Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ASpermine_synt_N_1e3c6mA3 A: beta meandersX: Spermidine synthase tetramerisation domain (From Topology)H: Spermidine synthase tetramerisation domain (From Topology)T: Spermidine synthase tetramerisation domainF: Spermine_synt_N_1ECOD (1.6)
AKOG1562e3c6mA1 A: a+b two layersX: TBP-likeH: S-adenosylmethionine decarboxylase-relatedT: Bacterial S-adenosylmethionine decarboxylaseF: KOG1562ECOD (1.6)
ASpermine_synthe3c6mA2 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: Spermine_synthECOD (1.6)
BSpermine_synt_N_1e3c6mB3 A: beta meandersX: Spermidine synthase tetramerisation domain (From Topology)H: Spermidine synthase tetramerisation domain (From Topology)T: Spermidine synthase tetramerisation domainF: Spermine_synt_N_1ECOD (1.6)
BKOG1562e3c6mB1 A: a+b two layersX: TBP-likeH: S-adenosylmethionine decarboxylase-relatedT: Bacterial S-adenosylmethionine decarboxylaseF: KOG1562ECOD (1.6)
BSpermine_synthe3c6mB4 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: Spermine_synthECOD (1.6)
CSpermine_synt_N_1e3c6mC2 A: beta meandersX: Spermidine synthase tetramerisation domain (From Topology)H: Spermidine synthase tetramerisation domain (From Topology)T: Spermidine synthase tetramerisation domainF: Spermine_synt_N_1ECOD (1.6)
CSpermine_synthe3c6mC1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: Spermine_synthECOD (1.6)
DKOG1562,Spermine_synt_N_1e3c6mD1 A: beta meandersX: Spermidine synthase tetramerisation domain (From Topology)H: Spermidine synthase tetramerisation domain (From Topology)T: Spermidine synthase tetramerisation domainF: KOG1562,Spermine_synt_N_1ECOD (1.6)
DSpermine_synthe3c6mD2 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: Spermine_synthECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D
PF17284Spermidine synthase tetramerisation domain (Spermine_synt_N)Spermidine synthase tetramerisation domainThis domain represents the N-terminal tetramerization domain from spermidine synthase.Domain
A, B, C, D
PF17950S-adenosylmethionine decarboxylase N -terminal (SpmSyn_N)S-adenosylmethionine decarboxylase N -terminalThis is the N-terminal domain found in human spermine synthase (EC 2.5.1.22). The N-terminal domain, which forms the major part of the dimerization interface, shows a considerable structural similarity to the AdoMetDC-like fold (S-adenosylmethionine ...This is the N-terminal domain found in human spermine synthase (EC 2.5.1.22). The N-terminal domain, which forms the major part of the dimerization interface, shows a considerable structural similarity to the AdoMetDC-like fold (S-adenosylmethionine decarboxylase, the enzyme that forms the aminopropyl donor substrate), Pfam:PF02675 . Deletion of the N-terminal domain led to a complete loss of spermine synthase activity, suggesting that dimerization may be required for activity. The N-terminal domain (amino acids 1-117) includes seven beta-strands and two alpha-helices [1].
Domain
A, B, C, D
PF01564Spermine/spermidine synthase domain (Spermine_synth)Spermine/spermidine synthase domainSpermine and spermidine are polyamines. This family includes spermidine synthase that catalyses the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase.Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C, D
Spermine synthase