D
IPR049577

GDP-mannose pyrophosphorylase, N-terminal domain

InterPro entry
Short nameGMPP_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

4.Bifunctional phosphomannose isomerase/GDP-D-mannose pyrophosphorylase is the point of control for GDP-D-mannose biosynthesis in Helicobacter pylori. Wu B, Zhang Y, Zheng R, Guo C, Wang PG. FEBS Lett 519, 87-92, (2002). PMID: 12023023

5.Purification of GTP:alpha-D-mannose-1-phosphate guanyltransferase. Smoot JW, Serif GS. Eur J Biochem 148, 83-7, (1985). PMID: 2983993

GO terms

biological process

  • None

cellular component

  • None

Cross References

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