Difference between revisions of "GuaB"
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* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
− | * '''Additional information:''' | + | * '''Additional information:''' the mRNA is very stable (half-life > 15 min) [http://www.ncbi.nlm.nih.gov/sites/entrez/12884008 PubMed] |
=Biological materials = | =Biological materials = |
Revision as of 09:07, 26 May 2009
- Description: IMP dehydrogenase
Gene name | guaB |
Synonyms | guaA |
Essential | yes PubMed |
Product | IMP dehydrogenase |
Function | biosynthesis of GMP |
MW, pI | 52 kDa, 6.168 |
Gene length, protein length | 1464 bp, 488 aa |
Immediate neighbours | yaaC, dacA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
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Contents
The gene
Basic information
- Coordinates:
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: Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH (according to Swiss-Prot)
- Protein family: IMPDH/GMPR family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylated (STY) PubMed, S-cysteinlyation after diamide stress (Cys-308) PubMed, PubMed
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- Swiss prot entry: P21879
- KEGG entry: BSU00090
- E.C. number: 1.1.1.205
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information: the mRNA is very stable (half-life > 15 min) PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
- Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
- Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
- Hochgräfe et al. (2007) S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress. J. Biol. Chem. 282: 25981-25985. PubMed