MgsA

• Description: methylglyoxal synthase
  
  

Gene name	mgsA
Synonyms	ypjF, jojF
Essential	no
Product	methylglyoxal synthase
Function	bypass of glycolysis
Gene expression levels in SubtiExpress: mgsA
Interactions involving this protein in SubtInteract: MgsA
Metabolic function and regulation of this protein in SubtiPathways: mgsA
MW, pI	14 kDa, 4.919
Gene length, protein length	411 bp, 137 aa
Immediate neighbours	bshB1, dapB
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

carbon core metabolism

This gene is a member of the following regulons

Spx regulon

The gene

Basic information

• Locus tag: BSU22480

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Glycerone phosphate = methylglyoxal + phosphate (according to Swiss-Prot)

• Protein family: RNase Z family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:
  • non-phosphorylated Crh interacts with MgsA to inhibit its activity PubMed

• Interactions:
  • Crh-MgsA (only non-phosphorylated Crh interacts with MgsA) PubMed

• Localization:

Database entries

• Structure: 1B93 (from Escherichia coli, 50% identity, 73% similarity) PubMed

• UniProt: P42980

• KEGG entry: [2]

• E.C. number: 4.2.3.3

Expression and regulation

• Operon: ypjD-dapB-mgsA-bshB1-bshA-cca-birA PubMed

• Expression browser: mgsA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by diamide stess (thiol depletion) (Spx) PubMed

• Regulatory mechanism:
  • Spx: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:
  • GP67 (mgsA::tet) PubMed, available in Jörg Stülke's lab
  • GP84 (mgsA::pX2(cat)), available in Jörg Stülke's lab

• Expression vector:
  • pGP1301 (N-terminal Strep-tag, purification from E. coli, in pGP172), available in Jörg Stülke's lab
  • pGP1180 (N-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP380), available in Jörg Stülke's lab
  • pGP1181 (C-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP382), available in Jörg Stülke's lab
  • pGP2207 (N-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP1459), available in Jörg Stülke's lab

• lacZ fusion:

• GFP fusion:

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

• FLAG-tag construct: GP86 (spc, based on pGP1331) PubMed, available in Jörg Stülke's lab

• Antibody:

Labs working on this gene/protein

• Boris Görke, University of Vienna, Austria
• Jörg Stülke, University of Göttingen, Germany, Homepage

References

Ahmed Gaballa, Haike Antelmann, Chris J Hamilton, John D Helmann
Regulation of Bacillus subtilis bacillithiol biosynthesis operons by Spx.
Microbiology (Reading): 2013, 159(Pt 10);2025-2035
[PubMed:23894131] [WorldCat.org] [DOI] (I p)

Rachit Jain, Yajun Yan
Dehydratase mediated 1-propanol production in metabolically engineered Escherichia coli.
Microb Cell Fact: 2011, 10;97
[PubMed:22074179] [WorldCat.org] [DOI] (I e)

Jens J Landmann, Ricarda A Busse, Jan-Hendrik Latz, Kalpana D Singh, Jörg Stülke, Boris Görke
Crh, the paralogue of the phosphocarrier protein HPr, controls the methylglyoxal bypass of glycolysis in Bacillus subtilis.
Mol Microbiol: 2011, 82(3);770-87
[PubMed:21992469] [WorldCat.org] [DOI] (I p)

Ahmed Gaballa, Gerald L Newton, Haike Antelmann, Derek Parsonage, Heather Upton, Mamta Rawat, Al Claiborne, Robert C Fahey, John D Helmann
Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli.
Proc Natl Acad Sci U S A: 2010, 107(14);6482-6
[PubMed:20308541] [WorldCat.org] [DOI] (I p)

D Saadat, D H Harrison
The crystal structure of methylglyoxal synthase from Escherichia coli.
Structure: 1999, 7(3);309-17
[PubMed:10368300] [WorldCat.org] [DOI] (P p)