YngG

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  • Description: 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) lyase

Gene name yngG
Synonyms
Essential no
Product 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) lyase
Function biosynthesis of ketone bodies
MW, pI 32 kDa, 5.753
Gene length, protein length 897 bp, 299 aa
Immediate neighbours yngF, yngH
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YngG context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU18230

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: (S)-3-hydroxy-3-methylglutaryl-CoA = acetyl-CoA + acetoacetate (according to Swiss-Prot)
  • Protein family: HMG-CoA lyase 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

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Operon:
  • 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

Raghavendra Joshi, Brian B McSpadden Gardener
Identification and Characterization of Novel Genetic Markers Associated with Biological Control Activities in Bacillus subtilis.
Phytopathology: 2006, 96(2);145-54
[PubMed:18943917] [WorldCat.org] [DOI] (P p)

Farhad Forouhar, Munif Hussain, Ramy Farid, Jordi Benach, Mariam Abashidze, William C Edstrom, Sergey M Vorobiev, Rong Xiao, Thomas B Acton, Zhuji Fu, Jung-Ja P Kim, Henry M Miziorko, Gaetano T Montelione, John F Hunt
Crystal structures of two bacterial 3-hydroxy-3-methylglutaryl-CoA lyases suggest a common catalytic mechanism among a family of TIM barrel metalloenzymes cleaving carbon-carbon bonds.
J Biol Chem: 2006, 281(11);7533-45
[PubMed:16330546] [WorldCat.org] [DOI] (P p)