Difference between revisions of "FolE2"
| Line 1: | Line 1: | ||
| − | * '''Description:''' | + | * '''Description:''' GTP cyclohydrolase IB<br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"|'''Gene name''' | |style="background:#ABCDEF;" align="center"|'''Gene name''' | ||
| − | |'' | + | |''folE2'' |
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' '' | + | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' yciA'' |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"| '''Product''' || | + | |style="background:#ABCDEF;" align="center"| '''Product''' || zinc-independent GTP cyclohydrolase IB |
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of folate |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 34 kDa, 7.831 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 34 kDa, 7.831 | ||
| Line 68: | Line 68: | ||
* '''Modification:''' | * '''Modification:''' | ||
| − | * '''Cofactor(s):''' | + | * '''Cofactor(s):''' activated by a variety of divalent cations {{PubMed|19767425}} |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| − | * '''Interactions:''' | + | * '''Interactions:''' homotetrameric {{PubMed|19767425}} |
* '''Localization:''' | * '''Localization:''' | ||
| Line 78: | Line 78: | ||
=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=3D1T 3D1T] {{PubMed|19767425}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P94398 P94398] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P94398 P94398] | ||
| Line 90: | Line 90: | ||
=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' ''[[ | + | * '''Operon:''' ''[[folE2]]-[[yciB]]-[[yciC]]'' {{PubMed|9811636}} |
* '''[[Sigma factor]]:''' [[SigA]] {{PubMed|12426338}} | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|12426338}} | ||
| Line 122: | Line 122: | ||
=References= | =References= | ||
| − | <pubmed>9811636 ,12426338,17032654</pubmed> | + | <pubmed>9811636 ,12426338,17032654 19767425 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 08:43, 22 September 2009
- Description: GTP cyclohydrolase IB
| Gene name | folE2 |
| Synonyms | yciA |
| Essential | no |
| Product | zinc-independent GTP cyclohydrolase IB |
| Function | biosynthesis of folate |
| MW, pI | 34 kDa, 7.831 |
| Gene length, protein length | 915 bp, 305 aa |
| Immediate neighbours | nasA, yciB |
| 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: BSU03340
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: GTP cyclohydrolase IV family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s): activated by a variety of divalent cations PubMed
- Effectors of protein activity:
- Interactions: homotetrameric PubMed
- Localization:
Database entries
- UniProt: P94398
- KEGG entry: [3]
- E.C. number: 3.5.4.16
Additional information
Expression and regulation
- 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)
Ahmed Gaballa, Tao Wang, Rick W Ye, John D Helmann
Functional analysis of the Bacillus subtilis Zur regulon.
J Bacteriol: 2002, 184(23);6508-14
[PubMed:12426338]
[WorldCat.org]
[DOI]
(P p)
A Gaballa, J D Helmann
Identification of a zinc-specific metalloregulatory protein, Zur, controlling zinc transport operons in Bacillus subtilis.
J Bacteriol: 1998, 180(22);5815-21
[PubMed:9811636]
[WorldCat.org]
[DOI]
(P p)
