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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 3: Spermidine synthase 1

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
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.
 25 A0A178W1L5 A0A178W1L5 A0A384L9M6 A0A384L9M6 A0A384L9M6 I1QA18 I1QA18 O48658 O48659 O48660
(15 more...)
Spermine synthase. [EC: 2.5.1.22]
S-adenosyl 3-(methylthio)propylamine + spermidine = S-methyl- 5'-thioadenosine + spermine.
  • The enzyme from mammalia is highly specific for spermidine, cf. EC 2.5.1.16 and EC 2.5.1.23.
 1 Q94BN2