ID   CAT_STRAG               Reviewed;         215 AA.
AC   Q03058;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Chloramphenicol acetyltransferase;
DE            Short=CAT;
DE            EC=2.3.1.28;
GN   Name=cat;
OS   Streptococcus agalactiae.
OG   Plasmid pIP501.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1461942; DOI=10.1016/0147-619x(92)90060-n;
RA   Trieu-Cuot P., de Cespedes G., Horaud T.;
RT   "Nucleotide sequence of the chloramphenicol resistance determinant of the
RT   streptococcal plasmid pIP501.";
RL   Plasmid 28:272-276(1992).
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; X65462; CAA46455.1; -; Genomic_DNA.
DR   PIR; JQ1951; JQ1951.
DR   RefSeq; NP_044466.1; NC_001797.1.
DR   RefSeq; WP_002331392.1; NZ_MVFG01000004.1.
DR   AlphaFoldDB; Q03058; -.
DR   SMR; Q03058; -.
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..215
FT                   /note="Chloramphenicol acetyltransferase"
FT                   /id="PRO_0000165879"
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
SQ   SEQUENCE   215 AA;  25789 MW;  7FD30D9B612BB7B9 CRC64;
     MTFNIIELEN WDRKEYFEHY FNQQTTYSIT KEIDITLFKD MIKKKGYEIY PSLIYAIMEV
     VNKNKVFRTG INSENKLGYW DKLNPLYTVF NKQTEKFTNI WTESDKNFIS FYNNYKNDLL
     EYKDKEEMFP KKPIPENTIP ISMIPWIDFS SFNLNIGNNS SFLLPIITIG KFYSENNKIY
     IPVALQLHHS VCDGYHASLF MNEFQDIIHR VDDWI