| Type: | Family | Name: | Mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase |
| Description: | This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase () (PMI) and mannose-1-phosphate guanylyltransferase () in Pseudomonas aeruginosa[], Xanthomonas campestris[, ], and Acetobacter xylinus. The literature on the enzyme from Escherichia coliattributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain lies at the C-terminal. Mannose-6-phosphate isomerase or phosphomannose isomerase (PMI) is the enzyme that catalyses the interconversion of mannose-6-phosphate and fructose-6-phosphate. In eukaryotes PMI is involved in the synthesis of GDP-mannose, a constituent of N- and O-linked glycans and GPI anchors and in prokaryotes it participates in a variety of pathways, including capsular polysaccharide biosynthesis and D-mannose metabolism. PMI's belong to the cupin superfamily whose functions range from isomerase and epimerase activities involved in the modification of cell wall carbohydrates in bacteria and plants, to non-enzymatic storage proteins in plant seeds, and transcription factors linked to congenital baldness in mammals []. Three classes of PMI have been defined []. | Short Name: | Man1P_GuaTrfase/Man6P_Isoase |
