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CATH Superfamily 3.40.50.1240

Phosphoglycerate mutase-like

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:

"
Phosphoglycerate mutase-like
".

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: Phosphoglycerate mutase

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
Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). [EC: 5.4.2.11]
2-phospho-D-glycerate = 3-phospho-D-glycerate.
  • The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor.
  • The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His(10) in man and Escherichia coli, His(8) in Saccharomyces cerevisiae).
  • This phosphate can be transferred to the free OH of 2-phospho-D- glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine.
  • Cf. EC 5.4.2.12.
  • The enzyme has no requirement for metal ions.
  • This enzyme also catalyze, slowly, the reactions of EC 5.4.2.4.
  • Formerly EC 2.7.5.3 and EC 5.4.2.1.
 505 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58
(495 more...)
Bisphosphoglycerate mutase. [EC: 5.4.2.4]
3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate.
  • In the direction shown, the enzyme is phosphorylated by 3-phosphoglyceroyl phosphate to give phosphoenzyme and 3-phosphoglycerate.
  • The latter is rephosphorylated by the enzyme to yield 2,3- diphosphoglycerate, but this reaction is slowed down by dissociation of 3-phosphoglycerate from the enzyme, which is therefore more active in the presence of added 3-phosphoglycerate.
  • Also catalyzes, slowly, the reaction of EC 5.4.2.12.
  • Formerly EC 2.7.5.4.
 505 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58 A0A0D9SA58
(495 more...)
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