Chloramphenicol acetyltransferase

Details

Name
Chloramphenicol acetyltransferase
Synonyms
  • 2.3.1.28
  • catB7
  • XAT
  • Xenobiotic acetyltransferase
Gene Name
cat
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Amino acid sequence
>lcl|BSEQ0021975|Chloramphenicol acetyltransferase
MGNYFESPFRGKLLSEQVSNPNIRVGRYSYYSGYYHGHSFDDCARYLMPDRDDVDKLVIG
SFCSIGSGAAFIMAGNQGHRAEWASTFPFHFMHEEPVFAGAVNGYQPAGDTLIGHDVWIG
TEAMFMPGVRVGHGAIIGSRALVTGDVEPYAIVGGNPARTIRKRFSDGDIQNLLEMAWWD
WPLADIEAAMPLLCTGDIPALYRHWKQRQATA
Number of residues
212
Molecular Weight
23524.385
Theoretical pI
6.07
GO Classification
Functions
chloramphenicol O-acetyltransferase activity
Processes
response to antibiotic
General Function
Chloramphenicol o-acetyltransferase activity
Specific Function
This enzyme is an effector of chloramphenicol (Cm) resistance in bacteria. Acetylates Cm but not 1-acetoxy-Cm.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0002621|639 bp
ATGGGCAACTATTTCGAGAGCCCCTTCAGGGGCAAGCTGCTCTCGGAACAGGTCAGCAAC
CCGAACATACGGGTGGGGCGCTACAGCTACTACTCCGGCTACTATCACGGGCATTCCTTC
GACGACTGCGCCCGCTACCTGATGCCGGACCGCGACGACGTGGACAAGCTGGTCATCGGC
AGTTTCTGCTCGATCGGCAGTGGCGCCGCCTTCATCATGGCCGGCAACCAGGGACACCGC
GCCGAATGGGCGTCGACCTTCCCCTTCCACTTCATGCACGAAGAGCCTGTCTTCGCCGGC
GCCGTGAACGGCTATCAGCCAGCCGGCGACACGCTGATCGGCCATGACGTCTGGATCGGT
ACCGAGGCGATGTTCATGCCCGGCGTACGGGTCGGCCACGGAGCCATCATCGGCAGCCGC
GCGCTGGTGACCGGCGATGTCGAGCCCTATGCCATCGTCGGCGGTAACCCGGCCCGGACC
ATTCGTAAGCGCTTTTCCGATGGCGATATCCAGAACCTGCTGGAAATGGCCTGGTGGGAC
TGGCCACTGGCCGATATCGAGGCAGCCATGCCACTGCTGTGTACTGGGGATATCCCCGCC
TTGTACCGGCACTGGAAACAGCGCCAGGCCACGGCCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP26841
UniProtKB Entry NameCAT4_PSEAE
GenBank Protein ID4104539
GenBank Gene IDAF036933
General References
  1. White PA, Stokes HW, Bunny KL, Hall RM: Characterisation of a chloramphenicol acetyltransferase determinant found in the chromosome of Pseudomonas aeruginosa. FEMS Microbiol Lett. 1999 Jun 1;175(1):27-35. [Article]
  2. Stover CK, Pham XQ, Erwin AL, Mizoguchi SD, Warrener P, Hickey MJ, Brinkman FS, Hufnagle WO, Kowalik DJ, Lagrou M, Garber RL, Goltry L, Tolentino E, Westbrock-Wadman S, Yuan Y, Brody LL, Coulter SN, Folger KR, Kas A, Larbig K, Lim R, Smith K, Spencer D, Wong GK, Wu Z, Paulsen IT, Reizer J, Saier MH, Hancock RE, Lory S, Olson MV: Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature. 2000 Aug 31;406(6799):959-64. [Article]
  3. Tian Y, Beaman TW, Roderick SL: Purification and crystallization of Pseudomonas aeruginosa chloramphenicol acetyltransferase. Proteins. 1997 Jun;28(2):298-300. [Article]
  4. Hindahl MS, Frank DW, Hamood A, Iglewski BH: Characterization of a gene that regulates toxin A synthesis in Pseudomonas aeruginosa. Nucleic Acids Res. 1988 Jun 24;16(12):5699. [Article]
  5. Beaman TW, Sugantino M, Roderick SL: Structure of the hexapeptide xenobiotic acetyltransferase from Pseudomonas aeruginosa. Biochemistry. 1998 May 12;37(19):6689-96. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01829Desulfo-coenzyme AexperimentalunknownDetails
DB00446Chloramphenicolapproved, vet_approved, withdrawnunknownsubstrateDetails