ybjI: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 |
YbjI |
|---|---|
| Synonyms |
conserved protein[1], YbjI[2][1], B0844[2][1] , ECK0834, JW5113, b0844 |
| Product description |
FMN and erythrose-4-P phosphatase; physiological role unknown; HAD15[4] |
| EC number (for enzymes) |
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| 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:0000287 |
magnesium ion binding |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
| GO:0043726 |
5-amino-6-(5-phosphoribitylamino)uracil phosphatase activity |
IDA: Inferred from Direct Assay |
F |
Seeded from EcoCyc |
complete | |||
| GO:0009231 |
riboflavin biosynthetic process |
IDA: Inferred from Direct Assay |
P |
Seeded from EcoCyc |
complete | |||
| GO:0005737 |
cytoplasm |
IBA: Inferred from Biological Aspect of Ancestor |
C |
Seeded from EcoCyc |
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 |
|---|---|---|---|---|
| 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 |
|---|---|---|---|---|
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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 |
MDGTFLSDQK TYNRERFMAQ YQQMKAQGIR FVVASGNQYY QLISFFPEIA NEIAFVAENG GWVVSEGKDV FNGELSKDAF ATVVEHLLTR PEVEIIACGK NSAYTLKKYD DAMKTVAEMY YHRLEYVDNF DNLEDIFFKF GLNLSDELIP QVQKALHEAI GDIMVSVHTG NGSIDLIIPG VHKANGLRQL QKLWGIDDSE VVVFGDGGND IEMLRQAGFS FAMENAGSAV VAAAKYRAGS NNREGVLDVI DKVLKHEAPF DQ |
| Length |
262 |
| Mol. Wt |
29.224 kDa |
| pI |
4.6 (calculated) |
| Extinction coefficient |
25,900 - 26,025 (calc based on 10 Y, 2 W, and 1 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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<motif_map/> |
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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 | ||
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Escherichia coli str. K-12 substr. MG1655 | ||
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Escherichia coli str. K-12 substr. MG1655 | ||
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Escherichia coli str. K-12 substr. MG1655 | ||
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Escherichia coli str. K-12 substr. MG1655 | ||
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Escherichia coli str. K-12 substr. MG1655 | ||
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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 |
|---|---|---|
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References
See Help:References for how to manage references in EcoliWiki.
- ↑ 1.0 1.1 1.2 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 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 Haase, I et al. (2013) Enzymes from the haloacid dehalogenase (HAD) superfamily catalyse the elusive dephosphorylation step of riboflavin biosynthesis. Chembiochem 14 2272-5 PubMed
- ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed
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