InterPro : IPR019490

Name  Bifunctional glucose-6-phosphate/mannose-6-phosphate isomerase, C-terminal Short Name  Glu6P/Mann6P_isomerase_C
Type  Domain Description  Phosphoglucose isomerase (PGI) catalyses the interconversion of phosphoglucose and phosphofructose, and is a component of many sugar metabolic pathways. In some archaea and bacteria PGI activity occurs via a bifunctional enzyme that also exhibits phosphomannose isomerase (PMI) activity. Though not closely related to eukaryotic PGIs, the bifunctional enzyme is similar enough that the sequence includes the cluster of threonines and serines that forms the sugar phosphate-binding site in conventional PGI. This entry represents the C-terminal half of the bifunctional PGI/PMI enzyme, which contains many of the active catalytic site residues. The enzyme is thought to use the same catalytic mechanisms for both glucose ring-opening and isomerisation for the interconversion of glucose 6-phosphate to fructose 6-phosphate [].
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1 Found In

Id Name Short Name Type
IPR011857 Bifunctional glucose-6-phosphate/mannose-6-phosphate isomerase Glu6P/Mann6P_isomerase Family

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1 Publications

First Author Title Year Journal Volume Pages
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)