Difference between revisions of "CitZ"

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= [[Categories]] containing this gene/protein =
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{{SubtiWiki category|[[carbon core metabolism]]}},
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{{SubtiWiki category|[[phosphoproteins]]}}
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= This gene is a member of the following [[regulons]] =
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{{SubtiWiki regulon|[[CcpA regulon]]}},
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{{SubtiWiki regulon|[[CcpC regulon]]}}
  
 
=The gene=
 
=The gene=
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= Categories containing this gene/protein =
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{{SubtiWiki category|[[carbon core metabolism]]}},
 
{{SubtiWiki category|[[phosphoproteins]]}}
 
 
=The protein=
 
=The protein=
  

Revision as of 22:20, 8 December 2010

  • Description: citrate synthase

Gene name citZ
Synonyms citA2
Essential no
Product citrate synthase II
Function TCA cycle
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 41 kDa, 5.451
Gene length, protein length 1116 bp, 372 aa
Immediate neighbours icd, ytwI
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
CitZ context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

carbon core metabolism, phosphoproteins

This gene is a member of the following regulons

CcpA regulon, CcpC regulon

The gene

Basic information

  • Locus tag: BSU29140

Phenotypes of a mutant

glutamate auxotrophy and a defect in sporulation PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Acetyl-CoA + H2O + oxaloacetate = citrate + CoA (according to Swiss-Prot)
  • Protein family: citrate synthase family (according to Swiss-Prot)

Extended information on the protein

  • Kinetic information: Michaelis-Menten (Random Sequential Reaction Mechanism) PubMed
  • Domains:
  • Modification: phosphorylation on Ser-284 PubMed
  • Cofactor(s):
  • Effectors of protein activity:
    • Inhibited by acetyl-CoA, 2-oxoglutarate and NADH PubMed FEBS Letters
    • Inhibited by citrate and CoA (competitively against acetyl-CoA and non-competitively against oxaloacetate) PubMed
    • Inhibited by ATP competitively in B. subtilis strain 168 and HS 1A17 PubMed PubMed
      • In B. subtilis strain HS 2A2, ATP inhibits a non-competitive fashion PubMed
    • Activated by AMP PubMed
  • Interactions:
  • Localization:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
    • CcpA: transcription repression, CcpC: transcription repression PubMed
    • CcpC: transcription repression (molecular inducer: citrate) PubMed
  • Additional information:
    • The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed

Biological materials

  • Mutant: GP678 (erm), available in Stülke lab
  • Expression vector:
    • pGP1120 (N-terminal Strep-tag, for SPINE, purification from B. subtilis, in pGP380) (available in Stülke lab)
    • pGP1776 (for expression, purification in E. coli with N-terminal Strep-tag, in pGP172, available in Stülke lab)
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab

Labs working on this gene/protein

Linc Sonenshein, Tufts University, Boston, MA, USA Homepage

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References

Reviews

G Wiegand, S J Remington
Citrate synthase: structure, control, and mechanism.
Annu Rev Biophys Biophys Chem: 1986, 15;97-117
[PubMed:3013232] [WorldCat.org] [DOI] (P p)

Original publications