ID A0A1C4QPS8_9ACTN Unreviewed; 501 AA.
AC A0A1C4QPS8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198};
DE AltName: Full=Putrescine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198};
DE Short=PAPT {ECO:0000256|HAMAP-Rule:MF_00198};
DE AltName: Full=Spermidine synthase {ECO:0000256|HAMAP-Rule:MF_00198};
DE Short=SPDS {ECO:0000256|HAMAP-Rule:MF_00198};
DE Short=SPDSY {ECO:0000256|HAMAP-Rule:MF_00198};
DE EC=2.5.1.16 {ECO:0000256|HAMAP-Rule:MF_00198};
GN Name=speE {ECO:0000256|HAMAP-Rule:MF_00198};
GN ORFNames=GA0115242_126940 {ECO:0000313|EMBL:SCE24774.1};
OS Streptomyces sp. SolWspMP-5a-2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1838281 {ECO:0000313|EMBL:SCE24774.1, ECO:0000313|Proteomes:UP000199131};
RN [1] {ECO:0000313|EMBL:SCE24774.1, ECO:0000313|Proteomes:UP000199131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SolWspMP-5a-2 {ECO:0000313|EMBL:SCE24774.1,
RC ECO:0000313|Proteomes:UP000199131};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the irreversible transfer of a propylamine group
CC from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to
CC putrescine (1,4-diaminobutane) to yield spermidine. {ECO:0000256|HAMAP-
CC Rule:MF_00198}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) +
CC S-methyl-5'-thioadenosine + spermidine; Xref=Rhea:RHEA:12721,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:326268; EC=2.5.1.16;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00198};
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC spermidine from putrescine: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_00198}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-Rule:MF_00198}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00198};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00198}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000256|ARBA:ARBA00007867, ECO:0000256|HAMAP-Rule:MF_00198}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00198}.
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DR EMBL; FMCI01000251; SCE24774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4QPS8; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000199131; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010487; F:thermospermine synthase activity; IEA:UniProt.
DR GO; GO:0008295; P:spermidine 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 Cell membrane {ECO:0000256|HAMAP-Rule:MF_00198};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00198};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|HAMAP-
KW Rule:MF_00198}; Spermidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00198};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00198}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_00198};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00198}.
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 73..98
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 110..134
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 146..169
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT DOMAIN 224..462
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT REGION 450..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198,
FT ECO:0000256|PROSITE-ProRule:PRU00354"
FT BINDING 252
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 284
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 306
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 326
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 360..361
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
SQ SEQUENCE 501 AA; 52695 MW; 188936C99E2DB3FD CRC64;
MRPGTGRFLV LACVFVCAAC GLVYELELVA LASYLIGDSV TQASVVLSVM VFAMGIGSLA
AKRLRWRAAA GFGAIEAALA LVGGCSAMAL YAVFAWTGGW GGLWASGSRW LLVAFSLAIG
LLIGAEVPLL MELIQRIRRQ DAGGAVADLF AADYVGALVG GLAFPFLLLP LLGQLTGALI
TGTVNAVAGG ALVLGLFRRD LSRRARWLLL VANLLVLGVL ASAAVLVDDF ERAARHAVYG
TDVRVALQTG VQEIILTGGT RGRPLDLFLD GRLRVSGRDE LPYHEALVHP AMNGPHARVL
VLGGGDGLAV REVLRHPGVR RVDVVELDAG LLRLARSDPG LARLNGHAYA DPRVHVTAED
AFGWLRGAPP SSYDVVVCDL PDPGITASTK LYSQEFYGLA RRALAPGGRL VVHAGPLASR
PRVFWTVDAT LRAAGLHTVP YRISGRASGF AGGPDRTTEA SRAARDWGVR PRRHRAAAPE
PRPRGAAPAH AHPGGPGGGR R
//
