Difference between revisions of "AlsS"
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=== Basic information === | === Basic information === | ||
− | * ''' | + | * '''Locus tag:''' |
===Phenotypes of a mutant === | ===Phenotypes of a mutant === |
Revision as of 10:40, 2 June 2009
- Description: acetolactate synthase
Gene name | alsS |
Synonyms | |
Essential | no |
Product | acetolactate synthase) |
Function | overflow metabolism |
MW, pI | 61 kDa, 5.164 |
Gene length, protein length | 1713 bp, 571 aa |
Immediate neighbours | alsD, alsR |
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:
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 2 pyruvate = 2-acetolactate + CO2 (according to Swiss-Prot)
- Protein family: TPP enzyme 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:
- Swiss prot entry: Q04789
- KEGG entry: BSU36010
- E.C. number: 2.2.1.6
Additional information
Expression and regulation
- Regulation: induction by acetate (AlsR) PubMed, repressed as long as terminal electron acceptors are available for respiration (Rex) PubMed
Note: since acetate formation requires ackA activation by CcpA there is an indirect effect of CcpA on the alsSD operon: the operon is not expressed in ccpA mutants
- Regulatory mechanism: AlsR: transcription activation in the presence of acetate PubMed, Rex: transcription repression if the ratio NADH2/NAD is high PubMed
- 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
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed