ID A0A2C9UNL0_MANES Unreviewed; 342 AA.
AC A0A2C9UNL0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=spermidine synthase {ECO:0000256|ARBA:ARBA00012455};
DE EC=2.5.1.16 {ECO:0000256|ARBA:ARBA00012455};
GN ORFNames=MANES_13G031400 {ECO:0000313|EMBL:OAY32607.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY32607.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY32607.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY32607.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) 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 Evidence={ECO:0000256|ARBA:ARBA00001199};
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC spermidine from putrescine: step 1/1. {ECO:0000256|ARBA:ARBA00005123}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000256|ARBA:ARBA00007867, ECO:0000256|RuleBase:RU003836}.
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DR EMBL; CM004399; OAY32607.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9UNL0; -.
DR STRING; 3983.A0A2C9UNL0; -.
DR EnsemblPlants; OAY32607; OAY32607; MANES_13G031400.
DR Gramene; OAY32607; OAY32607; MANES_13G031400.
DR OMA; EYTIEAK; -.
DR OrthoDB; 1126121at2759; -.
DR Proteomes; UP000091857; Chromosome lg13.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004766; F:spermidine synthase activity; IBA:GO_Central.
DR GO; GO:0008295; P:spermidine biosynthetic process; IBA:GO_Central.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.30.140.10; Spermidine synthase, tetramerisation domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 NCBIfam; NF037959; MFS_SpdSyn; 1.
DR NCBIfam; TIGR00417; speE; 1.
DR PANTHER; PTHR11558:SF11; SPERMIDINE SYNTHASE; 1.
DR PANTHER; PTHR11558; SPERMIDINE/SPERMINE SYNTHASE; 1.
DR Pfam; PF17284; Spermine_synt_N; 1.
DR Pfam; PF01564; Spermine_synth; 1.
DR PIRSF; PIRSF000502; Spermidine_synth; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 3: Inferred from homology;
KW Polyamine biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00354};
KW Reference proteome {ECO:0000313|Proteomes:UP000091857};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}.
FT DOMAIN 53..290
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 209
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ SEQUENCE 342 AA; 37486 MW; 8DC8321E0401E920 CRC64;
MAEEGVAVSN DLPVKRPRED GENVPSPTTV VMETEGNAEN NNSNNDHISS VIPGWFSEIS
PMWPGEAHSL KVEKILFQGK SDYQNVMVFQ SSTYGKVLVL DGVIQLTERD ECAYQEMITH
LPLCSIPNPK KVLVIGGGDG GVLREVARHS SVEQIVICEI DQMVVDVSKE FFPDIAVGYE
DPRVTLHVGD GVAFLKDVPA GTYDAIIVDS SDPIGPAKEL FEKPFFESVA KALRPGGVVC
TQAESIWLHM HLIEDIVANC RQVFKGSVNY AWTTVPTYPS GVIGFMLCST EGPAVDFKHP
VNPIDADDDN SRRPMKFYNS EIHTAAFCLP SFAKKVIDSK AK
//
