Difference between revisions of "Pgm"
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* '''Operon:''' | * '''Operon:''' | ||
** ''[[cggR]]-[[gapA]]-[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]'' | ** ''[[cggR]]-[[gapA]]-[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]'' | ||
| − | ** ''[[ | + | ** ''[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]'' |
* '''Sigma factor:''' [[SigA]] | * '''Sigma factor:''' [[SigA]] | ||
| − | * '''Regulation:''' neg. regulated by [[CggR]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+ | + | * '''Regulation:''' |
| + | ''[[cggR]]'': neg. regulated by [[CggR]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11489127 PubMed], induced by sugar | ||
| − | * '''Regulatory mechanism:''' | + | ''[[pgk]]'': constitutive [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11489127 PubMed] |
| + | |||
| + | * '''Regulatory mechanism:''' transcription repression by [[CggR]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11489127 PubMed] | ||
* '''Additional information:''' | * '''Additional information:''' | ||
Revision as of 17:39, 14 January 2009
- Description: phosphoglycerate mutase, glycolytic/ gluconeogenic enzyme
| Gene name | pgm |
| Synonyms | gpmI |
| Essential | yes |
| Product | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase |
| Function | enzyme in glycolysis/ gluconeogenesis |
| MW, pI | 56,1 kDa, 5.21 |
| Gene length, protein length | 1533 bp, 511 amino acids |
| Immediate neighbours | tpi, eno |
| Gene sequence (+200bp) | Protein sequence |
Genetic context 
| |
Contents
The gene
Basic information
- Coordinates: 3476911 - 3478443
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 2-phospho-D-glycerate = 3-phospho-D-glycerate
- Protein family: BPG-independent phosphoglycerate mutase family
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylation PubMed
- Cofactor(s): 2 manganese ions per subunit
- Effectors of protein activity:
- Interactions: Pgm-PfkA
- Localization: cytoplasm PubMed
Database entries
- Structure: Geobacillus stearothermophilus, complex with 2-phosphoglycerate NCBI, Geobacillus stearothermophilus, complex with 3-phosphoglycerate NCBI
- Swiss prot entry: [3]
- KEGG entry: [4]
- E.C. number: [5]
Additional information
is pH sensitive
Expression and regulation
- Sigma factor: SigA
- Regulation:
cggR: neg. regulated by CggR PubMed, induced by sugar
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- Antibody:
Labs working on this gene/protein
Jörg Stülke, University of Göttingen, Germany Homepage
Your additional remarks
References
- Jannière, L., Canceill, D., Suski, C., Kanga, S., Dalmais, B., Lestini, R., Monnier, A. F., Chapuis, J., Bolotin, A., Titok, M., Le Chatelier, E., and Ehrlich, S. D. (2007) Genetic evidence for a link between glycolysis and DNA replication. PLoS ONE 2, e447. PubMed
- Leyva-Vazquez, M. A., and Setlow, P. (1994) Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis. J Bacteriol 176: 3903-3910. PubMed
- Ludwig, H., Homuth, G., Schmalisch, M., Dyka, F. M., Hecker, M. & Stülke, J. (2001) Transcription of glycolytic genes and operons in Bacillus subtilis: Evidence for the presence of multiple levels of control of the gapA operon. Mol. Microbiol. 41: 409-422. PubMed
