MULTISPECIES: CatB-related O-acetyltransferase

LOCUS       WP_000867989             269 aa            linear   BCT 31-MAR-2023
            [Enterobacteriaceae].
ACCESSION   WP_000867989
VERSION     WP_000867989.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10129626
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..269
                     /product="CatB-related O-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=30941
     Region          76..222
                     /region_name="LbH_XAT"
                     /note="Xenobiotic acyltransferase (XAT): The XAT class of
                     hexapeptide acyltransferases is composed of a large number
                     of microbial enzymes that catalyze the CoA-dependent
                     acetylation of a variety of hydroxyl-bearing acceptors
                     such as chloramphenicol and...; cd03349"
                     /db_xref="CDD:100040"
     Site            order(82,84,100,112..113,118,120,122,157,159,162,181,197,
                     205)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:100040"
     Site            order(84,86,111..112,114,123..124,159,162,179..180,185,
                     193,195..196,198,202)
                     /site_type="active"
                     /db_xref="CDD:100040"
     Site            order(84,86,111,123..124)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100040"
     Site            order(112,114,148,159,162,167,179..180,185,193,195..196,
                     198,202)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:100040"
ORIGIN      
        1 mkvqlykfte dknktltfrw tkkhfefcmd nkiflnhkgk ksykernlfl fskgdkitie
       61 dnviaeeyst mpvknfssvg afsfptchfs gnirigrfcs iasnvkimgg nhplnrftth
      121 mmtyngefdk famsefersw tlkpfitkpe npiigndvwi gndvvlkggi aigdgaviaa
      181 nsvvtkdvpp yaivagvpak iirfrfdsnv idellrikww nynysdlpdn nkcddinyfv
      241 eemnrlisng niqerdykkf nlsevfrgl