Difference between revisions of "FruK"
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=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=2JG5 2JG5] (from ''Staphylococcus aureus'', 45% identity, 63% similarity) |
* '''UniProt:''' [http://www.uniprot.org/uniprot/O31714 O31714] | * '''UniProt:''' [http://www.uniprot.org/uniprot/O31714 O31714] | ||
Revision as of 13:20, 17 February 2010
- Description: fructose-1-phosphate kinase
| Gene name | fruK |
| Synonyms | fruB |
| Essential | no |
| Product | fructose-1-phosphate kinase |
| Function | fructose utilization |
| Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism | |
| MW, pI | 32 kDa, 4.885 |
| Gene length, protein length | 909 bp, 303 aa |
| Immediate neighbours | fruR, fruA |
| 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: BSU14390
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + D-fructose 1-phosphate = ADP + D-fructose 1,6-bisphosphate (according to Swiss-Prot)
- Protein family: carbohydrate kinase pfkB family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 2JG5 (from Staphylococcus aureus, 45% identity, 63% similarity)
- UniProt: O31714
- KEGG entry: [3]
- E.C. number: 2.7.1.56
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Jonathan Reizer, Steffi Bachem, Aiala Reizer, Maryvonne Arnaud, Milton H Saier, Jörg Stülke
Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis.
Microbiology (Reading): 1999, 145 ( Pt 12);3419-3429
[PubMed:10627040]
[WorldCat.org]
[DOI]
(P p)
