mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]

mannose-1-phosphate guanyltransferase; Provisional

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis].

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose. GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes 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. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.

Mannose-6-phosphate isomerase. All of the members of this Pfam entry belong to family 2 of the mannose-6-phosphate isomerases. The type II phosphomannose isomerases are bifunctional enzymes. This Pfam entry covers the isomerase domain. The guanosine diphospho-D-mannose pyrophosphorylase domain is in another Pfam entry, see pfam00483.

Crystalstructure of mannose-6-phosphate isomerase from Helicobacter pylori [Helicobacter pylori 26695],2QH5_B Crystal structure of mannose-6-phosphate isomerase from Helicobacter pylori [Helicobacter pylori 26695]

Crystalstructure of mannose-1-phosphate geranyltransferase from Thermus thermophilus HB8 [Thermus thermophilus HB8]

Crystalstructure of T. maritima GDP-mannose pyrophosphorylase in apo state. [Thermotoga maritima MSB8],2X5S_B Crystal structure of T. maritima GDP-mannose pyrophosphorylase in apo state. [Thermotoga maritima MSB8],2X5Z_A Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with GDP-mannose. [Thermotoga maritima MSB8],2X5Z_B Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with GDP-mannose. [Thermotoga maritima MSB8],2X60_A Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with GTP. [Thermotoga maritima MSB8],2X60_B Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with GTP. [Thermotoga maritima MSB8],2X65_A Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with mannose-1-phosphate. [Thermotoga maritima MSB8],2X65_B Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with mannose-1-phosphate. [Thermotoga maritima MSB8]

Xanthan biosynthesis protein XanB OS=Xanthomonas campestris pv. campestris (strain B100) OX=509169 GN=xanB PE=3 SV=1

Xanthan biosynthesis protein XanB OS=Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) OX=190485 GN=xanB PE=3 SV=1

Mannose-1-phosphate guanylyltransferase 1 OS=Escherichia coli O157:H7 OX=83334 GN=manC1 PE=1 SV=1

Mannose-1-phosphate guanylyltransferase OS=Escherichia coli (strain K12) OX=83333 GN=manC PE=3 SV=3

Mannose-1-phosphate guanylyltransferase ManC OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=manC PE=3 SV=1