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CATH Superfamily 3.40.1450.10

BPG-independent phosphoglycerate mutase, domain B

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
BPG-independent phosphoglycerate mutase, domain B
".

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 1215: 2,3-bisphosphoglycerate-independent phosphoglycera...

There are 1 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-independent). [EC: 5.4.2.12]
2-phospho-D-glycerate = 3-phospho-D-glycerate.
  • The enzymes from higher plants, algae, fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate.
  • Cf. EC 5.4.2.11.
  • The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position.
  • Both metal ions are involved in the reaction.
  • Formerly EC 2.7.5.3 and EC 5.4.2.1.
 15 B1AIH0 B1RUV1 B1RW85 B1RX46 B2D9F7 B2DA65 B2NEE6 B2NGI8 B3XT70 B3XUU4
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