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