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  • This record is a non-redundant protein sequence. Please read more here.

MULTISPECIES: NeuD/PglB/VioB family sugar acetyltransferase [Corynebacterium]

NCBI Reference Sequence: WP_070429134.1

Identical Proteins FASTA Graphics 

LOCUS       WP_070429134             231 aa            linear   BCT 16-JUN-2023
DEFINITION  MULTISPECIES: NeuD/PglB/VioB family sugar acetyltransferase
            [Corynebacterium].
ACCESSION   WP_070429134
VERSION     WP_070429134.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Kaundinya,C.R., Savithri,H.S., Rao,K.K. and Balaji,P.V.
  TITLE     EpsM from Bacillus subtilis 168 has
            UDP-2,4,6-trideoxy-2-acetamido-4-amino glucose acetyltransferase
            activity in vitro
  JOURNAL   Biochem Biophys Res Commun 505 (4), 1057-1062 (2018)
   PUBMED   30314705
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Nguyen,L.C., Yamamoto,M., Ohnishi-Kameyama,M., Andi,S., Taguchi,F.,
            Iwaki,M., Yoshida,M., Ishii,T., Konishi,T., Tsunemi,K. and
            Ichinose,Y.
  TITLE     Genetic analysis of genes involved in synthesis of modified
            4-amino-4,6-dideoxyglucose in flagellin of Pseudomonas syringae pv.
            tabaci
  JOURNAL   Mol Genet Genomics 282 (6), 595-605 (2009)
   PUBMED   19787374
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Steenbergen,S.M., Lee,Y.C., Vann,W.F., Vionnet,J., Wright,L.F. and
            Vimr,E.R.
  TITLE     Separate pathways for O acetylation of polymeric and monomeric
            sialic acids and identification of sialyl O-acetyl esterase in
            Escherichia coli K1
  JOURNAL   J Bacteriol 188 (17), 6195-6206 (2006)
   PUBMED   16923886
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Lewis,A.L., Hensler,M.E., Varki,A. and Nizet,V.
  TITLE     The group B streptococcal sialic acid O-acetyltransferase is
            encoded by neuD, a conserved component of bacterial sialic acid
            biosynthetic gene clusters
  JOURNAL   J Biol Chem 281 (16), 11186-11192 (2006)
   PUBMED   16490781
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Annunziato,P.W., Wright,L.F., Vann,W.F. and Silver,R.P.
  TITLE     Nucleotide sequence and genetic analysis of the neuD and neuB genes
            in region 2 of the polysialic acid gene cluster of Escherichia coli
            K1
  JOURNAL   J Bacteriol 177 (2), 312-319 (1995)
   PUBMED   7814319
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  :: HMM
            Evidence Accession :: TIGR03570.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..231
                     /product="NeuD/PglB/VioB family sugar acetyltransferase"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24040
     Region          13..224
                     /region_name="LbetaH"
                     /note="Left-handed parallel beta-Helix (LbetaH or LbH)
                     domain: The alignment contains 5 turns, each containing
                     three imperfect tandem repeats of a hexapeptide repeat
                     motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing
                     hexapeptide repeats are often enzymes...; cl00160"
                     /db_xref="CDD:469633"
     Site            order(136,138,142,144,154,160,162,172,177..178,180,190,
                     194,196,198)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:100050"
     Site            order(172,174..175,180,192,198)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:100050"
ORIGIN      
        1 mpkqwinntt tekivivgag gfgrevashi rdindyaven glpqqweilg liddgtpdmt
       61 yfhklgieyl gdtnilkdlp kdvhyvvaig ngaarrsiah radstglipa tlvhpdttig
      121 avvsigpgtv vcpgaritcn ieigahcqvh vnvevghdav tnnfvsifpl aaisgfvtlg
      181 aestigansv inpgvavgeg syvgsgaavn kdvpeytlva gvpakvkktl r
//
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