Difference between revisions of "Pgm"
Cadu Cunha (talk | contribs) (→Database entries) |
Cadu Cunha (talk | contribs) (→Extended information on the protein) |
||
| Line 62: | Line 62: | ||
=== Extended information on the protein === | === Extended information on the protein === | ||
| − | * '''Kinetic information:''' | + | * '''Kinetic information:''' Reversible Michaelis-Menten [http://www.ncbi.nlm.nih.gov/pubmed/33963 PubMed] |
* '''Domains:''' | * '''Domains:''' | ||
| Line 68: | Line 68: | ||
* '''Modification:''' phosphorylation on Ser-62 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed] | * '''Modification:''' phosphorylation on Ser-62 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed] | ||
| − | * '''Cofactor(s):''' | + | * '''Cofactor(s):''' Mn2+ |
| − | * '''Effectors of protein activity:''' | + | * '''Effectors of protein activity:''' |
| + | ** Inhibited by diverse divalent heavy-metal ions and 2,3-butanedione [http://www.ncbi.nlm.nih.gov/sites/entrez/33963 PubMed] | ||
| + | ** 2,3-Diphosphoglycerate has NO role on this enzyme regulation [http://www.ncbi.nlm.nih.gov/sites/entrez/33963 PubMed] | ||
* '''Interactions:''' Pgm-[[PfkA]] | * '''Interactions:''' Pgm-[[PfkA]] | ||
Revision as of 13:01, 10 June 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 |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Locus tag: BSU33910
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 (according to Swiss-Prot)
- Protein family: BPG-independent phosphoglycerate mutase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information: Reversible Michaelis-Menten PubMed
- Domains:
- Cofactor(s): Mn2+
- Effectors of protein activity:
- Interactions: Pgm-PfkA
- Localization: Cytoplasm (Homogeneous) PubMed
Database entries
- Structure: 1EJJ (Geobacillus stearothermophilus, complex with 3-phosphoglycerate), 1EQJ (Geobacillus stearothermophilus, complex with 2-phosphoglycerate), Geobacillus stearothermophilus, complex with 2-phosphoglycerate NCBI, Geobacillus stearothermophilus, complex with 3-phosphoglycerate NCBI
- Swiss prot entry: [3]
- KEGG entry: [4]
- E.C. number: 5.4.2.1]
Additional information
is pH sensitive
Expression and regulation
- Sigma factor: SigA
- Regulation: expression activated by glucose (7.3 fold) PubMed
cggR: neg. regulated by CggR PubMed, induced by sugar
- Additional information:
Biological materials
- Mutant:
- Expression vector: pGP1101 (N-terminal His-tag, in pWH844), pGP396 (Pgm-S62A, N-terminal His-tag, in pWH844), pGP92 (N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380), available in Stülke lab
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody:
Labs working on this gene/protein
Jörg Stülke, University of Göttingen, Germany Homepage
Mark J. Jedrzejas, Research Center Oakland, CA, USA Homepage
Your additional remarks
References
