气候变化领域集成服务门户(CCPortal): Glycoconjugate pathway connections revealed by sequence similarity network analysis of the monotopic phosphoglycosyl transferases

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DOI	10.1073/pnas.2018289118
	Glycoconjugate pathway connections revealed by sequence similarity network analysis of the monotopic phosphoglycosyl transferases
	O’Toole K.H.; Imperiali B.; Allen K.N.
发表日期	2021
ISSN	00278424
卷号	118 期号:4
英文摘要	The monotopic phosphoglycosyl transferase (monoPGT) superfamily comprises over 38,000 nonredundant sequences represented in bacterial and archaeal domains of life. Members of the superfamily catalyze the first membrane-committed step in en bloc oligosaccharide biosynthetic pathways, transferring a phosphosugar from a soluble nucleoside diphosphosugar to a membrane-resident polyprenol phosphate. The singularity of the monoPGT fold and its employment in the pivotal first membrane-committed step allows confident assignment of both protein and corresponding pathway. The diversity of the family is revealed by the generation and analysis of a sequence similarity network for the superfamily, with fusion of monoPGTs with other pathway members being the most frequent and extensive elaboration. Three common fusions were identified: sugar-modifying enzymes, glycosyl transferases, and regulatory domains. Additionally, unexpected fusions of the monoPGT with members of the polytopic PGT superfamily were discovered, implying a possible evolutionary link through the shared polyprenol phosphate substrate. Notably, a phylogenetic reconstruction of the monoPGT superfamily shows a radial burst of functionalization, with a minority of members comprising only the minimal PGT catalytic domain. The commonality and identity of the fusion partners in the monoPGT superfamily is consistent with advantageous colocalization of pathway members at membrane interfaces. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Enzyme evolution; Glycan biosynthetic pathway; Membrane-associated pathway; Phylogenetic reconstruction; Sequence similarity network
语种	英语
scopus关键词	fusion protein; glycoconjugate; glycosyltransferase; phosphoglycosyltransferase; regulator protein; unclassified drug; acylation; Article; Campylobacter concisus; Campylobacter jejuni; crystal structure; Escherichia coli; glycosylation; membrane binding; Mycobacterium smegmatis; Neisseria gonorrhoeae; Neisseria meningitidis; network analysis; nonhuman; oxidation reduction reaction; phylogenetic tree; priority journal; protein domain; Salmonella enterica; Salmonella enterica serovar Pullorum; sequence similarity network analysis
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/180884
作者单位	Department of Chemistry, Boston University, Boston, MA 02215, United States; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, United States; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, United States
推荐引用方式 GB/T 7714	O’Toole K.H.,Imperiali B.,Allen K.N.. Glycoconjugate pathway connections revealed by sequence similarity network analysis of the monotopic phosphoglycosyl transferases[J],2021,118(4).
APA	O’Toole K.H.,Imperiali B.,&Allen K.N..(2021).Glycoconjugate pathway connections revealed by sequence similarity network analysis of the monotopic phosphoglycosyl transferases.Proceedings of the National Academy of Sciences of the United States of America,118(4).
MLA	O’Toole K.H.,et al."Glycoconjugate pathway connections revealed by sequence similarity network analysis of the monotopic phosphoglycosyl transferases".Proceedings of the National Academy of Sciences of the United States of America 118.4(2021).