ID   NAT_MYCTO               Reviewed;         283 AA.
AC   P9WJI4; L0TCY1; P0A5L8; P96848;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Arylamine N-acetyltransferase;
DE            Short=NAT;
DE            EC=2.3.1.5 {ECO:0000250|UniProtKB:P9WJI5};
GN   Name=nat; OrderedLocusNames=MT3671;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the transfer of the acetyl group from acetyl
CC       coenzyme A to the free amino group of arylamines and hydrazines. Is
CC       able to utilize not only acetyl-CoA, but also n-propionyl-CoA and
CC       acetoacetyl-CoA as acyl donors, although at a lower rate. As acetyl-CoA
CC       and propionyl-CoA are products of cholesterol catabolism and the nat
CC       gene is likely present in the same operon than genes involved in
CC       cholesterol degradation, this enzyme could have a role in the
CC       utilization and regulation of these CoA species.
CC       {ECO:0000250|UniProtKB:P9WJI5}.
CC   -!- FUNCTION: It has been reported that overexpression of this enzyme may
CC       be responsible for increased resistance to the front-line
CC       antitubercular drug isoniazid, by acetylating and hence inactivating
CC       the prodrug. However, isoniazid is an extremely poor substrate for the
CC       enzyme; therefore, the expression of this enzyme is unlikely to be a
CC       significant cause of isoniazid resistance in M.tuberculosis.
CC       {ECO:0000250|UniProtKB:P9WJI5}.
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:0000250|UniProtKB:P9WJI5};
CC   -!- SUBUNIT: Homodimer and homotetramer. {ECO:0000250|UniProtKB:O86309}.
CC   -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK48028.1; -; Genomic_DNA.
DR   RefSeq; WP_003419364.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJI4; -.
DR   SMR; P9WJI4; -.
DR   EnsemblBacteria; AAK48028; AAK48028; MT3671.
DR   KEGG; mtc:MT3671; -.
DR   PATRIC; fig|83331.31.peg.3951; -.
DR   HOGENOM; CLU_049918_1_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0004060; F:arylamine N-acetyltransferase activity; IEA:UniProtKB-EC.
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   SUPFAM; SSF54001; SSF54001; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Transferase.
FT   CHAIN           1..283
FT                   /note="Arylamine N-acetyltransferase"
FT                   /id="PRO_0000427824"
FT   ACT_SITE        70
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WJI5"
FT   ACT_SITE        110
FT                   /evidence="ECO:0000250|UniProtKB:P9WJI5"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000250|UniProtKB:P9WJI5"
SQ   SEQUENCE   283 AA;  31029 MW;  9C8D98E3256D088A CRC64;
     MALDLTAYFD RINYRGATDP TLDVLQDLVT VHSRTIPFEN LDPLLGVPVD DLSPQALADK
     LVLRRRGGYC FEHNGLMGYV LAELGYRVRR FAARVVWKLA PDAPLPPQTH TLLGVTFPGS
     GGCYLVDVGF GGQTPTSPLR LETGAVQPTT HEPYRLEDRV DGFVLQAMVR DTWQTLYEFT
     TQTRPQIDLK VASWYASTHP ASKFVTGLTA AVITDDARWN LSGRDLAVHR AGGTEKIRLA
     DAAAVVDTLS ERFGINVADI GERGALETRI DELLARQPGA DAP