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Database: UniProt
Entry: A0A223CX35_9BACL
LinkDB: A0A223CX35_9BACL
Original site: A0A223CX35_9BACL 
ID   A0A223CX35_9BACL        Unreviewed;       276 AA.
AC   A0A223CX35;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   08-NOV-2023, entry version 24.
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=CIG75_01435 {ECO:0000313|EMBL:ASS73765.1};
OS   Tumebacillus algifaecis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Tumebacillus.
OX   NCBI_TaxID=1214604 {ECO:0000313|EMBL:ASS73765.1, ECO:0000313|Proteomes:UP000214688};
RN   [1] {ECO:0000313|EMBL:ASS73765.1, ECO:0000313|Proteomes:UP000214688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=THMBR28 {ECO:0000313|EMBL:ASS73765.1,
RC   ECO:0000313|Proteomes:UP000214688};
RX   PubMed=25858243; DOI=10.1099/ijs.0.000240;
RA   Wu Y.F., Zhang B., Xing P., Wu Q.L., Liu S.J.;
RT   "Tumebacillus algifaecis sp. nov., isolated from decomposing algal scum.";
RL   Int. J. Syst. Evol. Microbiol. 65:2194-2198(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}.
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DR   EMBL; CP022657; ASS73765.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A223CX35; -.
DR   KEGG; tab:CIG75_01435; -.
DR   OrthoDB; 9793120at2; -.
DR   UniPathway; UPA00248; UER00314.
DR   Proteomes; UP000214688; Chromosome.
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:UP000214688};
KW   Spermidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00198,
KW   ECO:0000256|RuleBase:RU003837};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00198}.
FT   DOMAIN          2..235
FT                   /note="PABS"
FT                   /evidence="ECO:0000259|PROSITE:PS51006"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198,
FT                   ECO:0000256|PROSITE-ProRule:PRU00354"
FT   BINDING         31
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         62
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         86
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         106
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         137..138
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         155..158
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         162
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
SQ   SEQUENCE   276 AA;  31249 MW;  B05CE66822253CB7 CRC64;
     MELWYTEKQT ENYGITVKIT NTLHTEKTEF QDLAMIETLQ WGKMLVLDGM VMTTDKDEFV
     YHEMITHLAM NTHPNPKTAL VVGGGDGGAI REILKYPSIE KAVLAEIDGR VIEVSREYLP
     QIAGKLDDPR VDVQVVDGIK YIHDNKDSFD VILVDSTEPV GPAVGLFARD FYQGIFEALK
     EDGIMVAQTE SPFFNADLIT RVYKDIAAIY PVTRYYTAAI PTYPSGLWSF TMGSKKYDPL
     EVDESKLIDP EGTKYYHKGM HKSVFNVPKF VMELLK
//
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