ID Q5SKV4_THET8 Unreviewed; 344 AA.
AC Q5SKV4;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=N(4)-bis(aminopropyl)spermidine synthase {ECO:0000256|HAMAP-Rule:MF_01947};
DE EC=2.5.1.128 {ECO:0000256|HAMAP-Rule:MF_01947};
DE AltName: Full=Branched-chain polyamine synthase A {ECO:0000256|HAMAP-Rule:MF_01947};
GN Name=bpsA {ECO:0000256|HAMAP-Rule:MF_01947};
GN OrderedLocusNames=TTHA0539 {ECO:0000313|EMBL:BAD70362.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852 {ECO:0000313|EMBL:BAD70362.1, ECO:0000313|Proteomes:UP000000532};
RN [1] {ECO:0000313|EMBL:BAD70362.1, ECO:0000313|Proteomes:UP000000532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8 {ECO:0000313|Proteomes:UP000000532};
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01947};
CC -!- PATHWAY: Amine and polyamine biosynthesis. {ECO:0000256|HAMAP-
CC Rule:MF_01947}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01947}.
CC -!- SIMILARITY: Belongs to the branched-chain polyamine synthase family.
CC {ECO:0000256|HAMAP-Rule:MF_01947}.
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DR EMBL; AP008226; BAD70362.1; -; Genomic_DNA.
DR RefSeq; WP_011228011.1; NC_006461.1.
DR RefSeq; YP_143805.1; NC_006461.1.
DR AlphaFoldDB; Q5SKV4; -.
DR EnsemblBacteria; BAD70362; BAD70362; BAD70362.
DR GeneID; 3168348; -.
DR KEGG; ttj:TTHA0539; -.
DR PATRIC; fig|300852.9.peg.538; -.
DR eggNOG; COG1568; Bacteria.
DR HOGENOM; CLU_042160_0_0_0; -.
DR PhylomeDB; Q5SKV4; -.
DR Proteomes; UP000000532; Chromosome.
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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 PANTHER; PTHR23290:SF0; RRNA N6-ADENOSINE-METHYLTRANSFERASE METTL5; 1.
DR PANTHER; PTHR23290; UNCHARACTERIZED; 1.
DR Pfam; PF01861; BpsA_C; 1.
DR PIRSF; PIRSF005895; UCP005895_mtase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01947};
KW Polyamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01947};
KW Reference proteome {ECO:0000313|Proteomes:UP000000532};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01947}.
FT DOMAIN 106..342
FT /note="N(4)-bis(aminopropyl)spermidine synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01861"
SQ SEQUENCE 344 AA; 38496 MW; 593DD1784137AD82 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 ATTY
//
