AraM

• 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 This image was kindly provided by SubtiList

Categories containing this gene/protein

biosynthesis of lipids, membrane proteins

This gene is a member of the following regulons

AraR regulon, CcpA regulon

The gene

Basic information

• Locus tag: BSU28760

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• Localization: cell membrane (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: P94527

• KEGG entry: [3]

• E.C. number: 1.1.1.261

Expression and regulation

• Operon: araA-araB-araD-araL-araM-araN-araP-araQ-abfA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by glucose (CcpA) PubMed
  • induced by arabinose (AraR) PubMed

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

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)