ID A0A395RQ56_9HYPO Unreviewed; 294 AA.
AC A0A395RQ56;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 18-JUN-2025, entry version 19.
DE SubName: Full=Spermidine synthase {ECO:0000313|EMBL:RGP62260.1};
GN ORFNames=FLONG3_10266 {ECO:0000313|EMBL:RGP62260.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP62260.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP62260.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP62260.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000256|ARBA:ARBA00007867, ECO:0000256|RuleBase:RU003836}.
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:RGP62260.1}.
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DR EMBL; PXOG01000292; RGP62260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395RQ56; -.
DR STRING; 694270.A0A395RQ56; -.
DR OrthoDB; 38125at2759; -.
DR Proteomes; UP000266234; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0004766; F:spermidine synthase activity; IEA:TreeGrafter.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:TreeGrafter.
DR CDD; cd02440; AdoMet_MTases; 1.
DR FunFam; 2.30.140.10:FF:000001; SPE3p Spermidine synthase; 1.
DR FunFam; 3.40.50.150:FF:000013; Spermidine synthase; 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; NF002010; PRK00811.1; 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:UP000266234};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}.
FT DOMAIN 13..249
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ SEQUENCE 294 AA; 33017 MW; 64FFBBE8AFD78FC6 CRC64;
MSNEEITHPT IVDGWFREIS DMWPGHAMTL RVEKVLAHEK SKYQDVLIFK STDFGNVLVL
DNVIQCTERD EFSYQEMIAH LALNSHPNPK KVLVIGGGDG GVLREIVKHD CVEEATLCDI
DEAVIRLSKE HLPSMACGFD HPKSKTHVGD GFKFLNDYKN EFDVIITDSS DPDGPAEALF
QKSYFQLLHD ALREGGVITT QGSESPWLHL PLIARLKKDC GAIFPVAEYA YTTIPTYPSG
QIGFMVCSKD PKADVKNPIR SWTKEEEDAK LRYYSSEIHK ASFVLPKFAA KALE
//
