ID   CAT_KLESP               Reviewed;         219 AA.
AC   P58777;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Chloramphenicol acetyltransferase;
DE            Short=CAT;
DE            EC=2.3.1.28;
GN   Name=cat;
OS   Klebsiella sp.
OG   Plasmid R429.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=576;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=390404; DOI=10.1038/282870a0;
RA   Shaw W.V., Packman L.C., Burleigh B.D., Dell A., Morris H.R., Hartley B.S.;
RT   "Primary structure of a chloramphenicol acetyltransferase specified by R
RT   plasmids.";
RL   Nature 282:870-872(1979).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=4628098; DOI=10.1073/pnas.69.10.3049;
RA   Shaw W.V., Sands L.C., Datta N.;
RT   "Hybridization of variants of chloramphenicol acetyltransferase specified
RT   by fi + and fi - R factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 69:3049-3053(1972).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chloramphenicol acetyltransferase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P58777; -.
DR   SMR; P58777; -.
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   1: Evidence at protein level;
KW   Acyltransferase; Antibiotic resistance; Direct protein sequencing; Plasmid;
KW   Transferase.
FT   CHAIN           1..219
FT                   /note="Chloramphenicol acetyltransferase"
FT                   /id="PRO_0000165866"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
SQ   SEQUENCE   219 AA;  25620 MW;  02C62A762830A18B CRC64;
     MEKKITGYTT VDISQWHRKE HFEAFQSVAQ CTYNQTVQLD ITAFLKTVKK NKHKFYPAFI
     HILARLMNAH PEFRMAMKDG ELVIWDSVHP CYTVFHEQTE TFSSLWSEYH DDFRQFLHIY
     SQDVACYGEN LAYFPKGFIE NMFFVSANPW VSFTSFDLNV AAMDNFFAPV FTMGKYYTQG
     DKVLMPLAIQ VHHAVCDGFH VGRMLNELQQ YCDEWQGGA