MetE

• Description: methionine synthase
  
  

Gene name	metE
Synonyms	metC
Essential	no
Product	methionine synthase
Function	biosynthesis of methionine
Metabolic function and regulation of this protein in SubtiPathways: Cys, Met & Sulfate assimilation
MW, pI	86 kDa, 4.839
Gene length, protein length	2286 bp, 762 aa
Immediate neighbours	guaD, ispA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU13180

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine (according to Swiss-Prot)

• Protein family: vitamin-B12 independent methionine synthase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylated on ser/ thr/ tyr PubMed, S-cysteinylation after diamide stress (C719) PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 1T7L (from Thermotoga maritima, 44% identity, 61% similarity) PubMed

• UniProt: P80877

• KEGG entry: [2]

• E.C. number: 2.1.1.14

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

• Operon: metE

• Sigma factor:

• Regulation:
  • repressed by casamino acids PubMed
  • repressed by methionine (about 1000-fold)(S-box) PubMed

• Regulatory mechanism: S-box: transcription termination/ antitermination, the S-box riboswitch binds S-adenosylmethionine resulting in termination PubMed

• Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Ana Gutiérrez-Preciado, Tina M Henkin, Frank J Grundy, Charles Yanofsky, Enrique Merino
Biochemical features and functional implications of the RNA-based T-box regulatory mechanism.
Microbiol Mol Biol Rev: 2009, 73(1);36-61
[PubMed:19258532] [WorldCat.org] [DOI] (I p)

Jerneja Tomsic, Brooke A McDaniel, Frank J Grundy, Tina M Henkin
Natural variability in S-adenosylmethionine (SAM)-dependent riboswitches: S-box elements in bacillus subtilis exhibit differential sensitivity to SAM In vivo and in vitro.
J Bacteriol: 2008, 190(3);823-33
[PubMed:18039762] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Falko Hochgräfe, Jörg Mostertz, Dierk-Christoph Pöther, Dörte Becher, John D Helmann, Michael Hecker
S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress.
J Biol Chem: 2007, 282(36);25981-5
[PubMed:17611193] [WorldCat.org] [DOI] (P p)

Falko Hochgräfe, Jörg Mostertz, Dirk Albrecht, Michael Hecker
Fluorescence thiol modification assay: oxidatively modified proteins in Bacillus subtilis.
Mol Microbiol: 2005, 58(2);409-25
[PubMed:16194229] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)

F J Grundy, T M Henkin
The S box regulon: a new global transcription termination control system for methionine and cysteine biosynthesis genes in gram-positive bacteria.
Mol Microbiol: 1998, 30(4);737-49
[PubMed:10094622] [WorldCat.org] [DOI] (P p)