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ybhA:Gene Product(s)
From EcoliWiki
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| 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 |
YbhA |
|---|---|
| Synonyms |
predicted hydrolase[1], YbhA[2][1], B0766[2][1], fructose 1,6-bisphosphatase III[2][1] |
| Product description |
Pyridoxal phosphate (PLP) phosphatase; phosphoramidase; physiological role unknown; HAD14[4] |
| EC number (for enzymes) |
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| edit table |
Notes
Function
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(s) | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0046872 |
metal ion binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [5] |
complete | |||
| GO:0016787 |
hydrolase activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [5] |
complete | |||
|
Deprecated | GO:0016020 |
membrane |
IEA: Inferred from Electronic Annotation |
C |
No membrane spanning segments were predicted for YbhA using TMHMM 3.0. This electronic annotation probably made because YbhA shares sequence similarity with the catalytic domain of P-type ATPases. |
complete | ||
|
Deprecated | GO:0015662 |
ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism |
IEA: Inferred from Electronic Annotation |
F |
YbhA has sequence similarity to only the catalytic domain of P-type ATPases. No predicted membrane spanning regions were identified in YbhA using TMHMM 3.0. |
complete | ||
| GO:0008152 |
metabolic process |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc [5] |
complete | |||
| GO:0006810 |
transport |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc 12.5 [6] |
complete | |||
| GO:0005524 |
ATP binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [5] |
complete | |||
| GO:0003824 |
catalytic activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [5] |
complete | |||
| GO:0000287 |
magnesium ion binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [5] |
complete | |||
| GO:0042822 |
pyridoxal phosphate metabolic process |
P |
Seeded from EcoCyc 11.1[3]. |
required fields missing | ||||
| GO:0006754 |
ATP biosynthetic process |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc [5] |
complete | |||
|
Under review | GO:0042132 |
fructose 1,6-bisphosphate 1-phosphatase activity |
F |
YbhA releases phosphate from fructose-1,6-bis-phosphate, but which phosphate is released wasn't determined. |
required field missing | |||
| GO:0050308 |
sugar-phosphatase activity |
IDA: Inferred from Direct Assay |
F |
complete | ||||
| GO:0050308 |
sugar-phosphatase activity |
IDA: Inferred from Direct Assay |
F |
complete | ||||
| GO:0016773 |
phosphotransferase activity, alcohol group as acceptor |
IDA: Inferred from Direct Assay |
F |
Purified YbhA will form glycerol phosphate from glycerol and inorganic phosphate (Table 4). The authors note that the phosphotransferase activity is lower than the phosphatase activity, and that other mono-phosphates can serve as the phosphate donor. |
complete | |||
| GO:0033883 |
pyridoxal phosphatase activity |
IDA: Inferred from Direct Assay |
F |
Figure 1 and Table 2. |
complete | |||
| GO:0016791 |
phosphatase activity |
IDA: Inferred from Direct Assay |
F |
YbhA had phosphatase activity on 8 of the 80 phosphorylated compounds tested. These were (in decreasing order of activity): pyridoxal-5-P, erythrose-4-P, Fructose-1,6-bis-P, flavin mononucleotide (FMN), thiamine pyrophosphate, phosphoribosyl pyrophosphate (PRPP), Glucose-1,6-di-P, and 6-phosphogluconate (Fig. 1). |
complete | |||
| GO:0000287 |
magnesium ion binding |
IDA: Inferred from Direct Assay |
F |
Km is 0.14±0.02 mM with pyridoxal-5-phosphate as the substrate (Suppl. Table 2). |
complete | |||
| edit table |
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 |
Experiment(s):EBI-1137896 | |||
|
Protein |
Experiment(s):EBI-1137896 | |||
| edit table |
Notes
Localization
See Help:Product_localization for how to add or edit information in this section of EcoliWiki.
| Compartment | Description | Evidence | Source | Notes |
|---|---|---|---|---|
| edit table |
Notes
Structure and Physical Properties
Physical Properties
See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.
| Sequence |
MTTRVIALDL DGTLLTPKKT LLPSSIEALA RAREAGYQLI IVTGRHHVAI HPFYQALALD TPAICCNGTY LYDYHAKTVL EADPMPVIKA LQLIEMLNEH HIHGLMYVDD AMVYEHPTGH VIRTSNWAQT LPPEQRPTFT QVASLAETAQ QVNAVWKFAL THDDLPQLQH FGKHVEHELG LECEWSWHDQ VDIARGGNSK GKRLTKWVEA QGWSMENVVA FGDNFNDISM LEAAGTGVAM GNADDAVKAR ANIVIGDNTT DSIAQFIYSH LI |
|---|---|
| Length |
272 |
| Mol. Wt |
30.2 kDa |
| pI |
5.8 (calculated) |
| Extinction coefficient |
44,920 - 45,295 (calc based on 8 Y, 6 W, and 3 C residues) |
| edit table |
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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
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| Resource type | Source | Notes/Reference |
|---|---|---|
| edit table |
Notes
Accessions in Other Databases
See Help:Gene_accessions for help with entering information into the Gene Accessions table.
| Database | Accession | Notes |
|---|---|---|
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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 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 5.3 5.4 5.5 5.6 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
- ↑ EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 7.0 7.1 7.2 7.3 7.4 Kuznetsova E et al. (2006) Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. J Biol Chem 281: 36149-61 PubMed EcoliWiki page
- ↑ 8.0 8.1 Saito N et al. (2006) Metabolomics approach for enzyme discovery. J Proteome Res 5: 1979-87 PubMed EcoliWiki page
- ↑ 9.0 9.1 Arifuzzaman M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16: 686-91 PubMed EcoliWiki page
