ECTA_OCEIH
ID ECTA_OCEIH Reviewed; 179 AA.
AC Q8ESU9;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=L-2,4-diaminobutyric acid acetyltransferase;
DE Short=DABA acetyltransferase;
DE EC=2.3.1.178;
GN Name=ectA; OrderedLocusNames=OB0517;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
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=BAC12473.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000028; BAC12473.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q8ESU9; -.
DR SMR; Q8ESU9; -.
DR STRING; 221109.22776196; -.
DR EnsemblBacteria; BAC12473; BAC12473; BAC12473.
DR KEGG; oih:OB0517; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_111896_0_0_9; -.
DR PhylomeDB; Q8ESU9; -.
DR UniPathway; UPA00067; UER00122.
DR Proteomes; UP000000822; 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..179
FT /note="L-2,4-diaminobutyric acid acetyltransferase"
FT /id="PRO_0000220089"
FT DOMAIN 12..153
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 179 AA; 20907 MW; 7A4AC2C95BBFF235 CRC64;
MAEKLKVDTD EYYFRRPTKE DGGPVWELVR EIGNLDLNSS YSYVLWCEVF AESSIVVEHK
ETQQIVGFIS GFMHPEKEDT LFIWQVAVSS TQRGKGLATK MLLQLLEWNE SVNFIEATVA
PSNKPSNYLF LGLARKIHTN WKISDYFKTD HFPAKDEEHE EELLFRIGPM RKNKNKRMI