The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Three monophyletic superfamilies account for the majority of the known glycosyltransferases
Open accessAbstract
Sixty‐five families of glycosyltransferases (EC 2.4.x.y) have been recognized on the basis of high‐sequence similarity to a founding member with experimentally demonstrated enzymatic activity. Although distant sequence relationships between some of these families have been reported, the natural history of glycosyltransferases is poorly understood. We used iterative searches of sequence databases, motif extraction, structural comparison, and analysis of completely sequenced genomes to track the origins of modern‐type glycosyltransferases. We show that >75% of recognized glycosyltransferase families belong to one of only three monophyletic superfamilies of proteins, namely, (1) a recently described GPGTF/GT‐B superfamily; (2) a nucleoside‐diphosphosugar transferase (GT‐A) superfamily, which is characterized by a DxD sequence signature and also includes nucleotidyltransferases; and (3) a GT‐C superfamily of integral membrane glycosyltransferases with a modified DxD signature in the first extracellular loop. Several developmental regulators in Metazoans, including Fringe and Egghead homologs, belong to the second superfamily. Interestingly, Tout‐velu/Exostosin family of developmental proteins found in all multicellular eukaryotes, contains separate domains belonging to the first and the second superfamilies, explaining multiple glycosyltransferase activities in one protein.
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Cites
Did DNA replication evolve twice independently?
Leipe, D. D., Aravind, L., & Koonin, E. V. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.17.3389 · Cited by 351 · cited 2×
“…a nucleotidyltransferase involved in copying its genomic nucleic acid; it has been proposed that such copying proceeded via an RNA intermediate (Leipe et al. 1999), and that said nucleotidyltransferase more than likely was of the palm-domain ferredoxin-like fold, consisting of four- or…”
BackgroundNAD-binding domains of dehydrogenases
Lesk, A. M. (1995) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(95)80010-7 · Cited by 239
Aravind, L., Anantharaman, V., & Koonin, E. V. (2002) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10064 · Cited by 153 · cited 4×
“…has been proposed that such copying proceeded via an RNA intermediate (Leipe et al. 1999), and that said nucleotidyltransferase more than likely was of the palm-domain ferredoxin-like fold, consisting of four- or five-stranded -sheet with two -helices packed against one side (Aravind et al. 2002b).”
BackgroundInfluential
Cited by
Glycosyltransferases: Structures, Functions, and Mechanisms
Lairson, L. L., Henrissat, B., Davies, G. J., & Withers, S. G. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.061005.092322 · Cited by 2,079
Natural Products Version 2.0: Connecting Genes to Molecules
Walsh, C. T., & Fischbach, M. A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja909118a · Cited by 468
How pathogenic bacteria evade mammalian sabotage in the battle for iron
Fischbach, M. A., Lin, H., Liu, D. R., & Walsh, C. T. (2006) · Nature Chemical Biology · doi:10.1038/nchembio771 · Cited by 321
Natural history of S-adenosylmethionine-binding proteins
Kozbial, P. Z., & Mushegian, A. R. (2005) · BMC Structural Biology · doi:10.1186/1472-6807-5-19 · Cited by 297
Self-citationBiosynthesis, Remodelling and Functions of Mammalian GPI-anchored Proteins: Recent Progress
Kinoshita, T., Fujita, M., & Maeda, Y. (2008) · Journal of Biochemistry · doi:10.1093/jb/mvn090 · Cited by 276
Metadata
- Authors
- Liu, J., & Mushegian, A.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2003-07
- Volume
- 12
- Issue
- 7
- Pages
- 1418-1431
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W2095529535
- Cited by
- 234
- References
- 3
- FWCI
- 2.79
- Type
- journal article
- Language
- en
- Open access
- green
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