CAT_SALTI
ID CAT_SALTI Reviewed; 219 AA.
AC P62580; P00483;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Chloramphenicol acetyltransferase;
DE Short=CAT;
DE EC=2.3.1.28;
GN Name=cat; OrderedLocusNames=HCM1.206;
OS Salmonella typhi.
OG Plasmid pHCM1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
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; AL513383; CAD09793.1; -; Genomic_DNA.
DR RefSeq; NP_569406.1; NC_003384.1.
DR RefSeq; WP_000412211.1; NZ_WSUR01000059.1.
DR AlphaFoldDB; P62580; -.
DR SMR; P62580; -.
DR DrugBank; DB02703; Fusidic acid.
DR DrugCentral; P62580; -.
DR GeneID; 66025204; -.
DR KEGG; sty:HCM1.206; -.
DR PATRIC; fig|220341.7.peg.5228; -.
DR HOGENOM; CLU_093121_0_0_6; -.
DR OMA; WNRKEHF; -.
DR Proteomes; UP000000541; Plasmid pHCM1.
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..219
FT /note="Chloramphenicol acetyltransferase"
FT /id="PRO_0000165867"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
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