ID   CAT_PROMI               Reviewed;         217 AA.
AC   P07641;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Chloramphenicol acetyltransferase;
DE            Short=CAT;
DE            EC=2.3.1.28;
GN   Name=cat;
OS   Proteus mirabilis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=584;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PM13;
RX   PubMed=3900035; DOI=10.1128/jb.164.1.123-129.1985;
RA   Charles I.G., Keyte J.W., Shaw W.V.;
RT   "Nucleotide sequence analysis of the cat gene of Proteus mirabilis:
RT   comparison with the type I (Tn9) cat gene.";
RL   J. Bacteriol. 164:123-129(1985).
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; M11587; AAA25655.1; -; Genomic_DNA.
DR   PIR; A24651; A24651.
DR   RefSeq; WP_063843208.1; NG_047569.1.
DR   AlphaFoldDB; P07641; -.
DR   SMR; P07641; -.
DR   KEGG; ag:AAA25655; -.
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..217
FT                   /note="Chloramphenicol acetyltransferase"
FT                   /id="PRO_0000165868"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
SQ   SEQUENCE   217 AA;  25313 MW;  08ABB443F9FC41C2 CRC64;
     MDTKRVGILV VDLSQWGRKE HFEAFQSFAQ CTFSQTVQLD ITSLLKTVKQ NGYKFYPTFI
     YIISLLVNKH AEFRMAMKDG ELVIWDSVNP GYNIFHEQTE TFSSLWSYYH KDINRFLKTY
     SEDIAQYGDD LAYFPKEFIE NMFFVSANPW VSFTSFNLNM ANINNFFAPV FTIGKYYTQG
     DKVLMPLAIQ VHHAVCDGFH VGRLLNEIQQ YCDEGCK