Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

N-hydroxyarylamine O-acetyltransferase

Gene

nhoA

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

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. 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.2 Publications1 Publication

Catalytic activityi

Acetyl-CoA + an N-hydroxyarylamine = CoA + an N-acetoxyarylamine.By similarity

Enzyme regulationi

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

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei69 – 691Acyl-thioester intermediateBy similarity
Active sitei107 – 1071By similarity
Active sitei122 – 1221By similarity

GO - Molecular functioni

  • arylamine N-acetyltransferase activity Source: EcoCyc
  • N-hydroxyarylamine O-acetyltransferase activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciEcoCyc:G6770-MONOMER.
ECOL316407:JW1458-MONOMER.
MetaCyc:G6770-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
N-hydroxyarylamine O-acetyltransferase1 Publication (EC:2.3.1.118By similarity)
Alternative name(s):
Arylamine N-acetyltransferaseCurated
Arylhydroxamate N,O-acetyltransferaseCurated
Gene namesi
Name:nhoA
Synonyms:yddI
Ordered Locus Names:b1463, JW1458
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13780. nhoA.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi127 – 1271G → A: No change in activity. 1 Publication
Mutagenesisi127 – 1271G → F: Significant decrease in activity. 1 Publication
Mutagenesisi214 – 2141K → Q: Decreases O-acetyltransferase activity. 1 Publication
Mutagenesisi214 – 2141K → R: Slightly decreases acetylation level. Decreases O- and N-acetyltransferase activities. 1 Publication
Mutagenesisi281 – 2811K → Q: Decreases O-acetyltransferase activity. 1 Publication
Mutagenesisi281 – 2811K → R: Markedly decreases acetylation level. Decreases O- and N-acetyltransferase activities. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 281281N-hydroxyarylamine O-acetyltransferasePRO_0000107915Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei214 – 2141N6-acetyllysine1 Publication
Modified residuei281 – 2811N6-acetyllysine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP77567.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4262892. 20 interactions.
IntActiP77567. 7 interactions.
STRINGi511145.b1463.

Structurei

3D structure databases

ProteinModelPortaliP77567.
SMRiP77567. Positions 1-273.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108MUX. Bacteria.
COG2162. LUCA.
HOGENOMiHOG000205436.
InParanoidiP77567.
KOiK00675.
OMAiHAGLYES.
OrthoDBiEOG6D2KV2.
PhylomeDBiP77567.

Family and domain databases

InterProiIPR001447. Arylamine_N-AcTrfase.
[Graphical view]
PANTHERiPTHR11786. PTHR11786. 1 hit.
PfamiPF00797. Acetyltransf_2. 1 hit.
[Graphical view]
PRINTSiPR01543. ANATRNSFRASE.

Sequencei

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
Checksum:iD6B777EE05B629D2
GO

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.

Genome annotation databases

EnsemblBacteriaiAAC74545; AAC74545; b1463.
BAA15100; BAA15100; BAA15100.
GeneIDi947251.
KEGGiecj:JW1458.
eco:b1463.
PATRICi32118218. VBIEscCol129921_1529.

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

ProteinModelPortaliP77567.
SMRiP77567. Positions 1-273.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262892. 20 interactions.
IntActiP77567. 7 interactions.
STRINGi511145.b1463.

Proteomic databases

PaxDbiP77567.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74545; AAC74545; b1463.
BAA15100; BAA15100; BAA15100.
GeneIDi947251.
KEGGiecj:JW1458.
eco:b1463.
PATRICi32118218. VBIEscCol129921_1529.

Organism-specific databases

EchoBASEiEB3542.
EcoGeneiEG13780. nhoA.

Phylogenomic databases

eggNOGiENOG4108MUX. Bacteria.
COG2162. LUCA.
HOGENOMiHOG000205436.
InParanoidiP77567.
KOiK00675.
OMAiHAGLYES.
OrthoDBiEOG6D2KV2.
PhylomeDBiP77567.

Enzyme and pathway databases

BioCyciEcoCyc:G6770-MONOMER.
ECOL316407:JW1458-MONOMER.
MetaCyc:G6770-MONOMER.

Miscellaneous databases

PROiP77567.

Family and domain databases

InterProiIPR001447. Arylamine_N-AcTrfase.
[Graphical view]
PANTHERiPTHR11786. PTHR11786. 1 hit.
PfamiPF00797. Acetyltransf_2. 1 hit.
[Graphical view]
PRINTSiPR01543. ANATRNSFRASE.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Purification and biochemical properties of an N-hydroxyarylamine O-acetyltransferase from Escherichia coli."
    Yamamura E., Sayama M., Kakikawa M., Mori M., Taketo A., Kodaira K.
    Biochim. Biophys. Acta 1475:10-16(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A N-ACETYLTRANSFERASE, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  5. "N-hydroxyarylamine O-acetyltransferase-deficient Escherichia coli strains are resistant to the mutagenicity of nitro compounds."
    Josephy P.D., Summerscales J., DeBruin L.S., Schlaeger C., Ho J.
    Biol. Chem. 383:977-982(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  6. "Reversibly acetylated lysine residues play important roles in the enzymatic activity of Escherichia coli N-hydroxyarylamine O-acetyltransferase."
    Zhang Q.F., Zhang Q., Gu J., Gong P., Wang X.D., Wang X., Tu S., Bi L.J., Bi L., Yu Z.N., Yu Z., Zhang Z.P., Zhang Z., Cui Z.Q., Cui Z., Wei H.P., Wei H., Tao S.C.
    , Tao S., Zhang X.E., Zhang X., Deng J.Y.
    FEBS J. 280:1966-1979(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-214 AND LYS-281, DEACETYLATION BY COBB, FUNCTION, MUTAGENESIS OF GLY-127; LYS-214 AND LYS-281.

Entry informationi

Entry nameiNHOA_ECOLI
AccessioniPrimary (citable) accession number: P77567
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 1, 1997
Last modified: July 6, 2016
This is version 113 of the entry and version 1 of the sequence. [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.