MNAT_ECOLI
ID MNAT_ECOLI Reviewed; 172 AA.
AC P76112; P77401;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=L-amino acid N-acyltransferase MnaT {ECO:0000305|PubMed:27941785, ECO:0000305|Ref.4};
DE EC=2.3.1.- {ECO:0000269|PubMed:27941785, ECO:0000269|Ref.4};
DE AltName: Full=L-methionine N-acyltransferase {ECO:0000305|PubMed:27941785};
DE AltName: Full=L-methionine sulfoximine/L-methionine sulfone N-acetyltransferase {ECO:0000305|Ref.4};
DE AltName: Full=L-phenylglycine N-acetyltransferase {ECO:0000305|PubMed:27941785};
GN Name=mnaT {ECO:0000303|Ref.4, ECO:0000312|EMBL:AAC74530.1}; Synonyms=yncA;
GN OrderedLocusNames=b1448, JW5233;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
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 [3]
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 [4]
RP FUNCTION AS AN ACYLTRANSFERASE, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Figge R., Barbier G., Bestel-Corre G.;
RT "Production of N-acylated sulphur-containing amino acids with
RT microorganisms having enhanced N-acyltransferase enzymatic activity.";
RL Patent number US0047880, 22-AUG-2008.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
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: Acyltransferase that appears to be required for E.coli
CC optimal growth rate and yield via the formation of N-acetylated amino
CC acids. Catalyzes the acylation of L-methionine using acetyl-CoA or
CC propanoyl-CoA as acyl donors, and the acetylation of L-phenylglycine
CC (PubMed:27941785). Is also able to N-acylate other free L-amino acids
CC and their derivatives using a CoA thioester as cosubstrate. Using
CC acetyl-CoA as an acyl donor, substrate specificity is methionine
CC sulfone > methionine sulfoximine > methionine sulfoxide > methionine.
CC Asparagine, lysine, glutamine, aspartate and glutamate are very poor
CC substrates. Using methionine as a substrate, acyl donor preference is
CC propanoyl-CoA > acetyl-CoA >> butyryl-CoA (Ref.4). Likely plays a role
CC in the resistance against the toxic effects of L-methionine sulfoximine
CC (MSX), via its ability to catalyze its acetylation; MSX is a rare amino
CC acid which inhibits glutamine synthetase (GlnA) (By similarity).
CC {ECO:0000250|UniProtKB:Q8ZPD3, ECO:0000269|PubMed:27941785,
CC ECO:0000269|Ref.4}.
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 ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionine + propanoyl-CoA = CoA + H(+) + N-propanoyl-L-
CC methioninate; Xref=Rhea:RHEA:52600, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:136704; Evidence={ECO:0000269|PubMed:27941785,
CC ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-alpha-phenylglycine = CoA + H(+) + N-acetyl-L-
CC alpha-phenylglycine; Xref=Rhea:RHEA:52680, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:136765,
CC ChEBI:CHEBI:136766; Evidence={ECO:0000269|PubMed:27941785};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-methionine sulfoximine = CoA + H(+) + N-acetyl-
CC L-methionine sulfoximine; Xref=Rhea:RHEA:47660, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:87826,
CC ChEBI:CHEBI:87827; Evidence={ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-methionine sulfone = CoA + H(+) + N-acetyl-L-
CC methionine sulfone; Xref=Rhea:RHEA:47656, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:87824,
CC ChEBI:CHEBI:87825; Evidence={ECO:0000269|Ref.4};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a reduced growth
CC rate and a markedly reduced yield in glucose minimal medium compared to
CC wild-type; this phenotype can be partially rescued by adding L-
CC phenylglycine to the medium, which reflects that other enzymes may also
CC catalyze its acetylation, but with lower affinities. The deletion
CC mutant strain also shows a consistent change in the level of several
CC metabolites whose masses can correspond to L-phenylglycine, L-
CC pipecolate or N4-acetylaminobutanal. {ECO:0000269|PubMed:27941785}.
CC -!- BIOTECHNOLOGY: Expression leads to increased levels of N-acylated L-
CC amino acids which could be used in a number of applications.
CC {ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. PAT/BAR subfamily.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74530.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15080.2; -; Genomic_DNA.
DR PIR; C64897; C64897.
DR RefSeq; NP_415965.1; NC_000913.3.
DR RefSeq; WP_001310799.1; NZ_SSZK01000021.1.
DR AlphaFoldDB; P76112; -.
DR SMR; P76112; -.
DR BioGRID; 4260194; 12.
DR STRING; 511145.b1448; -.
DR jPOST; P76112; -.
DR PaxDb; P76112; -.
DR PRIDE; P76112; -.
DR EnsemblBacteria; AAC74530; AAC74530; b1448.
DR EnsemblBacteria; BAA15080; BAA15080; BAA15080.
DR GeneID; 946010; -.
DR KEGG; ecj:JW5233; -.
DR KEGG; eco:b1448; -.
DR PATRIC; fig|1411691.4.peg.820; -.
DR EchoBASE; EB3533; -.
DR eggNOG; COG1247; Bacteria.
DR HOGENOM; CLU_013985_4_4_6; -.
DR InParanoid; P76112; -.
DR OMA; IFAHNQP; -.
DR PhylomeDB; P76112; -.
DR BioCyc; EcoCyc:G6759-MON; -.
DR BioCyc; MetaCyc:G6759-MON; -.
DR PRO; PR:P76112; -.
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; IEA:InterPro.
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..172
FT /note="L-amino acid N-acyltransferase MnaT"
FT /id="PRO_0000074577"
FT DOMAIN 1..163
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 85..87
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
FT BINDING 93..98
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
FT BINDING 124
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
FT BINDING 133
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
SQ SEQUENCE 172 AA; 19248 MW; 4DAA0DC5198CDBD1 CRC64;
MSIRFARKAD CAAIAEIYNH AVLYTAAIWN DQTVDADNRI AWFEARTLAG YPVLVSEENG
VVTGYASFGD WRSFDGFRHT VEHSVYVHPD HQGKGLGRKL LSRLIDEARD CGKHVMVAGI
ESQNQASLHL HQSLGFVVTA QMPQVGTKFG RWLDLTFMQL QLDERTEPDA IG
