EC number:3.1.3.80

Enzyme

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     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.80
Description:2,3-bisphosphoglycerate 3-phosphatase.
Alternative Name: 2,3-BPG 3-phosphatase.
Prosite: PDOC00538;
PDB:
PDBScop

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.80
BRENDA Enzyme Link: BRENDA 3.1.3.80
KEGG Enzyme Link: KEGG3.1.3.80
BioCyc Enzyme Link: BioCyc 3.1.3.80
ExPASy Enzyme Link: ExPASy3.1.3.80
EC2PDB Enzyme Link: EC2PDB 3.1.3.80
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.80
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.80
IntEnz Enzyme Link: IntEnz 3.1.3.80
MEDLINE Enzyme Link: MEDLINE 3.1.3.80

EC number:3.1.3.80

MSA:

3.1.3.80;
Phylogenetic Tree:

3.1.3.80;
Uniprot:
M-CSA:
RHEA:27381 2,3-bisphospho-D-glycerate + H2O = 2-phospho-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
Molecular cloning and expression of a rat hepatic multiple inositol polyphosphate phosphatase.Craxton A, Caffrey JJ, Burkhart W, Safrany ST, Shears SB1997 Nov 159359836
Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt.Cho J, King JS, Qian X, Harwood AJ, Shears SB2008 Apr 2218413611
Multiple inositol polyphosphate phosphatase: evolution as a distinct group within the histidine phosphatase family and chromosomal localization of the human and mouse genes to chromosomes 10q23 and 19.Chi H, Tiller GE, Dasouki MJ, Romano PR, Wang J, O'keefe RJ, Puzas JE, Rosier RN, Reynolds PR1999 Mar 1510087200