ID   ECTA_STRAQ              Reviewed;         176 AA.
AC   Q6QUZ0;
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; Synonyms=thpA;
OS   Streptomyces anulatus (Streptomyces chrysomallus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1892;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11523 / DSM 40128 / JCM 4296 / LMG 20459 / NBRC 15393;
RX   PubMed=15128576; DOI=10.1128/aem.70.5.3130-3132.2004;
RA   Prabhu J., Schauwecker F., Grammel N., Keller U., Bernhard M.;
RT   "Functional expression of the ectoine hydroxylase gene (thpD) from
RT   Streptomyces chrysomallus in Halomonas elongata.";
RL   Appl. Environ. Microbiol. 70:3130-3132(2004).
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   ---------------------------------------------------------------------------
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; AY524544; AAS02094.1; -; Genomic_DNA.
DR   RefSeq; WP_057661885.1; NZ_CM003601.1.
DR   AlphaFoldDB; Q6QUZ0; -.
DR   SMR; Q6QUZ0; -.
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..176
FT                   /note="L-2,4-diaminobutyric acid acetyltransferase"
FT                   /id="PRO_0000220091"
FT   DOMAIN          16..171
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   176 AA;  19312 MW;  1B5211FED6AFEA9F CRC64;
     MTAAPADFAR ARSEFLSIDA PRVEDGAAIW RIARDSQVLD LNSSYSYLLW CRDFAATSAV
     ARGENGEPIA FVTGYVRPDR PQTLVVWQVA VDQAHRGKGL AAALLDALTA RVAADQVLSS
     VETTITPDNT ASDRLFTSYA QRHDVALEKE VLFDGELFPE ETHLPEVLYR IGPFAT