ID A0A0M2GE08_9ACTN Unreviewed; 551 AA.
AC A0A0M2GE08;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=UK15_30010 {ECO:0000313|EMBL:KJK35610.1};
OS Streptomyces variegatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=284040 {ECO:0000313|EMBL:KJK35610.1, ECO:0000313|Proteomes:UP000034786};
RN [1] {ECO:0000313|Proteomes:UP000034786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16380 {ECO:0000313|Proteomes:UP000034786};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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}.
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:KJK35610.1}.
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DR EMBL; JYJH01000028; KJK35610.1; -; Genomic_DNA.
DR RefSeq; WP_031142420.1; NZ_JYJH01000028.1.
DR AlphaFoldDB; A0A0M2GE08; -.
DR STRING; 284040.UK15_30010; -.
DR PATRIC; fig|284040.3.peg.4394; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000034786; 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 37..63
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 96..120
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 140..159
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 180..201
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 207..226
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 238..256
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT DOMAIN 253..504
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 408
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198,
FT ECO:0000256|PROSITE-ProRule:PRU00354"
FT BINDING 281
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 313
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 335
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 355
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 389..390
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
SQ SEQUENCE 551 AA; 58024 MW; C7E7B5EDEF33BBC7 CRC64;
MIEPHAPAPP GCPPPWSDPG GPAGQARLPV RPGTGRFLVL AGVFVCAACG LVYELELVAL
ASYLMGDSVT QASVVLSVMV FAMGIGSLAA KRLRPLAAAG FGAVEAGLAL VGGCSAMALY
AVFAWTGDWG GMWANGPRCL LVAFSLATGL LIGAEVPLLM ELIQRIRRQD AGGAVADLSA
ADYVGALVGG LAFPFLLLPF LGQLTGALLT GAVNAVVGGA LVLGLFRRDL TRRARWLLLL
GNALVLAILA SAAVLVDDFE RAARRAVYGE DVRVALQTEV QEVVLTGGTH GRPLDLFLGG
RLRVSGRDEL RYHEALVHPA MSGPHTRVLI LGGGDGLAVR EVLRHPGVDR VDVVELDAEV
IRLARTDPAL SALNRHAFGD PRVRVTTEDA FGWMRGATPA TYDVVVSDLP DPGITASTKL
YSQEFYGLAR RVLAPGGRLV VHAGPVAAGP RVYWTVEATV RAAGFRTAPY GTRGRHTAFD
AGSDRTPAGR SRALRDWGFV LAARTDPRLR LDPDGPRPSV LTEASLAAGE RSARRTRIAG
LPASTLVHPR Y
//
