ID   ECTA_ALKHC              Reviewed;         189 AA.
AC   Q9KED3;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=L-2,4-diaminobutyric acid acetyltransferase;
DE            Short=DABA acetyltransferase;
DE            EC=2.3.1.178;
GN   Name=ectA; OrderedLocusNames=BH0920;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
CC   -!- FUNCTION: Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to
CC       gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl
CC       coenzyme A. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-2,4-diaminobutanoate = (2S)-4-acetamido-2-
CC         aminobutanoate + CoA + H(+); Xref=Rhea:RHEA:16901, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58761,
CC         ChEBI:CHEBI:58929; EC=2.3.1.178;
CC   -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC       ectoine from L-aspartate 4-semialdehyde: step 2/3.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. EctA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BA000004; BAB04639.1; -; Genomic_DNA.
DR   PIR; H83764; H83764.
DR   AlphaFoldDB; Q9KED3; -.
DR   SMR; Q9KED3; -.
DR   STRING; 272558.10173535; -.
DR   EnsemblBacteria; BAB04639; BAB04639; BAB04639.
DR   KEGG; bha:BH0920; -.
DR   eggNOG; COG0456; Bacteria.
DR   HOGENOM; CLU_111896_0_0_9; -.
DR   OMA; DGAAIWR; -.
DR   UniPathway; UPA00067; UER00122.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0033816; F:diaminobutyrate acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0019491; P:ectoine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR012772; Ectoine_EctA.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR02406; ectoine_EctA; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..189
FT                   /note="L-2,4-diaminobutyric acid acetyltransferase"
FT                   /id="PRO_0000220080"
FT   DOMAIN          32..183
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   189 AA;  21048 MW;  EC22A372BDCAACDC CRC64;
     MQVQCNEKAF KGGFIINSQI ATAPPKTLDT TITIGKPTVE DGAAMWELVN KSTLDTNSPY
     KYIMMCEYFA ETCVVAKENE RLVGFVTAFI PPEHQDVIFV WQIGVDSSQR GKGLASKLLQ
     ELISRDICSN VNYVEATVTP SNKASQALFQ KLAREYNTQC EVSECFSEDL FPGDDHEAEL
     TFRIGPLHP