ID   ARY1_RABIT              Reviewed;         290 AA.
AC   P18605;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 104.
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=New Zealand white; TISSUE=Liver;
RX   PubMed=2402454; DOI=10.1093/nar/18.17.5287;
RA   Blum M., Heim M., Meyer U.A.;
RT   "Nucleotide sequence of rabbit NAT1 encoding monomorphic arylamine N-
RT   acetyltransferase.";
RL   Nucleic Acids Res. 18:5287-5287(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=2071601; DOI=10.1016/s0021-9258(18)98830-7;
RA   Sasaki Y., Ohsako S., Deguchi T.;
RT   "Molecular and genetic analyses of arylamine N-acetyltransferase
RT   polymorphism of rabbit liver.";
RL   J. Biol. Chem. 266:13243-13250(1991).
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; X53765; CAA37785.1; -; Genomic_DNA.
DR   EMBL; D10108; BAA00989.1; -; Genomic_DNA.
DR   PIR; C39870; XYRBM.
DR   RefSeq; NP_001164620.1; NM_001171149.1.
DR   RefSeq; XP_008265477.1; XM_008267255.2.
DR   AlphaFoldDB; P18605; -.
DR   SMR; P18605; -.
DR   STRING; 9986.ENSOCUP00000024297; -.
DR   GeneID; 100328959; -.
DR   KEGG; ocu:100328959; -.
DR   CTD; 9; -.
DR   eggNOG; ENOG502RD0D; Eukaryota.
DR   InParanoid; P18605; -.
DR   OrthoDB; 1545569at2759; -.
DR   TreeFam; TF106311; -.
DR   Proteomes; UP000001811; 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   3: Inferred from homology;
KW   Acetylation; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..290
FT                   /note="Arylamine N-acetyltransferase 1"
FT                   /id="PRO_0000107913"
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         104
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         214
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"
FT   CONFLICT        285
FT                   /note="N -> H (in Ref. 2; BAA00989)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   290 AA;  33780 MW;  31175E83651EE693 CRC64;
     MDIEAYYQRI GYKNPRNKLD LESLTDIFQH QIRTVPYENL SIHCGESMEL DLEAIFDQIV
     RRNRGGWCLQ VNYLLYWALT TTGFETTMLG GFVCGSHTDK YSTGMIHLIV QVTINGRNYI
     VDAGFGRSYQ MWQPVELISG KDQPQVPSIF RLREEGETWY LDQIRRQQHV PDQEFLNSEL
     LERKTHRKLY CFTLQPRTIE EFESANTYLQ ISPSSPFLDK SICSLQTPEG VHCLVGLILT
     FRTYNYKENT DLVEFKVLTE EEVEEVLKTI FNISLGKKLV SKNGNLFFTI