AAAT_ECOLI
ID AAAT_ECOLI Reviewed; 162 AA.
AC P46854; Q2M7A4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=L-amino acid N-acetyltransferase AaaT {ECO:0000303|PubMed:27941785};
DE AltName: Full=L-methionine N-acetyltransferase {ECO:0000305|PubMed:27941785};
DE EC=2.3.1.- {ECO:0000269|PubMed:27941785};
DE AltName: Full=L-phenylalanine N-acetyltransferase {ECO:0000305|PubMed:27941785};
DE EC=2.3.1.53 {ECO:0000269|PubMed:27941785};
GN Name=aaaT {ECO:0000303|PubMed:27941785};
GN Synonyms=yhhY {ECO:0000312|EMBL:AAC76466.1};
GN OrderedLocusNames=b3441, JW3405;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION.
RX PubMed=25002546; DOI=10.1128/jb.01584-14;
RA Kazakov T., Kuznedelov K., Semenova E., Mukhamedyarov D., Datsenko K.A.,
RA Metlitskaya A., Vondenhoff G.H., Tikhonov A., Agarwal V., Nair S.,
RA Van Aerschot A., Severinov K.;
RT "The RimL transacetylase provides resistance to translation inhibitor
RT microcin C.";
RL J. Bacteriol. 196:3377-3385(2014).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=27941785; DOI=10.1038/nmeth.4103;
RA Sevin D.C., Fuhrer T., Zamboni N., Sauer U.;
RT "Nontargeted in vitro metabolomics for high-throughput identification of
RT novel enzymes in Escherichia coli.";
RL Nat. Methods 14:187-194(2017).
CC -!- FUNCTION: Catalyzes the N-acetylation of L-phenylalanine and L-
CC methionine using acetyl-CoA as acetyl donor in vitro. Cannot accept L-
CC tyrosine as substrate and propionyl-CoA, succinyl-CoA or (S)-
CC methylmalonyl-CoA as acyl donors (PubMed:27941785). Is also able to
CC acetylate and thus detoxify several nonhydrolyzable aminoacyl
CC adenylates, but not the processed form of the peptide-nucleotide
CC antibiotic microcin C (McC). When overproduced, provides complete
CC resistance to leucyl sulfamoyl adenylate (LSA) and partial resistance
CC to alanyl sulfamoyl adenylate (ASA) and phenylalanyl sulfamoyl
CC adenylate (FSA). Therefore, may protect bacteria from various toxic
CC aminoacyl nucleotides, either exogenous or those generated inside the
CC cell during normal metabolism (PubMed:25002546).
CC {ECO:0000269|PubMed:25002546, ECO:0000269|PubMed:27941785}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-phenylalanine = CoA + H(+) + N-acetyl-L-
CC phenylalanine; Xref=Rhea:RHEA:17801, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57702,
CC ChEBI:CHEBI:58095; EC=2.3.1.53;
CC Evidence={ECO:0000269|PubMed:27941785};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-methionine = CoA + H(+) + N(alpha)-acetyl-L-
CC methionine; Xref=Rhea:RHEA:44144, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:71670; Evidence={ECO:0000269|PubMed:27941785};
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; U18997; AAA58239.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76466.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77852.1; -; Genomic_DNA.
DR PIR; D65140; D65140.
DR RefSeq; NP_417898.1; NC_000913.3.
DR RefSeq; WP_001295206.1; NZ_SSZK01000008.1.
DR AlphaFoldDB; P46854; -.
DR SMR; P46854; -.
DR BioGRID; 4259623; 13.
DR IntAct; P46854; 4.
DR STRING; 511145.b3441; -.
DR jPOST; P46854; -.
DR PaxDb; P46854; -.
DR PRIDE; P46854; -.
DR EnsemblBacteria; AAC76466; AAC76466; b3441.
DR EnsemblBacteria; BAE77852; BAE77852; BAE77852.
DR GeneID; 66672676; -.
DR GeneID; 947943; -.
DR KEGG; ecj:JW3405; -.
DR KEGG; eco:b3441; -.
DR PATRIC; fig|511145.12.peg.3538; -.
DR EchoBASE; EB2779; -.
DR eggNOG; COG1247; Bacteria.
DR HOGENOM; CLU_013985_19_8_6; -.
DR InParanoid; P46854; -.
DR OMA; FGMGVKD; -.
DR PhylomeDB; P46854; -.
DR BioCyc; EcoCyc:G7758-MON; -.
DR PRO; PR:P46854; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0103045; F:methione N-acyltransferase activity; IEA:RHEA.
DR GO; GO:0008080; F:N-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0050176; F:phenylalanine N-acetyltransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..162
FT /note="L-amino acid N-acetyltransferase AaaT"
FT /id="PRO_0000074613"
FT DOMAIN 4..162
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 162 AA; 18794 MW; F7565FA6906418E4 CRC64;
MSEIVIRHAE TRDYEAIRQI HAQPEVYCNT LQVPHPSDHM WQERLADRPG IKQLVACIDG
DVVGHLTIDV QQRPRRSHVA DFGICVDSRW KNRGVASALM REMIEMCDNW LRVDRIELTV
FVDNAPAIKV YKKYGFEIEG TGKKYALRNG EYVDAYYMAR VK
