EC number:3.1.3.37

Enzyme

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EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.37
Description:Sedoheptulose-bisphosphatase.
Alternative Name: Sedoheptulose-1,7-bisphosphatase.
Prosite: PDOC00114;
PDB:
PDBScop
Cath: 3.30.540.10; 3.90.460.10; 3.40.190.80; 3.40.190.90; 3.40.50.1240;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.37
BRENDA Enzyme Link: BRENDA 3.1.3.37
KEGG Enzyme Link: KEGG3.1.3.37
BioCyc Enzyme Link: BioCyc 3.1.3.37
ExPASy Enzyme Link: ExPASy3.1.3.37
EC2PDB Enzyme Link: EC2PDB 3.1.3.37
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.37
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.37
IntEnz Enzyme Link: IntEnz 3.1.3.37
MEDLINE Enzyme Link: MEDLINE 3.1.3.37

EC number:3.1.3.37

MSA:

3.1.3.37;
Phylogenetic Tree:

3.1.3.37;
Uniprot:
M-CSA:
RHEA:17461 H2O + sedoheptulose 1,7-bisphosphate = D-sedoheptulose 7-phosphate + 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
Riboneogenesis in yeast.Clasquin MF, Melamud E, Singer A, Gooding JR, Xu X, Dong A, Cui H, Campagna SR, Savchenko A, Yakunin AF, Rabinowitz JD, Caudy AA2011 Jun 1021663798
Structure and activity of the metal-independent fructose-1,6-bisphosphatase YK23 from Saccharomyces cerevisiae.Kuznetsova E, Xu L, Singer A, Brown G, Dong A, Flick R, Cui H, Cuff M, Joachimiak A, Savchenko A, Yakunin AF2010 Jul 220427268