Literature summary for 2.4.1.B69 extracted from

Anonsen, J.H.; Vik, A.; Borud, B.; Viburiene, R.; Aas, F.E.; Kidd, S.W.; Aspholm, M.; Koomey, M.
Characterization of a unique tetrasaccharide and distinct glycoproteome in the O-linked protein glycosylation system of Neisseria elongata subsp. glycolytica (2016), J. Bacteriol., 198, 256-267.

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Organism

Organism	UniProt	Comment	Textmining
Neisseria elongata subsp. glycolytica	A0A0N7IL44	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-D-glucose + diNAcBac-PP-tritrans,heptacis-undecaprenol	-	Neisseria elongata subsp. glycolytica	glucosyl-diNAcBac-PP-tritrans,heptacis-undecaprenol	-	?

Synonyms

Synonyms	Comment	Organism
PglH	-	Neisseria elongata subsp. glycolytica

General Information

General Information	Comment	Organism
physiological function	a null mutation in PglH leads to the expression of a diNAcBac monosaccharide glycoform. PglH protein participates in the synthesis of Und-PP-diNAcBac-Glc (i.e. undecaprenyl diphosphate-4-glyceramido-2-acetamido-2,4,6-trideoxy-alpha-D-hexose) similarly to its gonococcal and meningococcal orthologues	Neisseria elongata subsp. glycolytica

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Release 2023.1 (January 2023)