ID   SPEE_HELP2              Reviewed;         262 AA.
AC   B6JM63;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=HPP12_0839;
OS   Helicobacter pylori (strain P12).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=570508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P12;
RA   Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT   "The complete genome sequence of Helicobacter pylori strain P12.";
RL   Submitted (OCT-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}.
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DR   EMBL; CP001217; ACJ07991.1; -; Genomic_DNA.
DR   RefSeq; WP_000265069.1; NC_011498.1.
DR   AlphaFoldDB; B6JM63; -.
DR   SMR; B6JM63; -.
DR   EnsemblBacteria; ACJ07991; ACJ07991; HPP12_0839.
DR   KEGG; hpp:HPP12_0839; -.
DR   HOGENOM; CLU_048199_0_0_7; -.
DR   OMA; EYTIEAK; -.
DR   OrthoDB; 1613081at2; -.
DR   UniPathway; UPA00248; UER00314.
DR   Proteomes; UP000008198; 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   PROSITE; PS51006; PABS_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Polyamine biosynthesis; Spermidine biosynthesis; Transferase.
FT   CHAIN           1..262
FT                   /note="Polyamine aminopropyltransferase"
FT                   /id="PRO_1000099285"
FT   DOMAIN          1..249
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         29
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         83
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ   SEQUENCE   262 AA;  30594 MW;  516B7657E58FD3FE CRC64;
     MWITQEITPY LRKEYTIEAK LLDVRSEHNI LEIFKSKDFG EIAMLNCQLL FKNFLHIESE
     LLAHMGGCTK KELKEVLIVD GFDLELAHQL FKYDTRIDFV QADEKILDSF ISFFPHFHEV
     KNNKNFTHAK QLLDLDIKKY DLILCLQEPD IHKIDGLKRM LKEDGVFISV AKHPLLEHVS
     MQNALKNLGD FFPITIPFVA PLRILSNKGY IYASFKTHPL KDLMTPKIEA LKSVRYYNED
     IHRAAFALPK NLQEVFKDNI KS