ID G2GD61_9ACTN Unreviewed; 480 AA.
AC G2GD61;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Spermidine synthase {ECO:0000313|EMBL:EGX58594.1};
DE EC=2.5.1.16 {ECO:0000313|EMBL:EGX58594.1};
DE Flags: Fragment;
GN ORFNames=SZN_17192 {ECO:0000313|EMBL:EGX58594.1};
OS Streptomyces zinciresistens K42.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX58594.1, ECO:0000313|Proteomes:UP000004217};
RN [1] {ECO:0000313|EMBL:EGX58594.1, ECO:0000313|Proteomes:UP000004217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K42 {ECO:0000313|EMBL:EGX58594.1,
RC ECO:0000313|Proteomes:UP000004217};
RA Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000256|ARBA:ARBA00007867}.
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:EGX58594.1}.
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; AGBF01000051; EGX58594.1; -; Genomic_DNA.
DR AlphaFoldDB; G2GD61; -.
DR Proteomes; UP000004217; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0010487; F:thermospermine synthase activity; IEA:UniProt.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00198; Spermidine_synth; 1.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR030374; PABS.
DR InterPro; IPR030373; PABS_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001045; Spermi_synthase.
DR NCBIfam; NF037959; MFS_SpdSyn; 1.
DR PANTHER; PTHR43317:SF9; POLYAMINE AMINOPROPYLTRANSFERASE 2; 1.
DR PANTHER; PTHR43317; THERMOSPERMINE SYNTHASE ACAULIS5; 1.
DR Pfam; PF01564; Spermine_synth; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|PROSITE-
KW ProRule:PRU00354}; Reference proteome {ECO:0000313|Proteomes:UP000004217};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 257..480
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 412
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
FT NON_TER 480
FT /evidence="ECO:0000313|EMBL:EGX58594.1"
SQ SEQUENCE 480 AA; 50842 MW; D0EB8E8B9EF8381E CRC64;
MRRPSRTVGS VIDPHAPAPP GTTPAWGGRP RLPVRPGTGR FLVLAGVFVC AACGLVYELE
LVALASYLIG DSVTQASVVL SVMVFAMGLG SLAAKRLRPY AAAAFGALEA LLALVGGSSA
LALYAVFAWT GDWGGLWADG PRWLLVAFSL TIGLLIGAEI PLLMELIQRI RRQEAGGAVA
DLFAADYVGG LVGGLAFPFL LLPLLGQLNS ALITGAVNAV VGAALVLGVF RRDLTRRARL
LLLAANLAVL AVLASAAVLA DDFERAARRE VYGQDVRVAV RTNRQEVVIT GGTRGRPLDL
FLDGRLRVGG RDERRYHEAL VHPAMSGPHG RVLILGGGDG LAAREVLRHP GVNRVDVVDA
DPGVVRLARR DPPLARLNGR VYDDGRVRVM ADDAFRRLRA TPPGTYDVVV SDLPDPGVTA
GTKLYSQEFY GLVRRALAPG GRLVVHAGPV ASRPRVFWTV EATLRAAGLR TTAYRLGGRG
//