ID   SPDE_SOLLC              Reviewed;         342 AA.
AC   Q9ZS45;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Spermidine synthase;
DE            Short=SPDSY;
DE            EC=2.5.1.16;
DE   AltName: Full=Putrescine aminopropyltransferase;
GN   Name=SPDSYN;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Rutgers;
RA   Alabadi D., Carbonell J.;
RT   "Molecular cloning and characterization of a tomato (Lycopersicon
RT   esculentum Mill.) spermidine synthase cDNA.";
RL   (er) Plant Gene Register PGR99-103(1999).
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.
CC   -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ006414; CAA07020.1; -; mRNA.
DR   RefSeq; NP_001234493.1; NM_001247564.2.
DR   AlphaFoldDB; Q9ZS45; -.
DR   SMR; Q9ZS45; -.
DR   STRING; 4081.Solyc05g005710.2.1; -.
DR   PaxDb; Q9ZS45; -.
DR   PRIDE; Q9ZS45; -.
DR   EnsemblPlants; Solyc05g005710.3.1; Solyc05g005710.3.1; Solyc05g005710.3.
DR   GeneID; 544177; -.
DR   Gramene; Solyc05g005710.3.1; Solyc05g005710.3.1; Solyc05g005710.3.
DR   KEGG; sly:544177; -.
DR   eggNOG; KOG1562; Eukaryota.
DR   HOGENOM; CLU_048199_3_2_1; -.
DR   InParanoid; Q9ZS45; -.
DR   OMA; DGLMVCQ; -.
DR   OrthoDB; 1059849at2759; -.
DR   PhylomeDB; Q9ZS45; -.
DR   UniPathway; UPA00248; UER00314.
DR   Proteomes; UP000004994; Chromosome 5.
DR   ExpressionAtlas; Q9ZS45; baseline and differential.
DR   GO; GO:0004766; F:spermidine synthase activity; IBA:GO_Central.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR030668; Spermi_synthase_euk.
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   PIRSF; PIRSF000502; Spermidine_synth; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00417; speE; 1.
DR   PROSITE; PS01330; PABS_1; 1.
DR   PROSITE; PS51006; PABS_2; 1.
PE   2: Evidence at transcript level;
KW   Polyamine biosynthesis; Reference proteome; Spermidine biosynthesis;
KW   Transferase.
FT   CHAIN           1..342
FT                   /note="Spermidine synthase"
FT                   /id="PRO_0000156455"
FT   DOMAIN          52..289
FT                   /note="PABS"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        208
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="putrescine"
FT                   /ligand_id="ChEBI:CHEBI:326268"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         189..190
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         208..211
FT                   /ligand="putrescine"
FT                   /ligand_id="ChEBI:CHEBI:326268"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="putrescine"
FT                   /ligand_id="ChEBI:CHEBI:326268"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   342 AA;  37679 MW;  1ACF37977B7C465A CRC64;
     MADECAAFMK GTELPVKRPR EEEAETEMEA ANNSNNGCEK EESSPYISSV LPGWFSEISP
     LWPGEAHSLK VEKILFQGKS DYQNVLVFQS STYGKVLVLD GVIQLTERDE CAYQEMITHL
     PLCSIPNPKK VLVIGGGDGG VLREVSRHSS VEQIDICEID KMVVEVAKQF FPDVAVGYED
     PRVNLHIGDG VAFLKNVPAG TYDAVIVDSS DPIGPAQELF EKPFFESIAK ALRPGGVVST
     QAESIWLHMH IIEEIVANCR QIFKGSVNYA WTTVPTYPSG MIGFMLCSTE GPAVDFKNPI
     NPIDDESPAK SIEPLKFYNS EIHQASFCLP SFAKRVIETK GK