CAT_ECOLX
ID CAT_ECOLX Reviewed; 219 AA.
AC P62577; P00483;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Chloramphenicol acetyltransferase;
DE Short=CAT;
DE EC=2.3.1.28;
GN Name=cat;
OS Escherichia coli.
OG Plasmid JR66B.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP PROTEIN SEQUENCE.
RC PLASMID=JR66B;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn9;
RX PubMed=390403; DOI=10.1038/282864a0;
RA Alton N.K., Vapnek D.;
RT "Nucleotide sequence analysis of the chloramphenicol resistance transposon
RT Tn9.";
RL Nature 282:864-869(1979).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=TnCAM204;
RX PubMed=7353655; DOI=10.1016/0014-5793(80)80011-1;
RA Marcoli R., Iida S., Bickle T.A.;
RT "The DNA sequence of an IS/-flanked transposon coding for resistance to
RT chloramphenicol and fusidic acid.";
RL FEBS Lett. 110:11-14(1980).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 5-217 IN COMPLEX WITH NOS2.
RX PubMed=9334294; DOI=10.1126/science.278.5337.425;
RA Crane B.R., Arvai A.S., Gachhui R., Wu C., Ghosh D.K., Getzoff E.D.,
RA Stuehr D.J., Tainer J.A.;
RT "The structure of nitric oxide synthase oxygenase domain and inhibitor
RT complexes.";
RL Science 278:425-431(1997).
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:0000269|PubMed:9334294}.
CC -!- BIOTECHNOLOGY: This protein is used as a marker in many commonly used
CC cloning vectors, such as pACYC184.
CC -!- MISCELLANEOUS: Transposon Tncam204 is derived from the R plasmid NR1.
CC {ECO:0000305|PubMed:7353655}.
CC -!- SIMILARITY: Belongs to the chloramphenicol acetyltransferase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Chloramphenicol acetyltransferase
CC entry;
CC URL="https://en.wikipedia.org/wiki/Chloramphenicol_acetyltransferase";
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DR EMBL; V00623; CAA23900.1; -; Genomic_DNA.
DR EMBL; V00622; CAA23899.1; -; Genomic_DNA.
DR PIR; A93220; XXECC1.
DR RefSeq; WP_000412211.1; NZ_WVWF01000083.1.
DR RefSeq; YP_001096419.1; NC_009133.1.
DR RefSeq; YP_001816591.1; NC_010558.1.
DR RefSeq; YP_008995272.1; NC_023277.2.
DR RefSeq; YP_008997430.1; NC_023289.2.
DR RefSeq; YP_009068571.1; NC_025141.1.
DR RefSeq; YP_009071093.1; NC_025179.1.
DR RefSeq; YP_009071408.1; NC_025181.1.
DR RefSeq; YP_025721.1; NC_005923.1.
DR PDB; 1NOC; X-ray; 2.60 A; B=1-219.
DR PDB; 1PD5; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-219.
DR PDB; 1Q23; X-ray; 2.18 A; A/B/C/D/E/F/G/H/I/J/K/L=1-219.
DR PDB; 3U9B; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I=1-219.
DR PDB; 3U9F; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/R/S=1-219.
DR PDBsum; 1NOC; -.
DR PDBsum; 1PD5; -.
DR PDBsum; 1Q23; -.
DR PDBsum; 3U9B; -.
DR PDBsum; 3U9F; -.
DR AlphaFoldDB; P62577; -.
DR SMR; P62577; -.
DR MINT; P62577; -.
DR GeneID; 66025204; -.
DR KEGG; ag:CAA23899; -.
DR OMA; WNRKEHF; -.
DR BRENDA; 2.3.1.28; 2026.
DR EvolutionaryTrace; P62577; -.
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; Transposable element.
FT CHAIN 1..219
FT /note="Chloramphenicol acetyltransferase"
FT /id="PRO_0000165865"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1Q23"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1Q23"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:1Q23"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:1Q23"
FT STRAND 31..40
FT /evidence="ECO:0007829|PDB:1Q23"
FT HELIX 42..50
FT /evidence="ECO:0007829|PDB:1Q23"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:1Q23"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1Q23"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1Q23"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1Q23"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:1Q23"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:1Q23"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1Q23"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:1Q23"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1Q23"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:1Q23"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:1Q23"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1Q23"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1Q23"
FT STRAND 182..192
FT /evidence="ECO:0007829|PDB:1Q23"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:1Q23"
FT HELIX 198..214
FT /evidence="ECO:0007829|PDB:1Q23"
SQ SEQUENCE 219 AA; 25663 MW; 02C92576273FA18B CRC64;
MEKKITGYTT VDISQWHRKE HFEAFQSVAQ CTYNQTVQLD ITAFLKTVKK NKHKFYPAFI
HILARLMNAH PEFRMAMKDG ELVIWDSVHP CYTVFHEQTE TFSSLWSEYH DDFRQFLHIY
SQDVACYGEN LAYFPKGFIE NMFFVSANPW VSFTSFDLNV ANMDNFFAPV FTMGKYYTQG
DKVLMPLAIQ VHHAVCDGFH VGRMLNELQQ YCDEWQGGA
