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  Domain Name: Phosphoglycerate_kin
Phosphoglycerate kinase (PGK) is a monomeric enzyme which catalyzes the transfer of the high-energy phosphate group of 1,3-bisphosphoglycerate to ADP, forming ATP and 3-phosphoglycerate. This reaction represents the first of the two substrate-level phosphorylation events in the glycolytic pathway. Substrate-level phosphorylation is defined as production of ATP by a process, which is catalyzed by water-soluble enzymes in the cytosol; not involving membranes and ion gradients.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 14
Total Disease Mutations Found: 13
This domain occurred 2 times on human genes (2 proteins).



  PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, AFULA
  PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, AMIENS
  PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, BARCELONA
  PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, HAMAMATSU
  PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, HERLEV
  PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, MATSUE
  PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, MICHIGAN
  PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, MUNCHEN
  PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, MURCIA
  PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, SHIZUOKA
  PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, TOKYO
  PHOSPHOGLYCERATE KINASE 1 DEFICIENCY, UPPSALA
  PHOSPHOGLYCERATE KINASE 1, PGK II


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Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
substrate binding site
catalytic site
ADP binding site
hinge regions





















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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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