ID   CAT_CLODI               Reviewed;         212 AA.
AC   P11504;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Chloramphenicol acetyltransferase;
DE            Short=CAT;
DE            EC=2.3.1.28;
GN   Name=catD;
OS   Clostridioides difficile (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=1496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Type W / Isolate W1;
RX   PubMed=2748343; DOI=10.1093/nar/17.12.4877;
RA   Wren B.W., Mullany P., Clayton C., Tabaqchali S.;
RT   "Nucleotide sequence of a chloramphenicol acetyl transferase gene from
RT   Clostridium difficile.";
RL   Nucleic Acids Res. 17:4877-4877(1989).
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; X15100; CAA33203.1; -; Genomic_DNA.
DR   PIR; S04711; S04711.
DR   RefSeq; WP_063843233.1; NG_047622.1.
DR   AlphaFoldDB; P11504; -.
DR   SMR; P11504; -.
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; Transferase.
FT   CHAIN           1..212
FT                   /note="Chloramphenicol acetyltransferase"
FT                   /id="PRO_0000165860"
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
SQ   SEQUENCE   212 AA;  24836 MW;  790F8448030E8B55 CRC64;
     MVFEKIDKNS WNRKEYFDHY FASVPCTYSM TVKVDITQIK EKGMKLYPAM LYYIAMIVNR
     HSEFRTAINQ DGELGIYDEM IPSYTIFHND TETFSSLWTE CKSDFKSFLA DYESDTQRYG
     NNHRMEGKPN APENIFNVSM IPWSTFDGFN LNLQKGYDYL IPIFTMGKII KKDNKIILPL
     AIQVHHAVCD GFHICRFVNE LQELIIVTQV CL