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:

"
Alkaline Phosphatase, subunit A
".

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 92: Alkaline phosphatase PafA

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
Alkaline phosphatase. [EC: 3.1.3.1]
A phosphate monoester + H(2)O = an alcohol + phosphate.
  • Active at a high pH optimum.
  • Wide specificity.
  • Also catalyzes transphosphorylations.
  • Some enzymes hydrolyze diphosphate (cf. EC 3.6.1.1).
10 A0A1T3EC65 A0A1T3EC65 A0A1T3EC65 Q55320 Q9KJX5 Q9KJX5 Q9KJX5 T0PKU3 T0PKU3 T0PKU3
P-type Ca(2+) transporter. [EC: 7.2.2.10]
ATP + H(2)O + Ca(2+)(Side 1) = ADP + phosphate + Ca(2+)(Side 2).
  • A P-type ATPase that undergoes covalent phosphorylation during the transport cycle.
  • This enzyme family comprises three types of Ca(2+)-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum, in yeast, and in some bacteria.
  • The enzymes from plasma membrane and from yeast have been shown to transport one ion per ATP hydrolyzed whereas those from the sarcoplasmic reticulum transport two ions per ATP hydrolyzed.
  • In muscle cells Ca(2+) is transported from the cytosol into the sarcoplasmic reticulum.
  • Formerly EC 3.6.1.38 and EC 3.6.3.8.
1 Q47910
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