ID A0A0N9MQ99_9ACTN Unreviewed; 175 AA.
AC A0A0N9MQ99;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=ACH46_08305 {ECO:0000313|EMBL:ALG84499.1};
OS Gordonia phthalatica.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1136941 {ECO:0000313|EMBL:ALG84499.1, ECO:0000313|Proteomes:UP000063789};
RN [1] {ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|Proteomes:UP000063789};
RA Jin D., Kong X., Bai Z.;
RT "Complete genome sequence and metabolic analysis of phthalate degradation
RT pathway in Gordonia sp. QH-11.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALG84499.1, ECO:0000313|Proteomes:UP000063789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-11 {ECO:0000313|EMBL:ALG84499.1,
RC ECO:0000313|Proteomes:UP000063789};
RX PubMed=29068282; DOI=10.1099/ijsem.0.002430;
RA Jin D., Kong X., Jia M., Yu X., Wang X., Zhuang X., Deng Y., Bai Z.;
RT "Gordonia phthalatica sp. nov., a di-n-butyl phthalate-degrading bacterium
RT isolated from activated sludge.";
RL Int. J. Syst. Evol. Microbiol. 67:5128-5133(2017).
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; CP011853; ALG84499.1; -; Genomic_DNA.
DR RefSeq; WP_062392485.1; NZ_CP011853.1.
DR AlphaFoldDB; A0A0N9MQ99; -.
DR STRING; 1136941.ACH46_08305; -.
DR KEGG; goq:ACH46_08305; -.
DR PATRIC; fig|1136941.3.peg.1689; -.
DR OrthoDB; 2436196at2; -.
DR UniPathway; UPA00067; UER00122.
DR Proteomes; UP000063789; 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 Transferase {ECO:0000256|RuleBase:RU365045, ECO:0000313|EMBL:ALG84499.1}.
FT DOMAIN 16..172
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 175 AA; 19476 MW; 58D3A7949A4EBEF3 CRC64;
MNPIENTPET DTGNTVAFRR PRARDGKRIW EIARDSRVLD VNSPYAYVLW SQDFSETSIV
AEIDGDVVGF VTGYRRPTAP DTLMVWQVAV DDAQRGKKIA RRMLCELFEH CAPAGVVAIN
TTISPDNEAS QRLFAGAARA LGLRFTREPF FSADLFLDSH QPEDLYLLTP AAAAE
//
