ID   ECTA_CHRSD              Reviewed;         192 AA.
AC   Q9ZEU8; Q1QWD0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=L-2,4-diaminobutyric acid acetyltransferase;
DE            Short=DABA acetyltransferase;
DE            EC=2.3.1.178;
GN   Name=ectA; OrderedLocusNames=Csal_1876;
OS   Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS   NCIMB 13768 / 1H11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9924816; DOI=10.1016/s0723-2020(98)80060-x;
RA   Canovas D., Vargas C., Calderon M.I., Ventosa A., Nieto J.J.;
RT   "Characterization of the genes for the biosynthesis of the compatible
RT   solute ectoine in the moderately halophilic bacterium Halomonas elongata
RT   DSM 3043.";
RL   Syst. Appl. Microbiol. 21:487-497(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX   PubMed=22675587; DOI=10.4056/sigs.2285059;
RA   Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA   Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT   "Complete genome sequence of the halophilic and highly halotolerant
RT   Chromohalobacter salexigens type strain (1H11(T)).";
RL   Stand. Genomic Sci. 5:379-388(2011).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE59228.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ011103; CAA09483.1; -; Genomic_DNA.
DR   EMBL; CP000285; ABE59228.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_035409657.1; NC_007963.1.
DR   AlphaFoldDB; Q9ZEU8; -.
DR   SMR; Q9ZEU8; -.
DR   STRING; 290398.Csal_1876; -.
DR   EnsemblBacteria; ABE59228; ABE59228; Csal_1876.
DR   KEGG; csa:Csal_1876; -.
DR   eggNOG; COG0456; Bacteria.
DR   HOGENOM; CLU_111896_0_0_6; -.
DR   OrthoDB; 1826274at2; -.
DR   UniPathway; UPA00067; UER00122.
DR   Proteomes; UP000000239; 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..192
FT                   /note="L-2,4-diaminobutyric acid acetyltransferase"
FT                   /id="PRO_0000220085"
FT   DOMAIN          31..192
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   192 AA;  21194 MW;  ED7FF57C0533FC41 CRC64;
     MTPTTENFTP SADLARPSVA DTVIGSAKKT LFIRKPTTDD GWGIYELVKA CPPLDVNSGY
     AYLLLATQFR DTCAVATDEE GEIVGFVSGY VKRNAPDTYF LWQVAVGEKA RGTGLARRLV
     EAVLMRPGMG DVRHLETTIT PDNEASWGLF KRLADRWQAP LNSREYFSTG QLGGEHDPEN
     LVRIGPFEPQ QI