MULTISPECIES: GNAT family N-acetyltransferase [Pseudomonas].

LOCUS       WP_003096834             149 aa            linear   BCT 31-DEC-2024
ACCESSION   WP_003096834
VERSION     WP_003096834.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
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 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..149
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16878
     Region          4..135
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          79..148
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mstslqirpv gagdhaawlp lwegyqrfyk teiaaatsda twqrfldade pmnaalawld
       61 eravglvhwi yhrscwtvgd ycylqdlfva eglrgegigr rliehvyaea gaagcsrvhw
      121 lthesnsdam klyeriadks gflqyrril