AC   MF_00198;
DC   Protein; auto
TR   HAMAP; MF_00198; -; 1; level=0
XX
Names: Spermidine_synth
XX
ID   SPEE
DE   RecName: Full=Polyamine aminopropyltransferase;
DE   AltName: Full=Spermidine synthase;
DE            Short=SPDSY;
DE            Short=SPDS;
DE            EC=2.5.1.16;
DE   AltName: Full=Putrescine aminopropyltransferase;
DE            Short=PAPT;
GN   Name=speE;
XX
CC   -!- FUNCTION: Catalyzes the irreversible transfer of a propylamine group
CC       from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to
CC       putrescine (1,4-diaminobutane) to yield spermidine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) +
CC         S-methyl-5'-thioadenosine + spermidine; Xref=Rhea:RHEA:12721,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443,
CC         ChEBI:CHEBI:57834, ChEBI:CHEBI:326268; EC=2.5.1.16;
CC   -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC       spermidine from putrescine: step 1/1.
case <Feature:Transmembrane>1>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
else case <Feature:Transmembrane==1>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
else
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
CC   -!- SUBUNIT: Homodimer or homotetramer.
CC   -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
case not <FTTag:Act_site>
CC   -!- CAUTION: Lacks the conserved Asp active site.
end case
XX
DR   Pfam; PF01564; Spermine_synth; 1; trigger=no
DR   NCBIfam; TIGR00417; SpeE; 1; trigger=no
DR   PROSITE; PS01330; PABS_1; 1; trigger=no
DR   PROSITE; PS51006; PABS_2; 1; trigger=yes
DR   General; Transmembrane; -; 7; trigger=yes
XX
KW   Polyamine biosynthesis
KW   Spermidine biosynthesis
KW   Transferase
case <Feature:Transmembrane>1>
KW   Cell membrane
KW   Membrane
KW   Transmembrane
KW   Transmembrane helix
else
KW   Cytoplasm
end case
XX
GO   GO:0004766; F:spermidine synthase activity
GO   GO:0008295; P:spermidine biosynthetic process
XX
FT   From: SPEE_PYRHO (O57950)
FT   BINDING         144..145
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT   Optional; Condition: [DNE]-[AGV]
FT   BINDING         161..164
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT   Optional; Condition: D-[SC]-x-[DNE]
FT   ACT_SITE        161
FT                   /note="Proton acceptor"
FT   Tag: Act_site; Condition: D
FT   BINDING         32
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT   Optional; Condition: [QNR]
FT   BINDING         63
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT   Optional; Condition: H
FT   BINDING         87
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT   Optional; Condition: [DNE]
FT   BINDING         107
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT   Optional; Condition: [ED]
FT   BINDING         168
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT   Optional; Condition: P
XX
Size: 261-574;
Related: None;
Template: P09158; P70998; Q9WZC2; Q8U4G1; O25503; O57950; Q9UXE4; Q5JFG9; Q5SK28;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: <Unknown>
 Cter: <Unknown>
Duplicate: in AQUAE, BACAN, BACCR, LEPIN, PSEAE, RALN1, STRCO, CALS4
Plasmid: in RALN1
Comments: None
XX
# Revision 1.47 2023/11/28
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