Difference between revisions of "Pgk"
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* '''Domains:''' | * '''Domains:''' | ||
| + | ** nucleotide binding domain (ATP) (350–353) | ||
| + | ** 2x substrate binding domain (21–23), (59–62) | ||
| + | |||
| + | |||
* '''Modification:''' phosphorylation [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], | * '''Modification:''' phosphorylation [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], | ||
Revision as of 14:39, 8 January 2009
- Description: catalyzes the reaktion of 1,3-phosphoglycerate to 3-Phosphoglycerate by phosphorylation of ADP and the reverse reaktion
| Gene name | pgk |
| Synonyms | |
| Essential | yes |
| Product | Phosphoglycerate kinase |
| Function | phosphorylation |
| MW, pI | 42,0 kDa, 4.77 |
| Gene length, protein length | 1182 bp, 394 amino acids |
| Immediate neighbours | gapA, tpi |
| 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: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
- Protein family: phosphoglycerate kinase family
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- nucleotide binding domain (ATP) (350–353)
- 2x substrate binding domain (21–23), (59–62)
- Modification: phosphorylation PubMed,
- Cofactor(s):
- Effectors of protein activity:
- Interactions: Pgk-GapA
- Localization: Cytoplasm PubMed
Database entries
- Structure: Geobacillus stearothermophilus NCBI
- Swiss prot entry: [3]
- KEGG entry: [4]
- E.C. number: [5]
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
Labs working on this gene/protein
Your additional remarks
References
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed