CAT4_PSEAE
ID CAT4_PSEAE Reviewed; 212 AA.
AC P26841; Q9S542;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Chloramphenicol acetyltransferase;
DE EC=2.3.1.28;
DE AltName: Full=Xenobiotic acetyltransferase;
DE Short=XAT;
GN Name=cat; Synonyms=catB7; OrderedLocusNames=PA0706;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=PAO222;
RX PubMed=10361706; DOI=10.1111/j.1574-6968.1999.tb13598.x;
RA White P.A., Stokes H.W., Bunny K.L., Hall R.M.;
RT "Characterisation of a chloramphenicol acetyltransferase determinant found
RT in the chromosome of Pseudomonas aeruginosa.";
RL FEMS Microbiol. Lett. 175:27-35(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CRYSTALLIZATION.
RC STRAIN=ATCC 29260 / PA103;
RX PubMed=9188747;
RX DOI=10.1002/(sici)1097-0134(199706)28:2<298::aid-prot18>3.3.co;2-3;
RA Tian Y., Beaman T.W., Roderick S.L.;
RT "Purification and crystallization of Pseudomonas aeruginosa chloramphenicol
RT acetyltransferase.";
RL Proteins 28:298-300(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65.
RC STRAIN=ATCC 29260 / PA103;
RX PubMed=3133641; DOI=10.1093/nar/16.12.5699;
RA Hindahl M.S., Frank D.W., Hamood A., Iglewski B.H.;
RT "Characterization of a gene that regulates toxin A synthesis in Pseudomonas
RT aeruginosa.";
RL Nucleic Acids Res. 16:5699-5699(1988).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RC STRAIN=ATCC 29260 / PA103;
RX PubMed=9578552; DOI=10.1021/bi980106v;
RA Beaman T.W., Sugantino M., Roderick S.L.;
RT "Structure of the hexapeptide xenobiotic acetyltransferase from Pseudomonas
RT aeruginosa.";
RL Biochemistry 37:6689-6696(1998).
CC -!- FUNCTION: This enzyme is an effector of chloramphenicol (Cm) resistance
CC in bacteria. Acetylates Cm but not 1-acetoxy-Cm.
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 -!- SUBUNIT: Homotrimer.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=X12366; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF036933; AAD02068.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04095.1; -; Genomic_DNA.
DR EMBL; X12366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C83557; C83557.
DR RefSeq; NP_249397.1; NC_002516.2.
DR RefSeq; WP_003112709.1; NZ_QZGE01000025.1.
DR PDB; 1XAT; X-ray; 3.20 A; A=1-212.
DR PDB; 2XAT; X-ray; 3.20 A; A=1-212.
DR PDBsum; 1XAT; -.
DR PDBsum; 2XAT; -.
DR AlphaFoldDB; P26841; -.
DR SMR; P26841; -.
DR STRING; 287.DR97_1411; -.
DR DrugBank; DB00446; Chloramphenicol.
DR DrugBank; DB01829; Desulfo-coenzyme A.
DR PaxDb; P26841; -.
DR DNASU; 878374; -.
DR EnsemblBacteria; AAG04095; AAG04095; PA0706.
DR GeneID; 878374; -.
DR KEGG; ag:AAD02068; -.
DR KEGG; pae:PA0706; -.
DR PATRIC; fig|208964.12.peg.740; -.
DR PseudoCAP; PA0706; -.
DR HOGENOM; CLU_051638_5_3_6; -.
DR InParanoid; P26841; -.
DR OMA; VGRYSYY; -.
DR PhylomeDB; P26841; -.
DR BioCyc; PAER208964:G1FZ6-717-MON; -.
DR EvolutionaryTrace; P26841; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008811; F:chloramphenicol O-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Antibiotic resistance; Reference proteome;
KW Repeat; Transferase.
FT CHAIN 1..212
FT /note="Chloramphenicol acetyltransferase"
FT /id="PRO_0000068661"
FT ACT_SITE 79
FT CONFLICT 97
FT /note="V -> A (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="D -> E (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="R -> Q (in Ref. 3)"
FT /evidence="ECO:0000305"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1XAT"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:1XAT"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1XAT"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2XAT"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:1XAT"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1XAT"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1XAT"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1XAT"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2XAT"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1XAT"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:1XAT"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1XAT"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:1XAT"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1XAT"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:1XAT"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:1XAT"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:1XAT"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:1XAT"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1XAT"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:1XAT"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:1XAT"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:1XAT"
SQ SEQUENCE 212 AA; 23525 MW; 306EEF39978C19FC CRC64;
MGNYFESPFR GKLLSEQVSN PNIRVGRYSY YSGYYHGHSF DDCARYLMPD RDDVDKLVIG
SFCSIGSGAA FIMAGNQGHR AEWASTFPFH FMHEEPVFAG AVNGYQPAGD TLIGHDVWIG
TEAMFMPGVR VGHGAIIGSR ALVTGDVEPY AIVGGNPART IRKRFSDGDI QNLLEMAWWD
WPLADIEAAM PLLCTGDIPA LYRHWKQRQA TA
