Difference between revisions of "IolA"

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* '''Additional information:'''
 
* '''Additional information:'''
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** number of protein molecules per cell (minimal medium with glucose and ammonium): 131 {{PubMed|24696501}}
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** number of protein molecules per cell (complex medium with amino acids, without glucose): 397 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 09:44, 17 April 2014

  • 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
MmsA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
IolA expression.png




























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

Phenotypes of a mutant

Database entries

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

Additional information

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)

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): Coenzyme A, NAD PubMed
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 131 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 397 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

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)