BLTD_BACSU
ID BLTD_BACSU Reviewed; 152 AA.
AC P39909;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Spermine/spermidine N(1)-acetyltransferase {ECO:0000305};
DE EC=2.3.1.57 {ECO:0000269|PubMed:10359661};
GN Name=bltD; Synonyms=bmr2D, bmtD; OrderedLocusNames=BSU26600;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BD170;
RX PubMed=7608059; DOI=10.1128/jb.177.14.3904-3910.1995;
RA Ahmed M., Lyass L., Markham P.N., Taylor S.S., Vazquez-Laslop N.,
RA Neyfakh A.A.;
RT "Two highly similar multidrug transporters of Bacillus subtilis whose
RT expression is differentially regulated.";
RL J. Bacteriol. 177:3904-3910(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=10359661; DOI=10.1042/bj3400753;
RA Woolridge D.P., Martinez J.D., Stringer D.E., Gerner E.W.;
RT "Characterization of a novel spermidine/spermine acetyltransferase, BltD,
RT from Bacillus subtilis.";
RL Biochem. J. 340:753-758(1999).
CC -!- FUNCTION: Acetylates both spermidine and spermine at primary propyl
CC amine moieties, with spermine being the preferred substrate.
CC {ECO:0000269|PubMed:10359661}.
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:0000269|PubMed:10359661};
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:0000269|PubMed:10359661};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + spermidine = CoA + H(+) + N(1)-acetylspermidine;
CC Xref=Rhea:RHEA:28150, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57834, ChEBI:CHEBI:58324; EC=2.3.1.57;
CC Evidence={ECO:0000269|PubMed:10359661};
CC -!- ACTIVITY REGULATION: Putrescine and N(8)-acetylspermidine are
CC competitive inhibitors of spermidine acetylation.
CC {ECO:0000269|PubMed:10359661}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=67 uM for spermine {ECO:0000269|PubMed:10359661};
CC KM=1200 uM for N(1)-acetylspermine {ECO:0000269|PubMed:10359661};
CC KM=200 uM for spermidine {ECO:0000269|PubMed:10359661};
CC KM=95 uM for acetyl-CoA {ECO:0000269|PubMed:10359661};
CC Vmax=19.5 nmol/min/mg enzyme with spermine as substrate
CC {ECO:0000269|PubMed:10359661};
CC Vmax=7.4 nmol/min/mg enzyme with N(1)-acetylspermine as substrate
CC {ECO:0000269|PubMed:10359661};
CC Vmax=0.6 nmol/min/mg enzyme with spermidine as substrate
CC {ECO:0000269|PubMed:10359661};
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000305}.
CC -!- PATHWAY: Amine and polyamine degradation; spermidine degradation.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; L32599; AAC36945.1; -; Genomic_DNA.
DR EMBL; D84432; BAA12354.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14601.1; -; Genomic_DNA.
DR PIR; B69595; B69595.
DR RefSeq; NP_390537.1; NC_000964.3.
DR RefSeq; WP_003229879.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P39909; -.
DR SMR; P39909; -.
DR STRING; 224308.BSU26600; -.
DR PaxDb; P39909; -.
DR PRIDE; P39909; -.
DR EnsemblBacteria; CAB14601; CAB14601; BSU_26600.
DR GeneID; 937632; -.
DR KEGG; bsu:BSU26600; -.
DR PATRIC; fig|224308.179.peg.2890; -.
DR eggNOG; COG0456; Bacteria.
DR InParanoid; P39909; -.
DR OMA; IEICYNP; -.
DR PhylomeDB; P39909; -.
DR BioCyc; BSUB:BSU26600-MON; -.
DR UniPathway; UPA00211; -.
DR UniPathway; UPA00250; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046203; P:spermidine catabolic process; IEA:UniProtKB-UniPathway.
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; Reference proteome; Transferase.
FT CHAIN 1..152
FT /note="Spermine/spermidine N(1)-acetyltransferase"
FT /id="PRO_0000064945"
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"
FT CONFLICT 85
FT /note="D -> I (in Ref. 1; AAC36945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 152 AA; 17838 MW; 4E6F7ACB3429DAE9 CRC64;
MSINIKAVTD DNRAAILDLH VSQNQLSYIE STKVCLEDAK ECHYYKPVGL YYEGDLVGFA
MYGLFPEYDE DNKNGRVWLD RFFIDERYQG KGLGKKMLKA LIQHLAELYK CKRIYLSIFE
NNIHAIRLYQ RFGFQFNGEL DFNGEKVMVK EL
