ID   CAT_CAMCO               Reviewed;         207 AA.
AC   P22782;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Chloramphenicol acetyltransferase;
DE            Short=CAT;
DE            EC=2.3.1.28;
OS   Campylobacter coli.
OG   Plasmid pNR9589.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2227449; DOI=10.1016/0378-1119(90)90463-2;
RA   Wang Y., Taylor D.E.;
RT   "Chloramphenicol resistance in Campylobacter coli: nucleotide sequence,
RT   expression, and cloning vector construction.";
RL   Gene 94:23-28(1990).
CC   -!- FUNCTION: This enzyme is an effector of chloramphenicol resistance in
CC       bacteria.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + chloramphenicol = chloramphenicol 3-acetate +
CC         CoA; Xref=Rhea:RHEA:18421, ChEBI:CHEBI:16730, ChEBI:CHEBI:17698,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.28;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10021};
CC   -!- SUBUNIT: Homotrimer.
CC   -!- SIMILARITY: Belongs to the chloramphenicol acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; M35190; AAA23018.1; -; Genomic_DNA.
DR   PIR; JQ0788; JQ0788.
DR   RefSeq; WP_040564913.1; NZ_LISF01000007.1.
DR   AlphaFoldDB; P22782; -.
DR   SMR; P22782; -.
DR   KEGG; ag:AAA23018; -.
DR   PATRIC; fig|195.1009.peg.614; -.
DR   GO; GO:0008811; F:chloramphenicol O-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR018372; Chloramphenicol_AcTrfase_AS.
DR   InterPro; IPR001707; Cmp_AcTrfase.
DR   PANTHER; PTHR38474; PTHR38474; 1.
DR   Pfam; PF00302; CAT; 1.
DR   PIRSF; PIRSF000440; CAT; 1.
DR   SMART; SM01059; CAT; 1.
DR   PROSITE; PS00100; CAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Antibiotic resistance; Plasmid; Transferase.
FT   CHAIN           1..207
FT                   /note="Chloramphenicol acetyltransferase"
FT                   /id="PRO_0000165858"
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
SQ   SEQUENCE   207 AA;  24292 MW;  6B15FCEF26E06314 CRC64;
     MQFTKIDINN WTRKEYFDHY FGNTPCTYSM TVKLDISKLK KDGKKLYPTL LYGVTTIINR
     HEEFRTALDE NGQVGVFSEM LPCYTVFHKE TETFSSIWTE FTADYTEFLQ NYQKDIDAFG
     ERMGMSAKPN PPENTFPVSM IPWTSFEGFN LNLKKGYDYL LPIFTFGKYY EEGGKYYIPL
     SIQVHHAVCD GFHVCRFLDE LQDLLNK