ID   SPDS2_PEA               Reviewed;         342 AA.
AC   Q9ZTR0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Spermidine synthase 2;
DE            Short=SPDSY 2;
DE            EC=2.5.1.16;
DE   AltName: Full=Putrescine aminopropyltransferase 2;
GN   Name=SPDSYN2;
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; AF043109; AAD02232.1; -; mRNA.
DR   AlphaFoldDB; Q9ZTR0; -.
DR   SMR; Q9ZTR0; -.
DR   PRIDE; Q9ZTR0; -.
DR   EnsemblPlants; Psat0s1463g0080.1; Psat0s1463g0080.1.cds; Psat0s1463g0080.
DR   Gramene; Psat0s1463g0080.1; Psat0s1463g0080.1.cds; Psat0s1463g0080.
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..342
FT                   /note="Spermidine synthase 2"
FT                   /id="PRO_0000156459"
FT   DOMAIN          52..289
FT                   /note="PABS"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..24
FT                   /note="Basic and acidic residues"
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;  37590 MW;  642A81926AD42D39 CRC64;
     MAAESTVELE SSMKEHRDDD EKSNGFSVSA VSMDVEGGDK DPSGNGVSSV IPGWFSEISP
     MWPGEAHSLK IEKILFQGKS EYQKVMVFQS STYGKVLVLD GVIQLTERDE CAYQEMITHL
     PLCSIPNPKK VLVIGGGDGG VLREVARHSS IEKIDICEID NMVVEVSKQF FPEVAVGFND
     PRVTLRIGDG VAFLKAAPEG TYDAVIVDSS DPIGPAQELF EKPFFQSVAR ALRPGGVMCT
     QAESIWLHMD IIEDIVSNCR HIFKGSVNYA WTTVPTYPSG MIGFMLCSTE GPLVDFKHPV
     NPIDQKDCQK SVRPLKFYNS EIHTAAFCLP SFAKRKIGSK ET