ID A0A0C5VNZ2_9GAMM Unreviewed; 162 AA.
AC A0A0C5VNZ2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=YC6258_03082 {ECO:0000313|EMBL:AJQ95118.1};
OS Gynuella sunshinyii YC6258.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Gynuella.
OX NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ95118.1, ECO:0000313|Proteomes:UP000032266};
RN [1] {ECO:0000313|EMBL:AJQ95118.1, ECO:0000313|Proteomes:UP000032266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC6258 {ECO:0000313|EMBL:AJQ95118.1,
RC ECO:0000313|Proteomes:UP000032266};
RA Khan H., Chung E.J., Chung Y.R.;
RT "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT YC6258T gen. nov., sp. nov.";
RL Submitted (JAN-2014) 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; CP007142; AJQ95118.1; -; Genomic_DNA.
DR RefSeq; WP_044617487.1; NZ_CP007142.1.
DR AlphaFoldDB; A0A0C5VNZ2; -.
DR STRING; 1445510.YC6258_03082; -.
DR KEGG; gsn:YC6258_03082; -.
DR PATRIC; fig|1445510.3.peg.3050; -.
DR HOGENOM; CLU_111896_0_0_6; -.
DR OrthoDB; 2436196at2; -.
DR UniPathway; UPA00067; UER00122.
DR Proteomes; UP000032266; 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 ECO:0000313|EMBL:AJQ95118.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032266};
KW Transferase {ECO:0000256|RuleBase:RU365045, ECO:0000313|EMBL:AJQ95118.1}.
FT DOMAIN 5..162
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 162 AA; 18227 MW; 772D36E2977D53D4 CRC64;
MDTEIEFRPP KSEDGAQVYD LIDQCPPLDT NSLYCNLLQC SHFSDTSVTA WLDSSLVGFI
SGYQLPNREN TLFVWQVAVS EQARGMGVAS GMMKNILNRP GSPDFSFIET TITAANQASW
SLFERLADKL NADMHRSVIF DEKKHFNGQH DSEFLVRIGP FN
//
