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Database: UniProt
Entry: T0AWP7_9RHOO
LinkDB: T0AWP7_9RHOO
Original site: T0AWP7_9RHOO 
ID   T0AWP7_9RHOO            Unreviewed;       142 AA.
AC   T0AWP7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=M622_17195 {ECO:0000313|EMBL:EPZ14973.1};
OS   Thauera terpenica 58Eu.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=1348657 {ECO:0000313|EMBL:EPZ14973.1, ECO:0000313|Proteomes:UP000015455};
RN   [1] {ECO:0000313|EMBL:EPZ14973.1, ECO:0000313|Proteomes:UP000015455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=58Eu {ECO:0000313|EMBL:EPZ14973.1,
RC   ECO:0000313|Proteomes:UP000015455};
RA   Liu B., Frostegard A.H., Shapleigh J.P.;
RT   "Draft genome sequence of Thauera terpenica.";
RL   Submitted (JUN-2013) 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:EPZ14973.1}.
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DR   EMBL; ATJV01000065; EPZ14973.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0AWP7; -.
DR   STRING; 1348657.M622_17195; -.
DR   PATRIC; fig|1348657.5.peg.2524; -.
DR   eggNOG; COG0456; Bacteria.
DR   UniPathway; UPA00067; UER00122.
DR   Proteomes; UP000015455; 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:UP000015455};
KW   Transferase {ECO:0000256|RuleBase:RU365045}.
FT   DOMAIN          1..132
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   142 AA;  15404 MW;  67E9821760624D1E CRC64;
     MVKATGELEP NTAYCYLLLA TDFADTCLVA EAAGQIVGAV IGYRPPREPD AAFVWQVGVL
     PDYRGLGLGL RMLTAWRDLP ANRNCRWVTA TVADDNPASQ SLFQRLAHSA GVECTVNPHF
     TADLFPVAHP AEPLHRIGPF SL
//
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