v5.1.0.3
Glycine data from LIS
Type | Domain |
Description | This entry represents a SurE-like structural domain with a 3-layer alpha/bete/alpha topology that bears some topological similarity to the N-terminal domain of the glutaminase/asparaginase family. This domain is found in the stationary phase survival protein SurE, a metal ion-dependent phosphatase found in eubacteria, archaea and eukaryotes. In Escherichia coli, SurE also has activity as a nucleotidase and exopolyphosphatase, and may be involved in the stress response []. E. coli cells with mutations in the surE gene survive poorly in stationary phase []. The structure of SurE homologues have been determined from Thermotoga maritima [] and the archaea Pyrobaculum aerophilum []. The T. maritima SurE homologue has phosphatase activity that is inhibited by vanadate or tungstate, both of which bind adjacent to the divalent metal ion. |
Short Name | SurE-like_Pase/nucleotidase |