Difference between revisions of "GuaB"
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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1464 bp, 488 aa | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1464 bp, 488 aa | ||
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− | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yaaC]]'', ''[[dacA]]'' |
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|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/guaB_nucleotide.txt Gene sequence (+200bp) ]''' | |style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/guaB_nucleotide.txt Gene sequence (+200bp) ]''' |
Revision as of 13:38, 20 February 2009
- Description: inosine-monophosphate dehydrogenase
Gene name | guaB |
Synonyms | guaA |
Essential | yes PubMed |
Product | inosine-monophosphate dehydrogenase (EC 1.1.1.205) |
Function | purine metabolism |
MW, pI | 52 kDa, 6.168 |
Gene length, protein length | 1464 bp, 488 aa |
Immediate neighbours | yaaC, dacA |
Gene sequence (+200bp) | Protein sequence |
Genetic context |
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:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- Swiss prot entry:
- KEGG entry:
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- 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
- 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