SPDE_NICSY
ID SPDE_NICSY Reviewed; 314 AA.
AC O48660;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Spermidine synthase;
DE EC=2.5.1.16;
DE AltName: Full=Putrescine aminopropyltransferase;
DE Short=Aminopropyltransferase;
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=9517003; DOI=10.1093/oxfordjournals.pcp.a029291;
RA Hashimoto T., Tamaki K., Suzuki K., Yamada Y.;
RT "Molecular cloning of plant spermidine synthases.";
RL Plant Cell Physiol. 39:73-79(1998).
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 -!- TISSUE SPECIFICITY: Root, stem and leaf.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000305}.
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DR EMBL; AB006692; BAA24535.1; -; mRNA.
DR PIR; T15045; T15045.
DR RefSeq; NP_001289514.1; NM_001302585.1.
DR AlphaFoldDB; O48660; -.
DR SMR; O48660; -.
DR STRING; 4096.XP_009777991.1; -.
DR GeneID; 104227438; -.
DR eggNOG; KOG1562; Eukaryota.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000189701; Unplaced.
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; Reference proteome; Spermidine biosynthesis;
KW Transferase.
FT CHAIN 1..314
FT /note="Spermidine synthase"
FT /id="PRO_0000156456"
FT DOMAIN 23..260
FT /note="PABS"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 160..161
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 179..182
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
SQ SEQUENCE 314 AA; 34512 MW; 6C7707D92F61E869 CRC64;
MEAANHNNNG CTNESPYISS VLPGWFSEIS PLWPGEAHSL KVEKILFQGK SDYQNVMVFQ
SSTYGKVLVL DGVIQLTERD ECAYQEMIAH LPLCSIPNPK KVLVIGGGDG GVLREVSRHS
SVEQIDICEI DKMVVEVSKQ FFPDVAVGYE DPRVNLHIGD GVAFLKNVAA GTYDAVIVDS
SDPIGPAQEL FEKPFFESIA RALRPGGVVS TQAESIWLHM HIIEEIVANC RQIFKGSVNY
AWTTVPTYPS GMIGFMLCST EGPAVDFKNP INPIDDDASH NKTLGPMKFY NSELHKASFC
LPSFAKRVIE SKGK