ID D3RZV7_FERPA Unreviewed; 344 AA.
AC D3RZV7;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=Ferp_1880 {ECO:0000313|EMBL:ADC66020.1};
OS Ferroglobus placidus (strain DSM 10642 / AEDII12DO).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Ferroglobus.
OX NCBI_TaxID=589924 {ECO:0000313|EMBL:ADC66020.1, ECO:0000313|Proteomes:UP000002613};
RN [1] {ECO:0000313|Proteomes:UP000002613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Holmes D.,
RA Lovley D., Kyrpides N., Anderson I.J., Woyke T.;
RT "Complete sequence of Ferroglobus placidus DSM 10642.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADC66020.1, ECO:0000313|Proteomes:UP000002613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RX PubMed=22180810; DOI=10.4056/sigs.2225018;
RA Anderson I., Risso C., Holmes D., Lucas S., Copeland A., Lapidus A.,
RA Cheng J.F., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Woyke T.,
RA Lovley D., Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Ferroglobus placidus AEDII12DO.";
RL Stand. Genomic Sci. 5:50-60(2011).
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; CP001899; ADC66020.1; -; Genomic_DNA.
DR RefSeq; WP_012966359.1; NC_013849.1.
DR AlphaFoldDB; D3RZV7; -.
DR STRING; 589924.Ferp_1880; -.
DR PaxDb; 589924-Ferp_1880; -.
DR GeneID; 8779410; -.
DR KEGG; fpl:Ferp_1880; -.
DR eggNOG; arCOG00913; Archaea.
DR HOGENOM; CLU_042160_0_0_2; -.
DR OrthoDB; 358909at2157; -.
DR Proteomes; UP000002613; 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 InterPro; IPR036390; WH_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.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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:UP000002613};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01947}.
FT DOMAIN 92..337
FT /note="N(4)-bis(aminopropyl)spermidine synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01861"
SQ SEQUENCE 344 AA; 39649 MW; 65702160719BA3A3 CRC64;
MMERIRKQIL QALAGGEISV YKLIDLQDAS LPEFFQLLQE MEEGEIIQIS DGKVGLTEKG
RELAEKLGAK YFDVSCEHCE YTGLKIHDFF KDVLDKYLEI AKERPETVEE YDQGYISPEG
VIKRVEFVYE RGDLLKSRIF VVGDDDLFSI AAALTGMPEK IFVVDIDERL INFINKVAEE
YSLPIEAMVY DVQQAFPEEL KKKFDVFVTD PVETIPGLKL FLSRGVSTLK GPGCSGYFGI
TTLEASRKKW YEIQKMIHDM GFVITDMRRK FSVYPQDEKN FFRFQEKLPI VEKLGAKIDY
DWYKSTLYRI EAVKDPKPLV EGEMIIDEAV YRDSESWATP YGAD
//
