phosphoglycerate mutase, glycolytic / gluconeogenic enzyme
function
enzyme in glycolysis / gluconeogenesis
product
2,3-bisphosphoglycerate-independent
phosphoglycerate mutase
Genomic Context
categories
[category|SW 2|Metabolism] → [category|SW 2.2|Carbon metabolism] → [category|SW 2.2.1|Carbon core metabolism] → [category|SW 2.2.1.1|Glycolysis][category|SW 2|Metabolism] → [category|SW 2.2|Carbon metabolism] → [category|SW 2.2.1|Carbon core metabolism] → [category|SW 2.2.1.2|Gluconeogenesis][category|SW 6|Groups of genes] → [category|SW 6.1|Essential genes][category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.5|Phosphorylation on a Ser residue][SW|Categories] containing this gene/protein
[SW|carbon core metabolism], [SW|essential genes], [SW|phosphoproteins]This gene is a member of the following [SW|regulons]
[SW|CggR regulon]Gene
Phenotypes of a mutant
Essential [Pubmed|12682299]The protein
Catalyzed reaction/ biological activity
2-phospho-D-glycerate = 3-phospho-D-glycerate (according to Swiss-Prot)Protein family
BPG-independent phosphoglycerate mutase family (according to Swiss-Prot)Kinetic information
Reversible Michaelis-Menten [Pubmed|33963]Modification
phosphorylation on Ser-62 [Pubmed|17218307], [Pubmed|17726680][SW|Cofactors]
Mn2+Effectors of protein activity
Inhibited by diverse divalent heavy-metal ions, EDTA and 2,3-butanedione [Pubmed|33963]2,3-Diphosphoglycerate has NO role on this enzyme regulation [Pubmed|33963]Structure
[PDB|1EJJ] (Geobacillus stearothermophilus, complex with 3-phosphoglycerate), [PDB|1EQJ] (Geobacillus stearothermophilus, complex with 2-phosphoglycerate), ''Geobacillus stearothermophilus'', complex with 2-phosphoglycerate [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=16359 NCBI], ''Geobacillus stearothermophilus'', complex with 3-phosphoglycerate [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=15578 NCBI][SW|Localization]
Cytoplasm (Homogeneous) [Pubmed|16479537][SW|Interactions]
Pgm-[protein|search|PfkA]Additional information
extensive information on the structure and enzymatic properties of Pgm can be found at [http://www.proteopedia.org/wiki/index.php/Phosphoglycerate_Mutase Proteopedia]Expression and Regulation
Operon
''[protein|search|cggR]-[protein|search|gapA]-[protein|search|pgk]-[protein|search|tpiA]-[protein|search|pgm]-[protein|search|eno]'' [Pubmed|11489127]''[protein|search|pgk]-[protein|search|tpiA]-[protein|search|pgm]-[protein|search|eno]'' [Pubmed|11489127][SW|Sigma factor]
[protein|search|SigA] [Pubmed|11489127]Regulation
expression activated by glucose (3.3 fold) [Pubmed|12850135]''[protein|search|cggR]'': induced by glycolytic substrates [protein|search|CggR] [Pubmed|11489127]''[protein|search|pgk]'': constitutive [Pubmed|11489127]Regulatory mechanism
transcription repression by [protein|search|CggR] [Pubmed|11489127]Biological materials
Mutant
GP593 (''pgm''::''cat''), available in [SW|Jörg Stülke]'s lab, [Pubmed|23420519]GP598 (''pgm''::''erm''), available in [SW|Jörg Stülke]'s lab, [Pubmed|23420519]GP698 (''pgm''-''eno''::cat), available in [SW|Jörg Stülke]'s lab, [Pubmed|23420519]Expression vector
pGP1425 (expression of ''pgm'' in ''B. subtilis'', in [SW|pBQ200]), available in [SW|Jörg Stülke]'s labpGP1500 (expression of ''pgm'' and ''eno'' in ''B. subtilis'', in [SW|pBQ200]), available in [SW|Jörg Stülke]'s labpGP1101 (N-terminal His-tag, in [SW|pWH844]), available in [SW|Jörg Stülke]'s labpGP396 (Pgm-S62A, N-terminal His-tag, in [SW|pWH844]), available in [SW|Jörg Stülke]'s labpGP92 (N-terminal Strep-tag, for [SW|SPINE], expression in B. subtilis, in [SW|pGP380]), available in [SW|Jörg Stülke]'s labtwo-hybrid system
''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW|Jörg Stülke]'s labLabs working on this gene/protein
[SW|Jörg Stülke], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage][Jedrzejas|search|Mark J. Jedrzejas], Research Center Oakland, CA, USA [http://www.chori.org/Principal_Investigators/Jedrzejas_Mark_J/jedrzejas_research.html Homepage]References
11514674,17085493,10764795,8215434,10747010,11712498,9830105,10388626,8636019,11827481,16479537,12850135,17726680,17505547,8021172,11489127,10388626,10747010,10764795,11712498,12729763,17085493,17218307,33963,23420519