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CATH Superfamily 3.40.50.300

P-loop containing nucleotide triphosphate hydrolases

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:

"
P-loop containing nucleotide triphosphate hydrolases
".

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 635466: Ribosome biogenesis GTPase A

There are 4 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
N(1)-acetylpolyamine oxidase. [EC: 1.5.3.13]
(1) N(1)-acetylspermidine + O(2) + H(2)O = putrescine + 3-acetamidopropanal + H(2)O(2). (2) N(1)-acetylspermine + O(2) + H(2)O = spermidine + 3-acetamidopropanal + H(2)O(2).
  • The enzyme also catalyzes the reaction: N(1),N(12)-diacetylspermine + O(2) + H(2)O = N(1)-acetylspermidine + 3-acetamamidopropanal + H(2)O(2).
  • No or very weak activity with spermine, or spermidine in absence of aldehydes.
  • In presence of aldehydes the enzyme catalyzes the reactions: 1.
  • spermine + O(2) + H(2)O = spermidine + 3-aminopropanal + H(2)O(2), and with weak efficiency 2.
  • spermidine + O(2) + H(2)O = putrescine + 3-aminopropanal + H(2)O(2).
  • Found in mammalian peroxisomes and oxidizes N(1)-acetylated polyamines at the exo (three-carbon) side of the secondary amine, forming 3-acetamamidopropanal.
  • Since the products of the reactions are deacetylated polyamines, this process is known as polyamine back-conversion.
  • Differs in specificity from EC 1.5.3.14, EC 1.5.3.15, EC 1.5.3.16 and EC 1.5.3.17.
  • Formerly EC 1.5.3.11, EC 1.5.3.n3, EC 1.5.3.n4 and EC 1.5.3.n10.
 3 A0A0B2PDD2 A0A0B2Q026 A0A0B2QTN8
Ribonuclease H. [EC: 3.1.26.4]
Endonucleolytic cleavage to 5'-phosphomonoester.
  • Acts on RNA-DNA hybrids.
 2 A0A0T7ZPZ5 A0A0T8YE40
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).
 1 C5LCK9
Nucleoside-triphosphate phosphatase. [EC: 3.6.1.15]
NTP + H(2)O = NDP + phosphate.
  • The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria.
  • Also hydrolyzes nucleoside diphosphates, thiamine diphosphate and FAD.
  • The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin.
 1 A0A0L1HQN9
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