Difference between revisions of "SerA"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
{{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}}, | {{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}}, | ||
| − | {{SubtiWiki category|[[membrane proteins]]}} | + | {{SubtiWiki category|[[membrane proteins]]}}, |
| + | [[most abundant proteins]] | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
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** active site Cys410 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species {{PubMed|21749987}} {{PubMed|22938038}} | ** active site Cys410 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species {{PubMed|21749987}} {{PubMed|22938038}} | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=serA_2411086_2412663_1 serA] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=serA_2411086_2412663_1 serA] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
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* '''Additional information:''' | * '''Additional information:''' | ||
| + | ** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}} | ||
=Biological materials = | =Biological materials = | ||
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=References= | =References= | ||
| − | <pubmed>22938038,17611193,7934830 ,18763711,15823035 21749987 23033921</pubmed> | + | <pubmed>22938038,17611193,7934830 ,18763711,15823035 21749987 23033921 15378759</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 13:21, 5 March 2014
- Description: phosphoglycerate dehydrogenase
| Gene name | serA |
| Synonyms | |
| Essential | no |
| Product | phosphoglycerate dehydrogenase |
| Function | biosynthesis of serine |
| Gene expression levels in SubtiExpress: serA | |
| Metabolic function and regulation of this protein in SubtiPathways: serA | |
| MW, pI | 56 kDa, 5.617 |
| Gene length, protein length | 1575 bp, 525 aa |
| Immediate neighbours | ypzE, aroC |
| 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, membrane proteins, most abundant 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:
- Modification:
- 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:
- strongly repressed in response to glucose starvation in M9 medium PubMed
- Regulatory mechanism:
- Additional information:
- belongs to the 100 most abundant proteins PubMed
Biological materials
- Expression vector:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Imke G de Jong, Jan-Willem Veening, Oscar P Kuipers
Single cell analysis of gene expression patterns during carbon starvation in Bacillus subtilis reveals large phenotypic variation.
Environ Microbiol: 2012, 14(12);3110-21
[PubMed:23033921]
[WorldCat.org]
[DOI]
(I p)
Bui Khanh Chi, Alexandra A Roberts, Tran Thi Thanh Huyen, Katrin Bäsell, Dörte Becher, Dirk Albrecht, Chris J Hamilton, Haike Antelmann
S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in firmicutes bacteria.
Antioxid Redox Signal: 2013, 18(11);1273-95
[PubMed:22938038]
[WorldCat.org]
[DOI]
(I p)
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)
Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759]
[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)
