Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 21335454Publication DOI: 10.1128/JB.01441-10Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: jtomas
ub.edu
Institutions: Departamento de Microbiologia, Facultad de Biologia, Universidad Barcelona, Diagonal 645, 08071 Barcelona, Spain
The Aeromonas hydrophila AH-3 WecP represents a new class of UDP-HexNAc:polyprenol-P HexNAc-1-P transferases. These enzymes use a membrane-associated polyprenol phosphate acceptor (undecaprenyl phosphate [Und-P]) and a cytoplasmic UDP-d-N-acetylhexosamine sugar nucleotide as the donor substrate. Until now, all the WecA enzymes tested were able to transfer UDP-GlcNAc to the Und-P. In this study, we present in vitro and in vivo proofs that A. hydrophila AH-3 WecP transfers GalNAc to Und-P and is unable to transfer GlcNAc to the same enzyme substrate. The molecular topology of WecP is more similar to that of WbaP (UDP-Gal polyprenol-P transferase) than to that of WecA (UDP-GlcNAc polyprenol-P transferase). WecP is the first UDP-HexNAc:polyprenol-P GalNAc-1-P transferase described.
enzyme, Aeromonas, sugar nucleotide, WecP
Structure type: suggested polymer biological repeating unit
Location inside paper: p.1944, fig.1C
The structure in this paper was incorrect:
Compound class: O-polysaccharide, core oligosaccharide, O-antigen
Contained glycoepitopes: IEDB_130701,IEDB_136044,IEDB_136105,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,SB_137,SB_165,SB_166,SB_187,SB_195,SB_29,SB_44,SB_67,SB_7,SB_72,SB_88
Methods: DNA sequencing, GC-MS, SDS-PAGE, DNA techniques, glycosyltransferase assays, genetic methods
Related record ID(s): 2162, 10463, 11786, 20641, 23054, 23640, 29281, 29647, 30268, 108701, 114155, 116994
NCBI Taxonomy refs (TaxIDs): 2162916Reference(s) to other database(s): GTC:G47971KQ, GlycomeDB:
27141
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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