ID A0A2A5QZM1_9EURY Unreviewed; 613 AA.
AC A0A2A5QZM1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CP557_18115 {ECO:0000313|EMBL:PCR92277.1};
OS Natrinema ejinorense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=373386 {ECO:0000313|EMBL:PCR92277.1, ECO:0000313|Proteomes:UP000219689};
RN [1] {ECO:0000313|EMBL:PCR92277.1, ECO:0000313|Proteomes:UP000219689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13890 {ECO:0000313|EMBL:PCR92277.1,
RC ECO:0000313|Proteomes:UP000219689};
RA Roh S.W., Kim Y.B., Kim J.Y.;
RT "Genome sequences of Natrinema ejinorence JCM 13890T.";
RL Submitted (SEP-2017) 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:PCR92277.1}.
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DR EMBL; NXNI01000001; PCR92277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5QZM1; -.
DR OrthoDB; 10538at2157; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000219689; 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; IPR030374; PABS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001045; Spermi_synthase.
DR PANTHER; PTHR43317:SF9; POLYAMINE AMINOPROPYLTRANSFERASE 2; 1.
DR PANTHER; PTHR43317; THERMOSPERMINE SYNTHASE ACAULIS5; 1.
DR Pfam; PF01564; Spermine_synth; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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|HAMAP-Rule:MF_00198,
KW ECO:0000256|PROSITE-ProRule:PRU00354};
KW 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 56..75
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 87..111
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 123..142
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 154..176
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 226..244
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 250..272
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 284..303
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT DOMAIN 309..561
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 475
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198,
FT ECO:0000256|PROSITE-ProRule:PRU00354"
FT BINDING 343
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 379
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 405
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 423
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 457..458
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
SQ SEQUENCE 613 AA; 67447 MW; 7785700145EE8E18 CRC64;
MAEDGTTNGT ETSGSESTDG AGSGRSDSVQ PEPSARARGR PEGGVSSRHF VTDRRVALSV
TFVVAFCSIA YELVYSELLT VFFGGTVLRY SITIGLYMFS LGIGSVLSAQ LGEPESNFFR
TEVYLAIAGP AGALAIVAIN SLPPIDVPGA GPTILVLSHV PILVVGVLSG FEVPLLTDLV
ENREETVFAS LGRLYPRRIV RGILGAFFTI DEPDDRSFSE VLGVDYLGSL AGTVVYALVL
YPRYGLVVSV FALGLLNALA ALGFAAWTFS NAARTLSRPT VGQWRAVVLV GVLLTGTYGG
LVAHPNAVDR AVTTTYLERT IEREYPPGVS DVETRSYDTT PYQTVLTYER DVQGHTGTET
CLHLDRAIQF CDRWVDSYHS GLVDIPMTTF DDPSSVDVLL IGGGDYIAVD HLRQYDVSVD
QVDIDGEFLE MAREREFFRQ YNDDAYEYDR LNTTTQDAFT YLQESDETYD LVLLDVPGVR
SDETMSLYST EFYTLLREHL SDDGLVVSWV YTSGDHPTHS KVYANTVRAA GFDQYLPYYV
YDDLDGDGGL EPGERFYVLS DGPTPTPDLE RAESDYVHAN AETFGEWQWR SLPEYRGVEP
NSVLHPNYDI IVD
//
