CATH Classification

Domain Context

CATH Clusters

Superfamily Alpha-D-phosphohexomutase, C-terminal domain
Functional Family Phosphomannomutase/phosphoglucomutase

Enzyme Information

5.4.2.8
Phosphomannomutase.
based on mapping to UniProt P26276
Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.
-!- Alpha-D-mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor. -!- Formerly EC 2.7.5.7.
5.4.2.2
Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent).
based on mapping to UniProt P26276
Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
-!- Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. -!- This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. -!- Also, more slowly, catalyzes the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. -!- Cf. EC 5.4.2.5. -!- Formerly EC 2.7.5.1.

UniProtKB Entries (1)

P26276
ALGC_PSEAE
Pseudomonas aeruginosa PAO1
Phosphomannomutase/phosphoglucomutase

PDB Structure

PDB 4MRQ
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Promotion of enzyme flexibility by dephosphorylation and coupling to the catalytic mechanism of a phosphohexomutase.
Lee, Y., Villar, M.T., Artigues, A., Beamer, L.J.
J.Biol.Chem.