ID   BPSA_METJA              Reviewed;         350 AA.
AC   Q58669;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
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}; OrderedLocusNames=MJ1273;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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; L77117; AAB99279.1; -; Genomic_DNA.
DR   PIR; H64458; H64458.
DR   RefSeq; WP_010870786.1; NC_000909.1.
DR   AlphaFoldDB; Q58669; -.
DR   SMR; Q58669; -.
DR   STRING; 243232.MJ_1273; -.
DR   EnsemblBacteria; AAB99279; AAB99279; MJ_1273.
DR   GeneID; 1452171; -.
DR   KEGG; mja:MJ_1273; -.
DR   eggNOG; arCOG00913; Archaea.
DR   HOGENOM; CLU_042160_0_0_2; -.
DR   InParanoid; Q58669; -.
DR   OMA; KSYMFRI; -.
DR   OrthoDB; 23573at2157; -.
DR   PhylomeDB; Q58669; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome; Transferase.
FT   CHAIN           1..350
FT                   /note="N(4)-bis(aminopropyl)spermidine synthase"
FT                   /id="PRO_0000107245"
SQ   SEQUENCE   350 AA;  40420 MW;  2F301BF8976C22BB CRC64;
     MERILEKVRA KSEIPVYDKS IENVLSAILT TNDFWKIVDL SEEPLPLVAD IIRILEEEGL
     VKISNGIEFT EKGNEFIKSY GIGAKDNSVC ECCEGRGVSL KNYQDLLERF KEIVKNRPMP
     KHEYDQGFVT PECTISRIAL MNSRGDLFNK DVLVLGDDDL TSIALMLSNL PKKIVVVDID
     DRLINFIKEV AEQLNYKNIE VITLDLRKPL PEKYSRAFDT FITDPPETVY AVKTFIGRGI
     SALKGERRAG YFGITRRESS LDKWREIQRT LINDFNVVIT DIIRNFNHYV NWGYEEETRA
     WKLAPVKKKP EDIWYKSYMF RIETLKDSRG FEEEVDVGDE LYNDAESSTT