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
//