ID A0A420W7V0_9BACT Unreviewed; 351 AA.
AC A0A420W7V0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
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 ORFNames=C7457_0221 {ECO:0000313|EMBL:RKQ63352.1};
OS Thermovibrio guaymasensis.
OC Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC Desulfurobacteriaceae; Thermovibrio.
OX NCBI_TaxID=240167 {ECO:0000313|EMBL:RKQ63352.1, ECO:0000313|Proteomes:UP000280881};
RN [1] {ECO:0000313|EMBL:RKQ63352.1, ECO:0000313|Proteomes:UP000280881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15521 {ECO:0000313|EMBL:RKQ63352.1,
RC ECO:0000313|Proteomes:UP000280881};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (OCT-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKQ63352.1}.
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DR EMBL; RBIE01000001; RKQ63352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420W7V0; -.
DR OrthoDB; 7593728at2; -.
DR Proteomes; UP000280881; Unassembled WGS sequence.
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 CDD; cd02440; AdoMet_MTases; 1.
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 112..350
FT /note="N(4)-bis(aminopropyl)spermidine synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01861"
SQ SEQUENCE 351 AA; 39694 MW; F3A1F2263446165A CRC64;
MEILERIAQE AEKNTQVPAY SRSVEKVLSA VMSSSNFWKI VDLSDEPLPL VAEILKLLNK
YDLVAFEGDQ ILLTEAGAEL VKKLGIQPFV SHRCPTCGGR GVVIDESLKP AFEKFFKIQE
NRPPAIHQYD QGYVTPENTF ARVALADDRG DLRGKRVCVL GDDDLMSIAL ALTGLPAKVT
ILEIDERLVN FIKEVSDEYN LNIDARVHDL RQPLPEDVVG AYDTFFTDPP ETVEAIKAFV
GRGVATLKGP RCAGYFGVTR RESSLDKWRR IQIELLNMGL VITDLLHNFN EYVNWDYYQE
MRGWQLTPVK VPPKEIWYKS TQFRVETVRG FKGFNDPIVG DIYNDAESST T
//
