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Database: UniProt
Entry: E8UW92_THEBF
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ID   E8UW92_THEBF            Unreviewed;       358 AA.
AC   E8UW92;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=Thebr_0649 {ECO:0000313|EMBL:ADV79247.1};
OS   Thermoanaerobacter brockii subsp. finnii (strain ATCC 43586 / DSM 3389 /
OS   AKO-1) (Thermoanaerobacter finnii).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=509193 {ECO:0000313|EMBL:ADV79247.1, ECO:0000313|Proteomes:UP000002062};
RN   [1] {ECO:0000313|EMBL:ADV79247.1, ECO:0000313|Proteomes:UP000002062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43586 / DSM 3389 / AKO-1
RC   {ECO:0000313|Proteomes:UP000002062};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Hemme C.L., Woyke T.;
RT   "Complete sequence of Thermoanaerobacter brockii finnii Ako-1.";
RL   Submitted (JAN-2011) 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; CP002466; ADV79247.1; -; Genomic_DNA.
DR   RefSeq; WP_004403525.1; NC_014964.1.
DR   AlphaFoldDB; E8UW92; -.
DR   KEGG; tbo:Thebr_0649; -.
DR   HOGENOM; CLU_042160_0_0_9; -.
DR   Proteomes; UP000002062; 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   Transferase {ECO:0000256|HAMAP-Rule:MF_01947}.
FT   DOMAIN          110..350
FT                   /note="N(4)-bis(aminopropyl)spermidine synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01861"
SQ   SEQUENCE   358 AA;  40689 MW;  6DD359DC14ABC40D CRC64;
     MESLQDIAHQ IYQKTGVMTS SKDVEKILSA AAATPHFWEI ISLSQKPFSV VAEIIELLRQ
     RNLLKVEKNG DIKFNSKGLE YLGSLKIAPK RTYTCHACEG RGINFSKLED LIKKFDQVTV
     NRPKAISDYD QGFVTTQTVV GRIALLAERG DLEGKKLLVL GDDDLVSIAA GLSGMPTEIV
     VMEIDDRLVE YINEVANKYN LPIKAMKYDF RDKLPEEYVG YFDTFITDPP ETIEALEICI
     GRGISALSKE GCAGYFGLTL IEASLEKWNV FQQILASKFK VVVTDIIHNF NHYVNWDYLL
     NTVGKQYEFV QVEPKLNWYR SSMYRIETLK DSKGIENEYK PCELYVDEEA LIYRGDKA
//
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