CAT_CLOBU
ID CAT_CLOBU Reviewed; 219 AA.
AC Q02736;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Chloramphenicol acetyltransferase;
DE Short=CAT;
DE EC=2.3.1.28;
GN Name=catB;
OS Clostridium butyricum.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1492;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1489203; DOI=10.1128/aac.36.11.2548;
RA Huggins A.S., Bannam T.L., Rood J.I.;
RT "Comparative sequence analysis of the catB gene from Clostridium
RT butyricum.";
RL Antimicrob. Agents Chemother. 36:2548-2551(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.
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; M93113; AAA73865.1; -; Genomic_DNA.
DR PIR; A48907; A48907.
DR RefSeq; WP_063843219.1; NG_047589.1.
DR AlphaFoldDB; Q02736; -.
DR SMR; Q02736; -.
DR KEGG; ag:AAA73865; -.
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..219
FT /note="Chloramphenicol acetyltransferase"
FT /id="PRO_0000165859"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
SQ SEQUENCE 219 AA; 26144 MW; 1D2BB096D2C4C183 CRC64;
MNFNLIDINH WSRKPYFEHY LNNVKCTYSM TANIEITDLL YEIKLKNIKF YPTLIYMIAT
VVNNHKEFRI CFDHKGSLGY WDSMNPSYTI FHKENETFSS IWTEYNKSFL RFYSDYLDDI
KNYGNIMKFT PKSNEPDNTF SVSSIPWVSF TGFNLNVYNE GTYLIPIFTA GKYFKQENKI
FIPISIQVHH AICDGYHASR FINEMQELAF SFQEWLENK