Difference between revisions of "YngG"
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Revision as of 11:02, 21 July 2009
- 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 
This image was kindly provided by SubtiList
| |
Contents
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
- Structure: 1YDO
- UniProt: O34873
- KEGG entry: [3]
- E.C. number: 4.1.3.4
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)
