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N-hydroxyarylamine O-acetyltransferase (EC 2.3.1.118) (Arylamine N-acetyltransferase) (Arylhydroxamate N,O-acetyltransferase)

 NHOA_ECOLI              Reviewed;         281 AA.
P77567;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
25-OCT-2017, entry version 120.
RecName: Full=N-hydroxyarylamine O-acetyltransferase {ECO:0000303|PubMed:10806332};
EC=2.3.1.118 {ECO:0000250|UniProtKB:Q00267};
AltName: Full=Arylamine N-acetyltransferase {ECO:0000305};
AltName: Full=Arylhydroxamate N,O-acetyltransferase {ECO:0000305};
Name=nhoA; Synonyms=yddI; OrderedLocusNames=b1463, JW1458;
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 A N-ACETYLTRANSFERASE, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=10806332; DOI=10.1016/S0304-4165(00)00038-6;
Yamamura E., Sayama M., Kakikawa M., Mori M., Taketo A., Kodaira K.;
"Purification and biochemical properties of an N-hydroxyarylamine O-
acetyltransferase from Escherichia coli.";
Biochim. Biophys. Acta 1475:10-16(2000).
[5]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=12222687; DOI=10.1515/BC.2002.104;
Josephy P.D., Summerscales J., DeBruin L.S., Schlaeger C., Ho J.;
"N-hydroxyarylamine O-acetyltransferase-deficient Escherichia coli
strains are resistant to the mutagenicity of nitro compounds.";
Biol. Chem. 383:977-982(2002).
[6]
ACETYLATION AT LYS-214 AND LYS-281, DEACETYLATION BY COBB, FUNCTION,
AND MUTAGENESIS OF GLY-127; LYS-214 AND LYS-281.
PubMed=23452042; DOI=10.1111/febs.12216;
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.;
"Reversibly acetylated lysine residues play important roles in the
enzymatic activity of Escherichia coli N-hydroxyarylamine O-
acetyltransferase.";
FEBS J. 280:1966-1979(2013).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:10806332, ECO:0000305|PubMed:12222687,
ECO:0000305|PubMed:23452042}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-hydroxyarylamine = CoA + an
N-acetoxyarylamine. {ECO:0000250|UniProtKB:Q00267}.
-!- ENZYME REGULATION: Inhibited by salicylic acid, acetylsalicylic
acid, 2,6-dichrolo-4-nitrophenol, N-ethylmaleimide and
iodoacetamide. {ECO:0000269|PubMed:10806332}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.55 mM for aniline {ECO:0000269|PubMed:10806332};
KM=0.41 mM for o-anisidine {ECO:0000269|PubMed:10806332};
KM=0.83 mM for p-anisidine {ECO:0000269|PubMed:10806332};
KM=0.48 mM for o-aminobenzoic acid
{ECO:0000269|PubMed:10806332};
KM=0.36 mM for p-aminobenzoic acid
{ECO:0000269|PubMed:10806332};
KM=1.94 mM for o-aminophenol {ECO:0000269|PubMed:10806332};
KM=1.71 mM for m-aminophenol {ECO:0000269|PubMed:10806332};
KM=0.54 mM for p-aminophenol {ECO:0000269|PubMed:10806332};
KM=0.63 mM for p-aminotoluene {ECO:0000269|PubMed:10806332};
KM=0.89 mM for p-phenetidine {ECO:0000269|PubMed:10806332};
KM=0.59 mM for isoniazid {ECO:0000269|PubMed:10806332};
Vmax=0.09 umol/min/mg enzyme with aniline as substrate
{ECO:0000269|PubMed:10806332};
Vmax=0.10 umol/min/mg enzyme with o-anisidine as substrate
{ECO:0000269|PubMed:10806332};
Vmax=0.47 umol/min/mg enzyme with p-anisidine as substrate
{ECO:0000269|PubMed:10806332};
Vmax=0.30 umol/min/mg enzyme with o-aminobenzoic acid as
substrate {ECO:0000269|PubMed:10806332};
Vmax=0.06 umol/min/mg enzyme with p-aminobenzoic acid as
substrate {ECO:0000269|PubMed:10806332};
Vmax=0.67 umol/min/mg enzyme with o-aminophenol as substrate
{ECO:0000269|PubMed:10806332};
Vmax=0.28 umol/min/mg enzyme with m-aminophenol as substrate
{ECO:0000269|PubMed:10806332};
Vmax=0.33 umol/min/mg enzyme with p-aminophenol as substrate
{ECO:0000269|PubMed:10806332};
Vmax=0.25 umol/min/mg enzyme with p-aminotoluene as substrate
{ECO:0000269|PubMed:10806332};
Vmax=0.50 umol/min/mg enzyme with p-phenetidine as substrate
{ECO:0000269|PubMed:10806332};
Vmax=0.17 umol/min/mg enzyme with isoniazid as substrate
{ECO:0000269|PubMed:10806332};
pH dependence:
Optimum pH is 7.4. {ECO:0000269|PubMed:10806332};
Temperature dependence:
Optimum temperature is 37 degrees Celsius.
{ECO:0000269|PubMed:10806332};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10806332}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q00267}.
-!- PTM: Acetylated on Lys-214 and Lys-281. Deacetylated by CobB.
{ECO:0000269|PubMed:23452042}.
-!- DISRUPTION PHENOTYPE: Deletion mutants show marked resistance to
nitro compound mutagenicity. {ECO:0000269|PubMed:12222687}.
-!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family.
{ECO:0000305}.
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EMBL; U00096; AAC74545.1; -; Genomic_DNA.
EMBL; AP009048; BAA15100.1; -; Genomic_DNA.
PIR; B64899; B64899.
RefSeq; NP_415980.1; NC_000913.3.
RefSeq; WP_000187925.1; NZ_LN832404.1.
ProteinModelPortal; P77567; -.
SMR; P77567; -.
BioGrid; 4262892; 20.
IntAct; P77567; 7.
STRING; 316385.ECDH10B_1594; -.
iPTMnet; P77567; -.
PaxDb; P77567; -.
PRIDE; P77567; -.
EnsemblBacteria; AAC74545; AAC74545; b1463.
EnsemblBacteria; BAA15100; BAA15100; BAA15100.
GeneID; 947251; -.
KEGG; ecj:JW1458; -.
KEGG; eco:b1463; -.
PATRIC; fig|1411691.4.peg.805; -.
EchoBASE; EB3542; -.
EcoGene; EG13780; nhoA.
eggNOG; ENOG4108MUX; Bacteria.
eggNOG; COG2162; LUCA.
HOGENOM; HOG000205436; -.
InParanoid; P77567; -.
KO; K00675; -.
PhylomeDB; P77567; -.
BioCyc; EcoCyc:G6770-MONOMER; -.
BioCyc; MetaCyc:G6770-MONOMER; -.
PRO; PR:P77567; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004060; F:arylamine N-acetyltransferase activity; IDA:EcoCyc.
GO; GO:0046990; F:N-hydroxyarylamine O-acetyltransferase activity; IMP:EcoCyc.
GO; GO:0008152; P:metabolic process; IEA:InterPro.
InterPro; IPR001447; Arylamine_N-AcTrfase.
PANTHER; PTHR11786; PTHR11786; 1.
Pfam; PF00797; Acetyltransf_2; 1.
PRINTS; PR01543; ANATRNSFRASE.
1: Evidence at protein level;
Acetylation; Acyltransferase; Complete proteome; Cytoplasm;
Reference proteome; Transferase.
CHAIN 1 281 N-hydroxyarylamine O-acetyltransferase.
/FTId=PRO_0000107915.
ACT_SITE 69 69 Acyl-thioester intermediate.
{ECO:0000250|UniProtKB:Q00267}.
ACT_SITE 107 107 {ECO:0000250|UniProtKB:Q00267}.
ACT_SITE 122 122 {ECO:0000250|UniProtKB:Q00267}.
MOD_RES 214 214 N6-acetyllysine.
{ECO:0000269|PubMed:23452042}.
MOD_RES 281 281 N6-acetyllysine.
{ECO:0000269|PubMed:23452042}.
MUTAGEN 127 127 G->A: No change in activity.
{ECO:0000269|PubMed:23452042}.
MUTAGEN 127 127 G->F: Significant decrease in activity.
{ECO:0000269|PubMed:23452042}.
MUTAGEN 214 214 K->Q: Decreases O-acetyltransferase
activity. {ECO:0000269|PubMed:23452042}.
MUTAGEN 214 214 K->R: Slightly decreases acetylation
level. Decreases O- and N-
acetyltransferase activities.
{ECO:0000269|PubMed:23452042}.
MUTAGEN 281 281 K->Q: Decreases O-acetyltransferase
activity. {ECO:0000269|PubMed:23452042}.
MUTAGEN 281 281 K->R: Markedly decreases acetylation
level. Decreases O- and N-
acetyltransferase activities.
{ECO:0000269|PubMed:23452042}.
SEQUENCE 281 AA; 32275 MW; D6B777EE05B629D2 CRC64;
MTPILNHYFA RINWSGAAAV NIDTLRALHL KHNCTIPFEN LDVLLPREIQ LDNQSPEEKL
VIARRGGYCF EQNGVFERVL RELGFNVRSL LGRVVLSNPP ALPPRTHRLL LVELEEEKWI
ADVGFGGQTL TAPIRLVSDL VQTTPHGEYR LLQEGDDWVL QFNHHQHWQS MYRFDLCEQQ
QSDYVMGNFW SAHWPQSHFR HHLLMCRHLP DGGKLTLTNF HFTHYENGHA VEQRNLPDVA
SLYAVMQEQF GLGVDDAKHG FTVDELALVM AAFDTHPEAG K


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