SPDS2_DATST
ID SPDS2_DATST Reviewed; 317 AA.
AC Q96557;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Spermidine synthase 2;
DE Short=SPDSY 2;
DE EC=2.5.1.16;
DE AltName: Full=Putrescine aminopropyltransferase 2;
OS Datura stramonium (Jimsonweed) (Common thornapple).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Datureae; Datura.
OX NCBI_TaxID=4076;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=D5/15; TISSUE=Root;
RA Michael A.J.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
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; Y08253; CAA69421.1; -; mRNA.
DR AlphaFoldDB; Q96557; -.
DR SMR; Q96557; -.
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..317
FT /note="Spermidine synthase 2"
FT /id="PRO_0000156452"
FT DOMAIN 27..264
FT /note="PABS"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 164..165
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 183..186
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
SQ SEQUENCE 317 AA; 34904 MW; 7B87AA509951D534 CRC64;
MEVANHNNNN NGCTNDKESP CISSVLPGWF SEISPLWPGE AHSLKVEKIL FQGKSDYQDV
MVFQSTTYGK VLVLDGVIQL TERDECAYQE MITHLPLCSI PNPKKVLVIG GGDGGVLREV
SRHSSVEQID ICEIDKMVVE VAKQFFPDVA VGYEDPRVNL HIGDGVAFLK NVPAGTYDAV
IVDSSDPIGP AQELFEKPFF ETIARALRPG GVVSTQAESI WLHMHIIEEI VANCREIFKG
SVNYAWTTVP TYPSGMIGFM LCSTEGPAVD FKNPINPIDD ESHGQTIGPL KFYNSEIHQA
SFCLPSFAKR VIETKGK