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L-amino acid N-acyltransferase MnaT (EC 2.3.1.-) (L-methionine N-acyltransferase) (L-methionine sulfoximine/L-methionine sulfone N-acetyltransferase) (L-phenylglycine N-acetyltransferase)

 MNAT_ECOLI              Reviewed;         172 AA.
P76112; P77401;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
05-DEC-2018, entry version 122.
RecName: Full=L-amino acid N-acyltransferase MnaT {ECO:0000305|PubMed:27941785, ECO:0000305|Ref.4};
EC=2.3.1.- {ECO:0000269|PubMed:27941785, ECO:0000269|Ref.4};
AltName: Full=L-methionine N-acyltransferase {ECO:0000305|PubMed:27941785};
AltName: Full=L-methionine sulfoximine/L-methionine sulfone N-acetyltransferase {ECO:0000305|Ref.4};
AltName: Full=L-phenylglycine N-acetyltransferase {ECO:0000305|PubMed:27941785};
Name=mnaT {ECO:0000303|Ref.4, ECO:0000312|EMBL:AAC74530.1};
Synonyms=yncA; OrderedLocusNames=b1448, JW5233;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
FUNCTION AS AN ACYLTRANSFERASE, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
STRAIN=K12 / MG1655 / ATCC 47076;
Figge R., Barbier G., Bestel-Corre G.;
"Production of N-acylated sulphur-containing amino acids with
microorganisms having enhanced N-acyltransferase enzymatic activity.";
Patent number US0047880, 22-AUG-2008.
[5]
FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
STRAIN=K12;
PubMed=27941785; DOI=10.1038/nmeth.4103;
Sevin D.C., Fuhrer T., Zamboni N., Sauer U.;
"Nontargeted in vitro metabolomics for high-throughput identification
of novel enzymes in Escherichia coli.";
Nat. Methods 14:187-194(2017).
-!- FUNCTION: Acyltransferase that appears to be required for E.coli
optimal growth rate and yield via the formation of N-acetylated
amino acids. Catalyzes the acylation of L-methionine using acetyl-
CoA or propanoyl-CoA as acyl donors, and the acetylation of L-
phenylglycine (PubMed:27941785). Is also able to N-acylate other
free L-amino acids and their derivatives using a CoA thioester as
cosubstrate. Using acetyl-CoA as an acyl donor, substrate
specificity is methionine sulfone > methionine sulfoximine >
methionine sulfoxide > methionine. Asparagine, lysine, glutamine,
aspartate and glutamate are very poor substrates. Using methionine
as a substrate, acyl donor preference is propanoyl-CoA > acetyl-
CoA >> butyryl-CoA (Ref.4). Likely plays a role in the resistance
against the toxic effects of L-methionine sulfoximine (MSX), via
its ability to catalyze its acetylation; MSX is a rare amino acid
which inhibits glutamine synthetase (GlnA) (By similarity).
{ECO:0000250|UniProtKB:Q8ZPD3, ECO:0000269|PubMed:27941785,
ECO:0000269|Ref.4}.
-!- CATALYTIC ACTIVITY:
Reaction=acetyl-CoA + L-methionine = CoA + H(+) + N(alpha)-acetyl-
L-methionine; Xref=Rhea:RHEA:44144, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57844,
ChEBI:CHEBI:71670; Evidence={ECO:0000269|PubMed:27941785,
ECO:0000269|Ref.4};
-!- CATALYTIC ACTIVITY:
Reaction=L-methionine + propanoyl-CoA = CoA + H(+) + N-propanoyl-
L-methioninate; Xref=Rhea:RHEA:52600, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:57844,
ChEBI:CHEBI:136704; Evidence={ECO:0000269|PubMed:27941785,
ECO:0000269|Ref.4};
-!- CATALYTIC ACTIVITY:
Reaction=acetyl-CoA + L-alpha-phenylglycine = CoA + H(+) + N-
acetyl-L-alpha-phenylglycine; Xref=Rhea:RHEA:52680,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
ChEBI:CHEBI:136765, ChEBI:CHEBI:136766;
Evidence={ECO:0000269|PubMed:27941785};
-!- CATALYTIC ACTIVITY:
Reaction=acetyl-CoA + L-methionine sulfoximine = CoA + H(+) + N-
acetyl-L-methionine sulfoximine; Xref=Rhea:RHEA:47660,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
ChEBI:CHEBI:87826, ChEBI:CHEBI:87827;
Evidence={ECO:0000269|Ref.4};
-!- CATALYTIC ACTIVITY:
Reaction=acetyl-CoA + L-methionine sulfone = CoA + H(+) + N-
acetyl-L-methionine sulfone; Xref=Rhea:RHEA:47656,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
ChEBI:CHEBI:87824, ChEBI:CHEBI:87825;
Evidence={ECO:0000269|Ref.4};
-!- DISRUPTION PHENOTYPE: Cells lacking this gene show a reduced
growth rate and a markedly reduced yield in glucose minimal medium
compared to wild-type; this phenotype can be partially rescued by
adding L-phenylglycine to the medium, which reflects that other
enzymes may also catalyze its acetylation, but with lower
affinities. The deletion mutant strain also shows a consistent
change in the level of several metabolites whose masses can
correspond to L-phenylglycine, L-pipecolate or N4-
acetylaminobutanal. {ECO:0000269|PubMed:27941785}.
-!- BIOTECHNOLOGY: Expression leads to increased levels of N-acylated
L-amino acids which could be used in a number of applications.
{ECO:0000269|Ref.4}.
-!- SIMILARITY: Belongs to the acetyltransferase family. PAT/BAR
subfamily. {ECO:0000305}.
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EMBL; U00096; AAC74530.1; -; Genomic_DNA.
EMBL; AP009048; BAA15080.2; -; Genomic_DNA.
PIR; C64897; C64897.
RefSeq; NP_415965.1; NC_000913.3.
RefSeq; WP_001310799.1; NZ_LN832404.1.
ProteinModelPortal; P76112; -.
SMR; P76112; -.
BioGrid; 4260194; 12.
STRING; 316385.ECDH10B_1578; -.
PaxDb; P76112; -.
PRIDE; P76112; -.
EnsemblBacteria; AAC74530; AAC74530; b1448.
EnsemblBacteria; BAA15080; BAA15080; BAA15080.
GeneID; 946010; -.
KEGG; ecj:JW5233; -.
KEGG; eco:b1448; -.
PATRIC; fig|1411691.4.peg.820; -.
EchoBASE; EB3533; -.
EcoGene; EG13770; mnaT.
eggNOG; ENOG4108Z7F; Bacteria.
eggNOG; COG1247; LUCA.
HOGENOM; HOG000078516; -.
InParanoid; P76112; -.
KO; K03823; -.
PhylomeDB; P76112; -.
BioCyc; EcoCyc:G6759-MONOMER; -.
BioCyc; MetaCyc:G6759-MONOMER; -.
PRO; PR:P76112; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IBA:GO_Central.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR000182; GNAT_dom.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS51186; GNAT; 1.
1: Evidence at protein level;
Acyltransferase; Complete proteome; Reference proteome; Transferase.
CHAIN 1 172 L-amino acid N-acyltransferase MnaT.
/FTId=PRO_0000074577.
DOMAIN 1 163 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
REGION 85 87 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q8ZPD3}.
REGION 93 98 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q8ZPD3}.
BINDING 124 124 Acetyl-CoA.
{ECO:0000250|UniProtKB:Q8ZPD3}.
BINDING 133 133 Acetyl-CoA.
{ECO:0000250|UniProtKB:Q8ZPD3}.
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


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