Difference between revisions of "Icd"
| Line 100: | Line 100: | ||
* '''Sigma factor:''' [[SigA]] | * '''Sigma factor:''' [[SigA]] | ||
| − | * '''Regulation:''' | + | * '''Regulation:''' |
| + | ** ''[[citZ]]'': catabolite repression ([[CcpA]]) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] | ||
** repressed in the presence of glucose and glutamate ([[CcpC]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/10656796 PubMed] | ** repressed in the presence of glucose and glutamate ([[CcpC]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/10656796 PubMed] | ||
| − | ''[[icd]]'': constitutive | + | ** ''[[icd]]'': constitutive |
| − | * '''Regulatory mechanism:''' [[CcpA]]: transcription repression | + | * '''Regulatory mechanism:''' |
| + | ** [[CcpA]]: transcription repression | ||
** [[CcpC]]: transcription repression (molecular inducer: citrate) [http://www.ncbi.nlm.nih.gov/sites/entrez/10656796 PubMed] | ** [[CcpC]]: transcription repression (molecular inducer: citrate) [http://www.ncbi.nlm.nih.gov/sites/entrez/10656796 PubMed] | ||
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<pubmed>10656796,12850135 10348849 11751849 18763711 17726680 16493705 4147570 </pubmed> | <pubmed>10656796,12850135 10348849 11751849 18763711 17726680 16493705 4147570 </pubmed> | ||
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# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | ||
Revision as of 20:12, 12 June 2009
- 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 | citZ, mdh |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Locus tag: BSU29130
Phenotypes of a mutant
reduced ability to sporulate 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:
- Cofactor(s): Mg2+, Mn2+
- Effectors of protein activity:
- Interactions:
- Localization: attached to the membrane PubMed
Database entries
- Structure: 1HQS
- Swiss prot entry: P39126
- KEGG entry: [3]
- E.C. number: 1.1.1.42
Additional information
This enzyme requires NADP+ exclusively. No activity was seen on the presence on NAD+ PubMed
Expression and regulation
- Sigma factor: SigA
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP666 (spc), GP672 (erm), available in Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody: available in Linc Sonenshein lab
Labs working on this gene/protein
[Linc Sonenshein|Linc Sonenshein]], Tufts University, Boston, MA, USA Homepage
Your additional remarks
References
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)
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)
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)
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
