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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 9: Polyamine aminopropyltransferase

There are 3 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.
 48 A0A0U5FJ86 A0A0U5FJ86 A0A0U5FJ86 A0A0U5FJ86 A0A1T1SM81 A0A1T1SM81 A0A1T1SM81 A0A1T1SM81 A0A3E1KKW5 A0A3E1KKW5
(38 more...)
N(1)-aminopropylagmatine synthase. [EC: 2.5.1.104]
S-adenosylmethioninamine + agmatine = S-methyl-5'-thioadenosine + N(1)- (3-aminopropyl)agmatine.
  • The enzyme is involved in the biosynthesis of spermidine from agmatine in some archaea and bacteria.
  • The enzyme from the Gram-negative bacterium Thermus thermophilus accepts agmatine, spermidine and norspermidine with similar catalytic efficiency.
  • The enzymes from the archaea Pyrococcus furiosus and Thermococcus kodakarensis prefer agmatine, but can utilize cadaverine, putrescine and propane-1,3-diamine with much lower catalytic efficiency.
  • Cf. EC 2.5.1.16 and EC 2.5.1.23.
 5 I6TY86 I6TY86 Q5JFG9 Q8U4G1 Q8U4G1
Sym-norspermidine synthase. [EC: 2.5.1.23]
S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine = S-methyl- 5'-thioadenosine + bis(3-aminopropyl)amine.
  • The enzyme has been originally characterized from the protist Euglena gracilis.
  • The enzyme from the archaeon Sulfolobus solfataricus can transfer the propylamine moiety from S-adenosyl 3-(methylsulfanyl)propylamine to putrescine, sym-norspermidine and spermidine with lower efficiency.
  • Cf. EC 2.5.1.16 and EC 2.5.1.22.
 4 I6TY86 I6TY86 Q8U4G1 Q8U4G1
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