ID A0A0F7SA10_9BASI Unreviewed; 769 AA.
AC A0A0F7SA10;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Probable chimeric spermidine synthase/saccharopine reductase {ECO:0000313|EMBL:CDU22918.1};
GN Name=SSCI36030.1 {ECO:0000313|EMBL:CDW97630.1};
GN ORFNames=SPSC_01548 {ECO:0000313|EMBL:CDU22918.1};
OS Sporisorium scitamineum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=49012 {ECO:0000313|EMBL:CDW97630.1, ECO:0000313|Proteomes:UP000242770};
RN [1] {ECO:0000313|EMBL:CDU22918.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SscI8 {ECO:0000313|EMBL:CDU22918.1};
RA Ju J., Zhang J.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000242770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman P.J.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CDW97630.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman J.Paul.;
RL Submitted (JUN-2014) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LK056662; CDU22918.1; -; Genomic_DNA.
DR EMBL; CCFA01002036; CDW97630.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7SA10; -.
DR STRING; 49012.A0A0F7SA10; -.
DR OrthoDB; 2184985at2759; -.
DR Proteomes; UP000242770; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009085; P:lysine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR030374; PABS.
DR InterPro; IPR030373; PABS_CS.
DR InterPro; IPR032095; Sacchrp_dh-like_C.
DR InterPro; IPR005097; Sacchrp_dh_NADP.
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; TIGR00417; speE; 1.
DR PANTHER; PTHR11133:SF25; ALPHA-AMINOADIPIC SEMIALDEHYDE SYNTHASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR Pfam; PF16653; Sacchrp_dh_C; 1.
DR Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR Pfam; PF17284; Spermine_synt_N; 1.
DR Pfam; PF01564; Spermine_synth; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Polyamine biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00354};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}.
FT DOMAIN 11..248
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 769 AA; 84186 MW; 1607D1974C0150CC CRC64;
MGVITHPNIR DGWFHETNSQ WPGQAMSLQV QRILHHEKSL FQDVLVFEST TFGNVLVLDG
VIQCTERDEF SYQEMIAHLP IASHPNPERV LVIGGGDGGV LREVVKHDSV KEAVLCDIDE
AVPRVSKQYL PKMAEGLTHP KSKVIIGDGF AFLQDPENKA SFDVIITDSS DPVGPAEALF
QQPYFALLKE ALKPGGHIST QAECVWIHLN LIGELRRSTK ELFPVADYAF TTIPTYPSGQ
IGFVVCSLDP QRNVREPLRE VPDCRYYNSQ VHKAAFTVPE FARKVIEDGA PAPGRVIPTG
EGVSNTQRAP KKVLLLGSGY VAGPFAQYVA RFPEYSLTVA SSKLENSQRL IEGLYNATAA
AVDVNDAAAL SEIIKGHDVV VSLIPYIYHA AVIKAACEHK VNVVTTSYVS DAIRALEPEI
QKAGITVMNE IGLDPGLDHL YAVKAIDDVH AEGGKIKSFL SYCGGLPAPE AADNPLGYKF
SWSSRGVLLA LRNAAKFWQD GKELTVSGHE LMAVAKSFYI NPAFAFVAYP NRDSTPFKQW
YNIPEAETVI RGTLRYQGFP EFILALVKLG FLDEEAKDFL AYNTKASWAE VTAKMVGAAS
TSETDLIAAI RAKVSFKSAQ EEETIIRGLR WLDLFNTKAT VTVRGTAAQE AEKVAGNPLD
SLCATLEEKC AYAPGERDMV MLQHKFEIET ASGEHKTLTS TLLDYGIPHG VSSMAKLVGV
PCAIATRLIL EGHPALSKTG ILAPYTKDIC DPIRLELEKE GIALEERYV
//
