CATH Classification
Domain Context
CATH Clusters
Superfamily | Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A |
Functional Family |
Enzyme Information
2.4.1.266 |
Glucosyl-3-phosphoglycerate synthase.
based on mapping to UniProt P9WMW9
NDP-glucose + 3-phospho-D-glycerate = NDP + 2-O-(alpha-D-glucopyranosyl)- 3-phospho-D-glycerate.
-!- The enzyme is involved in biosynthesis of 2-O-(alpha-D- glucopyranosyl)-D-glycerate via the two-step pathway in which glucosyl-3-phosphoglycerate synthase catalyzes the conversion of GDP- glucose and 3-phospho-D-glycerate into 2-O-(alpha-D-glucopyranosyl)- 3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D- glucopyranosyl)-D-glycerate by EC 3.1.3.85. -!- The activity is dependent on divalent cations (Mn(2+), Co(2+), or Mg(2+)). -!- The enzyme from Persephonella marina shows moderate flexibility on the sugar donor concerning the nucleotide moiety (UDP-glucose, ADP- glucose, GDP-glucose) but is strictly specific for glucose. -!- The enzyme is also strictly specific for 3-phospho-D-glycerate as acceptor. -!- The enzyme from Methanococcoides burtonii is strictly specific for GDP-glucose and 3-phospho-D-glycerate. -!- This enzyme catalyzes the first glucosylation step in methylglucose lipopolysaccharide biosynthesis in mycobacteria.
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UniProtKB Entries (1)
P9WMW9 |
GPGS_MYCTU
Mycobacterium tuberculosis H37Rv
Glucosyl-3-phosphoglycerate synthase
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PDB Structure
PDB | 4Y7F |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
A Native Ternary Complex Trapped in a Crystal Reveals the Catalytic Mechanism of a Retaining Glycosyltransferase.
Angew.Chem.Int.Ed.Engl.
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