Phosphoglycerate kinase

Phosphoglycerate kinase
Identifiers
EC no.2.7.2.3
CAS no.9001-83-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Phosphoglycerate kinase
Structure of yeast phosphoglycerate kinase.
Identifiers
SymbolPGK
PfamPF00162
InterProIPR001576
PROSITEPDOC00102
SCOP23pgk / SCOPe / SUPFAM
Available protein structures:
PDB  IPR001576 PF00162 (ECOD; PDBsum)  
AlphaFold

Phosphoglycerate kinase (EC 2.7.2.3) (PGK 1) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglyceric acid (1,3-BPG) to adenosine diphosphate (ADP) producing 3-phosphoglyceric acid (3-PG) and adenosine triphosphate (ATP):

Like all kinases it is a transferase. PGK is a major enzyme used in glycolysis, in the first ATP-generating step of the glycolytic pathway. In gluconeogenesis, the reaction catalyzed by PGK proceeds in the opposite direction, generating ADP and 1,3-BPG.

In humans, two isozymes of PGK have been so far identified, PGK1 and PGK2. The isozymes have 87-88% identical amino acid sequence identity and though they are structurally and functionally similar, they have different localizations: PGK2, encoded by an autosomal gene, is unique to meiotic and postmeiotic spermatogenic cells, while PGK1, encoded on the X-chromosome, is ubiquitously expressed in all cells.