ID A0A2T0FHB2_9ASCO Unreviewed; 283 AA.
AC A0A2T0FHB2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Spermidine synthase {ECO:0000313|EMBL:PRT54374.1};
GN ORFNames=B9G98_01994 {ECO:0000313|EMBL:PRT54374.1};
OS Wickerhamiella sorbophila.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trichomonascaceae; Wickerhamiella.
OX NCBI_TaxID=45607 {ECO:0000313|EMBL:PRT54374.1, ECO:0000313|Proteomes:UP000238350};
RN [1] {ECO:0000313|EMBL:PRT54374.1, ECO:0000313|Proteomes:UP000238350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS02 {ECO:0000313|EMBL:PRT54374.1,
RC ECO:0000313|Proteomes:UP000238350};
RA Ahn J.O.;
RT "Genome sequencing of [Candida] sorbophila.";
RL Submitted (APR-2017) 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:PRT54374.1}.
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DR EMBL; NDIQ01000021; PRT54374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0FHB2; -.
DR STRING; 45607.A0A2T0FHB2; -.
DR OrthoDB; 1126121at2759; -.
DR Proteomes; UP000238350; 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; 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 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:UP000238350};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}.
FT DOMAIN 4..240
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ SEQUENCE 283 AA; 31689 MW; FC7A1C0CBEFD6AF9 CRC64;
MLENGWFREE NESWNGQSLS LQVDKVLYVG KTMFQDVLVF RSTNYGNVLV LDGVIQATER
DEFAYQEMIC HLPLMSHPNP KRVLVVGGGD GGCLREVVKH AGVETIEMVE IDQTVVDLAK
RFLPNMACAF DNPRVTLHIA DGFEFLANNQ SKYDVIISDT SDPEGPAEKL FEESYFQLLS
DALAPGGIVA MQASENVWLK LDILKSLQER CKNVFPTVNY ATVCVPTYTS GQLGMMICAK
DPQTNLQAPA AKKHIPEDVR YYNEGIHRAS FVLPTFAKKY INN
//
