Difference between revisions of "GuaB"

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|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''guaA ''
 
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''guaA ''
 
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|style="background:#ABCDEF;" align="center"| '''Essential''' ||  
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|style="background:#ABCDEF;" align="center"| '''Essential''' || yes [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
 
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|style="background:#ABCDEF;" align="center"| '''Product''' || inosine-monophosphate dehydrogenase (EC 1.1.1.205)
 
|style="background:#ABCDEF;" align="center"| '''Product''' || inosine-monophosphate dehydrogenase (EC 1.1.1.205)

Revision as of 15:46, 11 February 2009

  • Description: inosine-monophosphate dehydrogenase

Gene name guaB
Synonyms guaA
Essential yes PubMed
Product inosine-monophosphate dehydrogenase (EC 1.1.1.205)
Function
MW, pI 52 kDa, 6.168
Gene length, protein length 1464 bp, 488 aa
Immediate neighbours
Gene sequence (+200bp) Protein sequence
Genetic context
GuaB context.gif



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:
  • Modification: phosphorylated (STY) PubMed, S-cysteinlyation after diamide stress (Cys-308) PubMed
  • 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

  1. Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
  2. 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