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SPEE_BUCAP
ID   SPEE_BUCAP              Reviewed;         286 AA.
AC   Q8K9T5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=BUsg_203;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67767.1; -; Genomic_DNA.
DR   RefSeq; WP_011053734.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9T5; -.
DR   SMR; Q8K9T5; -.
DR   STRING; 198804.BUsg_203; -.
DR   EnsemblBacteria; AAM67767; AAM67767; BUsg_203.
DR   KEGG; bas:BUsg_203; -.
DR   eggNOG; COG0421; Bacteria.
DR   HOGENOM; CLU_048199_1_0_6; -.
DR   OMA; LWPGQSF; -.
DR   OrthoDB; 1613081at2; -.
DR   UniPathway; UPA00248; UER00314.
DR   Proteomes; UP000000416; 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; IPR030373; PABS_CS.
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; PS01330; PABS_1; 1.
DR   PROSITE; PS51006; PABS_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Polyamine biosynthesis; Spermidine biosynthesis; Transferase.
FT   CHAIN           1..286
FT                   /note="Polyamine aminopropyltransferase"
FT                   /id="PRO_0000156473"
FT   DOMAIN          5..238
FT                   /note="PABS"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   ACT_SITE        158
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         64
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         88
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         108
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         140..141
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         158..161
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ   SEQUENCE   286 AA;  33548 MW;  B9F99B8ECCBF7F77 CRC64;
     MINEKIWHEK LHRHVGQYFS IDKILYQKKN KYHDIIIFQN SIMGRIMAID GVVQTTEKDE
     FIYHEMLTHV PIFYHGLIKN VLIVGGGDGG ILREICRHKS IENITMVEID LNIIDLCKQF
     FPKHNNNAYK DPRLKIVIDN GLNFVQKTKE KFDLIISDST DPIGCGKDLF LSDFYFHCKN
     CLVKNGIFVG QNGVFFLQKN DINQSYKNLK KNFHDVSFYQ ATIPSYYGGT MMFSWGTDNI
     DFRQINIKNL EKRIKDKKLT FNYYNSNIHI SSFYLPQYII NTLDKS
 
 
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