ID   ECTA_META2              Reviewed;         172 AA.
AC   Q4JQJ5; G4T4A4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=L-2,4-diaminobutyric acid acetyltransferase;
DE            Short=DABA acetyltransferase;
DE            EC=2.3.1.178;
GN   Name=ectA; OrderedLocusNames=MEALZ_3250;
OS   Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM
OS   B-2133 / 20Z) (Methylomicrobium alcaliphilum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylotuvimicrobium.
OX   NCBI_TaxID=1091494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RC   STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z;
RX   PubMed=16283251; DOI=10.1007/s00203-005-0042-z;
RA   Reshetnikov A.S., Khmelenina V.N., Trotsenko Y.A.;
RT   "Characterization of the ectoine biosynthesis genes of haloalkalotolerant
RT   obligate methanotroph 'Methylomicrobium alcaliphilum 20Z'.";
RL   Arch. Microbiol. 184:286-297(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z;
RX   PubMed=22207753; DOI=10.1128/jb.06392-11;
RA   Vuilleumier S., Khmelenina V.N., Bringel F., Reshetnikov A.S., Lajus A.,
RA   Mangenot S., Rouy Z., Op den Camp H.J., Jetten M.S., Dispirito A.A.,
RA   Dunfield P., Klotz M.G., Semrau J.D., Stein L.Y., Barbe V., Medigue C.,
RA   Trotsenko Y.A., Kalyuzhnaya M.G.;
RT   "Genome sequence of the haloalkaliphilic methanotrophic bacterium
RT   Methylomicrobium alcaliphilum 20Z.";
RL   J. Bacteriol. 194:551-552(2012).
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.
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         Evidence={ECO:0000269|PubMed:16283251};
CC   -!- ACTIVITY REGULATION: Inhibited by zinc and cadmium.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=400 uM for L-2,4-diaminobutanoate {ECO:0000269|PubMed:16283251};
CC         KM=36.6 uM for acetyl-CoA {ECO:0000269|PubMed:16283251};
CC       pH dependence:
CC         Optimum pH is 9.5. {ECO:0000269|PubMed:16283251};
CC       Temperature dependence:
CC         Optimum temperature is 20 degrees Celsius.
CC         {ECO:0000269|PubMed:16283251};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC       ectoine from L-aspartate 4-semialdehyde: step 2/3.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16283251}.
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; DQ016501; AAY96770.1; -; Genomic_DNA.
DR   EMBL; FO082060; CCE24915.1; -; Genomic_DNA.
DR   RefSeq; WP_014149673.1; NC_016112.1.
DR   AlphaFoldDB; Q4JQJ5; -.
DR   SMR; Q4JQJ5; -.
DR   STRING; 1091494.MEALZ_3250; -.
DR   EnsemblBacteria; CCE24915; CCE24915; MEALZ_3250.
DR   KEGG; mah:MEALZ_3250; -.
DR   PATRIC; fig|271065.3.peg.3344; -.
DR   HOGENOM; CLU_111896_0_0_6; -.
DR   OMA; DGAAIWR; -.
DR   OrthoDB; 1826274at2; -.
DR   UniPathway; UPA00067; UER00122.
DR   Proteomes; UP000008315; 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   1: Evidence at protein level;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..172
FT                   /note="L-2,4-diaminobutyric acid acetyltransferase"
FT                   /id="PRO_0000308172"
FT   DOMAIN          11..165
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   172 AA;  18883 MW;  088A573FB8EF0424 CRC64;
     MLPDKTALPI ITLSQPTAEV GAQVHRLISK CPPLDPNSMY CNLLQSSHFS ETAVAAKIGD
     ELVGFVSGYR IPQRPDTLFV WQVAVGEKAR GQGLATRMLK AILARPVNQD INRIETTITP
     NNKASWALFE GLAKKLDTQI GSAVMFDKTR HFADQHETEM LVKVGPFKAV QA