ID A0A101P375_9ACTN Unreviewed; 175 AA.
AC A0A101P375;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=AQI95_21805 {ECO:0000313|EMBL:KUN04067.1};
OS Streptomyces yokosukanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67386 {ECO:0000313|EMBL:KUN04067.1, ECO:0000313|Proteomes:UP000053127};
RN [1] {ECO:0000313|EMBL:KUN04067.1, ECO:0000313|Proteomes:UP000053127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40224 {ECO:0000313|EMBL:KUN04067.1,
RC ECO:0000313|Proteomes:UP000053127};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces yokosukanensis DSM 40224, type
RT strain for the species Streptomyces yokosukanensis.";
RL Submitted (OCT-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUN04067.1}.
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DR EMBL; LMWN01000032; KUN04067.1; -; Genomic_DNA.
DR RefSeq; WP_067126022.1; NZ_KQ948213.1.
DR AlphaFoldDB; A0A101P375; -.
DR STRING; 67386.AQI95_21805; -.
DR OrthoDB; 2436196at2; -.
DR UniPathway; UPA00067; UER00122.
DR Proteomes; UP000053127; Unassembled WGS sequence.
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:UP000053127};
KW Transferase {ECO:0000256|RuleBase:RU365045, ECO:0000313|EMBL:KUN04067.1}.
FT DOMAIN 8..163
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 175 AA; 18760 MW; 38160369ABCC352B CRC64;
MTAAPADLLI DQPAVTDGAA LWRLAKESKT LDLNSSYSYL LWCRDFAGTS AVARGEGGEP
VGFVTGYVRP ERPRTLLVWQ VAVDSAHRGL GIAAALLDGL TARLTAEHGV TDVETTITPG
NTASERLFAS FAARHGARLE REVLFPAELF PEGAHDPEVL YRIGPLTDVT PHSAH
//
