ID   BLTD_BACNB              Reviewed;         152 AA.
AC   D4FZ53;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Probable spermine N(1)-acetyltransferase {ECO:0000305};
DE            EC=2.3.1.57 {ECO:0000305|PubMed:29142164};
GN   Name=bltD {ECO:0000303|PubMed:29142164};
GN   ORFNames=BSNT_09050 {ECO:0000312|EMBL:BAI86134.1};
OS   Bacillus subtilis subsp. natto (strain BEST195).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=645657;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BEST195;
RX   PubMed=20398357; DOI=10.1186/1471-2164-11-243;
RA   Nishito Y., Osana Y., Hachiya T., Popendorf K., Toyoda A., Fujiyama A.,
RA   Itaya M., Sakakibara Y.;
RT   "Whole genome assembly of a natto production strain Bacillus subtilis natto
RT   from very short read data.";
RL   BMC Genomics 11:243-243(2010).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=BEST195;
RX   PubMed=25329997; DOI=10.1371/journal.pone.0109999;
RA   Kamada M., Hase S., Sato K., Toyoda A., Fujiyama A., Sakakibara Y.;
RT   "Whole genome complete resequencing of Bacillus subtilis natto by combining
RT   long reads with high-quality short reads.";
RL   PLoS ONE 9:E109999-E109999(2014).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INDUCTION.
RC   STRAIN=BEST195;
RX   PubMed=29142164; DOI=10.2323/jgam.2017.02.007;
RA   Kobayashi K., Kubo Y., Horii Y., Nishiwaki T., Kamiyama S., Sone H.,
RA   Watanabe S.;
RT   "Bacterial degradation of spermine and expression of spermidine/spermine
RT   acetyltransferase in Bacillus subtilis (natto) under liquid cultivation.";
RL   J. Gen. Appl. Microbiol. 63:373-376(2018).
CC   -!- FUNCTION: Probably acetylates spermine to N(1)-acetylspermine.
CC       {ECO:0000305|PubMed:29142164}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + an alkane-alpha,omega-diamine = an N-
CC         acetylalkane-alpha,omega-diamine + CoA + H(+); Xref=Rhea:RHEA:11116,
CC         Rhea:RHEA-COMP:9766, Rhea:RHEA-COMP:9767, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:70977,
CC         ChEBI:CHEBI:70988; EC=2.3.1.57;
CC         Evidence={ECO:0000305|PubMed:29142164};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + spermine = CoA + H(+) + N(1)-acetylspermine;
CC         Xref=Rhea:RHEA:33099, ChEBI:CHEBI:15378, ChEBI:CHEBI:45725,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58101; EC=2.3.1.57;
CC         Evidence={ECO:0000305|PubMed:29142164};
CC   -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC       {ECO:0000305|PubMed:29142164}.
CC   -!- INDUCTION: Expression is strongly induced by spermine, but not by
CC       agmatine, putrescine or spermidine. {ECO:0000269|PubMed:29142164}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP011541; BAI86134.1; -; Genomic_DNA.
DR   RefSeq; WP_014480351.1; NC_017196.2.
DR   SMR; D4FZ53; -.
DR   STRING; 86029.AWV81_13535; -.
DR   EnsemblBacteria; BAI86134; BAI86134; BSNT_09050.
DR   KEGG; bso:BSNT_09050; -.
DR   PATRIC; fig|645657.3.peg.3551; -.
DR   HOGENOM; CLU_111226_4_2_9; -.
DR   BRENDA; 2.3.1.57; 17289.
DR   UniPathway; UPA00211; -.
DR   Proteomes; UP000006805; Chromosome.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0046208; P:spermine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.287.900; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR027455; Sper_AcTfrase_N.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Transferase.
FT   CHAIN           1..152
FT                   /note="Probable spermine N(1)-acetyltransferase"
FT                   /id="PRO_0000453461"
FT   DOMAIN          3..152
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A951"
FT   BINDING         82..84
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT   BINDING         89..95
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT   BINDING         122..131
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9KL03"
SQ   SEQUENCE   152 AA;  17818 MW;  4E7A870301D412C9 CRC64;
     MSINIKAVTD DNRAAILDLH VSQNQLSYIE STKVCLEDAK ECHYYKPVGL YYEGDLVGFA
     MYGLFPEYDE DNKNGRVWLD RFFIDKHYQG KGLGKKMLKA LIQHLAELYK CKRIYLSIFE
     NNIHAIRLYQ RFGFQFNGEL DFNGEKVMVK EL