IolA

• Description: methylmalonate-semialdehyde dehydrogenase (acylating)
  
  

Gene name	iolA
Synonyms	mmsA, yxdA
Essential	no
Product	methylmalonate-semialdehyde dehydrogenase (acylating)
Function	myo-inositol catabolism
Gene expression levels in SubtiExpress: iolA
Metabolic function and regulation of this protein in SubtiPathways: iolA
MW, pI	53 kDa, 5.139
Gene length, protein length	1461 bp, 487 aa
Immediate neighbours	iolB, iolR
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

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: NAD-dependent oxidation of methylmalonate semialdehyde (MMSA) to propionyl-CoA via acylation and deacylation steps

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

• Paralogous protein(s): YfmT, AldY, YcbD, GabD, GbsA, DhaS, PutC, RocA, AldX, YwdH

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s): Coenzyme A, NAD PubMed

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 1T90 PubMed

• 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

• Expression browser: iolA 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

Additional publications: PubMed

Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538] [WorldCat.org] [DOI] (I e)

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)