ThiO

• Description: FAD-dependent glycine oxidase
  
  

Gene name	thiO
Synonyms	goxB, yjbR
Essential	no
Product	glycine oxidase
Function	biosynthesis of thiamine
Metabolic function and regulation of this protein in SubtiPathways: Thiamin
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 This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU11670

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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: FAD PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions: the FAD-containing holoenzyme is a homotetramer PubMed

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 1NG3 (complex with acetyl-glycine), 1RYI

• UniProt: O31616

• KEGG entry: [3]

• E.C. number: 1.4.3.19

Expression and regulation

• Operon: tenA-tenI-thiO-thiS-thiG-thiF-thiD PubMed

• Sigma factor:

• Regulation:
  • repressed by thiamine (Thi-box) PubMed

• Regulatory mechanism:
  • Thi-box: RNA switch PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original publications

Farrukh Jamil, Qurra-Tul-Ann Afza Gardner, Qamar Bashir, Naeem Rashid, Muhammad Akhtar
Mechanistic and stereochemical studies of glycine oxidase from Bacillus subtilis strain R5.
Biochemistry: 2010, 49(34);7377-83
[PubMed:20690620] [WorldCat.org] [DOI] (I p)

Mattia Pedotti, Elena Rosini, Gianluca Molla, Tommaso Moschetti, Carmelinda Savino, Beatrice Vallone, Loredano Pollegioni
Glyphosate resistance by engineering the flavoenzyme glycine oxidase.
J Biol Chem: 2009, 284(52);36415-36423
[PubMed:19864430] [WorldCat.org] [DOI] (I p)

Laura Caldinelli, Mattia Pedotti, Laura Motteran, Gianluca Molla, Loredano Pollegioni
FAD binding in glycine oxidase from Bacillus subtilis.
Biochimie: 2009, 91(11-12);1499-508
[PubMed:19751796] [WorldCat.org] [DOI] (I p)

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)

Joo-Heon Park, Pieter C Dorrestein, Huili Zhai, Cynthia Kinsland, Fred W McLafferty, Tadhg P Begley
Biosynthesis of the thiazole moiety of thiamin pyrophosphate (vitamin B1).
Biochemistry: 2003, 42(42);12430-8
[PubMed:14567704] [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)