ID A0A222XD45_9CELL Unreviewed; 521 AA.
AC A0A222XD45;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=CBP52_14470 {ECO:0000313|EMBL:ASR56102.1};
OS Cellulomonas sp. PSBB021.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2003551 {ECO:0000313|EMBL:ASR56102.1, ECO:0000313|Proteomes:UP000214627};
RN [1] {ECO:0000313|EMBL:ASR56102.1, ECO:0000313|Proteomes:UP000214627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB021 {ECO:0000313|EMBL:ASR56102.1,
RC ECO:0000313|Proteomes:UP000214627};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-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}.
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DR EMBL; CP021430; ASR56102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222XD45; -.
DR KEGG; cez:CBP52_14470; -.
DR OrthoDB; 9793120at2; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000214627; Chromosome.
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 24..49
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 55..76
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 88..109
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 115..140
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 152..175
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 213..234
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT DOMAIN 209..459
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 378
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 282
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 521 AA; 55676 MW; 57DDBCFCEA8F0460 CRC64;
MTATEVEHPA ATGRSRARRM DRPTVFAAAL LVAVGGIVYE LILGTAASYL VGDSVVSFSV
ATGLSLFGMG IGSLLAPRLP GPSGIAFVRN ELVLGLLGGS SVLVLFWAYG QTELYWPVFV
LLAVGIGIGI GIEIPLLVAL LKEHGRDESV GLLSKVLALD YLGALLASLL FPFLLLPVLG
LVRTALAVAI LNVAVALFML ARMGHQPRWT WTTGGALAAL LAVFAASSGL EAALSTRLYQ
DPVVAAATSR YQKLVVTDYQ GDVRLYLNDQ LQFSSVDEAR YHETLAHSAL TSVRAPASVA
ILGGGDGLLA REVLRYPTVR EVVVVDLDPA VTDLARSNRL LRDLNEGSLD DERVRVVNAD
AFGWVRDTGA TFDAVLVDLV DPSDERVAKL YSTEFYSSVV AHLRPGGVLA TQATSSYFTP
HAYWQVVATL RAGGPGRTVV PLSVNVPSFG EWGFALSLPG AGDTFLTATP LPDGLRFHDH
RSLAGTARLP GDLSPVEMPA STLLAPVVYR TYQQDMRHWR Y
//
