IPR049577
GDP-mannose pyrophosphorylase, N-terminal domain
InterPro entry
Short name | GMPP_N |
Overlapping homologous superfamilies | |
domain relationships |
Description
This entry represents the N-terminal domain of GDP-mannose-1-phosphate guanylyltransferase, also known as GDP-mannose pyrophosphorylase (GDP-MP). GDP-MP catalyses the formation of GDP-mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. The isomerase function of these members is located at the C-terminal half (
IPR001538)
[4, 5, 2, 1, 3].
References
1.An evolving hierarchical family classification for glycosyltransferases. Coutinho PM, Deleury E, Davies GJ, Henrissat B. J. Mol. Biol. 328, 307-17, (2003). View articlePMID: 12691742
2.A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities Campbell JA, Davies GJ, Bulone V V, Henrissat B. Biochem. J. 329 (Pt 3), 719, (1998). View articlePMID: 9445404
3.Conserved domains of glycosyltransferases. Kapitonov D, Yu RK. Glycobiology 9, 961-78, (1999). View articlePMID: 10521532
GO terms
biological process
- None
molecular function
cellular component
- None
Cross References
Contributing Member Database Entry
- CDD:cd02509