CAT3_ECOLX
ID CAT3_ECOLX Reviewed; 213 AA.
AC P00484;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Chloramphenicol acetyltransferase 3;
DE EC=2.3.1.28;
DE AltName: Full=Chloramphenicol acetyltransferase III;
DE Short=CAT-III;
GN Name=cat3;
OS Escherichia coli.
OG Plasmid IncK R387.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3048245; DOI=10.1042/bj2520173;
RA Murray I.A., Hawkins A.R., Keyte J.W., Shaw W.V.;
RT "Nucleotide sequence analysis and overexpression of the gene encoding a
RT type III chloramphenicol acetyltransferase.";
RL Biochem. J. 252:173-179(1988).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RX PubMed=3288984; DOI=10.1073/pnas.85.12.4133;
RA Leslie A.G.W., Moody P.C.E., Shaw W.V.;
RT "Structure of chloramphenicol acetyltransferase at 1.75-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4133-4137(1988).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RX PubMed=2187098; DOI=10.1016/s0022-2836(05)80129-9;
RA Leslie A.G.W.;
RT "Refined crystal structure of type III chloramphenicol acetyltransferase at
RT 1.75-A resolution.";
RL J. Mol. Biol. 213:167-186(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 -!- SIMILARITY: Belongs to the chloramphenicol acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X07848; CAA30695.1; -; Genomic_DNA.
DR PIR; A00567; XXECC3.
DR RefSeq; WP_004920769.1; NZ_SPZH01000060.1.
DR PDB; 1CIA; X-ray; 2.50 A; A=1-213.
DR PDB; 1CLA; X-ray; 2.34 A; A=1-213.
DR PDB; 1QCA; X-ray; 2.20 A; A=1-213.
DR PDB; 2CLA; X-ray; 2.35 A; A=1-213.
DR PDB; 3CLA; X-ray; 1.75 A; A=1-213.
DR PDB; 4CLA; X-ray; 2.00 A; A=1-213.
DR PDB; 6X7Q; X-ray; 1.68 A; A/B/C=1-213.
DR PDBsum; 1CIA; -.
DR PDBsum; 1CLA; -.
DR PDBsum; 1QCA; -.
DR PDBsum; 2CLA; -.
DR PDBsum; 3CLA; -.
DR PDBsum; 4CLA; -.
DR PDBsum; 6X7Q; -.
DR AlphaFoldDB; P00484; -.
DR SMR; P00484; -.
DR DrugBank; DB00446; Chloramphenicol.
DR DrugBank; DB07565; Chloramphenicol succinate.
DR DrugBank; DB02703; Fusidic acid.
DR KEGG; ag:CAA30695; -.
DR EvolutionaryTrace; P00484; -.
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 3D-structure; Acyltransferase; Antibiotic resistance;
KW Direct protein sequencing; Plasmid; Transferase.
FT CHAIN 1..213
FT /note="Chloramphenicol acetyltransferase 3"
FT /id="PRO_0000165877"
FT ACT_SITE 189
FT /note="Proton acceptor"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:6X7Q"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:6X7Q"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:6X7Q"
FT STRAND 26..35
FT /evidence="ECO:0007829|PDB:6X7Q"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:6X7Q"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:6X7Q"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6X7Q"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:6X7Q"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:6X7Q"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:6X7Q"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:6X7Q"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:6X7Q"
FT HELIX 108..122
FT /evidence="ECO:0007829|PDB:6X7Q"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:6X7Q"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:6X7Q"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:6X7Q"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:6X7Q"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6X7Q"
FT STRAND 178..188
FT /evidence="ECO:0007829|PDB:6X7Q"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:6X7Q"
FT HELIX 194..208
FT /evidence="ECO:0007829|PDB:6X7Q"
SQ SEQUENCE 213 AA; 24994 MW; 4A96839AB590CB1D CRC64;
MNYTKFDVKN WVRREHFEFY RHRLPCGFSL TSKIDITTLK KSLDDSAYKF YPVMIYLIAQ
AVNQFDELRM AIKDDELIVW DSVDPQFTVF HQETETFSAL SCPYSSDIDQ FMVNYLSVME
RYKSDTKLFP QGVTPENHLN ISALPWVNFD SFNLNVANFT DYFAPIITMA KYQQEGDRLL
LPLSVQVHHA VCDGFHVARF INRLQELCNS KLK
