ID F5L6N6_CALTT Unreviewed; 286 AA.
AC F5L6N6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 ECO:0000313|EMBL:QZT34584.1};
GN ORFNames=CathTA2_1486 {ECO:0000313|EMBL:EGL82987.1}, HUR95_04250
GN {ECO:0000313|EMBL:QZT34584.1};
OS Caldalkalibacillus thermarum (strain TA2.A1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldalkalibacillus.
OX NCBI_TaxID=986075 {ECO:0000313|EMBL:EGL82987.1, ECO:0000313|Proteomes:UP000010716};
RN [1] {ECO:0000313|EMBL:EGL82987.1, ECO:0000313|Proteomes:UP000010716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA2.A1 {ECO:0000313|EMBL:EGL82987.1,
RC ECO:0000313|Proteomes:UP000010716};
RX PubMed=21685297; DOI=10.1128/JB.05035-11;
RA Kalamorz F., Keis S., McMillan D.G., Olsson K., Stanton J.A., Stockwell P.,
RA Black M.A., Klingeman D.M., Land M.L., Han C.S., Martin S.L., Becher S.A.,
RA Peddie C.J., Morgan H.W., Matthies D., Preiss L., Meier T., Brown S.D.,
RA Cook G.M.;
RT "Draft genome sequence of the thermoalkaliphilic Caldalkalibacillus
RT thermarum strain TA2.A1.";
RL J. Bacteriol. 193:4290-4291(2011).
RN [2] {ECO:0000313|EMBL:QZT34584.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TA2.A1 {ECO:0000313|EMBL:QZT34584.1};
RX PubMed=33030592;
RA de Jong S.I., van den Broek M.A., Merkel A.Y., de la Torre Cortes P.,
RA Kalamorz F., Cook G.M., van Loosdrecht M.C.M., McMillan D.G.G.;
RT "Genomic analysis of Caldalkalibacillus thermarum TA2.A1 reveals aerobic
RT alkaliphilic metabolism and evolutionary hallmarks linking alkaliphilic
RT bacteria and plant life.";
RL Extremophiles 24:923-935(2020).
RN [3] {ECO:0000313|EMBL:QZT34584.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TA2.A1 {ECO:0000313|EMBL:QZT34584.1};
RA de Jong S., van den Broek M., Merkel A., de la Torre Cortes P.,
RA Kalamorz F., Cook G., van Loosdrecht M., McMillan D.;
RL Submitted (AUG-2021) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00198}.
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DR EMBL; AFCE01000130; EGL82987.1; -; Genomic_DNA.
DR EMBL; CP082237; QZT34584.1; -; Genomic_DNA.
DR RefSeq; WP_007504456.1; NZ_CP082237.1.
DR AlphaFoldDB; F5L6N6; -.
DR KEGG; cthu:HUR95_04250; -.
DR eggNOG; COG0421; Bacteria.
DR OrthoDB; 9793120at2; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000010716; Unassembled WGS sequence.
DR Proteomes; UP000825179; Chromosome.
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; NF037959; MFS_SpdSyn; 1.
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:UP000010716};
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 14..247
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198,
FT ECO:0000256|PROSITE-ProRule:PRU00354"
FT BINDING 43
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 98
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 118
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 149..150
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 167..170
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 174
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
SQ SEQUENCE 286 AA; 32822 MW; 06B06D79CE54CD76 CRC64;
MSTKLEWLKE IDGQLWLVED EKENLRLYYR VKEVIHAEQS PFQHVMIVDT YEFGPTLVLD
GVIQTTSRDG HIYNEMITHI PLLTHPNPKR VLIIGGGDCG AAREVCKYAQ VEHIDMVEID
ELVVKVSKQY LTEVSGNLSD PRVRFIYEDG TTFVKNQNST YDVVIVDSSD PIGPAEQLFS
YEFYRDIEQA LKPDGLMVCQ SQSPIFHMDV LKQTYERISK LFPIARVYQA VVPTYPGGLW
SFTLGSKKYR PEQLEDKWNK EAKYVNKGIL KACFHLPESV RQALGV
//
