Difference between revisions of "MetA"

From SubtiWiki
Jump to: navigation, search
Line 16: Line 16:
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU21910 metA]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU21910 metA]
 
|-
 
|-
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/lys_threo.html Lys, Thr], [http://subtiwiki.uni-goettingen.de/pathways/cys_meth_and_sulfate_assimilation.html Cys, Met & Sulfate assimilation]'''
+
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=metA metA]'''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 25 kDa, 6.414   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 25 kDa, 6.414   

Revision as of 11:02, 7 January 2014

  • 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:
metA
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)