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Database: UniProt
Entry: A0A0A0F021_9GAMM
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ID   A0A0A0F021_9GAMM        Unreviewed;       283 AA.
AC   A0A0A0F021;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=N799_04925 {ECO:0000313|EMBL:KGM56139.1};
OS   Lysobacter arseniciresistens ZS79.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=913325 {ECO:0000313|EMBL:KGM56139.1, ECO:0000313|Proteomes:UP000029989};
RN   [1] {ECO:0000313|EMBL:KGM56139.1, ECO:0000313|Proteomes:UP000029989}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS79 {ECO:0000313|EMBL:KGM56139.1,
RC   ECO:0000313|Proteomes:UP000029989};
RX   PubMed=26516404; DOI=10.1186/s40793-015-0070-5;
RA   Liu L., Zhang S., Luo M., Wang G.;
RT   "Genomic information of the arsenic-resistant bacterium Lysobacter
RT   arseniciresistens type strain ZS79(T) and comparison of Lysobacter draft
RT   genomes.";
RL   Stand. Genomic Sci. 10:88-88(2015).
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         ECO:0000256|RuleBase:RU003837};
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   -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC       {ECO:0000256|ARBA:ARBA00007867, ECO:0000256|HAMAP-Rule:MF_00198,
CC       ECO:0000256|RuleBase:RU003836}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGM56139.1}.
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DR   EMBL; AVPT01000015; KGM56139.1; -; Genomic_DNA.
DR   RefSeq; WP_036211105.1; NZ_AVPT01000015.1.
DR   AlphaFoldDB; A0A0A0F021; -.
DR   STRING; 913325.N799_04925; -.
DR   eggNOG; COG0421; Bacteria.
DR   OrthoDB; 9793120at2; -.
DR   UniPathway; UPA00248; UER00314.
DR   Proteomes; UP000029989; Unassembled WGS sequence.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.30.140.10; Spermidine synthase, tetramerisation domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   NCBIfam; TIGR00417; speE; 1.
DR   PANTHER; PTHR11558:SF11; SPERMIDINE SYNTHASE; 1.
DR   PANTHER; PTHR11558; SPERMIDINE/SPERMINE SYNTHASE; 1.
DR   Pfam; PF17284; Spermine_synt_N; 1.
DR   Pfam; PF01564; Spermine_synth; 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   Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|HAMAP-
KW   Rule:MF_00198}; Reference proteome {ECO:0000313|Proteomes:UP000029989};
KW   Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP-
KW   Rule:MF_00198};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00198}.
FT   DOMAIN          5..241
FT                   /note="PABS"
FT                   /evidence="ECO:0000259|PROSITE:PS51006"
FT   ACT_SITE        160
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198,
FT                   ECO:0000256|PROSITE-ProRule:PRU00354"
FT   BINDING         35
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         66
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         90
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         110
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         141..142
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         160..163
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         167
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
SQ   SEQUENCE   283 AA;  31236 MW;  66CDF7C793BC33E3 CRC64;
     MNAATSWHYE NFDPSGSAIG YRITGKLDEV QSPFQKIEIY GSTDWGNLML IDGAMMLTAR
     DNFLYHEMMS HPALFTHAAP KNVVIIGGGD CGTLREVLRH PGVERAVQCD IDEQVTRMAE
     KWFPELCESN GDPRAQLLFD DGIAYMANRE PGSLDIVIVD STDPVGPAEG LFNKAFYESC
     FRALKDDGIL VQQSESPLVL LELIKEMRGE MGKAGFTAFQ TLPFPQPCYP TGWWSCTLAR
     KSGGFDFRET DARAKAFDTK YYSADIHKGA QALPPFVAAA LGG
//
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