SPEE1_RALSO
ID SPEE1_RALSO Reviewed; 525 AA.
AC Q8XQC8;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Polyamine aminopropyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Putrescine aminopropyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=PAPT 1 {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Spermidine synthase 1 {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDS 1 {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDSY 1 {ECO:0000255|HAMAP-Rule:MF_00198};
DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198};
GN Name=speE1 {ECO:0000255|HAMAP-Rule:MF_00198}; Synonyms=speE2;
GN OrderedLocusNames=RSp1306; ORFNames=RS05693;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG Plasmid megaplasmid Rsp.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_00198};
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC spermidine from putrescine: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00198}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_00198}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00198};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00198}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00198}.
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DR EMBL; AL646053; CAD18457.1; -; Genomic_DNA.
DR RefSeq; WP_011004585.1; NC_003296.1.
DR AlphaFoldDB; Q8XQC8; -.
DR SMR; Q8XQC8; -.
DR STRING; 267608.RSp1306; -.
DR EnsemblBacteria; CAD18457; CAD18457; RSp1306.
DR GeneID; 60504244; -.
DR KEGG; rso:RSp1306; -.
DR eggNOG; COG4262; Bacteria.
DR HOGENOM; CLU_034289_1_0_4; -.
DR OMA; AWTGDWG; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000001436; Plasmid megaplasmid Rsp.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 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 SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Plasmid; Polyamine biosynthesis;
KW Reference proteome; Spermidine biosynthesis; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..525
FT /note="Polyamine aminopropyltransferase 1"
FT /id="PRO_0000156501"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT DOMAIN 220..464
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT REGION 222..471
FT /note="Spermidine synthase"
FT ACT_SITE 385
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 259
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 289
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 313
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 333
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 367..368
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ SEQUENCE 525 AA; 58094 MW; 60ACBEDBA8CC3B34 CRC64;
MPTPPPDALD ASPQPVNRGN ALLVLAVFVV ASCGLAYELI AGALASYLLG DSILQFSSII
GAYLFAMGIG SWVSRYVADD ALLARFVDLE LLVGLFGGVS AAALFLLFAL ESAPFRLVLY
ALVTVIGVLV GMEIPLVMRM LHRRQAKFSD LVSRVLTFDY LGALAVSLLF PLVLAPRLGL
VRTGFLFGLC NTAIAVWTLW HFRAELGLSA RLRGAMAWRA GMVGAALLAG FAASDRLTHW
SERALFGDEI IHAISSPYQR LVVTRWKDDL RLYINGNLQF SSRDEYRYHE ALVLPALESV
RGARRVLVLG GGDGLALRQI LKYPQVEHVT LVDLDPRMTS LFSHAEALVA LNQHAFSDPR
VTVVNADAGQ WLQTAADMFD VAIVDFPDPS NFSIGKLYSV PFYRLLSRHV ADTGLVVIQA
TSPYFAPRSY WCVDATLKEA GYRTWPYHAL VPSFGEWGFI LAAPGRADFR PPTTYRVPTR
FLDADTTHQM FSFAPDMPRP QVEPNRLNNQ SLVRYFEEDW HGVLR
