Difference between revisions of "MetA"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
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* '''[[Domains]]:'''  
  
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):'''
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* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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=Expression and regulation=
 
=Expression and regulation=
  
* '''Operon:''' ''metA'' (according to [http://dbtbs.hgc.jp/COG/prom/metA.html DBTBS])
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* '''Operon:''' ''[[metA]]-[[ugtP]]'' {{PubMed|22383849}}
  
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=metA_2305378_2306283_1 metA] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=metA_2305378_2306283_1 metA] {{PubMed|22383849}}
  
* '''Sigma factor:''' [[SigM]] [http://www.ncbi.nlm.nih.gov/sites/entrez/18179421 PubMed]
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* '''[[Sigma factor]]:''' [[SigM]] [http://www.ncbi.nlm.nih.gov/sites/entrez/18179421 PubMed]
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  

Revision as of 17:29, 14 December 2013

  • Description: homoserine O-succinyltransferase

Gene name metA
Synonyms metB
Essential no
Product homoserine O-succinyltransferase
Function biosynthesis of methionine
Gene expression levels in SubtiExpress: metA
Metabolic function and regulation of this protein in SubtiPathways:
Lys, Thr, Cys, Met & Sulfate assimilation
MW, pI 25 kDa, 6.414
Gene length, protein length 672 bp, 224 aa
Immediate neighbours bsaA, ugtP
Sequences Protein DNA DNA_with_flanks
Genetic context
MetA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MetA expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids cell envelope stress proteins (controlled by SigM, V, W, X, Y)

This gene is a member of the following regulons

SigM regulon

The gene

Basic information

  • Locus tag: BSU21910

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine (according to Swiss-Prot) O(4)-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure: 2GHR (from Bacillus cereus, 60% identity, 77% similarity) PubMed
  • KEGG entry: [3]

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

Warawan Eiamphungporn, John D Helmann
The Bacillus subtilis sigma(M) regulon and its contribution to cell envelope stress responses.
Mol Microbiol: 2008, 67(4);830-48
[PubMed:18179421] [WorldCat.org] [DOI] (P p)

Chloe Zubieta, S Sri Krishna, Daniel McMullan, Mitchell D Miller, Polat Abdubek, Sanjay Agarwalla, Eileen Ambing, Tamara Astakhova, Herbert L Axelrod, Dennis Carlton, Hsiu-Ju Chiu, Thomas Clayton, Marc Deller, Michael DiDonato, Lian Duan, Marc-André Elsliger, Slawomir K Grzechnik, Joanna Hale, Eric Hampton, Gye Won Han, Justin Haugen, Lukasz Jaroszewski, Kevin K Jin, Heath E Klock, Mark W Knuth, Eric Koesema, Abhinav Kumar, David Marciano, Andrew T Morse, Edward Nigoghossian, Silvya Oommachen, Ron Reyes, Christopher L Rife, Henry van den Bedem, Dana Weekes, Aprilfawn White, Qingping Xu, Keith O Hodgson, John Wooley, Ashley M Deacon, Adam Godzik, Scott A Lesley, Ian A Wilson
Crystal structure of homoserine O-succinyltransferase from Bacillus cereus at 2.4 A resolution.
Proteins: 2007, 68(4);999-1005
[PubMed:17546672] [WorldCat.org] [DOI] (I p)