InterPro : IPR011857

Name  Bifunctional glucose-6-phosphate/mannose-6-phosphate isomerase Short Name  Glu6P/Mann6P_isomerase
Type  Family 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.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

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0 Child Features

2 Contains

Id Name Short Name Type
IPR001347 Sugar isomerase (SIS) SIS Domain
IPR019490 Bifunctional glucose-6-phosphate/mannose-6-phosphate isomerase, C-terminal Glu6P/Mann6P_isomerase_C Domain

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4 Publications

First Author Title Year Journal Volume Pages
Proudfoot AE Purification, cDNA cloning and heterologous expression of human phosphomannose isomerase. 1994 Eur J Biochem 219 415-23
Clissold PM JmjC: cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta. 2001 Trends Biochem Sci 26 7-9
Hansen T Bifunctional phosphoglucose/phosphomannose isomerases from the Archaea Aeropyrum pernix and Thermoplasma acidophilum constitute a novel enzyme family within the phosphoglucose isomerase superfamily. 2004 J Biol Chem 279 2262-72
Swan MK A novel phosphoglucose isomerase (PGI)/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum is a member of the PGI superfamily: structural evidence at 1.16-A resolution. 2004 J Biol Chem 279 39838-45



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)