Difference between revisions of "FolE2"
(→Extended information on the protein) |
|||
Line 80: | Line 80: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' homotetrameric {{PubMed|19767425}} | + | * '''[[SubtInteract|Interactions]]:''' homotetrameric {{PubMed|19767425}} |
− | * '''Localization:''' | + | * '''[[Localization]]:''' |
=== Database entries === | === Database entries === |
Revision as of 20:05, 11 August 2011
- Description: GTP cyclohydrolase IB, replaces FolE under conditions of zinc starvation
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
Categories containing this gene/protein
This gene is a member of the following regulons
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
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)