ID   ARY1_MESAU              Reviewed;         290 AA.
AC   P50292;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Arylamine N-acetyltransferase 1;
DE            EC=2.3.1.5;
DE   AltName: Full=Arylamide acetylase 1;
DE   AltName: Full=Monomorphic arylamine N-acetyltransferase;
DE            Short=MNAT;
DE   AltName: Full=N-acetyltransferase type 1;
DE            Short=NAT-1;
GN   Name=NAT1; Synonyms=AAC1;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=2009137; DOI=10.1002/mc.2940040112;
RA   Abu-Zeid M., Nagata K., Miyata M., Ozawa S., Fukuhara M., Yamazoe Y.;
RT   "An arylamine acetyltransferase (AT-I) from Syrian golden hamster liver:
RT   cloning, complete nucleotide sequence, and expression in mammalian cells.";
RL   Mol. Carcinog. 4:81-88(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Heart;
RX   PubMed=8081415;
RA   Ferguson R.J., Doll M.A., Rustan T.D., Baumstark B.R., Hein D.W.;
RT   "Syrian hamster monomorphic N-acetyltransferase (NAT1) alleles:
RT   amplification, cloning, sequencing, and expression in E. coli.";
RL   Pharmacogenetics 4:82-90(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7915937; DOI=10.1097/00008571-199404000-00006;
RA   Nagata K., Ozawa S., Miyata M., Shimada M., Yamazoe Y., Kato R.;
RT   "Primary structure and molecular basis of polymorphic appearance of an
RT   acetyltransferase (AT-II)* in hamsters.";
RL   Pharmacogenetics 4:91-100(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7756838; DOI=10.1006/prep.1995.1007;
RA   Bergstrom C.P., Wagner C.R., Ann D.K., Hanna P.E.;
RT   "Hamster monomorphic arylamine N-acetyltransferase: expression in
RT   Escherichia coli and purification.";
RL   Protein Expr. Purif. 6:45-55(1995).
CC   -!- FUNCTION: Participates in the detoxification of a plethora of hydrazine
CC       and arylamine drugs.
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; X54142; CAA38081.1; -; mRNA.
DR   EMBL; U05271; AAB60522.1; -; Genomic_DNA.
DR   EMBL; S72004; AAB31916.1; -; Genomic_DNA.
DR   PIR; A61397; A61397.
DR   RefSeq; NP_001268750.1; NM_001281821.1.
DR   RefSeq; XP_012972602.1; XM_013117148.1.
DR   RefSeq; XP_012972603.1; XM_013117149.1.
DR   RefSeq; XP_012972604.1; XM_013117150.1.
DR   RefSeq; XP_012972605.1; XM_013117151.1.
DR   RefSeq; XP_012972606.1; XM_013117152.1.
DR   RefSeq; XP_012972608.1; XM_013117154.1.
DR   AlphaFoldDB; P50292; -.
DR   SMR; P50292; -.
DR   STRING; 10036.XP_005075250.1; -.
DR   GeneID; 101840278; -.
DR   CTD; 9; -.
DR   eggNOG; ENOG502RD0D; Eukaryota.
DR   BRENDA; 2.3.1.5; 3239.
DR   BRENDA; 2.3.1.56; 3239.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   PRINTS; PR01543; ANATRNSFRASE.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..290
FT                   /note="Arylamine N-acetyltransferase 1"
FT                   /id="PRO_0000107906"
FT   ACT_SITE        68
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        122
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         106..107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P18440"
SQ   SEQUENCE   290 AA;  33500 MW;  06C26A0CCEACAF02 CRC64;
     MDIEAYFERI GYNNPVYTLD LATLTEVLQH QMRTIPFENL NMHCGEAMDL GLEATFDQIV
     RKKRGGWCLQ VNHLLYWALT QMGFETTMLG GYVYIVPVSK YSSEMIHLLV QVTISDRNYI
     VDAAYGGSYQ MWEPVELASG KDQPQVPAIF RLTEENETWY LDQIRREQHV PNQEFVNSDL
     LEKNTYRKIY SFTLQPRTIE DFEYANTYLQ ISPVSVFVNT SFCSLQTSEG VCCLIGSTIA
     RRKFSYKENV DLVEFKNVSE EEIEDVLKTA FGVSLERKFV PKNGNLSFSI