SPDE_COFAR
ID SPDE_COFAR Reviewed; 316 AA.
AC O82147;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Spermidine synthase;
DE Short=SPDSY;
DE EC=2.5.1.16;
DE AltName: Full=Putrescine aminopropyltransferase;
OS Coffea arabica (Arabian coffee).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX NCBI_TaxID=13443;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Callus;
RA Hatanaka T., Sano H., Kusano T.;
RT "Molecular cloning and characterization of coffee cDNA encoding spermidine
RT synthase.";
RL Plant Sci. 140:161-168(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; AB015599; BAA29033.1; -; mRNA.
DR AlphaFoldDB; O82147; -.
DR SMR; O82147; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000515148; Genome assembly.
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..316
FT /note="Spermidine synthase"
FT /id="PRO_0000156450"
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 316 AA; 34501 MW; E2718735F284988B CRC64;
MADAVNSNSK EEAAQLPDGV SSVIPGWFSE ISPMWPGEAH SLKVEKILFQ GKSDYQNVMV
FQSSTYGKVL VLDGVIQLTE RDECAYQEMI AHLPLCSIPS PKKVLVIGGG DGGVLREVAR
HLSVEQIDIC EIDKMVVDVS KQFFPDVAVG FEDPRVVLHI GDGVAFLKAV PEGTYDAIIV
DSSDPIGPAQ ELFEKPFFES VAKALRPGGV VCTQAESIWL HMHIIEDIVA NCRQIFKGSV
NYAWTTVPTY PSGVIGFMLC STEGPPVDFK HPINPIDAND GRSKTMKPLK FYNSEIHSAA
FCLPSFAKKV IDSKAN