ID BPSA_THEKO Reviewed; 351 AA.
AC Q5JIZ3;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=N(4)-bis(aminopropyl)spermidine synthase {ECO:0000255|HAMAP-Rule:MF_01947, ECO:0000305};
DE EC=2.5.1.128 {ECO:0000255|HAMAP-Rule:MF_01947, ECO:0000269|PubMed:24610711};
DE AltName: Full=Branched-chain polyamine synthase A {ECO:0000255|HAMAP-Rule:MF_01947, ECO:0000303|PubMed:24610711};
GN Name=bpsA {ECO:0000255|HAMAP-Rule:MF_01947, ECO:0000303|PubMed:24610711};
GN OrderedLocusNames=TK1691 {ECO:0000312|EMBL:BAD85880.1};
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=24610711; DOI=10.1128/jb.01515-14;
RA Okada K., Hidese R., Fukuda W., Niitsu M., Takao K., Horai Y., Umezawa N.,
RA Higuchi T., Oshima T., Yoshikawa Y., Imanaka T., Fujiwara S.;
RT "Identification of a novel aminopropyltransferase involved in the synthesis
RT of branched-chain polyamines in hyperthermophiles.";
RL J. Bacteriol. 196:1866-1876(2014).
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 Can also use spermine to produce N(4)-aminopropylspermine.
CC {ECO:0000269|PubMed:24610711}.
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 ECO:0000269|PubMed:24610711};
CC -!- PATHWAY: Amine and polyamine biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_01947, ECO:0000269|PubMed:24610711}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01947,
CC ECO:0000269|PubMed:24610711}.
CC -!- DISRUPTION PHENOTYPE: Grows at 85 degrees Celsius with a slightly
CC longer lag phase, but is unable to grow at 93 degrees Celsius.
CC {ECO:0000269|PubMed:24610711}.
CC -!- SIMILARITY: Belongs to the branched-chain polyamine synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_01947, ECO:0000305}.
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DR EMBL; AP006878; BAD85880.1; -; Genomic_DNA.
DR RefSeq; WP_011250642.1; NC_006624.1.
DR PDB; 5XNC; X-ray; 1.84 A; A/B/C/D/E/F/G=1-351.
DR PDB; 5XNF; X-ray; 1.90 A; A/B=1-351.
DR PDB; 5XNH; X-ray; 1.95 A; A/H=1-351.
DR PDB; 6J26; X-ray; 2.00 A; A/B=1-351.
DR PDBsum; 5XNC; -.
DR PDBsum; 5XNF; -.
DR PDBsum; 5XNH; -.
DR PDBsum; 6J26; -.
DR AlphaFoldDB; Q5JIZ3; -.
DR SMR; Q5JIZ3; -.
DR STRING; 69014.TK1691; -.
DR EnsemblBacteria; BAD85880; BAD85880; TK1691.
DR GeneID; 78448220; -.
DR KEGG; tko:TK1691; -.
DR PATRIC; fig|69014.16.peg.1649; -.
DR eggNOG; arCOG00913; Archaea.
DR HOGENOM; CLU_042160_0_0_2; -.
DR InParanoid; Q5JIZ3; -.
DR OrthoDB; 358909at2157; -.
DR PhylomeDB; Q5JIZ3; -.
DR BioCyc; MetaCyc:MONOMER-21054; -.
DR BRENDA; 2.5.1.128; 5246.
DR Proteomes; UP000000536; 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; IDA:UniProtKB.
DR GO; GO:0006596; P:polyamine biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Polyamine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..351
FT /note="N(4)-bis(aminopropyl)spermidine synthase"
FT /id="PRO_0000432214"
FT HELIX 1..9
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 18..30
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:5XNC"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:5XNC"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:5XNC"
FT TURN 92..96
FT /evidence="ECO:0007829|PDB:5XNC"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:5XNC"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:5XNC"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:5XNC"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 182..195
FT /evidence="ECO:0007829|PDB:5XNC"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:5XNC"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 230..243
FT /evidence="ECO:0007829|PDB:5XNC"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:5XNC"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 262..274
FT /evidence="ECO:0007829|PDB:5XNC"
FT STRAND 279..290
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:5XNC"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:5XNC"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:5XNC"
SQ SEQUENCE 351 AA; 40229 MW; 06FC2F12957B4568 CRC64;
MREIIERVKE KTTIPVYERT IENVLSAIQA SGDVWRIVDL SEEPLPLVVA VVTALYELGY
VAFENNQVIL TRKGKELVEK YGIGPRADYT CSHCQGRTVE IDAFSELLEQ FKEITRDRPE
PAHQFDQAYV TPETTVARVA LMHSRGDLEN KEVFVLGDDD LTSVALMLSG LPKRIAVLDI
DERLTKFIEK AADEIGYENI EIFTFDLRKP LPDYALHKFD TFITDPPETV EAIRAFVGRG
IATLKGPGCA GYFGITRRES SLDKWREIQR VLLNEFGVVI TDIIRNFNEY VNWGYVEETR
AWRLLPIKVK PSYNWYKSYM FRIQTLEGSK GFEDEITVGQ ELYDDEESST T
//
