Difference between revisions of "MenD"
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=== Database entries === | === Database entries === | ||
− | * '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId= | + | * '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=2X7J 2X7J] {{PubMed|20600129}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P23970 P23970] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P23970 P23970] |
Revision as of 13:37, 24 August 2010
- Description: 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase / 2-oxoglutarate decarboxylase
Gene name | menD |
Synonyms | |
Essential | yes PubMed |
Product | 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase / 2-oxoglutarate decarboxylase |
Function | biosynthesis of menaquinone |
Metabolic function and regulation of this protein in SubtiPathways: Menaquinone | |
MW, pI | 63 kDa, 5.655 |
Gene length, protein length | 1740 bp, 580 aa |
Immediate neighbours | ytxM, menF |
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: BSU30820
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: Isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2 (according to Swiss-Prot)
- Protein family: MenD subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s): thiamine pyrophosphate, divalent metal ion such as Mn(2+)) PubMed
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- UniProt: P23970
- KEGG entry: [3]
- E.C. number: 2.2.1.9
Additional information
Expression and regulation
- 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
Alice Dawson, Minjiao Chen, Paul K Fyfe, Zhihong Guo, William N Hunter
Structure and reactivity of Bacillus subtilis MenD catalyzing the first committed step in menaquinone biosynthesis.
J Mol Biol: 2010, 401(2);253-64
[PubMed:20600129]
[WorldCat.org]
[DOI]
(I p)
Alia Lapidus, Nathalie Galleron, Alexei Sorokin, S Dusko Ehrlich
Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region.
Microbiology (Reading): 1997, 143 ( Pt 11);3431-3441
[PubMed:9387221]
[WorldCat.org]
[DOI]
(P p)
X Qin, H W Taber
Transcriptional regulation of the Bacillus subtilis menp1 promoter.
J Bacteriol: 1996, 178(3);705-13
[PubMed:8550504]
[WorldCat.org]
[DOI]
(P p)
J R Driscoll, H W Taber
Sequence organization and regulation of the Bacillus subtilis menBE operon.
J Bacteriol: 1992, 174(15);5063-71
[PubMed:1629163]
[WorldCat.org]
[DOI]
(P p)