folE:Gene Product(s)
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| Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
| Nomenclature | Function | Interactions | Localization | Sequence | Domains | Structure | Resources | Accessions | Links | References | Suggestions |
Nomenclature
See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.
| Standard name |
FolE |
|---|---|
| Synonyms |
GTP cyclohydrolase I[1], B2153[2][1], FolE[2][1] , ECK2146, JW2140, b2153 |
| Product description |
Component of GTP cyclohydrolase I[2][3] GTP cyclohydrolase I[4] |
| EC number (for enzymes) | |
| edit table |
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Notes
Function
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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.
| Qualifier | GO ID | GO term name | Reference | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0005737 |
cytoplasm |
IDA: Inferred from Direct Assay |
C |
FolE was present in the supernatant after subcellular fractionation. Seeded from Riley et al 2006 [1]. |
complete | |||
| GO:0005737 |
cytoplasm |
IDA: Inferred from Direct Assay |
C |
GTP cyclohyrdolase I activity was purified from the supernatant after subcellular fractionation. |
complete | |||
| GO:0003934 |
GTP cyclohydrolase I activity |
GOA:hamap |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
| GO:0003934 |
GTP cyclohydrolase I activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
| GO:0005525 |
GTP binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
| GO:0003934 |
GTP cyclohydrolase I activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
| GO:0032991 |
protein-containing complex |
IDA: Inferred from Direct Assay |
C |
Based on biochemical characterization. |
complete | |||
| GO:0003934 |
GTP cyclohydrolase I activity |
GOA:spec |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
| GO:0032991 |
protein-containing complex |
IDA: Inferred from Direct Assay |
C |
FolE is a homodecamer based on X-ray crystallography. |
complete | |||
| GO:0005525 |
GTP binding |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
| GO:0006730 |
one-carbon metabolic process |
GOA:hamap |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
| GO:0006730 |
one-carbon metabolic process |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
| GO:0008270 |
zinc ion binding |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
| GO:0046654 |
tetrahydrofolate biosynthetic process |
GOA:hamap |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
| GO:0046654 |
tetrahydrofolate biosynthetic process |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
| GO:0046654 |
tetrahydrofolate biosynthetic process |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.
| Partner Type | Partner | Notes | References | Evidence |
|---|---|---|---|---|
|
Protein |
Subunits of GTP cyclohydrolase I |
could be indirect |
| |
| edit table |
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Notes
Localization
See Help:Product_localization for how to add or edit information in this section of EcoliWiki.
| Compartment | Description | Evidence | Reference/Source | Notes |
|---|---|---|---|---|
| edit table |
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Notes
Structure and Physical Properties
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Physical Properties
See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.
| Name | |
|---|---|
| Sequence |
MPSLSKEAAL VHEALVARGL ETPLRPPVHE MDNETRKSLI AGHMTEIMQL LNLDLADDSL METPHRIAKM YVDEIFSGLD YANFPKITLI ENKMKVDEMV TVRDITLTST CEHHFVTIDG KATVAYIPKD SVIGLSKINR IVQFFAQRPQ VQERLTQQIL IALQTLLGTN NVAVSIDAVH YCVKARGIRD ATSATTTTSL GGLFKSSQNT RHEFLRAVRH HN |
| Length |
222 |
| Mol. Wt |
24.83 kDa |
| pI |
7.4 (calculated) |
| Extinction coefficient |
5,960 - 6,210 (calc based on 4 Y, 0 W, and 2 C residues) |
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Domains/Motifs/Modification Sites
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See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.
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Structure
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Structure figures<protect> | ||||||
Notes
Gene Product Resources
See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.
| Resource type | Source | Notes/Reference |
|---|---|---|
| edit table |
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Notes
Accessions in Other Databases
See Help:Gene_accessions for help with entering information into the Gene Accessions table.
| Database | Accession | Notes |
|---|---|---|
|
Escherichia coli str. K-12 substr. MG1655 | ||
|
Escherichia coli str. K-12 substr. MG1655 | ||
|
Escherichia coli str. K-12 substr. MG1655 | ||
|
Escherichia coli str. K-12 substr. MG1655 | ||
|
Escherichia coli str. K-12 substr. MG1655 | ||
|
Escherichia coli str. K-12 substr. MG1655 | ||
|
Escherichia coli str. K-12 substr. MG1655 | ||
|
Escherichia coli str. K-12 substr. MG1655 | ||
|
Escherichia coli str. K-12 substr. MG1655 | ||
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Notes
Links
| Name | URL | Comments |
|---|---|---|
| edit table |
References
See Help:References for how to manage references in EcoliWiki.
- ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
- ↑ 5.0 5.1 5.2 Yim, JJ & Brown, GM (1976) Characteristics of guanosine triphosphate cyclohydrolase I purified from Escherichia coli. J. Biol. Chem. 251 5087-94 PubMed
- ↑ Burg, AW & Brown, GM (1968) The biosynthesis of folic acid. 8. Purification and properties of the enzyme that catalyzes the production of formate from carbon atom 8 of guanosine triphosphate. J. Biol. Chem. 243 2349-58 PubMed
- ↑ Nar, H et al. (1995) Atomic structure of GTP cyclohydrolase I. Structure 3 459-66 PubMed
- ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed
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