ID   BPSA_THETH              Reviewed;         343 AA.
AC   P25125;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=N(4)-bis(aminopropyl)spermidine synthase {ECO:0000255|HAMAP-Rule:MF_01947};
DE            EC=2.5.1.128 {ECO:0000255|HAMAP-Rule:MF_01947};
DE   AltName: Full=Branched-chain polyamine synthase A {ECO:0000255|HAMAP-Rule:MF_01947};
GN   Name=bpsA {ECO:0000255|HAMAP-Rule:MF_01947};
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33923 / DSM 674 / AT-62;
RX   PubMed=2034208; DOI=10.1007/bf00273580;
RA   Nishiyama M., Horinouchi S., Beppu T.;
RT   "Characterization of an operon encoding succinyl-CoA synthetase and malate
RT   dehydrogenase from Thermus flavus AT-62 and its expression in Escherichia
RT   coli.";
RL   Mol. Gen. Genet. 226:1-9(1991).
CC   -!- FUNCTION: Involved in the biosynthesis of branched-chain polyamines,
CC       which support the growth of thermophiles under high-temperature
CC       conditions. Catalyzes the sequential condensation of spermidine with
CC       the aminopropyl groups of decarboxylated S-adenosylmethionines to
CC       produce N(4)-bis(aminopropyl)spermidine via N(4)-aminopropylspermidine.
CC       {ECO:0000255|HAMAP-Rule:MF_01947}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = 2
CC         H(+) + N(4)-bis(aminopropyl)spermidine + 2 S-methyl-5'-thioadenosine;
CC         Xref=Rhea:RHEA:44132, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
CC         ChEBI:CHEBI:57443, ChEBI:CHEBI:57834, ChEBI:CHEBI:82771;
CC         EC=2.5.1.128; Evidence={ECO:0000255|HAMAP-Rule:MF_01947};
CC   -!- PATHWAY: Amine and polyamine biosynthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_01947}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01947}.
CC   -!- SIMILARITY: Belongs to the branched-chain polyamine synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01947}.
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DR   EMBL; X54073; CAA38005.1; -; Genomic_DNA.
DR   PIR; S15949; S15949.
DR   AlphaFoldDB; P25125; -.
DR   SMR; P25125; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProtKB-UniRule.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01947; Aminopropyltransf_BpsA; 1.
DR   InterPro; IPR014435; BpsA.
DR   InterPro; IPR002723; BpsA_C.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF01861; DUF43; 1.
DR   PIRSF; PIRSF005895; UCP005895_mtase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Polyamine biosynthesis; Transferase.
FT   CHAIN           1..343
FT                   /note="N(4)-bis(aminopropyl)spermidine synthase"
FT                   /id="PRO_0000066474"
SQ   SEQUENCE   343 AA;  38395 MW;  5721784137AD823B CRC64;
     MNKEALVQVA EEVRRATGLP VGWRDVERTL GALRATRDLW EAVRLSRVPL RFLVPIWEGL
     ARRGLLRVEE GLDLLAEVPA PRPGEAACPA CEGRGLVGER LPGRAAERFL AWAKERPEAI
     QDFDQGYVTP ESTLARVALA WNWGDLEGKE VLVLGDDDLT GLAAALTGLP KRVVVLDADP
     RIVRFLERAA KAEGLPLEAH VHDLREPLPE AWVHAFHTFF TDPVEGPLGL QAFVGRGLLA
     LEGEGCAGYV GLTHVEASLA KWADFQRFLL ENGAVITELR DGFHVYENWG YIEQMRAWPW
     LPVKRRPEKP WYTSALIRLE LLRRADLENA RVEGDLQDEE ATY