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Entry version 131 (13 Nov 2019)
Sequence version 1 (01 Feb 1997)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei124Acetyl-CoABy similarity1
Binding sitei133Acetyl-CoABy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAcyltransferase, Transferase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:G6759-MONOMER
ECOL316407:JW5233-MONOMER
MetaCyc:G6759-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:mnaT1 PublicationImported
Synonyms:yncA
Ordered Locus Names:b1448, JW5233
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000745771 – 172L-amino acid N-acyltransferase MnaTAdd BLAST172

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P76112

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P76112

PRoteomics IDEntifications database

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PRIDEi
P76112

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
4260194, 12 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b1448

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P76112

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 163N-acetyltransferasePROSITE-ProRule annotationAdd BLAST163

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni85 – 87Acetyl-CoA bindingBy similarity3
Regioni93 – 98Acetyl-CoA bindingBy similarity6

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4108Z7F Bacteria
COG1247 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000078516

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P76112

KEGG Orthology (KO)

More...
KOi
K03823

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P76112

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016181 Acyl_CoA_acyltransferase
IPR000182 GNAT_dom

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55729 SSF55729, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51186 GNAT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4DAA0DC5198CDBD1
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC74530.1
AP009048 Genomic DNA Translation: BAA15080.2

Protein sequence database of the Protein Information Resource

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PIRi
C64897

NCBI Reference Sequences

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RefSeqi
NP_415965.1, NC_000913.3
WP_001310799.1, NZ_SSZK01000021.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74530; AAC74530; b1448
BAA15080; BAA15080; BAA15080

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946010

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW5233
eco:b1448

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.820

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_SSZK01000021.1

3D structure databases

SMRiP76112
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4260194, 12 interactors
STRINGi511145.b1448

Proteomic databases

jPOSTiP76112
PaxDbiP76112
PRIDEiP76112

Genome annotation databases

EnsemblBacteriaiAAC74530; AAC74530; b1448
BAA15080; BAA15080; BAA15080
GeneIDi946010
KEGGiecj:JW5233
eco:b1448
PATRICifig|1411691.4.peg.820

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB3533

Phylogenomic databases

eggNOGiENOG4108Z7F Bacteria
COG1247 LUCA
HOGENOMiHOG000078516
InParanoidiP76112
KOiK03823
PhylomeDBiP76112

Enzyme and pathway databases

BioCyciEcoCyc:G6759-MONOMER
ECOL316407:JW5233-MONOMER
MetaCyc:G6759-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P76112

Family and domain databases

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMNAT_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P76112
Secondary accession number(s): P77401
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 1, 1997
Last modified: November 13, 2019
This is version 131 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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