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CATH Superfamily 1.10.150.240

Putative phosphatase; domain 2

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:

"
Putative phosphatase; domain 2
".

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 1: Haloacid dehalogenase-like hydrolase domain

There are 5 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
Riboflavin kinase. [EC: 2.7.1.26]
ATP + riboflavin = ADP + FMN.
  • The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B(6), vitamin B12 and folates.
  • While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2.
  • In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP.
 4 A0A178V341 A0A178V341 Q84MD8 Q84MD8
FMN hydrolase. [EC: 3.1.3.102]
FMN + H(2)O = riboflavin + phosphate.
  • The enzyme, found in many isoforms purified from both bacteria and plants, is a member of the haloacid dehalogenase superfamily.
  • Most of the isoforms have a wide substrate specificity, but isoforms specific for FMN also exist.
 4 A0A178V341 A0A178V341 Q84MD8 Q84MD8
Pseudouridine 5'-phosphatase. [EC: 3.1.3.96]
Pseudouridine 5'-phosphate + H(2)O = pseudouridine + phosphate.
  • The enzyme, isolated from animals, dephosphorylates pseudouridine 5'-phosphate, a potential intermediate in rRNA degradation.
  • Formerly EC 3.1.3.n6.
 2 Q08623 Q9D5U5
Glycerol-1-phosphatase. [EC: 3.1.3.21]
Glycerol 1-phosphate + H(2)O = glycerol + phosphate.
  • The Dunaliella enzyme acts more rapidly on sn-glycerol 1-phosphate than on the 3-phosphate.
  • The enzyme from Saccharomyces cerevisiae also acts on propane-1,2- diol 1-phosphate, but not on a variety of other phosphate esters.
 2 F4JTE7 Q8VZP1
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase. [EC: 3.1.3.104]
5-amino-6-(5-phospho-D-ribitylamino)uracil + H(2)O = 5-amino-6- (D-ribitylamino)uracil + phosphate.
  • The enzyme, which is found in plants and bacteria, is part of a pathway for riboflavin biosynthesis.
  • Most forms of the enzyme has a broad substrate specificity.
 1 F4JTE7