(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 120.
DE   RecName: Full=Spermine/spermidine acetyltransferase;
DE            EC=2.3.1.57;
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, AND BIOPHYSICOCHEMICAL 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   -!- 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         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; putrescine degradation; N-
CC       acetylputrescine from putrescine: step 1/1.
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   SMR; P39909; -.
DR   STRING; 224308.BSU26600; -.
DR   PaxDb; P39909; -.
DR   PRIDE; P39909; -.
DR   EnsemblBacteria; CAB14601; CAB14601; BSU26600.
DR   GeneID; 937632; -.
DR   KEGG; bsu:BSU26600; -.
DR   PATRIC; fig|224308.179.peg.2890; -.
DR   eggNOG; COG0454; LUCA.
DR   HOGENOM; HOG000067992; -.
DR   InParanoid; P39909; -.
DR   KO; K00657; -.
DR   OMA; IEICYNP; -.
DR   PhylomeDB; P39909; -.
DR   BioCyc; BSUB:BSU26600-MONOMER; -.
DR   UniPathway; UPA00188; UER00363.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004145; F:diamine N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009447; P:putrescine 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;
DR   PRODOM; P39909.
DR   SWISS-2DPAGE; P39909.
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..152
FT                   /note="Spermine/spermidine acetyltransferase"
FT                   /id="PRO_0000064945"
FT   DOMAIN          3..152
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
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
//

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