ID   CAT2_CLOPF              Reviewed;         207 AA.
AC   P26826;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Chloramphenicol acetyltransferase;
DE            Short=CAT;
DE            EC=2.3.1.28;
GN   Name=catP;
OS   Clostridium perfringens.
OG   Plasmid pIP401.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1502;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TRANSPOSON=Tn4451;
RX   PubMed=2541053; DOI=10.1016/0378-1119(89)90282-5;
RA   Steffen C., Matzura H.;
RT   "Nucleotide sequence analysis and expression studies of a chloramphenicol-
RT   acetyltransferase-coding gene from Clostridium perfringens.";
RL   Gene 75:349-354(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1513878; DOI=10.1016/0147-619x(92)90023-4;
RA   Sloan J., Warner T.A., Scott P.T., Bannam T.L., Berryman D.I., Rood J.I.;
RT   "Construction of a sequenced Clostridium perfringens-Escherichia coli
RT   shuttle plasmid.";
RL   Plasmid 27:207-219(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CP590;
RX   PubMed=7565113; DOI=10.1111/j.1365-2958.1995.tb02417.x;
RA   Bannam T.L., Crellin P.K., Rood J.I.;
RT   "Molecular genetics of the chloramphenicol-resistance transposon Tn4451
RT   from Clostridium perfringens: the TnpX site-specific recombinase excises a
RT   circular transposon molecule.";
RL   Mol. Microbiol. 16:535-551(1995).
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; M74769; AAA23213.1; -; Genomic_DNA.
DR   EMBL; M77169; AAA73115.1; -; Genomic_DNA.
DR   EMBL; L02937; AAC36952.1; -; Genomic_DNA.
DR   EMBL; U15027; AAB51421.1; -; Genomic_DNA.
DR   PIR; S78535; I40797.
DR   RefSeq; WP_002570989.1; NG_047623.1.
DR   RefSeq; YP_009063396.1; NC_025042.1.
DR   AlphaFoldDB; P26826; -.
DR   SMR; P26826; -.
DR   GeneID; 20469234; -.
DR   KEGG; ag:AAB51421; -.
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;
KW   Transposable element.
FT   CHAIN           1..207
FT                   /note="Chloramphenicol acetyltransferase"
FT                   /id="PRO_0000165862"
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
SQ   SEQUENCE   207 AA;  24381 MW;  98AF451E40E52B8B CRC64;
     MVFEKIDKNS WNRKEYFDHY FASVPCTYSM TVKVDITQIK EKGMKLYPAM LYYIAMIVNR
     HSEFRTAINQ DGELGIYDEM IPSYTIFHND TETFSSLWTE CKSDFKSFLA DYESDTQRYG
     NNHRMEGKPN APENIFNVSM IPWSTFDGFN LNLQKGYDYL IPIFTMGKYY KEDNKIILPL
     AIQVHHAVCD GFHICRFVNE LQELINS