EC number:3.1.3.85

Enzyme

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EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.85
Description:Glucosyl-3-phosphoglycerate phosphatase.
Cath: 3.90.550.10; 3.40.50.1240;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.85
BRENDA Enzyme Link: BRENDA 3.1.3.85
KEGG Enzyme Link: KEGG3.1.3.85
BioCyc Enzyme Link: BioCyc 3.1.3.85
ExPASy Enzyme Link: ExPASy3.1.3.85
EC2PDB Enzyme Link: EC2PDB 3.1.3.85
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.85
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.85
IntEnz Enzyme Link: IntEnz 3.1.3.85
MEDLINE Enzyme Link: MEDLINE 3.1.3.85

EC number:3.1.3.85

MSA:

3.1.3.85;
Phylogenetic Tree:

3.1.3.85;
Uniprot:
M-CSA:
RHEA:31343 2-O-(alpha-D-glucopyranosyl)-3-O-phospho-D-glycerate + H2O = 2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
RULE(radius=1) [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[OH2;+0:7]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Mycobacterium tuberculosis Rv2419c, the missing glucosyl-3-phosphoglycerate phosphatase for the second step in methylglucose lipopolysaccharide biosynthesis.Mendes V, Maranha A, Alarico S, da Costa MS, Empadinhas N201122355692
Glucosylglycerate biosynthesis in the deepest lineage of the Bacteria: characterization of the thermophilic proteins GpgS and GpgP from Persephonella marina.Costa J, Empadinhas N, da Costa MS2007 Mar17189358
Characterization of the biosynthetic pathway of glucosylglycerate in the archaeon Methanococcoides burtonii.Costa J, Empadinhas N, Gonçalves L, Lamosa P, Santos H, da Costa MS2006 Feb16428406