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ECTA_VIRPA
ID   ECTA_VIRPA              Reviewed;         159 AA.
AC   Q6PR33;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=L-2,4-diaminobutyric acid acetyltransferase;
DE            Short=DABA acetyltransferase;
DE            EC=2.3.1.178;
GN   Name=ectA;
OS   Virgibacillus pantothenticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=1473;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kuhlmann A.U., Gimpel S., Hoffmann T., Bremer E.;
RT   "Synthesis of compatible solute ectoine in Virgibacillus pantothenticus is
RT   induced by high osmolality and growth in the cold.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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; AY585263; AAS93806.1; -; Genomic_DNA.
DR   RefSeq; WP_050352488.1; NZ_LT727682.1.
DR   AlphaFoldDB; Q6PR33; -.
DR   SMR; Q6PR33; -.
DR   GeneID; 66870976; -.
DR   OrthoDB; 1826274at2; -.
DR   UniPathway; UPA00067; UER00122.
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; Transferase.
FT   CHAIN           1..159
FT                   /note="L-2,4-diaminobutyric acid acetyltransferase"
FT                   /id="PRO_0000220095"
FT   DOMAIN          1..138
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   159 AA;  17960 MW;  86EC996CD5C37D47 CRC64;
     MPTKNDGAAV WELIHQIDNL DLNSSYSYLL WCDMFSETSI VVEEEGEVVG FISGFIHPNK
     PNTLFIWQVA VEAAQRGKGL GTHMLLQLLN RKRIAQVQYI EATVAPSNLP SQYLFLGLAK
     KLDTECVVGN YYTSVDFPRT GHEDEQLYKI GPIRRANNK
 
 
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