ID A0A1F8A9P5_9EURO Unreviewed; 293 AA.
AC A0A1F8A9P5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 18-JUN-2025, entry version 27.
DE SubName: Full=Spermidine synthase {ECO:0000313|EMBL:OGM48470.1};
GN ORFNames=ABOM_002445 {ECO:0000313|EMBL:OGM48470.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM48470.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM48470.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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:OGM48470.1}.
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DR EMBL; LYCR01000015; OGM48470.1; -; Genomic_DNA.
DR RefSeq; XP_022392187.1; XM_022529575.1.
DR AlphaFoldDB; A0A1F8A9P5; -.
DR STRING; 109264.A0A1F8A9P5; -.
DR GeneID; 34445835; -.
DR OrthoDB; 38125at2759; -.
DR Proteomes; UP000179179; 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:UP000179179};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}.
FT DOMAIN 11..247
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ SEQUENCE 293 AA; 33327 MW; 83842BE3EEF76670 CRC64;
MSEITHPTIK DGWFSEQSGM WPGQAMNLKV NQILHHEKSK YQDVLIFESS DYGTVLVLDN
VIQCTERDEF SYQEMITHLA MNSHPNPKKV LVIGGGDGGV LREVVKHETV EEAILCDIDE
AVIRLSKKYL PGMSIGFQHP NVKTHVGDGF EFLKTHQNEF DVIITDSSDP EGPAESLFQK
PYFELLRDAL REGGVITTQG SENQWLHLSL ITDLKKACKE VFPVAEYAYT TIPTYPSGQI
GFMVCCKDAT RNVREPVRKW SAEEEERLCR YYNQDIHRAS FVLPNFARKA LNN
//
