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CATH Superfamily 3.60.40.10

PPM-type phosphatase domain

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:

"
PPM-type phosphatase 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 11501: Phosphatase 2C family protein

There are 3 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
Protein-serine/threonine phosphatase. [EC: 3.1.3.16]
[a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate.
  • A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48).
  • The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1).
 82 A0A0D3HG80 A0A0D9YWK3 A0A0D9ZDI0 A0A0E0BDB2 A0A0E0F0K0 A0A0E0G605 A0A0E0GW08 A0A0E0IVY0 A0A0E0JBJ2 A0A0E0NJC6
(72 more...)
[Pyruvate dehydrogenase (acetyl-transferring)]-phosphatase. [EC: 3.1.3.43]
[Pyruvate dehydrogenase (acetyl-transferring)] phosphate + H(2)O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate.
  • A mitochondrial enzyme associated with EC 1.2.4.1 in the pyruvate dehydrogenase complex.
 14 A0A0B2Q2H6 A0A0B2SBV6 A0A0B2SGC7 A0A0B2SGX0 A0A0F4YTP9 A0A151SKI3 A0A151TXC9 A2QBM6 A2RB88 B7QLI2
(4 more...)
2-methoxy-6-polyprenyl-1,4-benzoquinol methylase. [EC: 2.1.1.201]
S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4- benzoquinol = S-adenosyl-L-homocysteine + 6-methoxy-3-methyl-2-all-trans- polyprenyl-1,4-benzoquinol.
  • This enzyme is involved in ubiquinone biosynthesis.
  • Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone- 9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units.
  • However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units.
  • For example, when the COQ5 gene from Saccharomyces cerevisiae is introduced into Escherichia coli, it complements the respiratory deficiency of an ubiE mutant.
  • The bifunctional enzyme from E.coli also catalyzes the methylation of demethylmenaquinol-8 (this activity is classified as EC 2.1.1.163).
 2 A0A0D9VAZ0 A0A0E0JUC2