ECTA_MARHA
ID ECTA_MARHA Reviewed; 172 AA.
AC O06059;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=L-2,4-diaminobutyric acid acetyltransferase;
DE Short=DABA acetyltransferase;
DE EC=2.3.1.178;
GN Name=ectA;
OS Marinococcus halophilus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Marinococcus.
OX NCBI_TaxID=1371;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 27964 / DSM 20408 / CIP 140819 / JCM 2479 / NBRC 102359 / NCIMB
RC 13496 / CCM 2706;
RX PubMed=9141677; DOI=10.1099/00221287-143-4-1141;
RA Louis P., Galinski E.A.;
RT "Characterization of genes for the biosynthesis of the compatible solute
RT ectoine from Marinococcus halophilus and osmoregulated expression in
RT Escherichia coli.";
RL Microbiology 143:1141-1149(1997).
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:0000269|PubMed:9141677}.
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 -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC ectoine from L-aspartate 4-semialdehyde: step 2/3.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. EctA subfamily.
CC {ECO:0000305}.
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DR EMBL; U66614; AAB57633.1; -; Genomic_DNA.
DR AlphaFoldDB; O06059; -.
DR SMR; O06059; -.
DR STRING; 1371.GCA_900166605_00961; -.
DR KEGG; ag:AAB57633; -.
DR UniPathway; UPA00067; UER00122.
DR GO; GO:0033816; F:diaminobutyrate acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0019491; P:ectoine biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR012772; Ectoine_EctA.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR02406; ectoine_EctA; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Transferase.
FT CHAIN 1..172
FT /note="L-2,4-diaminobutyric acid acetyltransferase"
FT /id="PRO_0000220087"
FT DOMAIN 15..166
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 172 AA; 19386 MW; 0E87A586342276C8 CRC64;
METKMTGTNG SVDSIVFDKP TVEDGADMWE LVKNSTLDLN SSYKYIMMCE FFAETCVVAK
ENDELVGFVT AFIPPEKQDT VFVWQVGVDT SQRGKGLASR LLNALLERDV CENVLYLEAT
ITPSNEASQA LFKKLAQKRE TEVTVSECFT EDLFPDDEHE EELTFRIGPF TK