Difference between revisions of "Pgm"
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=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' | + | * '''Structure:''' ''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] |
* '''Swiss prot entry:''' [http://www.expasy.ch/cgi-bin/sprot-search-ac?P39773] | * '''Swiss prot entry:''' [http://www.expasy.ch/cgi-bin/sprot-search-ac?P39773] | ||
Revision as of 16:50, 8 January 2009
- Description: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate
| Gene name | pgm |
| Synonyms | gpmI |
| Essential | yes |
| Product | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase |
| Function | isomerase |
| 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 File:GenE context.gif | |
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
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
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
- Additional information:
Biological materials
Labs working on this gene/protein
Jörg Stülke, University of Göttingen, Germany Homepage
Your additional remarks
References
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
