Difference between revisions of "SucD"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
 
{{SubtiWiki category|[[ATP synthesis]]}},
 
{{SubtiWiki category|[[ATP synthesis]]}},
 
{{SubtiWiki category|[[carbon core metabolism]]}},
 
{{SubtiWiki category|[[carbon core metabolism]]}},
{{SubtiWiki category|[[phosphoproteins]]}}
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{{SubtiWiki category|[[phosphoproteins]]}},
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[[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===
 
 
 
  
 
=The protein=
 
=The protein=
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* '''Kinetic information:''' Reversible Michaelis-Menten [http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6T36-44C8RWC-SH&_user=5731894&_coverDate=01%2F01%2F1985&_rdoc=28&_fmt=high&_orig=browse&_srch=doc-info(%23toc%234938%231985%23998209998%23270526%23FLP%23display%23Volume)&_cdi=4938&_sort=d&_docanchor=&_ct=40&_acct=C000043105&_version=1&_urlVersion=0&_userid=5731894&md5=f14f4734123ab1177d7217cab6c7ce7d FEBS Letters]  
 
* '''Kinetic information:''' Reversible Michaelis-Menten [http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6T36-44C8RWC-SH&_user=5731894&_coverDate=01%2F01%2F1985&_rdoc=28&_fmt=high&_orig=browse&_srch=doc-info(%23toc%234938%231985%23998209998%23270526%23FLP%23display%23Volume)&_cdi=4938&_sort=d&_docanchor=&_ct=40&_acct=C000043105&_version=1&_urlVersion=0&_userid=5731894&md5=f14f4734123ab1177d7217cab6c7ce7d FEBS Letters]  
  
* '''Domains:'''  
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* '''[[Domains]]:'''  
  
 
* '''Modification:''' phosphorylation on (Ser-19 OR Thr-20) [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed]
 
* '''Modification:''' phosphorylation on (Ser-19 OR Thr-20) [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed]
  
* '''Cofactor(s):'''
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* '''[[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=sucD_1681617_1682519_1 sucD] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sucD_1681617_1682519_1 sucD] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
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* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:''' repressed by glucose (2.4-fold) ([[CcpA]]) {{PubMed|12850135}}   
 
* '''Regulation:''' repressed by glucose (2.4-fold) ([[CcpA]]) {{PubMed|12850135}}   
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* '''Additional information:'''
 
* '''Additional information:'''
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** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
  
 
=Biological materials =
 
=Biological materials =
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=References=
 
=References=
  
<pubmed>12850135 17218307 11976317 20933603</pubmed>
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<pubmed>12850135 17218307 11976317 20933603 15378759</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:15, 5 March 2014

  • Description: succinyl-CoA synthetase (alpha subunit)

Gene name sucD
Synonyms
Essential no
Product succinyl-CoA synthetase (alpha subunit)
Function TCA cycle
Gene expression levels in SubtiExpress: sucD
Interactions involving this protein in SubtInteract: SucD
Metabolic function and regulation of this protein in SubtiPathways:
sucD
MW, pI 31 kDa, 5.587
Gene length, protein length 900 bp, 300 aa
Immediate neighbours sucC, dprA
Sequences Protein DNA DNA_with_flanks
Genetic context
SucD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SucD expression.png















Categories containing this gene/protein

ATP synthesis, carbon core metabolism, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

CcpA regulon

The gene

Basic information

  • Locus tag: BSU16100

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + succinate + CoA = ADP + phosphate + succinyl-CoA (according to Swiss-Prot)
  • Protein family: succinate/malate CoA ligase alpha subunit family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: Reversible Michaelis-Menten FEBS Letters
  • Modification: phosphorylation on (Ser-19 OR Thr-20) PubMed
  • Effectors of protein activity:

Database entries

  • Structure: 1JKJ (E. coli)
  • KEGG entry: [3]

Additional information

  • extensive information on the structure and enzymatic properties of succinyl-CoA synthetase can be found at Proteopedia

Expression and regulation

  • Regulation: repressed by glucose (2.4-fold) (CcpA) PubMed
  • Regulatory mechanism: CcpA: transcription repression PubMed

Biological materials

  • Expression vector:
  • lacZ fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Frederik M Meyer, Jan Gerwig, Elke Hammer, Christina Herzberg, Fabian M Commichau, Uwe Völker, Jörg Stülke
Physical interactions between tricarboxylic acid cycle enzymes in Bacillus subtilis: evidence for a metabolon.
Metab Eng: 2011, 13(1);18-27
[PubMed:20933603] [WorldCat.org] [DOI] (I p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [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)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

Ciarán Condon, Jordi Rourera, Dominique Brechemier-Baey, Harald Putzer
Ribonuclease M5 has few, if any, mRNA substrates in Bacillus subtilis.
J Bacteriol: 2002, 184(10);2845-9
[PubMed:11976317] [WorldCat.org] [DOI] (P p)