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Protein

L-amino acid N-acyltransferase MnaT

Gene

mnaT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity2 Publications

Catalytic activityi

Acetyl-CoA + L-methionine = CoA + N-acetyl-L-methionine.2 Publications
Propanoyl-CoA + L-methionine = CoA + N-propanoyl-L-methionine.2 Publications
Acetyl-CoA + L-phenylglycine = CoA + N-acetyl-L-phenylglycine.1 Publication
Acetyl-CoA + L-methionine sulfoximine = CoA + N-acetyl-L-methionine sulfoximine.1 Publication
Acetyl-CoA + L-methionine sulfone = CoA + N-acetyl-L-methionine sulfone.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei124Acetyl-CoABy similarity1
Binding sitei133Acetyl-CoABy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase

Enzyme and pathway databases

BioCyciEcoCyc:G6759-MONOMER.
MetaCyc:G6759-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
L-amino acid N-acyltransferase MnaT2 Publications (EC:2.3.1.-2 Publications)
Alternative name(s):
L-methionine N-acyltransferase1 Publication
L-methionine sulfoximine/L-methionine sulfone N-acetyltransferase1 Publication
L-phenylglycine N-acetyltransferase1 Publication
Gene namesi
Name:mnaT1 PublicationImported
Synonyms:yncA
Ordered Locus Names:b1448, JW5233
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13770. mnaT.

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Biotechnological usei

Expression leads to increased levels of N-acylated L-amino acids which could be used in a number of applications.1 Publication

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000745771 – 172L-amino acid N-acyltransferase MnaTAdd BLAST172

Proteomic databases

PaxDbiP76112.
PRIDEiP76112.

Interactioni

Protein-protein interaction databases

BioGridi4260194. 12 interactors.
STRINGi511145.b1448.

Structurei

3D structure databases

ProteinModelPortaliP76112.
SMRiP76112.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 163N-acetyltransferasePROSITE-ProRule annotationAdd BLAST163

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni85 – 87Acetyl-CoA bindingBy similarity3
Regioni93 – 98Acetyl-CoA bindingBy similarity6

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108Z7F. Bacteria.
COG1247. LUCA.
HOGENOMiHOG000078516.
InParanoidiP76112.
KOiK03823.
OMAiVTGQMPQ.
PhylomeDBiP76112.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiView protein in InterPro
IPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiView protein in PROSITE
PS51186. GNAT. 1 hit.

Sequencei

Sequence statusi: Complete.

P76112-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIRFARKAD CAAIAEIYNH AVLYTAAIWN DQTVDADNRI AWFEARTLAG
60 70 80 90 100
YPVLVSEENG VVTGYASFGD WRSFDGFRHT VEHSVYVHPD HQGKGLGRKL
110 120 130 140 150
LSRLIDEARD CGKHVMVAGI ESQNQASLHL HQSLGFVVTA QMPQVGTKFG
160 170
RWLDLTFMQL QLDERTEPDA IG
Length:172
Mass (Da):19,248
Last modified:February 1, 1997 - v1
Checksum:i4DAA0DC5198CDBD1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74530.1.
AP009048 Genomic DNA. Translation: BAA15080.2.
PIRiC64897.
RefSeqiNP_415965.1. NC_000913.3.
WP_001310799.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74530; AAC74530; b1448.
BAA15080; BAA15080; BAA15080.
GeneIDi946010.
KEGGiecj:JW5233.
eco:b1448.
PATRICi32118188. VBIEscCol129921_1514.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74530.1.
AP009048 Genomic DNA. Translation: BAA15080.2.
PIRiC64897.
RefSeqiNP_415965.1. NC_000913.3.
WP_001310799.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP76112.
SMRiP76112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260194. 12 interactors.
STRINGi511145.b1448.

Proteomic databases

PaxDbiP76112.
PRIDEiP76112.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74530; AAC74530; b1448.
BAA15080; BAA15080; BAA15080.
GeneIDi946010.
KEGGiecj:JW5233.
eco:b1448.
PATRICi32118188. VBIEscCol129921_1514.

Organism-specific databases

EchoBASEiEB3533.
EcoGeneiEG13770. mnaT.

Phylogenomic databases

eggNOGiENOG4108Z7F. Bacteria.
COG1247. LUCA.
HOGENOMiHOG000078516.
InParanoidiP76112.
KOiK03823.
OMAiVTGQMPQ.
PhylomeDBiP76112.

Enzyme and pathway databases

BioCyciEcoCyc:G6759-MONOMER.
MetaCyc:G6759-MONOMER.

Miscellaneous databases

PROiPR:P76112.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiView protein in InterPro
IPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiView protein in PROSITE
PS51186. GNAT. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMNAT_ECOLI
AccessioniPrimary (citable) accession number: P76112
Secondary accession number(s): P77401
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 1, 1997
Last modified: April 12, 2017
This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.