pgm
168
phosphoglycerate mutase, glycolytic / gluconeogenic enzyme
Locus
BSU_33910
Molecular weight
56.14 kDa
Isoelectric point
5.21
Function
enzyme in glycolysis / gluconeogenesis
Product
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Essential
Yes
E.C.
5.4.2.1
Synonyms
pgm, gpmI
Outlinks
Genomic Context
Categories containing this gene/protein
List of homologs in different organisms, belongs to COG0696 (Galperin et al., 2021)
This gene is a member of the following regulons
Gene
The protein
Catalyzed reaction/ biological activity
(2R)-2-phosphoglycerate --> 3-phosphoglycerate (according to UniProt)
Protein family
BPG-independent phosphoglycerate mutase family (single member, according to UniProt)
Mn2+
Structure
1EJJ (PDB) (Geobacillus stearothermophilus, complex with 3-phosphoglycerate), 1EQJ (PDB) (Geobacillus stearothermophilus, complex with 2-phosphoglycerate), Geobacillus stearothermophilus, complex with 2-phosphoglycerate NCBI, Geobacillus stearothermophilus, complex with 3-phosphoglycerate NCBI
Modification
Effectors of protein activity
Inhibited by diverse divalent heavy-metal ions, EDTA and 2,3-butanedione PubMed
2,3-Diphosphoglycerate has NO role on this enzyme regulation PubMed
Kinetic information
Reversible Michaelis-Menten PubMed
Cytoplasm (Homogeneous) PubMed
Additional information
extensive information on the structure and enzymatic properties of Pgm can be found at Proteopedia
Expression and Regulation
Operons
Biological materials
Mutant
Expression vectors
Two-hybrid system
Labs working on this gene/protein
Mark J. Jedrzejas, Research Center Oakland, CA, USA Homepage
References
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Time of last update: 2025-04-01 20:01:49
Author of last update: Jstuelk