ID A0A9J5Y7H4_SOLCO Unreviewed; 299 AA.
AC A0A9J5Y7H4;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 05-FEB-2025, entry version 8.
DE RecName: Full=thermospermine synthase {ECO:0000256|ARBA:ARBA00049721};
DE EC=2.5.1.79 {ECO:0000256|ARBA:ARBA00049721};
GN ORFNames=H5410_037250 {ECO:0000313|EMBL:KAG5596018.1};
OS Solanum commersonii (Commerson's wild potato) (Commerson's nightshade).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4109 {ECO:0000313|EMBL:KAG5596018.1, ECO:0000313|Proteomes:UP000824120};
RN [1] {ECO:0000313|EMBL:KAG5596018.1, ECO:0000313|Proteomes:UP000824120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LZ3.2 {ECO:0000313|EMBL:KAG5596018.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG5596018.1};
RA Cho K.;
RT "De no assembly of potato wild relative species, Solanum commersonii.";
RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl 3-(methylsulfanyl)propylamine + spermidine =
CC thermospermine + S-methyl-5'-thioadenosine + H(+);
CC Xref=Rhea:RHEA:30515, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
CC ChEBI:CHEBI:57443, ChEBI:CHEBI:57834, ChEBI:CHEBI:59903; EC=2.5.1.79;
CC Evidence={ECO:0000256|ARBA:ARBA00048874};
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000256|ARBA:ARBA00007867}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG5596018.1}.
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DR EMBL; JACXVP010000007; KAG5596018.1; -; Genomic_DNA.
DR OrthoDB; 38125at2759; -.
DR Proteomes; UP000824120; Chromosome 7.
DR GO; GO:0010487; F:thermospermine synthase activity; IEA:TreeGrafter.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-UniRule.
DR FunFam; 3.40.50.150:FF:000088; Polyamine aminopropyltransferase; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001045; Spermi_synthase.
DR InterPro; IPR035246; Spermidine_synt_N.
DR InterPro; IPR037163; Spermidine_synt_N_sf.
DR NCBIfam; NF037959; MFS_SpdSyn; 1.
DR PANTHER; PTHR43317; THERMOSPERMINE SYNTHASE ACAULIS5; 1.
DR PANTHER; PTHR43317:SF6; THERMOSPERMINE SYNTHASE ACAULIS5-LIKE; 1.
DR Pfam; PF17284; Spermine_synt_N; 1.
DR Pfam; PF01564; Spermine_synth; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 3: Inferred from homology;
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|PROSITE-
KW ProRule:PRU00354}; Reference proteome {ECO:0000313|Proteomes:UP000824120};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}.
FT DOMAIN 17..255
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ SEQUENCE 299 AA; 33820 MW; 4201E03FE5C0F25E CRC64;
MEQTIENEIV DSNGKNVEWF EESLEVDLKW SLAINSVLYK ATTKFQDVIL LDTKHFGKVL
VIDGKMQSAE KDEFIYHESL IHPALLLHDN PRRVFIMGGG EGSAAREALK HDNIHKVVIS
DIDQEVVNIC RKHLMANQEA FADCRLHVII NDAKVELEKS DEYKYDVIVG DLCDPREGGP
CNHLYLKSFY QHIIKPKLNH NGIFVTQAGF AGVLSHQAFF SSVYNTAKQV FNHVIAYTAH
VPSLADTRGW VLASDQPLKL DAEVINNRIK ERIKGSDLQF IDAAFMLAFT VMNKTVHTT
//
