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Database: UniProt
Entry: A0A1T1H8J2_OCELI
LinkDB: A0A1T1H8J2_OCELI
Original site: A0A1T1H8J2_OCELI 
ID   A0A1T1H8J2_OCELI        Unreviewed;       286 AA.
AC   A0A1T1H8J2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=BTA35_0214285 {ECO:0000313|EMBL:OOV86148.1};
OS   Oceanospirillum linum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Oceanospirillum.
OX   NCBI_TaxID=966 {ECO:0000313|EMBL:OOV86148.1, ECO:0000313|Proteomes:UP000190064};
RN   [1] {ECO:0000313|EMBL:OOV86148.1, ECO:0000313|Proteomes:UP000190064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11336 {ECO:0000313|EMBL:OOV86148.1,
RC   ECO:0000313|Proteomes:UP000190064};
RA   Trachtenberg A.M., Carney J.G., Linnane J.D., Rheaume B.A., Pitts N.L.,
RA   Mykles D.L., Maclea K.S.;
RT   "Draft Genome Sequence of the Salt Water Bacterium Oceanospirillum linum
RT   ATCC 11336.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:OOV86148.1}.
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DR   EMBL; MTSD02000008; OOV86148.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T1H8J2; -.
DR   STRING; 966.BTA35_0214285; -.
DR   UniPathway; UPA00248; UER00314.
DR   Proteomes; UP000190064; 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:UP000190064};
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          7..244
FT                   /note="PABS"
FT                   /evidence="ECO:0000259|PROSITE:PS51006"
FT   ACT_SITE        162
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198,
FT                   ECO:0000256|PROSITE-ProRule:PRU00354"
FT   BINDING         37
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         68
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         92
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         112
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         143..144
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         162..165
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         169
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
SQ   SEQUENCE   286 AA;  32067 MW;  D961703C26B97888 CRC64;
     MSEQLDNNWF TEVFTSCGSG FSLKVKAKLH EEQSPYQKLE IYDTETYGNL MVIDGCVMLT
     DRDNFLYHEM MSHPALFSHP EPKRVVIIGG GDCGTLREVL KHPGVEKVTQ IDIDKLVTDL
     SEKYFPALCD SNNDPRAELL FEDGVKWVDE CPEESIDLII VDSTDPVGPA EGLFKVDFFK
     RCFRILKQGG VMVQQSESPL YHTDSIIKNL HVDMQAAGFS TTATLPFPQP VYPSGWWSCT
     LAGKGTDVKS FREADSAAKG FETDYYTVDM HRGALTLPPF MKKVLG
//
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