KEGG   ENZYME: 3.1.3.85Help
Entry
EC 3.1.3.85                 Enzyme                                 

Name
glucosyl-3-phosphoglycerate phosphatase;
GpgP protein
Class
Hydrolases;
Acting on ester bonds;
Phosphoric-monoester hydrolases
BRITE hierarchy
Sysname
alpha-D-glucosyl-3-phospho-D-glycerate phosphohydrolase
Reaction(IUBMB)
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O = 2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate [RN:R09664]
Reaction(KEGG)
Substrate
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate [CPD:C19791];
H2O [CPD:C00001]
Product
2-O-(alpha-D-glucopyranosyl)-D-glycerate [CPD:C19792];
phosphate [CPD:C00009]
Comment
The enzyme is involved in biosynthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate via the two-step pathway in which EC 2.4.1.266 (glucosyl-3-phosphoglycerate synthase) catalyses 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 glucosyl-3-phosphoglycerate phosphatase. In vivo the enzyme catalyses the dephosphorylation of 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate with lower efficiency [1,2]. Divalent metal ions (Mg2+, Mn2+ or Co2+) stimulate activity [1,2].
History
EC 3.1.3.85 created 2011
Reference
1  [PMID:17189358]
  Authors
Costa J, Empadinhas N, da Costa MS
  Title
Glucosylglycerate biosynthesis in the deepest lineage of the Bacteria: characterization of the thermophilic proteins GpgS and GpgP from Persephonella marina.
  Journal
J. Bacteriol. 189 (2007) 1648-54.
  Sequence
Reference
2  [PMID:16428406]
  Authors
Costa J, Empadinhas N, Goncalves L, Lamosa P, Santos H, da Costa MS
  Title
Characterization of the biosynthetic pathway of glucosylglycerate in the archaeon Methanococcoides burtonii.
  Journal
J. Bacteriol. 188 (2006) 1022-30.
  Sequence
[mbu:Mbur_0736]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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