Difference between revisions of "FolE"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[mtrB]]'', ''[[hbs]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[mtrB]]'', ''[[hbs]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU22780 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU22780 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU22780 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU22780 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU22780 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU22780 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:mtrA_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:mtrA_context.gif]]

Revision as of 10:34, 14 May 2013

  • 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
Sequences Protein DNA DNA_with_flanks
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)