SPEE_LEPIC
ID SPEE_LEPIC Reviewed; 498 AA.
AC Q72V65;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Putrescine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=PAPT {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Spermidine synthase {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198};
DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198};
GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; OrderedLocusNames=LIC_10437;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS (strain Fiocruz L1-130).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=267671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fiocruz L1-130;
RX PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT insights into physiology and pathogenesis.";
RL J. Bacteriol. 186:2164-2172(2004).
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; AE016823; AAS69059.1; -; Genomic_DNA.
DR RefSeq; WP_001192499.1; NC_005823.1.
DR AlphaFoldDB; Q72V65; -.
DR SMR; Q72V65; -.
DR PaxDb; Q72V65; -.
DR EnsemblBacteria; AAS69059; AAS69059; LIC_10437.
DR GeneID; 61143790; -.
DR KEGG; lic:LIC_10437; -.
DR HOGENOM; CLU_034289_1_0_12; -.
DR OMA; SFGEWGY; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000007037; Chromosome I.
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; IPR030373; PABS_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001045; Spermi_synthase.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Polyamine biosynthesis; Spermidine biosynthesis;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..498
FT /note="Polyamine aminopropyltransferase"
FT /id="PRO_0000156484"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT DOMAIN 200..439
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT REGION 196..446
FT /note="Spermidine synthase"
FT ACT_SITE 360
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 234
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 264
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 288
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 308
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 342..343
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ SEQUENCE 498 AA; 56751 MW; 819569F2413E5770 CRC64;
MQTALYISVL IISSCGLVYE LLAGTIASYL LGETVTQFSL IIGTYLFSMG VGSWLSKYLE
KDLIPKFLEI ELAIGLVGGF SSAILYLSFG QIRYFQIPLF LLVILIGILV GLEIPVLLRI
LKKELQFKEL VSRVLSLDYV GALLASILFP IFFAPKLGLM RTGFIFGILN VGVALWGTWV
LPLRQSKIII LRAQSVVVLT LLILGFSYSD LITYYSEESL YTDEIILSKQ TQYQRIIVTR
WKNEIRLFLN GHLQFSSRDE YRYHETLVHP ALLAHPTPKK VLVLGGGDGL AVREILKHKN
VESVTLVDLD SAITNLFSEH GILKKLNEES LKNSKVTVIN TDAFLWLEES DQIFDVVLID
FPDPSNFSLG KLYTTAFFHT LKRRMNETSV LEIQSTSPLF ARSSYWCIER TIASLGFYTL
PLHVYVPSFG EWGFVLAGQR PIQFKKDFPK DLKFLNIQEL ESIQTFPQDM SRVPVEINRL
DNQALVRYYD REWNRILD
