ID A0A1B2R1Q6_9BORD Unreviewed; 182 AA.
AC A0A1B2R1Q6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=L-2,4-diaminobutyric acid acetyltransferase {ECO:0000256|ARBA:ARBA00017935, ECO:0000256|RuleBase:RU365045};
DE Short=DABA acetyltransferase {ECO:0000256|RuleBase:RU365045};
DE EC=2.3.1.178 {ECO:0000256|ARBA:ARBA00012355, ECO:0000256|RuleBase:RU365045};
GN Name=ectA {ECO:0000256|RuleBase:RU365045};
GN ORFNames=AKI39_08430 {ECO:0000313|EMBL:AOB30715.1};
OS Bordetella sp. H567.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1697043 {ECO:0000313|EMBL:AOB30715.1, ECO:0000313|Proteomes:UP000093512};
RN [1] {ECO:0000313|Proteomes:UP000093512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H567 {ECO:0000313|Proteomes:UP000093512};
RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL Submitted (AUG-2015) 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:0000256|RuleBase:RU365045}.
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:0000256|ARBA:ARBA00000400,
CC ECO:0000256|RuleBase:RU365045};
CC -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC ectoine from L-aspartate 4-semialdehyde: step 2/3.
CC {ECO:0000256|ARBA:ARBA00004978, ECO:0000256|RuleBase:RU365045}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. EctA subfamily.
CC {ECO:0000256|ARBA:ARBA00010712, ECO:0000256|RuleBase:RU365045}.
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DR EMBL; CP012334; AOB30715.1; -; Genomic_DNA.
DR RefSeq; WP_066634442.1; NZ_CP012334.1.
DR AlphaFoldDB; A0A1B2R1Q6; -.
DR STRING; 1697043.AKI39_08430; -.
DR KEGG; boh:AKI39_08430; -.
DR PATRIC; fig|1697043.4.peg.1735; -.
DR OrthoDB; 2436196at2; -.
DR UniPathway; UPA00067; UER00122.
DR Proteomes; UP000093512; Chromosome.
DR GO; GO:0033816; F:diaminobutyrate acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019491; P:ectoine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR012772; Ectoine_EctA.
DR InterPro; IPR000182; GNAT_dom.
DR NCBIfam; TIGR02406; ectoine_EctA; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU365045};
KW Reference proteome {ECO:0000313|Proteomes:UP000093512};
KW Transferase {ECO:0000256|RuleBase:RU365045, ECO:0000313|EMBL:AOB30715.1}.
FT DOMAIN 20..175
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 182 AA; 20032 MW; EAD5AF249D0B74E4 CRC64;
MTEGVDKRAT APLVAQEPSH LFRPPRLADG AVIHRLVADC PPLDLNAVYA YLLLCEHFPA
TCVVAESPGG SIDGFVSAYV PPGRADRLFV WQVAVHDRAR GQRLARRMLH ALLRRPELAD
IRHLETTVGP DNHASRRTFT SLAADLGAHA AEQPFFGKQL FGQSDHDDEM LLRIGPFASI
PR
//
