AraM

From SubtiWiki
Revision as of 17:36, 14 July 2011 by Jstuelk (talk | contribs) (Categories containing this gene/protein)
Jump to: navigation, search
  • Description: glycerol-1-phosphate dehydrogenase, L-arabinose operon

Gene name araM
Synonyms yseB
Essential no
Product glycerol-1-phosphate dehydrogenase
Function biosynthesis of phosphoglycerolipids
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
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
AraM context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

poorly characterized/ putative enzymes, membrane 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:
  • Localization: cell membrane (according to Swiss-Prot)

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 Sa-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)