ID   SPEE_CLOBB              Reviewed;         284 AA.
AC   B2TMY2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198};
DE   AltName: Full=Putrescine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198};
DE            Short=PAPT {ECO:0000255|HAMAP-Rule:MF_00198};
DE   AltName: Full=Spermidine synthase {ECO:0000255|HAMAP-Rule:MF_00198};
DE            Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198};
DE            Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198};
DE            EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198};
GN   Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; OrderedLocusNames=CLL_A1013;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00198}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00198};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC       spermidine from putrescine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00198}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_00198}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
CC   -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00198}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001056; ACD24838.1; -; Genomic_DNA.
DR   RefSeq; WP_012425564.1; NC_018648.1.
DR   AlphaFoldDB; B2TMY2; -.
DR   SMR; B2TMY2; -.
DR   EnsemblBacteria; ACD24838; ACD24838; CLL_A1013.
DR   KEGG; cbk:CLL_A1013; -.
DR   PATRIC; fig|935198.13.peg.962; -.
DR   HOGENOM; CLU_048199_0_0_9; -.
DR   OMA; EYTIEAK; -.
DR   OrthoDB; 1613081at2; -.
DR   UniPathway; UPA00248; UER00314.
DR   Proteomes; UP000001195; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.140.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00198; Spermidine_synth; 1.
DR   InterPro; IPR030374; PABS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR001045; Spermi_synthase.
DR   InterPro; IPR035246; Spermidine_synt_N.
DR   InterPro; IPR037163; Spermidine_synt_N_sf.
DR   PANTHER; PTHR11558; PTHR11558; 1.
DR   Pfam; PF17284; Spermine_synt_N; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00417; speE; 1.
DR   PROSITE; PS51006; PABS_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Polyamine biosynthesis; Spermidine biosynthesis; Transferase.
FT   CHAIN           1..284
FT                   /note="Polyamine aminopropyltransferase"
FT                   /id="PRO_1000099279"
FT   DOMAIN          2..237
FT                   /note="PABS"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         31
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         62
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         86
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         106
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         137..138
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         155..158
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         162
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ   SEQUENCE   284 AA;  33126 MW;  9EC99A909EEC97CE CRC64;
     MELWYTEKHT EYVKFSIKVD RELYTEQSKF QRIDILESKE FGKFFTLDGL MMVTEKDEFI
     YHDMIVHVPM ATNPNIKNVL VIGAGDGGTI RELTRYKTIE KIDMVEIDER VVEVCKKYLP
     KTAGKLEEER VNIVYEDGLK FVRNKENEYD LIIVDSTDPF GPGEGLFTKE FYGNCYKALS
     EDGILVNQHE SPYYEYYAKS MKDAHEKIQG LFKINKVYQA HIPTYPSGHW LFGFASKKYD
     PIKDLNAEAW NSLGLKTKYY NTDLHVGCFA LPTYVIDMLN ENKE