Difference between revisions of "Icd"

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(The protein)
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* '''Domains:'''  
 
* '''Domains:'''  
  
* '''Modification:''' phosphorylated [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed], ''in vitro'' phosphorylated by [[PrkC]] on Thr-138, Thr-147, and Thr-396 {{PubMed|20389117}}
+
* '''Modification:'''  
 +
** phosphorylated [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed]
 +
** ''in vitro'' phosphorylated by [[PrkC]] on Thr-138, Thr-147, and Thr-396 {{PubMed|20389117}}
  
* '''Cofactor(s):''' Mg2+, Mn2+
+
* '''Cofactor(s):''' Mg2+, Mn2+, NADP+  
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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=== Additional information===
 
=== Additional information===
This enzyme requires NADP+ exclusively. No activity was seen on the presence on NAD+ [http://www.ncbi.nlm.nih.gov/pubmed/4147570 PubMed]
+
* This enzyme requires NADP+ exclusively. No activity was seen on the presence on NAD+ [http://www.ncbi.nlm.nih.gov/pubmed/4147570 PubMed]
 +
* extensive information on the structure and enzymatic properties of Icd can be found at [http://www.proteopedia.org/wiki/index.php/Isocitrate_dehydrogenase Proteopedia]
  
 
=Expression and regulation=
 
=Expression and regulation=

Revision as of 10:45, 19 February 2011

  • Description: isocitrate dehydrogenase

Gene name icd
Synonyms citC
Essential no
Product isocitrate dehydrogenase
Function TCA cycle
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 46 kDa, 4.833
Gene length, protein length 1269 bp, 423 aa
Immediate neighbours mdh, citZ
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Icd context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

carbon core metabolism, membrane proteins, phosphoproteins

This gene is a member of the following regulons

CcpA regulon, CcpC regulon

The gene

Basic information

  • Locus tag: BSU29130

Phenotypes of a mutant

    • reduced ability to sporulate PubMed
    • growth and sporulation defects of the mutant could be partially bypassed by deletion of the major citrate synthase gene (citZ) PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH (according to Swiss-Prot)
  • Protein family: isocitrate and isopropylmalate dehydrogenases family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: Reversible Michaelis-Menten PubMed
  • Domains:
  • Modification:
  • Cofactor(s): Mg2+, Mn2+, NADP+
  • Effectors of protein activity:
    • Inhibited by glyoxylate, oxaloacetate and oxalomalate PubMed
      • Better inhibition when glyoxylate and oxaloacetate is combined, probably due to the non-enzymatic conversion into oxalomalate, which is a strong inhibitor PubMed
  • Localization: attached to the membrane PubMed

Database entries

  • KEGG entry: [3]

Additional information

  • This enzyme requires NADP+ exclusively. No activity was seen on the presence on NAD+ PubMed
  • extensive information on the structure and enzymatic properties of Icd can be found at Proteopedia

Expression and regulation

  • Regulatory mechanism:
    • CcpA: transcription repression, CcpC: transcription repression PubMed
    • CcpC: transcription repression (molecular inducer: citrate) PubMed
  • Additional information:

Biological materials

  • Mutant: GP666 (spc), GP672 (erm), available in Stülke lab
  • Expression vector:
    • pGP1121 (N-terminal Strep-tag, for SPINE, purification from B. subtilis, in pGP380) (available in Stülke lab)
    • for expression, purification in E. coli with N-terminal His-tag, in pWH844: pGP931, 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

Your additional remarks

References