ID E4QCT4_CALH1 Unreviewed; 355 AA.
AC E4QCT4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=Calhy_0562 {ECO:0000313|EMBL:ADQ06303.1};
OS Caldicellulosiruptor hydrothermalis (strain DSM 18901 / VKM B-2411 / 108).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=632292 {ECO:0000313|EMBL:ADQ06303.1, ECO:0000313|Proteomes:UP000006890};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=108;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., Blumer-Schuette S.E., Kelly R.M., Woyke T.;
RT "Complete sequence of Caldicellulosiruptor hydrothermalis 108.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ06303.1, ECO:0000313|Proteomes:UP000006890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18901 / VKM B-2411 / 108
RC {ECO:0000313|Proteomes:UP000006890};
RX PubMed=21216991; DOI=10.1128/JB.01515-10;
RA Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A.,
RA Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., Woyke T.,
RA Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., Detter J.C.,
RA Walston-Davenport K., Han S., Adams M.W., Kelly R.M.;
RT "Complete genome sequences for the anaerobic, extremely thermophilic plant
RT biomass-degrading bacteria Caldicellulosiruptor hydrothermalis,
RT Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor kronotskyensis,
RT Caldicellulosiruptor owensenis, and Caldicellulosiruptor lactoaceticus.";
RL J. Bacteriol. 193:1483-1484(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; CP002219; ADQ06303.1; -; Genomic_DNA.
DR RefSeq; WP_013402510.1; NC_014652.1.
DR AlphaFoldDB; E4QCT4; -.
DR STRING; 632292.Calhy_0562; -.
DR KEGG; chd:Calhy_0562; -.
DR eggNOG; COG1568; Bacteria.
DR HOGENOM; CLU_042160_0_0_9; -.
DR OrthoDB; 7593728at2; -.
DR Proteomes; UP000006890; 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..349
FT /note="N(4)-bis(aminopropyl)spermidine synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01861"
SQ SEQUENCE 355 AA; 40766 MW; E14A8AA003AFDB9C CRC64;
MDVLKGAVDF VQNKTKVEIN QRDIEKILSA LNSTNHFWEV IFLSQKPFAV VRETINYLIS
IDFVKTDESG NLILTEKGKE FISANNIPVV KNYTCSYCEG RGIVFSEIKD AYEKFKEIVK
TRPDAIVEYD QGYVTEETAY SRIALMIKKG DLVGKRLIVF GDDDLVSIAA ALTKLPKEVI
VLEIDKRLVD FINQAAKEHN LNLKAIEYDF RNKLPDDFVK SFDTFTIDPP ETIEALDLCF
TRTISSLKGA GCAGYFGLTN IEASLSKWHE FQKLLLNKFN AVITDIIENF NHYVNWNYLL
PSLESSLTFV NVQPKLNWYT SSMYRIELVK DVDIKNEYIN CELYIDKEAI LYKEN
//
