Difference between revisions of "CitG"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 2427 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 2427 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 9880 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 9880 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 7597 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 4282 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 4666 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''  
 
* '''Mutant:'''  
 
** GP718 (spec), available in [[Jörg Stülke]]'s lab
 
** GP718 (spec), available in [[Jörg Stülke]]'s lab

Revision as of 14:04, 17 April 2014

  • Description: fumarase

Gene name citG
Synonyms
Essential no
Product fumarate hydratase
Function TCA cycle
Gene expression levels in SubtiExpress: citG
Interactions involving this protein in SubtInteract: CitG
Metabolic function and regulation of this protein in SubtiPathways:
citG
MW, pI 50 kDa, 5.475
Gene length, protein length 1386 bp, 462 aa
Immediate neighbours yuxN, yvzF
Sequences Protein DNA DNA_with_flanks
Genetic context
CitG context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CitG expression.png















Categories containing this gene/protein

carbon core metabolism, most abundant proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU33040

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: (S)-malate = fumarate + H2O (according to Swiss-Prot)
  • Protein family: Fumarase subfamily (according to Swiss-Prot)
  • Paralogous protein(s): AnsB

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure: 3R6Q (aspartase from Bacillus sp. YM55-1, 43% identity, 77% similarity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: constitutive
  • Regulatory mechanism:
  • Additional information:
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 2427 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 9880 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 7597 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 4282 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 4666 PubMed

Biological materials

  • Expression vector:
  • GFP fusion: GP1433 (spc, based on pGP1870), available in the Stülke lab
  • 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

Guntur Fibriansah, Vinod Puthan Veetil, Gerrit J Poelarends, Andy-Mark W H Thunnissen
Structural basis for the catalytic mechanism of aspartate ammonia lyase.
Biochemistry: 2011, 50(27);6053-62
[PubMed:21661762] [WorldCat.org] [DOI] (I p)

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)

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 A Price, I M Feavers, A Moir
Role of sigma H in expression of the fumarase gene (citG) in vegetative cells of Bacillus subtilis 168.
J Bacteriol: 1989, 171(11);5933-9
[PubMed:2509423] [WorldCat.org] [DOI] (P p)

K M Tatti, H L Carter, A Moir, C P Moran
Sigma H-directed transcription of citG in Bacillus subtilis.
J Bacteriol: 1989, 171(11);5928-32
[PubMed:2509422] [WorldCat.org] [DOI] (P p)

I M Feavers, V Price, A Moir
The regulation of the fumarase (citG) gene of Bacillus subtilis 168.
Mol Gen Genet: 1988, 211(3);465-71
[PubMed:3130545] [WorldCat.org] [DOI] (P p)

J S Miles, J R Guest
Complete nucleotide sequence of the fumarase gene (citG) of Bacillus subtilis 168.
Nucleic Acids Res: 1985, 13(1);131-40
[PubMed:3923430] [WorldCat.org] [DOI] (P p)