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Entry version 129 (18 Sep 2019)
Sequence version 1 (01 Feb 1997)
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Protein

Arylamine N-acetyltransferase

Gene

nhoA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 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

Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene (PubMed:10806332, PubMed:23452042). N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O-acetyltransferase activity (Probable).2 Publications2 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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by salicylic acid, acetylsalicylic acid, 2,6-dichrolo-4-nitrophenol, N-ethylmaleimide and iodoacetamide.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.55 mM for aniline1 Publication
  2. KM=0.41 mM for o-anisidine1 Publication
  3. KM=0.83 mM for p-anisidine1 Publication
  4. KM=0.48 mM for o-aminobenzoic acid1 Publication
  5. KM=0.36 mM for p-aminobenzoic acid1 Publication
  6. KM=1.94 mM for o-aminophenol1 Publication
  7. KM=1.71 mM for m-aminophenol1 Publication
  8. KM=0.54 mM for p-aminophenol1 Publication
  9. KM=0.63 mM for p-aminotoluene1 Publication
  10. KM=0.89 mM for p-phenetidine1 Publication
  11. KM=0.59 mM for isoniazid1 Publication
  1. Vmax=0.09 µmol/min/mg enzyme with aniline as substrate1 Publication
  2. Vmax=0.10 µmol/min/mg enzyme with o-anisidine as substrate1 Publication
  3. Vmax=0.47 µmol/min/mg enzyme with p-anisidine as substrate1 Publication
  4. Vmax=0.30 µmol/min/mg enzyme with o-aminobenzoic acid as substrate1 Publication
  5. Vmax=0.06 µmol/min/mg enzyme with p-aminobenzoic acid as substrate1 Publication
  6. Vmax=0.67 µmol/min/mg enzyme with o-aminophenol as substrate1 Publication
  7. Vmax=0.28 µmol/min/mg enzyme with m-aminophenol as substrate1 Publication
  8. Vmax=0.33 µmol/min/mg enzyme with p-aminophenol as substrate1 Publication
  9. Vmax=0.25 µmol/min/mg enzyme with p-aminotoluene as substrate1 Publication
  10. Vmax=0.50 µmol/min/mg enzyme with p-phenetidine as substrate1 Publication
  11. Vmax=0.17 µmol/min/mg enzyme with isoniazid as substrate1 Publication

pH dependencei

Optimum pH is 7.4.1 Publication

Temperature dependencei

Optimum temperature is 37 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei69Acyl-thioester intermediateBy similarity1
Active sitei107By similarity1
Active sitei122By 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:G6770-MONOMER
ECOL316407:JW1458-MONOMER
MetaCyc:G6770-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P77567

<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:
Arylamine N-acetyltransferaseCurated (EC:2.3.1.51 Publication)
Alternative name(s):
Arylhydroxamate N,O-acetyltransferaseCurated
N-hydroxyarylamine O-acetyltransferase1 Publication (EC:2.3.1.118By similarity)
<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:nhoA
Synonyms:yddI
Ordered Locus Names:b1463, JW1458
<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

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG13780 nhoA

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<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 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

Deletion mutants show marked resistance to nitro compound mutagenicity.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi127G → A: No change in activity. 1 Publication1
Mutagenesisi127G → F: Significant decrease in activity. 1 Publication1
Mutagenesisi214K → Q: Decreases O-acetyltransferase activity. 1 Publication1
Mutagenesisi214K → R: Slightly decreases acetylation level. Decreases O- and N-acetyltransferase activities. 1 Publication1
Mutagenesisi281K → Q: Decreases O-acetyltransferase activity. 1 Publication1
Mutagenesisi281K → R: Markedly decreases acetylation level. Decreases O- and N-acetyltransferase activities. 1 Publication1

<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_00001079151 – 281Arylamine N-acetyltransferaseAdd BLAST281

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei214N6-acetyllysine1 Publication1
Modified residuei281N6-acetyllysine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Acetylated on Lys-214 and Lys-281. Deacetylated by CobB.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

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

More...
PaxDbi
P77567

PRoteomics IDEntifications database

More...
PRIDEi
P77567

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P77567

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4262892, 20 interactors

Protein interaction database and analysis system

More...
IntActi
P77567, 7 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b1463

<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
P77567

Database of comparative protein structure models

More...
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

<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
ENOG4108MUX Bacteria
COG2162 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000205436

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P77567

KEGG Orthology (KO)

More...
KOi
K00675

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P77567

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001447 Arylamine_N-AcTrfase
IPR038765 Papain-like_cys_pep_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11786 PTHR11786, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00797 Acetyltransf_2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01543 ANATRNSFRASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54001 SSF54001, 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.

P77567-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTPILNHYFA RINWSGAAAV NIDTLRALHL KHNCTIPFEN LDVLLPREIQ
60 70 80 90 100
LDNQSPEEKL VIARRGGYCF EQNGVFERVL RELGFNVRSL LGRVVLSNPP
110 120 130 140 150
ALPPRTHRLL LVELEEEKWI ADVGFGGQTL TAPIRLVSDL VQTTPHGEYR
160 170 180 190 200
LLQEGDDWVL QFNHHQHWQS MYRFDLCEQQ QSDYVMGNFW SAHWPQSHFR
210 220 230 240 250
HHLLMCRHLP DGGKLTLTNF HFTHYENGHA VEQRNLPDVA SLYAVMQEQF
260 270 280
GLGVDDAKHG FTVDELALVM AAFDTHPEAG K
Length:281
Mass (Da):32,275
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:iD6B777EE05B629D2
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
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: AAC74545.1
AP009048 Genomic DNA Translation: BAA15100.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B64899

NCBI Reference Sequences

More...
RefSeqi
NP_415980.1, NC_000913.3
WP_000187925.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74545; AAC74545; b1463
BAA15100; BAA15100; BAA15100

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947251

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1458
eco:b1463

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.805

<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: AAC74545.1
AP009048 Genomic DNA Translation: BAA15100.1
PIRiB64899
RefSeqiNP_415980.1, NC_000913.3
WP_000187925.1, NZ_LN832404.1

3D structure databases

SMRiP77567
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4262892, 20 interactors
IntActiP77567, 7 interactors
STRINGi511145.b1463

PTM databases

iPTMnetiP77567

Proteomic databases

PaxDbiP77567
PRIDEiP77567

Genome annotation databases

EnsemblBacteriaiAAC74545; AAC74545; b1463
BAA15100; BAA15100; BAA15100
GeneIDi947251
KEGGiecj:JW1458
eco:b1463
PATRICifig|1411691.4.peg.805

Organism-specific databases

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

More...
EchoBASEi
EB3542
EcoGeneiEG13780 nhoA

Phylogenomic databases

eggNOGiENOG4108MUX Bacteria
COG2162 LUCA
HOGENOMiHOG000205436
InParanoidiP77567
KOiK00675
PhylomeDBiP77567

Enzyme and pathway databases

BioCyciEcoCyc:G6770-MONOMER
ECOL316407:JW1458-MONOMER
MetaCyc:G6770-MONOMER
SABIO-RKiP77567

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P77567

Family and domain databases

InterProiView protein in InterPro
IPR001447 Arylamine_N-AcTrfase
IPR038765 Papain-like_cys_pep_sf
PANTHERiPTHR11786 PTHR11786, 1 hit
PfamiView protein in Pfam
PF00797 Acetyltransf_2, 1 hit
PRINTSiPR01543 ANATRNSFRASE
SUPFAMiSSF54001 SSF54001, 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 nameiNHOA_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: P77567
<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: December 1, 2000
Last sequence update: February 1, 1997
Last modified: September 18, 2019
This is version 129 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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