MleA

• Description: malic enzyme
  
  

Gene name	mleA
Synonyms	yqkJ
Essential	no
Product	NAD-dependent malate dehydrogenase
Function	malate utilization
Gene expression levels in SubtiExpress: mleA
Metabolic function and regulation of this protein in SubtiPathways: mleA
MW, pI	45 kDa, 4.895
Gene length, protein length	1317 bp, 439 aa
Immediate neighbours	yqkK, mleN
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

AnsR regulon, CcpA regulon

The gene

Basic information

• Locus tag: BSU23550

Database entries

• BsubCyc: BSU23550

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: (S)-malate + NAD⁺ = pyruvate + CO₂ + NADH (according to Swiss-Prot) malate --> pyruvate

• Protein family: malic enzymes family (according to Swiss-Prot)

• Paralogous protein(s): YtsJ

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU23550

• Structure:

• UniProt: P54572

• KEGG entry: [2]

• E.C. number: 1.1.1.38

Expression and regulation

• Operon:
  • ansA-ansB-mleN-mleA PubMed
  • mleN-mleA PubMed

• Expression browser: mleA PubMed

• Sigma factor:
  • ansA: SigA PubMed
  • mleN: SigA PubMed

• Regulation:
  • ansA: expressed in the presence of asparagine (AnsR) PubMed
  • mleN: repressed by glucose (CcpA) PubMed

• Regulatory mechanism:
  • AnsR: transcription repression PubMed
  • CcpA: transcription repression PubMed

• Additional information:

Biological materials

• Mutant: GP1136 (cat) available in Stülke lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Additional publications: PubMed

Frederik M Meyer, Jörg Stülke
Malate metabolism in Bacillus subtilis: distinct roles for three classes of malate-oxidizing enzymes.
FEMS Microbiol Lett: 2013, 339(1);17-22
[PubMed:23136871] [WorldCat.org] [DOI] (I p)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Guillaume Lerondel, Thierry Doan, Nicola Zamboni, Uwe Sauer, Stéphane Aymerich
YtsJ has the major physiological role of the four paralogous malic enzyme isoforms in Bacillus subtilis.
J Bacteriol: 2006, 188(13);4727-36
[PubMed:16788182] [WorldCat.org] [DOI] (P p)

Susan H Fisher, Lewis V Wray
Bacillus subtilis 168 contains two differentially regulated genes encoding L-asparaginase.
J Bacteriol: 2002, 184(8);2148-54
[PubMed:11914346] [WorldCat.org] [DOI] (P p)