ID   ECTA_HALED              Reviewed;         192 AA.
AC   O52249; E1VCW7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=L-2,4-diaminobutyric acid acetyltransferase;
DE            Short=DABA acetyltransferase {ECO:0000303|PubMed:9864317};
DE            EC=2.3.1.178 {ECO:0000269|PubMed:9864317};
GN   Name=ectA; OrderedLocusNames=HELO_2588;
OS   Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS   / 1H9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=768066;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX   PubMed=9570121; DOI=10.1111/j.1574-6968.1998.tb12960.x;
RA   Goeller K., Ofer A., Galinski E.A.;
RT   "Construction and characterization of an NaCl-sensitive mutant of Halomonas
RT   elongata impaired in ectoine biosynthesis.";
RL   FEMS Microbiol. Lett. 161:293-300(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX   PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA   Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA   Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA   Kunte H.J.;
RT   "A blueprint of ectoine metabolism from the genome of the industrial
RT   producer Halomonas elongata DSM 2581(T).";
RL   Environ. Microbiol. 13:1973-1994(2011).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   CHARACTERIZATION.
RC   STRAIN=OUT30018;
RX   PubMed=9864317; DOI=10.1128/jb.181.1.91-99.1999;
RA   Ono H., Sawada K., Khunajakr N., Tao T., Yamamoto M., Hiramoto M.,
RA   Shinmyo A., Takano M., Murooka Y.;
RT   "Characterization of biosynthetic enzymes for ectoine as a compatible
RT   solute in a moderately halophilic eubacterium, Halomonas elongata.";
RL   J. Bacteriol. 181:91-99(1999).
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. Does not acetylate amino acids like GABA, L-ornithine, L-
CC       lysine and L-aspartate. {ECO:0000269|PubMed:9864317}.
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         Evidence={ECO:0000269|PubMed:9864317};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.2. {ECO:0000269|PubMed:9864317};
CC       Temperature dependence:
CC         Optimum temperature is 20 degrees Celsius.
CC         {ECO:0000269|PubMed:9864317};
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   ---------------------------------------------------------------------------
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; AF031489; AAC15881.1; -; Genomic_DNA.
DR   EMBL; FN869568; CBV42472.1; -; Genomic_DNA.
DR   RefSeq; WP_013332344.1; NC_014532.2.
DR   AlphaFoldDB; O52249; -.
DR   SMR; O52249; -.
DR   STRING; 768066.HELO_2588; -.
DR   EnsemblBacteria; CBV42472; CBV42472; HELO_2588.
DR   KEGG; hel:HELO_2588; -.
DR   eggNOG; COG0456; Bacteria.
DR   HOGENOM; CLU_111896_0_0_6; -.
DR   OMA; DGAAIWR; -.
DR   BioCyc; MetaCyc:MON-802; -.
DR   UniPathway; UPA00067; UER00122.
DR   Proteomes; UP000008707; 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   1: Evidence at protein level;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..192
FT                   /note="L-2,4-diaminobutyric acid acetyltransferase"
FT                   /id="PRO_0000220086"
FT   DOMAIN          31..192
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   192 AA;  21170 MW;  DB4CFC5402EAF852 CRC64;
     MNATTEPFTP SADLAKPSVA DAVVGHEASP LFIRKPSPDD GWGIYELVKS CPPLDVNSAY
     AYLLLATQFR DSCAVATNEE GEIVGFVSGY VKSNAPDTYF LWQVAVGEKA RGTGLARRLV
     EAVMTRPEMA EVHHLETTIT PDNQASWGLF RRLADRWQAP LNSREYFSTD QLGGEHDPEN
     LVRIGPFQTD QI