y., Taniguchi N., Ikeda Y. "Fucosylation of chitooligosaccharides by human alpha1,6-fucosyltransferase requires a nonreducing terminal chitotriose unit as a minimal structure." Glycobiology 20:1021-1033(2010). PubMed=20466647; DOI=10.1093/glycob/cwq064 [ 3] Brzezinski K., Stepkowski T., Panjikar S., Bujacz G., Jaskolski M. "High-resolution structure of NodZ fucosyltransferase involved in the biosynthesis of the nodulation factor." Acta Biochim. Pol. 54:537-549(2007). PubMed=17762900 [ 4] Brzezinski K., Dauter Z., Jaskolski M. "Structures of NodZ alpha1,6-fucosyltransferase in complex with GDP and GDP-fucose." Acta Crystallogr. D 68:160-168(2012). PubMed=22281745; DOI=10.1107/S0907444911053157 [E1] http://www.cazy.org/GT23.html -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}