| Type: | Family | Name: | Bifunctional glucose-6-phosphate/mannose-6-phosphate isomerase |
| Description: | 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 [].These bifunctional isomerases form a distinct phylogenetic cluster within the larger phosphoglucose isomerase (PGI) superfamily []. They show relatively low sequence identity to other PGIs, but contain similar structural elements and show almost complete conservation of the catalytic residues in the active site, indicating they use a similar catalytic mechanism []. The family appears to have originated in the archaea, with the bacterial proteins being acquired through horizontal transfer. | Short Name: | Glu6P/Mann6P_isomerase |
| GO Term | Gene Name |
|---|---|
| GO:0004347 | IPR011857 |
| GO:0004476 | IPR011857 |
| GO:0005975 | IPR011857 |
| DB identifier | UniProt Accession | Secondary Identifier | Organism Name | Length |
|---|---|---|---|---|
| Pp3s34_500V3.1.p | PAC:32948304 | Physcomitrium patens |
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