Enzyme

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     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.82
Description:D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase.
Cath: 3.40.50.1000;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.82
BRENDA Enzyme Link: BRENDA 3.1.3.82
KEGG Enzyme Link: KEGG3.1.3.82
BioCyc Enzyme Link: BioCyc 3.1.3.82
ExPASy Enzyme Link: ExPASy3.1.3.82
EC2PDB Enzyme Link: EC2PDB 3.1.3.82
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.82
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.82
IntEnz Enzyme Link: IntEnz 3.1.3.82
MEDLINE Enzyme Link: MEDLINE 3.1.3.82
MSA:

3.1.3.82;

Phylogenetic Tree:

3.1.3.82;

Uniprot:
M-CSA:
RHEA:28518 D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
RULE(radius=1) [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Divergence of biochemical function in the HAD superfamily: D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB).Wang L, Huang H, Nguyen HH, Allen KN, Mariano PS, Dunaway-Mariano D2010 Feb 1620050615
Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides.Valvano MA, Messner P, Kosma P2002 Jul12101286
Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia coli.Kneidinger B, Marolda C, Graninger M, Zamyatina A, McArthur F, Kosma P, Valvano MA, Messner P2002 Jan11751812