SPEE1_AQUAE
ID SPEE1_AQUAE Reviewed; 280 AA.
AC O66473;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=speE;
GN OrderedLocusNames=aq_062;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00198}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000657; AAC06436.1; -; Genomic_DNA.
DR PIR; F70305; F70305.
DR RefSeq; NP_213033.1; NC_000918.1.
DR RefSeq; WP_010879971.1; NC_000918.1.
DR AlphaFoldDB; O66473; -.
DR SMR; O66473; -.
DR STRING; 224324.aq_062; -.
DR EnsemblBacteria; AAC06436; AAC06436; aq_062.
DR KEGG; aae:aq_062; -.
DR PATRIC; fig|224324.8.peg.50; -.
DR eggNOG; COG0421; Bacteria.
DR HOGENOM; CLU_048199_1_0_0; -.
DR InParanoid; O66473; -.
DR OMA; LWPGQSF; -.
DR OrthoDB; 1613081at2; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004766; F:spermidine synthase activity; IBA:GO_Central.
DR GO; GO:0008295; P:spermidine biosynthetic process; IBA:GO_Central.
DR Gene3D; 2.30.140.10; -; 1.
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 InterPro; IPR035246; Spermidine_synt_N.
DR InterPro; IPR037163; Spermidine_synt_N_sf.
DR PANTHER; PTHR11558; PTHR11558; 1.
DR Pfam; PF17284; Spermine_synt_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00417; speE; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Polyamine biosynthesis; Reference proteome;
KW Spermidine biosynthesis; Transferase.
FT CHAIN 1..280
FT /note="Polyamine aminopropyltransferase 1"
FT /id="PRO_0000156463"
FT DOMAIN 3..237
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 33
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 64
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 88
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 108
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 139..140
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 157..160
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ SEQUENCE 280 AA; 32594 MW; 084358BF0D508792 CRC64;
MRDIVFIERD PYAPIRHCYT VSKILYQGKS PYQEIQVIES PEFGRMLILD GVVQLDEKYE
FLYHEYLAHV PLHAHPNPRN VLIIGGGDGG TLREVLKHDI VERAVLVDID KEVIEVSKKY
LPTLSVGFQD PRAIVVNEDG YKYVQDYENE FDVIIVDSTD PVGFAHVLTT EDFFRHVYKA
LKEDGIFVAQ TESIHYHLEM VSNIQQRLKK VFPIVDLYTS VIPIYAGYWW TFSIASKKYP
VRTPAREVKV QTKIYDADMH EYAFLPESFY NKIVNGEYKY
