Difference between revisions of "FolE"

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|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of folate  
 
|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of folate  
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU22780 folE]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/phenyl_tyr_tryp.html Phe, Tyr, Trp], [http://subtiwiki.uni-goettingen.de/pathways/folate_biosynthesis.html Folate]'''
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/phenyl_tyr_tryp.html Phe, Tyr, Trp], [http://subtiwiki.uni-goettingen.de/pathways/folate_biosynthesis.html Folate]'''

Revision as of 11:07, 7 August 2012

  • Description: GTP cyclohydrolase I

Gene name folE
Synonyms mtrA
Essential no
Product GTP cyclohydrolase IA
Function biosynthesis of folate
Gene expression levels in SubtiExpress: folE
Metabolic function and regulation of this protein in SubtiPathways:
Phe, Tyr, Trp, Folate
MW, pI 21 kDa, 6.335
Gene length, protein length 570 bp, 190 aa
Immediate neighbours mtrB, hbs
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
MtrA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
FolE expression.png




























Categories containing this gene/protein

biosynthesis of cofactors

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU22780

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate (according to Swiss-Prot)
  • Protein family: citrate synthase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): zinc-dependent enzyme PubMed
  • Effectors of protein activity:

Database entries

  • Structure: 3D2O (enzyme from Neisseria gonorrhoeae) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: constitutive PubMed
  • 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

Banumathi Sankaran, Shilah A Bonnett, Kinjal Shah, Scott Gabriel, Robert Reddy, Paul Schimmel, Dmitry A Rodionov, Valérie de Crécy-Lagard, John D Helmann, Dirk Iwata-Reuyl, Manal A Swairjo
Zinc-independent folate biosynthesis: genetic, biochemical, and structural investigations reveal new metal dependence for GTP cyclohydrolase IB.
J Bacteriol: 2009, 191(22);6936-49
[PubMed:19767425] [WorldCat.org] [DOI] (I p)

Basma El Yacoubi, Shilah Bonnett, Jessica N Anderson, Manal A Swairjo, Dirk Iwata-Reuyl, Valérie de Crécy-Lagard
Discovery of a new prokaryotic type I GTP cyclohydrolase family.
J Biol Chem: 2006, 281(49);37586-93
[PubMed:17032654] [WorldCat.org] [DOI] (P p)

P Babitzke, P Gollnick, C Yanofsky
The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis.
J Bacteriol: 1992, 174(7);2059-64
[PubMed:1551827] [WorldCat.org] [DOI] (P p)

P Gollnick, S Ishino, M I Kuroda, D J Henner, C Yanofsky
The mtr locus is a two-gene operon required for transcription attenuation in the trp operon of Bacillus subtilis.
Proc Natl Acad Sci U S A: 1990, 87(22);8726-30
[PubMed:2123343] [WorldCat.org] [DOI] (P p)