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:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
− | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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=Expression and regulation= | =Expression and regulation= | ||
− | * '''Operon:''' ''metA'' | + | * '''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] | + | * '''[[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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
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
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
- UniProt: P54167
- KEGG entry: [3]
- E.C. number: 2.3.1.46 8 2.5.1.48]
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)