SPDS1_HYONI
ID SPDS1_HYONI Reviewed; 315 AA.
AC O48658;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Spermidine synthase 1;
DE Short=SPDSY 1;
DE EC=2.5.1.16;
DE AltName: Full=Putrescine aminopropyltransferase 1;
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; AB006690; BAA24533.1; -; mRNA.
DR AlphaFoldDB; O48658; -.
DR SMR; O48658; -.
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..315
FT /note="Spermidine synthase 1"
FT /id="PRO_0000156453"
FT DOMAIN 25..262
FT /note="PABS"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 162..163
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 181..184
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
SQ SEQUENCE 315 AA; 34661 MW; 384192D51CE7BABF CRC64;
MEVTNQSNGC SNNEKESPYI SSVLPGWFSE ISPLWPGEAH SLKVEKILFQ GKSDYQNVMV
FQSSTYGKVL VLDGVIQLTE RDECAYQEMI THLPLCSIPN PKKVLVIGGG DGGVLREVSR
HSSVEQIDIC EIDKMVVEVA KEFFPDVAVG YEDPRVNLHI GDGVAFLKNV PAGTYDAVIV
DSSDPIGPAQ ELFEKPFFES IARALRPGGV VSTQAESIWL HMHIIEEIVA NCRQIFKGSV
NYAWTTVPTY PSGMIGFMLC STEGPAVDFK NPINPIDDES GPKTIAPLKF YNSEIHQASF
CLPSFAKRVI ESKGK