ID   SPEE_SYNJA              Reviewed;         312 AA.
AC   Q2JQS1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=CYA_0575;
OS   Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS   A-Prime).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=321327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-3-3Ab;
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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}.
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DR   EMBL; CP000239; ABC98791.1; -; Genomic_DNA.
DR   RefSeq; WP_011429478.1; NC_007775.1.
DR   AlphaFoldDB; Q2JQS1; -.
DR   SMR; Q2JQS1; -.
DR   STRING; 321327.CYA_0575; -.
DR   EnsemblBacteria; ABC98791; ABC98791; CYA_0575.
DR   KEGG; cya:CYA_0575; -.
DR   eggNOG; COG0421; Bacteria.
DR   HOGENOM; CLU_048199_0_1_3; -.
DR   OMA; WIPSFGY; -.
DR   OrthoDB; 1613081at2; -.
DR   UniPathway; UPA00248; UER00314.
DR   Proteomes; UP000008818; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; 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; 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; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR001045; Spermi_synthase.
DR   InterPro; IPR035246; Spermidine_synt_N.
DR   InterPro; IPR037163; Spermidine_synt_N_sf.
DR   Pfam; PF17284; Spermine_synt_N; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51006; PABS_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Polyamine biosynthesis; Spermidine biosynthesis; Transferase.
FT   CHAIN           1..312
FT                   /note="Polyamine aminopropyltransferase"
FT                   /id="PRO_1000012023"
FT   DOMAIN          7..247
FT                   /note="PABS"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   ACT_SITE        165
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         36
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         67
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         95
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         115
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         147..148
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT   BINDING         174
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ   SEQUENCE   312 AA;  34721 MW;  BF60B3C978193765 CRC64;
     MNTPKSFFWA QEYFTPWDYT ARAITRILAY RKTRFQEMLI AETGAYGKGL MLDGHWQSTT
     ADEFLYHEAL VHPALVQVVQ AGGIPRRVLI LGGAEGATLR EVLRWRSVEQ VVMVDIDGEV
     VEACREHLPE MHQGSFADPR AEVVIADALD FLGQTEPIWD AILSDLSDPV EAGPAYRLFT
     QEFFRQVRSK LQTAGAFVIQ AGPTGPVELW QHTRIVHTLK TVFAAVQPYA IYAPTYGGPL
     GFALAAQDPI SSRPEPEQVD QILAQHLDPD RGALRFIDGI TLLGLYQVPA HLRRAIAAET
     TVYTLANPPQ VE