Protein: Polyamine aminopropyltransferase (Agmatine aminopropyltransferase) (EC 2.5.1.104) (Cadaverine aminopropyltransferase) (EC 2.5.1.-) (N1-aminopropylagmatine synthase) (Putrescine aminopropyltransferase) (PAPT) (Spermidine synthase) (SPDS) (SPDSY) (EC 2.5.1.16) (Q5JFG9)
Organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Function: Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to agmatine to yield N1-aminopropylagmatine. It can also use cadaverine (1,5-diaminopentane) and putrescine (1,4-diaminobutane) as substrate with a lower activity than that of agmatine. The reaction involves a nucleophilic attack on the C-3 methylene of the propylamine moiety adjacent to the positively charged sulfur of decarboxy-AdoMet.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:20675472}.
Sequence: MGYNEQERAFIEWYPRGYGVGFKVKRRLFETQTEYQRLEIYETEGFGKLLVLDGTVQLVEVGEESYHEVLVHPVMLAHPNPRKVLVIGGGDGGTLREVLRHDTVEKAIMVEIDEGVVEASYLYLDVAKDLLDRLIKKEEPRAELIIGDGVKYLRETDERFDVIIVDSTDPVGPAKLLFSEEFYRDAYEKLNEKGLYVTQAGSVYLFTNELLDAYKAMKKVFDRVYYFSFPVIGYASPWSFLVGVKGDVDFTRIDLERAKKLDLYYYDPERHETLFQMPRYVRKLLEGQ
InterPro domains: - IPR035246: Spermidine synthase, tetramerisation domain (domain) [10-60]
- IPR037163: Spermidine synthase, tetramerisation domain superfamily (homologous_superfamily) [7-59]
- IPR030374: Polyamine biosynthesis domain (domain) [11-245]
- IPR029063: S-adenosyl-L-methionine-dependent methyltransferase superfamily (homologous_superfamily) [9-287]
- IPR001045: Spermidine/spermine synthases (family) [8-287]
- IPR030373: Polyamine biosynthesis domain, conserved site (conserved_site) [84-97]
Interaction partners: - S-adenosylmethionine decarboxylase proenzyme
- N
- Arginase
- Arginase
- S-methyl-5'-thioadenosine phosphorylase
- Probable 6-oxopurine nucleoside phosphorylase
- 5-methylthioadenosine/S-adenosylhomocysteine deaminase
- Hypothetical membrane protein, conserved
- Pyruvoyl-dependent arginine decarboxylase
- Hypothetical membrane protein, conserved
Gene Ontology annotations:
Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016740 (transferase activity), GO:0016765 (transferase activity, transferring alkyl or aryl (other than methyl) groups)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0009987 (cellular process), GO:0009058 (biosynthetic process), GO:0044237 (cellular metabolic process), GO:0071704 (organic substance metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0044249 (cellular biosynthetic process), GO:0034641 (cellular nitrogen compound metabolic process), GO:1901576 (organic substance biosynthetic process), GO:1901564 (organonitrogen compound metabolic process), GO:1901566 (organonitrogen compound biosynthetic process), GO:0009308 (amine metabolic process), GO:0044271 (cellular nitrogen compound biosynthetic process), GO:0006576 (biogenic amine metabolic process), GO:0009309 (amine biosynthetic process), GO:0042401 (biogenic amine biosynthetic process), GO:0006595 (polyamine metabolic process), GO:0006596 (polyamine biosynthetic process), GO:0008216 (spermidine metabolic process), GO:0008295 (spermidine biosynthetic process)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005737 (cytoplasm), GO:0005622 (intracellular anatomical structure)