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ECTA_NOCFA
ID   ECTA_NOCFA              Reviewed;         193 AA.
AC   Q5YW78;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=L-2,4-diaminobutyric acid acetyltransferase;
DE            Short=DABA acetyltransferase;
DE            EC=2.3.1.178;
GN   Name=ectA; OrderedLocusNames=NFA_27160;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(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}.
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DR   EMBL; AP006618; BAD57563.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5YW78; -.
DR   SMR; Q5YW78; -.
DR   STRING; 247156.NFA_27160; -.
DR   EnsemblBacteria; BAD57563; BAD57563; NFA_27160.
DR   KEGG; nfa:NFA_27160; -.
DR   eggNOG; COG0456; Bacteria.
DR   HOGENOM; CLU_111896_0_0_11; -.
DR   OMA; DGAAIWR; -.
DR   UniPathway; UPA00067; UER00122.
DR   Proteomes; UP000006820; 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..193
FT                   /note="L-2,4-diaminobutyric acid acetyltransferase"
FT                   /id="PRO_0000220088"
FT   DOMAIN          33..185
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   193 AA;  21062 MW;  C162015FF0A0DBC1 CRC64;
     MSLQTLSTPT AEPVEEPRPV EAPWQVSDRI GTALLRAPQL GDAAEIWRIA KDSRVLDTNS
     SYAYLLWCRD FPGTTVVAEV DGRAVGFVIG YLRPESPDTV FVWQVAVSPT ERGRGTGTAL
     IQKLLDRVAP HGVTALETTI SPDNPASIAM FAAVARRRGA QLTKQPLFDA GVFPDEHAPE
     DLYRIAPIAQ EIR
 
 
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