IolA

• Description: methylmalonate-semialdehyde dehydrogenase (acylating)
  
  

Gene name	iolA
Synonyms	mmsA, yxdA
Essential	no
Product	methylmalonate-semialdehyde dehydrogenase (acylating)
Function	myo-inositol catabolism
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism
MW, pI	53 kDa, 5.139
Gene length, protein length	1461 bp, 487 aa
Immediate neighbours	iolB, iolR
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

CcpA regulon, IolR regulon

The gene

Basic information

• Locus tag: BSU39760

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 3-oxopropanoate + CoA + NAD(P)⁺ = acetyl-CoA + CO₂ + NAD(P)H (according to Swiss-Prot)

• Protein family: IolA subfamily (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 1T90

• UniProt: P42412

• KEGG entry: [3]

• E.C. number: 1.2.1.27

Expression and regulation

• Operon: iolA-iolB-iolC-iolD-iolE-iolF-iolG-iolH-iolI-iolJ PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by glucose (CcpA) PubMed
  • induced by inositol (IolR) PubMed

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

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

• Yasutaro Fujita, University of Fukuyama, Japan
• Ken-ichi Yoshida, Kobe University, Japan

References

François Talfournier, Claire Stines-Chaumeil, Guy Branlant
Methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis: substrate specificity and coenzyme A binding.
J Biol Chem: 2011, 286(25);21971-81
[PubMed:21515690] [WorldCat.org] [DOI] (I p)

Ken-ichi Yoshida, Masanori Yamaguchi, Tetsuro Morinaga, Masaki Kinehara, Maya Ikeuchi, Hitoshi Ashida, Yasutaro Fujita
myo-Inositol catabolism in Bacillus subtilis.
J Biol Chem: 2008, 283(16);10415-24
[PubMed:18310071] [WorldCat.org] [DOI] (P p)

Claire Stines-Chaumeil, François Talfournier, Guy Branlant
Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis.
Biochem J: 2006, 395(1);107-15
[PubMed:16332250] [WorldCat.org] [DOI] (I p)

Y Miwa, Y Fujita
Involvement of two distinct catabolite-responsive elements in catabolite repression of the Bacillus subtilis myo-inositol (iol) operon.
J Bacteriol: 2001, 183(20);5877-84
[PubMed:11566986] [WorldCat.org] [DOI] (P p)

Y Miwa, A Nakata, A Ogiwara, M Yamamoto, Y Fujita
Evaluation and characterization of catabolite-responsive elements (cre) of Bacillus subtilis.
Nucleic Acids Res: 2000, 28(5);1206-10
[PubMed:10666464] [WorldCat.org] [DOI] (I p)

K I Yoshida, T Shibayama, D Aoyama, Y Fujita
Interaction of a repressor and its binding sites for regulation of the Bacillus subtilis iol divergon.
J Mol Biol: 1999, 285(3);917-29
[PubMed:9887260] [WorldCat.org] [DOI] (P p)

K I Yoshida, D Aoyama, I Ishio, T Shibayama, Y Fujita
Organization and transcription of the myo-inositol operon, iol, of Bacillus subtilis.
J Bacteriol: 1997, 179(14);4591-8
[PubMed:9226270] [WorldCat.org] [DOI] (P p)