The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

Alpha-D-phosphohexomutase, C-terminal domain

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 7: Phosphomannomutase/phosphoglucomutase

There are 2 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Phosphomannomutase. [EC:]
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
10 A0A2V3FAA0 A0A2V3FAA0 A0A2V3FAA0 P26276 P26276 P26276 Q02E40 Q02E40 Q02E40 Q88BD4
Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent). [EC:]
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
  • Formerly EC
10 A0A2V3FAA0 A0A2V3FAA0 A0A2V3FAA0 P26276 P26276 P26276 Q02E40 Q02E40 Q02E40 Q88BD4