AraM

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  • Description: glycerol-1-phosphate dehydrogenase, L-arabinose operon

Gene name araM
Synonyms yseB
Essential no
Product glycerol-1-phosphate dehydrogenase
Function biosynthesis of phosphoglycerolipids
Gene expression levels in SubtiExpress: araM
Metabolic function and regulation of this protein in SubtiPathways:
Sugar catabolism
MW, pI 42 kDa, 5.628
Gene length, protein length 1182 bp, 394 aa
Immediate neighbours araN, araL
Sequences Protein DNA DNA_with_flanks
Genetic context
AraM context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AraM expression.png




























Categories containing this gene/protein

poorly characterized/ putative enzymes, membrane proteins, sporulation proteins

This gene is a member of the following regulons

AraR regulon, CcpA regulon

The gene

Basic information

  • Locus tag: BSU28760

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: sn-glycerol-1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H (according to Swiss-Prot)
  • Protein family: glycerol-1-phosphate dehydrogenase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Harald Guldan, Reinhard Sterner, Patrick Babinger
Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis.
Biochemistry: 2008, 47(28);7376-84
[PubMed:18558723] [WorldCat.org] [DOI] (I p)

José Manuel Inácio, Carla Costa, Isabel de Sá-Nogueira
Distinct molecular mechanisms involved in carbon catabolite repression of the arabinose regulon in Bacillus subtilis.
Microbiology (Reading): 2003, 149(Pt 9);2345-2355
[PubMed:12949161] [WorldCat.org] [DOI] (P p)

L J Mota, P Tavares, I Sá-Nogueira
Mode of action of AraR, the key regulator of L-arabinose metabolism in Bacillus subtilis.
Mol Microbiol: 1999, 33(3);476-89
[PubMed:10417639] [WorldCat.org] [DOI] (P p)

Isabel S-Nogueira, Teresa V Nogueira, Snia Soares, Hermnia de Lencastre
The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence, genetic organization and expression.
Microbiology (Reading): 1997, 143 ( Pt 3);957-969
[PubMed:9084180] [WorldCat.org] [DOI] (P p)