SPEE_OCEIH
ID SPEE_OCEIH Reviewed; 512 AA.
AC Q8CV14;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=OB0943;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(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; BA000028; BAC12899.1; -; Genomic_DNA.
DR RefSeq; WP_011065345.1; NC_004193.1.
DR AlphaFoldDB; Q8CV14; -.
DR SMR; Q8CV14; -.
DR STRING; 221109.22776624; -.
DR EnsemblBacteria; BAC12899; BAC12899; BAC12899.
DR KEGG; oih:OB0943; -.
DR eggNOG; COG4262; Bacteria.
DR HOGENOM; CLU_034289_1_0_9; -.
DR OMA; SFGEWGY; -.
DR OrthoDB; 1613081at2; -.
DR PhylomeDB; Q8CV14; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000000822; Chromosome.
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; Reference proteome;
KW Spermidine biosynthesis; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..512
FT /note="Polyamine aminopropyltransferase"
FT /id="PRO_0000156492"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT DOMAIN 215..450
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT REGION 217..457
FT /note="Spermidine synthase"
FT ACT_SITE 371
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 245
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 275
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 299
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 319
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 353..354
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ SEQUENCE 512 AA; 57494 MW; 78D5AC386F1327BF CRC64;
MLNDKAIRQS KIIYWSSGIV SICGIIFEVL FGALGSYILG DGVKQYTLTI SLFLTGMGIG
ASLSEKFMRN LIIKFVWIEF CVALIGGFSS FIMFGITAFA PAGTDAFYLY SITLIIGALT
GVELPILIRK ANEIGVTLNK STARVLFSDY AGGLIGGVLF VFLFRPYFGM VKTAFLVGLI
NLTVALIVLW LFRKEIRHFI VHAVIGGVIG VLLIAGLFFG EEMAFNFEQK LYQDPIIHME
ESSYQKITVT QDEKDIRLYL DGSLQFSSVD EHRYHEVLVH PAMANVETPE NVLILGGGDG
IAAKEVLKYQ DVKQVTLVDL DPAVVELANE NRHLLEINEG ALMDEKVEVK NMDAFQFLED
TSEWYDVILV DLPDPNNESL NKLYTKEFYS LVRNHLKPEG TLMVQATSPV FAREVYWTIS
ETISSTNLNT ENLHVDVPSF GNWGFVMASR EEIDLDIMEI PVSTRFLTDD MMPALTAFGK
DEDQQIPNFE LKANTLIDPH LIQIYEKAWE NY
