function
biosynthesis of methionine
product
methionine synthase
Genomic Context
categories
[category|SW 2|Metabolism] → [category|SW 2.3|Amino acid/ nitrogen metabolism] → [category|SW 2.3.1|Biosynthesis/ acquisition of amino acids] → [category|SW 2.3.1.10|Biosynthesis/ acquisition of methionine/ S-adenosylmethionine][category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.8|Phosphorylation on either a Ser, Thr or Tyr residue][SW|Categories] containing this gene/protein
[SW|biosynthesis/ acquisition of amino acids], [SW|phosphoproteins], [SW|most abundant proteins]This gene is a member of the following [SW|regulons]
[SW|S-box]Gene
Coordinates on the chromosome (coding sequence)
1,383,320 -> 1,385,608
The protein
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)Modification
phosphorylated on ser/ thr/ tyr [Pubmed|17726680], S-cysteinylation after diamide stress (C719) [Pubmed|17611193]Cys719 and Cys730 are S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species [Pubmed|21749987] [Pubmed|22938038]MetE is generally most strongly S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species [Pubmed|21749987] [Pubmed|22938038]Structure
[PDB|1T7L] (from ''Thermotoga maritima'', 44% identity, 61% similarity) [Pubmed|15630480][SW|Interactions]
[protein|search|BrxA]-[protein|search|MetE], to de-bacillithiolate S-bacillithiolated [protein|search|MetE] [Pubmed|24313874][protein|search|BrxB]-[protein|search|MetE], to de-bacillithiolate S-bacillithiolated [protein|search|MetE] [Pubmed|24313874]Additional information
subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids= 17981983 PubMed]Expression and Regulation
Operon
''metERegulation
repressed by casamino acids [Pubmed|12107147]repressed by methionine (about 1000-fold)([protein|search|S-box]) [Pubmed|10094622]Regulatory mechanism
[protein|search|S-box]: transcription termination/ antitermination, the [protein|search|S-box] [SW|riboswitch] binds S-adenosylmethionine resulting in termination [Pubmed|10094622]Additional information
subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids= 17981983 PubMed]belongs to the 100 [SW|most abundant proteins] [PubMed|15378759]Biological materials
Mutant
1A607 ( ''metE''::''erm''), [Pubmed|3015878], available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A607&Search=1A607 BGSC]References
Reviews
Original Publications
21749987,22938038,21749987,19258532,16194229,10094622,17611193,18039762,17726680,12107147,24313874,24163341,15378759 
