Difference between revisions of "SerA"
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* '''Domains:''' | * '''Domains:''' | ||
− | * '''Modification:''' S-cysteinylation after diamide stress (C410)[http://www.ncbi.nlm.nih.gov/sites/entrez/17611193 PubMed] | + | * '''Modification:''' |
+ | ** S-cysteinylation after diamide stress (C410)[http://www.ncbi.nlm.nih.gov/sites/entrez/17611193 PubMed] | ||
+ | ** S-bacillithiolation upon hypochlorite stress on Cys-410 {{PubMed|21749987}} | ||
* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
Line 81: | Line 83: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
* '''Localization:''' membrane [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] | * '''Localization:''' membrane [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] | ||
Line 129: | Line 131: | ||
=References= | =References= | ||
− | <pubmed>17611193,7934830 ,18763711,15823035 | + | <pubmed>17611193,7934830 ,18763711,15823035 21749987 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 08:27, 14 July 2011
- Description: phosphoglycerate dehydrogenase
Gene name | serA |
Synonyms | |
Essential | no |
Product | phosphoglycerate dehydrogenase |
Function | biosynthesis of serine |
Metabolic function and regulation of this protein in SubtiPathways: Ala, Gly, Ser | |
MW, pI | 56 kDa, 5.617 |
Gene length, protein length | 1575 bp, 525 aa |
Immediate neighbours | ypzE, aroC |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU23070
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 3-phospho-D-glycerate + NAD+ = 3-phosphonooxypyruvate + NADH (according to Swiss-Prot)
- Protein family: D-isomer specific 2-hydroxyacid dehydrogenase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: membrane PubMed
Database entries
- UniProt: P35136
- KEGG entry: [3]
- E.C. number: 1.1.1.95
Additional information
Expression and regulation
- Operon: serA PubMed
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Bui Khanh Chi, Katrin Gronau, Ulrike Mäder, Bernd Hessling, Dörte Becher, Haike Antelmann
S-bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics.
Mol Cell Proteomics: 2011, 10(11);M111.009506
[PubMed:21749987]
[WorldCat.org]
[DOI]
(I p)
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I 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)
James R Thompson, Jessica K Bell, Judy Bratt, Gregory A Grant, Leonard J Banaszak
Vmax regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase.
Biochemistry: 2005, 44(15);5763-73
[PubMed:15823035]
[WorldCat.org]
[DOI]
(P p)
V Azevedo, A Sorokin, S D Ehrlich, P Serror
The transcriptional organization of the Bacillus subtilis 168 chromosome region between the spoVAF and serA genetic loci.
Mol Microbiol: 1993, 10(2);397-405
[PubMed:7934830]
[WorldCat.org]
[DOI]
(P p)