ID   SPDS1_PEA               Reviewed;         334 AA.
AC   Q9ZTR1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Spermidine synthase 1;
DE            Short=SPDSY 1;
DE            EC=2.5.1.16;
DE   AltName: Full=Putrescine aminopropyltransferase 1;
GN   Name=SPDSYN1;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Alaska; TISSUE=Ovary;
RX   PubMed=10344199; DOI=10.1023/a:1006158819849;
RA   Alabadi D., Carbonell J.;
RT   "Differential expression of two spermidine synthase genes during early
RT   fruit development and in vegetative tissues of pea.";
RL   Plant Mol. Biol. 39:933-943(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; AF043108; AAD02231.1; -; mRNA.
DR   AlphaFoldDB; Q9ZTR1; -.
DR   SMR; Q9ZTR1; -.
DR   UniPathway; UPA00248; UER00314.
DR   GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-EC.
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; Spermidine biosynthesis; Transferase.
FT   CHAIN           1..334
FT                   /note="Spermidine synthase 1"
FT                   /id="PRO_0000156458"
FT   DOMAIN          44..281
FT                   /note="PABS"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        200
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="putrescine"
FT                   /ligand_id="ChEBI:CHEBI:326268"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         181..182
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         200..203
FT                   /ligand="putrescine"
FT                   /ligand_id="ChEBI:CHEBI:326268"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="putrescine"
FT                   /ligand_id="ChEBI:CHEBI:326268"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   334 AA;  36701 MW;  0E466EC9CF8D1913 CRC64;
     MAAPENTLHS TDSPLKRQRE DEVNGVSDTL SKEPQPNGLS SVIPGWFSEI SPMWPGEAHS
     LKVEKILFQG KSDYQDVMVF QSATYGKVLI LDGVIQLTER DECAYQEMIT HLPLCSIPNP
     KKVLVIGGGD GGVLREVARH SSVEKIDICE IDKMVVDVSK EYFPDIAVGF ADPRVTLNIG
     DGVAFLKAAP EGTYDAVIVD SSDPIGPAQE LFEKPFFESV ARALRPGGVV CTQAESIWLH
     MHIIEDIVVN CRQVFKGSVN YAWTTVPTYP SGMIGFMLCS TEGPSVDFKH PVNPIDENDS
     QQAARPLKFY NREIHSAAFC LPSFAKRAIA SKEN