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CATH Superfamily 2.30.140.10

Spermidine synthase, tetramerisation domain

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:

"
Spermidine synthase, tetramerisation 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 14: Polyamine aminopropyltransferase

There are 1 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
Spermidine synthase. [EC: 2.5.1.16]
S-adenosyl 3-(methylthio)propylamine + putrescine = 5'-S-methyl- 5'-thioadenosine + spermidine.
  • The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor.
  • The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant toward other amine acceptors, such as spermidine and cadaverine.
  • Cf. EC 2.5.1.22 and EC 2.5.1.23.
 18 A0A1W0VPA7 A0A1W0VPA7 A0A1Y3E0I5 A0A1Y3E0I5 A0A1Y3E0I5 A0A2J9KIT2 A0A2J9KIT2 A0A2J9KIT2 B2USZ6 B5Z7J7
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