PanB

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  • Description: 3-methyl-2-oxobutanoate hydroxymethyltransferase

Gene name panB
Synonyms
Essential no
Product 3-methyl-2-oxobutanoate hydroxymethyltransferase
Function biosynthesis of coenzyme A
Gene expression levels in SubtiExpress: panB
Metabolic function and regulation of this protein in SubtiPathways:
Coenzyme A
MW, pI 29 kDa, 5.282
Gene length, protein length 831 bp, 277 aa
Immediate neighbours panC, birA
Sequences Protein DNA DNA_with_flanks
Genetic context
PanB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PanB expression.png




























Categories containing this gene/protein

biosynthesis of cofactors

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU22430

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 3EZ4 (from Burkholderia pseudomallei, 44% identity, 64% similarity)
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Regulation:
    • induced upon fatty acid biosynthesis inhibition PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Michaela Wenzel, Malay Patra, Dirk Albrecht, David Y-K Chen, K C Nicolaou, Nils Metzler-Nolte, Julia E Bandow
Proteomic signature of fatty acid biosynthesis inhibition available for in vivo mechanism-of-action studies.
Antimicrob Agents Chemother: 2011, 55(6);2590-6
[PubMed:21383089] [WorldCat.org] [DOI] (I p)