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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | Phosphoglucomutases interconvert D-glucose 1-phosphate and D-glucose 6-phosphate, a reaction which is important for energy metabolism in many organisms and for cell wall biosynthesis in bacteria [ , ]. Beta-phosphoglucomutases are monomeric enzymes which interconvert the beta anomers of these compounds using Mg2+ as a cofactor.This entry groups together three clades: the characterised beta-phosphoglucomutases (bPGMs) (including those from Escherichia coli, Bacillus subtilis and Lactococcus lactis, a clade of putative bPGMs from mycobacteria and a clade including the uncharacterised E. coli and Haemophilus influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the 'variant 3' Glu-Asp version of the third conserved HAD domain.The Lactococcus enzyme has been crystallised and studied in detail [ ]. It is composed of two distinct regions, an α/β core domain similar to that found in other HAD family members, and a helical cap domain. The core domain contains a central six-stranded parallel β sheet surrounded by six α helices, while the cap domain consists of an antiparallel four α-helix bundle. Overall, the monomer forms a "kidney-bean"shape similar to that observed in other HAD family members such as phosphoserine phosphatase. The active site of the enzyme is located at the interface of the two domains. | Name | Beta-phosphoglucomutase hydrolase |
| Short Name | B-phosphoglucomutase_hydrolase | Type | Domain |
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