ID A0A401KUC9_ASPAW Unreviewed; 318 AA.
AC A0A401KUC9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Spermidine synthase {ECO:0000313|EMBL:GCB22787.1};
GN ORFNames=AAWM_05672 {ECO:0000313|EMBL:GCB22787.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB22787.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB22787.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB22787.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:GCB22787.1}.
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DR EMBL; BDHI01000014; GCB22787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401KUC9; -.
DR STRING; 105351.A0A401KUC9; -.
DR Proteomes; UP000286921; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-UniRule.
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; 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; 2.
DR PIRSF; PIRSF000502; Spermidine_synth; 2.
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:UP000286921};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}.
FT DOMAIN 11..272
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 318 AA; 36180 MW; 9126FEE2B49220DC CRC64;
MSDITHPTIK DGWFSEQSDM WPGQAMNLKV NQILHHEKSK YQDVLVFESS DYGTVLVLDN
VIQCTERDEF SYQEMITHLA MNSHPNPKKV LVIGGGDGGV LREVVKHETV EEATLCDIDE
AVIRVSKKYL PGMSIGFQHP NVKVHVGDGF QFLKERQNEF DVIITDSSDP EGPAESLFQK
PYFELLRDAL REGGVITTQG SNLVTPQTTR PLTRDRFGFV FSTHTAENQW LHLSLITDLK
KACKEVFPVA EYAYTTIPTY PSGQIGFMVC CKDATRNVKE PVRSWTREEE EKLCRYYNQD
IHRASFVLPN FARKALDA
//
