ID   CAT_VIBAN               Reviewed;         216 AA.
AC   P49417;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Chloramphenicol acetyltransferase;
DE            Short=CAT;
DE            EC=2.3.1.28;
GN   Name=cat;
OS   Vibrio anguillarum (Listonella anguillarum).
OG   Plasmid pJA7324.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=55601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PT24;
RX   PubMed=1406372; DOI=10.1111/j.1348-0421.1992.tb02072.x;
RA   Zhao J., Aoki T.;
RT   "Cloning and nucleotide sequence analysis of a chloramphenicol
RT   acetyltransferase gene from Vibrio anguillarum.";
RL   Microbiol. Immunol. 36:695-705(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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chloramphenicol acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; S48276; AAB23649.1; -; Genomic_DNA.
DR   RefSeq; WP_032488555.1; NG_047573.1.
DR   AlphaFoldDB; P49417; -.
DR   SMR; P49417; -.
DR   KEGG; ag:AAB23649; -.
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..216
FT                   /note="Chloramphenicol acetyltransferase"
FT                   /id="PRO_0000165880"
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
SQ   SEQUENCE   216 AA;  25471 MW;  4BEB1E95C4164ADD CRC64;
     MEFRLVDLKT WKRKEYFTHY FESVPCTYSM TVKLDITTIK TGKAKLYPAL LYAVSTVVNR
     HEEFRMTVDD EGQIGIFSEM MPCYTIFQKD TEMFSNIWTE YIGDYTEFCK QYEKDMQQYG
     ENKGMMAKPN PPVNTFPVSM IPWTTFEGFN LNLQKGYGYL LPIFTFGRYY EENGKYWIPL
     SIQVHHAVCD GFHTCRFINE LQDVIQSLQN HGGDEE