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:

"
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.
« Back to all FunFams

FunFam 11646: Ectonucleotide pyrophosphatase/phosphodiesterase f...

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
Phosphodiesterase I. [EC: 3.1.4.1]
Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
  • Hydrolyzes both ribonucleotides and deoxyribonucleotides.
  • Has low activity toward polynucleotides.
  • A 3'-phosphate terminus on the substrate inhibits hydrolysis.
30 A0A061IFP6 A0A061IFP6 A0A061IGQ6 A0A061IGQ6 A0A0F7Z2Q3 A0A0F7Z2Q3 A2T3U8 A2T3U8 J3SBP3 J3SBP3
(20 more...)
Nucleotide diphosphatase. [EC: 3.6.1.9]
A nucleoside triphosphate + H(2)O = a nucleotide + diphosphate.
  • The enzyme preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates.
  • In vitro the enzyme also acts as a nucleotidohydrolase on ADP, NAD(+), NADP(+), FAD, and CoA.
  • Formerly EC 3.6.1.19.
24 A0A0F7Z2Q3 A0A0F7Z2Q3 A2T3U8 A2T3U8 J3SBP3 J3SBP3 J3SEZ3 J3SEZ3 O14638 O14638
(14 more...)
CATH-Gene3D is a Global Biodata Core Resource Learn more...