SPDS2_HYONI
ID SPDS2_HYONI Reviewed; 308 AA.
AC O48659;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Spermidine synthase 2;
DE Short=SPDSY 2;
DE EC=2.5.1.16;
DE AltName: Full=Putrescine aminopropyltransferase 2;
OS Hyoscyamus niger (Black henbane).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae;
OC Hyoscyamus.
OX NCBI_TaxID=4079;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Root;
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 -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000305}.
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DR EMBL; AB006691; BAA24534.1; -; mRNA.
DR AlphaFoldDB; O48659; -.
DR SMR; O48659; -.
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..308
FT /note="Spermidine synthase 2"
FT /id="PRO_0000156454"
FT DOMAIN 17..254
FT /note="PABS"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 154..155
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 173..176
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
SQ SEQUENCE 308 AA; 33917 MW; 18E42E9DA82283EB CRC64;
MEEQGNNESA YISSILPGWF SEISPLWPGE AHSLKVEKIL FQGKSDYQNV VVFQSSTYGK
VLVLDGVIQL TERDECAYQE MITHLPLCSI PNPKKVLVIG GGDGGVLREV SRHSSVEQID
ICEIDKMVID VSKQFFPNVA IGYEDPRVKL HVGDGVAFLK NVPEGTYDAV IVDSSDPIGP
AQELFEKPFF ESVARALCPG GVVCTQAESI WLHMHIIEDI VSNCRQIFKG SVNYAWTTVP
TYPSGVIGFM LCSTEGPAVD FKNPINPIDA DDSHTKTRGP LKFYNSEIHS ASFCLPSFAK
RVIESNAK