Difference between revisions of "Pgm"
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|style="background:#ABCDEF;" align="center"|'''Function''' || enzyme in glycolysis / gluconeogenesis | |style="background:#ABCDEF;" align="center"|'''Function''' || enzyme in glycolysis / gluconeogenesis | ||
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+ | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/Pgm Pgm] | ||
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]''' |
Revision as of 13:23, 28 July 2011
- 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 |
Interactions involving this protein in SubtInteract: Pgm | |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 56,1 kDa, 5.21 |
Gene length, protein length | 1533 bp, 511 amino acids |
Immediate neighbours | eno, tpi |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
carbon core metabolism, phosphoproteins
This gene is a member of the following regulons
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
- UniProt: P39773
- KEGG entry: [3]
- E.C. number: 5.4.2.1]
Additional information
- extensive information on the structure and enzymatic properties of Pgm can be found at Proteopedia
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- pGP1425 (expression of pgm in B. subtilis, in pBQ200), available in Stülke lab
- pGP1500 (expression of pgm and eno in B. subtilis, in pBQ200), available in Stülke lab
- pGP1101 (N-terminal His-tag, in pWH844), available in Stülke lab
- pGP396 (Pgm-S62A, N-terminal His-tag, in pWH844), available in Stülke lab
- 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