Difference between revisions of "Icd"

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(Biological materials)
Line 149: Line 149:
** 1A1000 ( ''icd''::''spec''), {{PubMed| }}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A1000&Search=1A1000 BGSC]
** 1A1000 ( ''icd''::''spec''), {{PubMed| }}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A1000&Search=1A1000 BGSC]
** 1A999 ( ''icd''::''spec''), {{PubMed| }}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A999&Search=1A999 BGSC]
** 1A999 ( ''icd''::''spec''), {{PubMed| }}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A999&Search=1A999 BGSC]
** GP790 (''citZ,icd,mdh''::''kan''), available in [[Jörg Stülke]]'s lab
* '''Expression vector:'''
* '''Expression vector:'''

Revision as of 13:06, 13 August 2013

  • Description: isocitrate dehydrogenase

Gene name icd
Synonyms citC
Essential no
Product isocitrate dehydrogenase
Function TCA cycle
Gene expression levels in SubtiExpress: icd
Interactions involving this protein in SubtInteract: Icd
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
Sequences Protein DNA DNA_with_flanks
Genetic context
Icd context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Icd expression.png

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

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

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

Labs working on this gene/protein

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

Your additional remarks


Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc. Natl. Acad. Sci. U.S.A.: 2012, 109(19);7451-6
[PubMed:22517742] [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)

Nico Pietack, Dörte Becher, Sebastian R Schmidl, Milton H Saier, Michael Hecker, Fabian M Commichau, Jörg Stülke
In vitro phosphorylation of key metabolic enzymes from Bacillus subtilis: PrkC phosphorylates enzymes from different branches of basic metabolism.
J. Mol. Microbiol. Biotechnol.: 2010, 18(3);129-40
[PubMed:20389117] [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)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [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)

Satinder K Singh, Stephen P Miller, Antony Dean, Leonard J Banaszak, David C LaPorte
Bacillus subtilis isocitrate dehydrogenase. A substrate analogue for Escherichia coli isocitrate dehydrogenase kinase/phosphatase.
J. Biol. Chem.: 2002, 277(9);7567-73
[PubMed:11751849] [WorldCat.org] [DOI] (P p)

S K Singh, K Matsuno, D C LaPorte, L J Banaszak
Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase.
J. Biol. Chem.: 2001, 276(28);26154-63
[PubMed:11290745] [WorldCat.org] [DOI] (P p)

C Jourlin-Castelli, N Mani, M M Nakano, A L Sonenshein
CcpC, a novel regulator of the LysR family required for glucose repression of the citB gene in Bacillus subtilis.
J. Mol. Biol.: 2000, 295(4);865-78
[PubMed:10656796] [WorldCat.org] [DOI] (P p)

K Matsuno, T Blais, A W Serio, T Conway, T M Henkin, A L Sonenshein
Metabolic imbalance and sporulation in an isocitrate dehydrogenase mutant of Bacillus subtilis.
J. Bacteriol.: 1999, 181(11);3382-91
[PubMed:10348849] [WorldCat.org] [DOI] (P p)

S Jin, P A Levin, K Matsuno, A D Grossman, A L Sonenshein
Deletion of the Bacillus subtilis isocitrate dehydrogenase gene causes a block at stage I of sporulation.
J. Bacteriol.: 1997, 179(15);4725-32
[PubMed:9244258] [WorldCat.org] [DOI] (P p)

R F Ramaley, M O Hudock
Purification and properties of isocitrate dehydrogenase (NADP) from Thermus aquaticus YT-1, Bacillus subtilis-168 and Chlamydomonas reinhardti-Y-2.
Biochim. Biophys. Acta: 1973, 315(1);22-36
[PubMed:4147570] [WorldCat.org] [DOI] (P p)