ID   CAT2_HAEIF              Reviewed;         213 AA.
AC   P22616;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Chloramphenicol acetyltransferase 2;
DE            EC=2.3.1.28;
DE   AltName: Full=Chloramphenicol acetyltransferase II;
DE            Short=CAT-II;
GN   Name=cat-IIH;
OS   Haemophilus influenzae.
OG   Plasmid p85098.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2268278; DOI=10.1042/bj2720505;
RA   Murray I.A., Martinez-Suarez J.V., Close T.J., Shaw W.V.;
RT   "Nucleotide sequences of genes encoding the type II chloramphenicol
RT   acetyltransferases of Escherichia coli and Haemophilus influenzae, which
RT   are sensitive to inhibition by thiol-reactive reagents.";
RL   Biochem. J. 272:505-510(1990).
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   -!- MISCELLANEOUS: Type II chloramphenicol acetyltransferases are sensitive
CC       to inhibition by thiol-reactive reagents. The inactivation occurs as a
CC       result of chemical modification of Cys-26.
CC   -!- SIMILARITY: Belongs to the chloramphenicol acetyltransferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X53797; CAA37806.1; -; Genomic_DNA.
DR   PIR; S13399; S13399.
DR   RefSeq; WP_063843222.1; NG_047593.1.
DR   AlphaFoldDB; P22616; -.
DR   SMR; P22616; -.
DR   PRIDE; P22616; -.
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..213
FT                   /note="Chloramphenicol acetyltransferase 2"
FT                   /id="PRO_0000165876"
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
SQ   SEQUENCE   213 AA;  24850 MW;  D20AE21520C74A78 CRC64;
     MNFTRIDLNT WNRREHFALY RQQIKCGFSL TTKLDITAFR TALAETDYKF YPVMIYLISR
     VVNQFPEFRM AMKDNALIYW DQTDPVFTVF HKETETFSAL FCRYCPDISE FMAGYNAVMA
     EYQHNTALFP QGALPENHLN ISSLPWVSFD GFNLNITGND DYFAPVFTMA KFQQEDNRVL
     LPVSVQVHHA VCDGFHAARF INTLQMMCDN ILK