Difference between revisions of "ThiO"
(→References) |
(→References) |
||
Line 118: | Line 118: | ||
=References= | =References= | ||
− | <pubmed> 19254749, 11744710, 12654003, 9827558 12627963 15105420 19751796 19864430 </pubmed> | + | <pubmed> 19254749, 11744710, 12654003, 9827558 12627963 15105420 19751796 19864430 14567704</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 08:58, 24 November 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 This image was kindly provided by SubtiList
|
Contents
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: 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
- UniProt: O31616
- KEGG entry: [3]
- E.C. number: 1.4.3.19
Additional information
Expression and regulation
- 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, 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)