NHOA_ECOLI
ID NHOA_ECOLI Reviewed; 281 AA.
AC P77567;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Arylamine N-acetyltransferase {ECO:0000305};
DE EC=2.3.1.5 {ECO:0000269|PubMed:10806332};
DE AltName: Full=Arylhydroxamate N,O-acetyltransferase {ECO:0000305};
DE AltName: Full=N-hydroxyarylamine O-acetyltransferase {ECO:0000303|PubMed:10806332};
DE EC=2.3.1.118 {ECO:0000250|UniProtKB:Q00267};
GN Name=nhoA; Synonyms=yddI; OrderedLocusNames=b1463, JW1458;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION AS A N-ACETYLTRANSFERASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=10806332; DOI=10.1016/s0304-4165(00)00038-6;
RA Yamamura E., Sayama M., Kakikawa M., Mori M., Taketo A., Kodaira K.;
RT "Purification and biochemical properties of an N-hydroxyarylamine O-
RT acetyltransferase from Escherichia coli.";
RL Biochim. Biophys. Acta 1475:10-16(2000).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12222687; DOI=10.1515/bc.2002.104;
RA Josephy P.D., Summerscales J., DeBruin L.S., Schlaeger C., Ho J.;
RT "N-hydroxyarylamine O-acetyltransferase-deficient Escherichia coli strains
RT are resistant to the mutagenicity of nitro compounds.";
RL Biol. Chem. 383:977-982(2002).
RN [6]
RP ACETYLATION AT LYS-214 AND LYS-281, DEACETYLATION BY COBB, FUNCTION,
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-127; LYS-214 AND LYS-281.
RX PubMed=23452042; DOI=10.1111/febs.12216;
RA Zhang Q.F., Zhang Q., Gu J., Gong P., Wang X.D., Wang X., Tu S., Bi L.J.,
RA Bi L., Yu Z.N., Yu Z., Zhang Z.P., Zhang Z., Cui Z.Q., Cui Z., Wei H.P.,
RA Wei H., Tao S.C., Tao S., Zhang X.E., Zhang X., Deng J.Y.;
RT "Reversibly acetylated lysine residues play important roles in the
RT enzymatic activity of Escherichia coli N-hydroxyarylamine O-
RT acetyltransferase.";
RL FEBS J. 280:1966-1979(2013).
CC -!- FUNCTION: Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic
CC amines, and, probably, the O-acetylation of N-hydroxyarylamines. In
CC vitro, catalyzes the N-acetylation of various arylamines such as
CC aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine,
CC aniline, isoniazid and 2-amino-fluorene (PubMed:10806332,
CC PubMed:23452042). N-hydroxyarylamine O-acetyltransferase activity has
CC not been assayed directly, however, NhoA activity is required for the
CC mutagenicity of nitroaromatic compounds, suggesting that it also has O-
CC acetyltransferase activity (Probable). {ECO:0000269|PubMed:10806332,
CC ECO:0000269|PubMed:23452042, ECO:0000305|PubMed:12222687,
CC ECO:0000305|PubMed:23452042}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an arylamine = an N-acetylarylamine + CoA;
CC Xref=Rhea:RHEA:16613, ChEBI:CHEBI:13790, ChEBI:CHEBI:50471,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.5;
CC Evidence={ECO:0000269|PubMed:10806332, ECO:0000269|PubMed:23452042};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an N-hydroxyarylamine = an N-acetoxyarylamine +
CC CoA; Xref=Rhea:RHEA:20277, ChEBI:CHEBI:13792, ChEBI:CHEBI:21494,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.118;
CC Evidence={ECO:0000250|UniProtKB:Q00267};
CC -!- ACTIVITY REGULATION: Inhibited by salicylic acid, acetylsalicylic acid,
CC 2,6-dichrolo-4-nitrophenol, N-ethylmaleimide and iodoacetamide.
CC {ECO:0000269|PubMed:10806332}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.55 mM for aniline {ECO:0000269|PubMed:10806332};
CC KM=0.41 mM for o-anisidine {ECO:0000269|PubMed:10806332};
CC KM=0.83 mM for p-anisidine {ECO:0000269|PubMed:10806332};
CC KM=0.48 mM for o-aminobenzoic acid {ECO:0000269|PubMed:10806332};
CC KM=0.36 mM for p-aminobenzoic acid {ECO:0000269|PubMed:10806332};
CC KM=1.94 mM for o-aminophenol {ECO:0000269|PubMed:10806332};
CC KM=1.71 mM for m-aminophenol {ECO:0000269|PubMed:10806332};
CC KM=0.54 mM for p-aminophenol {ECO:0000269|PubMed:10806332};
CC KM=0.63 mM for p-aminotoluene {ECO:0000269|PubMed:10806332};
CC KM=0.89 mM for p-phenetidine {ECO:0000269|PubMed:10806332};
CC KM=0.59 mM for isoniazid {ECO:0000269|PubMed:10806332};
CC Vmax=0.09 umol/min/mg enzyme with aniline as substrate
CC {ECO:0000269|PubMed:10806332};
CC Vmax=0.10 umol/min/mg enzyme with o-anisidine as substrate
CC {ECO:0000269|PubMed:10806332};
CC Vmax=0.47 umol/min/mg enzyme with p-anisidine as substrate
CC {ECO:0000269|PubMed:10806332};
CC Vmax=0.30 umol/min/mg enzyme with o-aminobenzoic acid as substrate
CC {ECO:0000269|PubMed:10806332};
CC Vmax=0.06 umol/min/mg enzyme with p-aminobenzoic acid as substrate
CC {ECO:0000269|PubMed:10806332};
CC Vmax=0.67 umol/min/mg enzyme with o-aminophenol as substrate
CC {ECO:0000269|PubMed:10806332};
CC Vmax=0.28 umol/min/mg enzyme with m-aminophenol as substrate
CC {ECO:0000269|PubMed:10806332};
CC Vmax=0.33 umol/min/mg enzyme with p-aminophenol as substrate
CC {ECO:0000269|PubMed:10806332};
CC Vmax=0.25 umol/min/mg enzyme with p-aminotoluene as substrate
CC {ECO:0000269|PubMed:10806332};
CC Vmax=0.50 umol/min/mg enzyme with p-phenetidine as substrate
CC {ECO:0000269|PubMed:10806332};
CC Vmax=0.17 umol/min/mg enzyme with isoniazid as substrate
CC {ECO:0000269|PubMed:10806332};
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:10806332};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:10806332};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10806332}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q00267}.
CC -!- PTM: Acetylated on Lys-214 and Lys-281. Deacetylated by CobB.
CC {ECO:0000269|PubMed:23452042}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants show marked resistance to nitro
CC compound mutagenicity. {ECO:0000269|PubMed:12222687}.
CC -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74545.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15100.1; -; Genomic_DNA.
DR PIR; B64899; B64899.
DR RefSeq; NP_415980.1; NC_000913.3.
DR RefSeq; WP_000187925.1; NZ_LN832404.1.
DR AlphaFoldDB; P77567; -.
DR SMR; P77567; -.
DR BioGRID; 4262892; 20.
DR IntAct; P77567; 7.
DR STRING; 511145.b1463; -.
DR iPTMnet; P77567; -.
DR PaxDb; P77567; -.
DR PRIDE; P77567; -.
DR EnsemblBacteria; AAC74545; AAC74545; b1463.
DR EnsemblBacteria; BAA15100; BAA15100; BAA15100.
DR GeneID; 947251; -.
DR KEGG; ecj:JW1458; -.
DR KEGG; eco:b1463; -.
DR PATRIC; fig|1411691.4.peg.805; -.
DR EchoBASE; EB3542; -.
DR eggNOG; COG2162; Bacteria.
DR HOGENOM; CLU_049918_1_1_6; -.
DR InParanoid; P77567; -.
DR OMA; CYEHNTL; -.
DR PhylomeDB; P77567; -.
DR BioCyc; EcoCyc:G6770-MON; -.
DR BioCyc; MetaCyc:G6770-MON; -.
DR SABIO-RK; P77567; -.
DR PRO; PR:P77567; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004060; F:arylamine N-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0046990; F:N-hydroxyarylamine O-acetyltransferase activity; IMP:EcoCyc.
DR InterPro; IPR001447; Arylamine_N-AcTrfase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR11786; PTHR11786; 1.
DR Pfam; PF00797; Acetyltransf_2; 1.
DR PRINTS; PR01543; ANATRNSFRASE.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..281
FT /note="Arylamine N-acetyltransferase"
FT /id="PRO_0000107915"
FT ACT_SITE 69
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q00267"
FT ACT_SITE 107
FT /evidence="ECO:0000250|UniProtKB:Q00267"
FT ACT_SITE 122
FT /evidence="ECO:0000250|UniProtKB:Q00267"
FT MOD_RES 214
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:23452042"
FT MOD_RES 281
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:23452042"
FT MUTAGEN 127
FT /note="G->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:23452042"
FT MUTAGEN 127
FT /note="G->F: Significant decrease in activity."
FT /evidence="ECO:0000269|PubMed:23452042"
FT MUTAGEN 214
FT /note="K->Q: Decreases O-acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:23452042"
FT MUTAGEN 214
FT /note="K->R: Slightly decreases acetylation level.
FT Decreases O- and N-acetyltransferase activities."
FT /evidence="ECO:0000269|PubMed:23452042"
FT MUTAGEN 281
FT /note="K->Q: Decreases O-acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:23452042"
FT MUTAGEN 281
FT /note="K->R: Markedly decreases acetylation level.
FT Decreases O- and N-acetyltransferase activities."
FT /evidence="ECO:0000269|PubMed:23452042"
SQ 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
