Difference between revisions of "ThiO"

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m (moved GoxB to ThiO)
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* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1NG3 1NG3] (complex with acetyl-glycine),  [http://www.rcsb.org/pdb/explore.do?structureId=1RYI 1RYI]
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1NG3 1NG3] (complex with acetyl-glycine),  [http://www.rcsb.org/pdb/explore.do?structureId=1RYI 1RYI]
  
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O31616 O31616]
+
* '''UniProt:''' [http://www.uniprot.org/uniprot/O31616 O31616]
  
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU11670]
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU11670]

Revision as of 11:56, 20 July 2009

  • Description: FAD-dependent glycine oxidase

Gene name thiO
Synonyms goxB, yjbR
Essential no
Product glycine oxidase
Function biosynthesis of thiamine
MW, pI 40 kDa, 5.898
Gene length, protein length 1107 bp, 369 aa
Immediate neighbours tenI, thiS
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
GoxB context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU11670

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Glycine + H2O + O2 = glyoxylate + NH3 + H2O2 (according to Swiss-Prot)
  • Protein family: DAMOX/DASOX 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: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure: 1NG3 (complex with acetyl-glycine), 1RYI
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • 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

Mattia Pedotti, Sandro Ghisla, Laura Motteran, Gianluca Molla, Loredano Pollegioni
Catalytic and redox properties of glycine oxidase from Bacillus subtilis.
Biochimie: 2009, 91(5);604-12
[PubMed:19254749] [WorldCat.org] [DOI] (I p)

Mario Mörtl, Kay Diederichs, Wolfram Welte, Gianluca Molla, Laura Motteran, Gabriella Andriolo, Mirella S Pilone, Loredano Pollegioni
Structure-function correlation in glycine oxidase from Bacillus subtilis.
J Biol Chem: 2004, 279(28);29718-27
[PubMed:15105420] [WorldCat.org] [DOI] (P p)

Gianluca Molla, Laura Motteran, Viviana Job, Mirella S Pilone, Loredano Pollegioni
Kinetic mechanisms of glycine oxidase from Bacillus subtilis.
Eur J Biochem: 2003, 270(7);1474-82
[PubMed:12654003] [WorldCat.org] [DOI] (P p)

Ethan C Settembre, Pieter C Dorrestein, Joo-Heon Park, Amy M Augustine, Tadhg P Begley, Steven E Ealick
Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis.
Biochemistry: 2003, 42(10);2971-81
[PubMed:12627963] [WorldCat.org] [DOI] (P p)

Viviana Job, Giorgia Letizia Marcone, Mirella S Pilone, Loredano Pollegioni
Glycine oxidase from Bacillus subtilis. Characterization of a new flavoprotein.
J Biol Chem: 2002, 277(9);6985-93
[PubMed:11744710] [WorldCat.org] [DOI] (P p)

Y Nishiya, T Imanaka
Purification and characterization of a novel glycine oxidase from Bacillus subtilis.
FEBS Lett: 1998, 438(3);263-6
[PubMed:9827558] [WorldCat.org] [DOI] (P p)