dhaM:Quickview: Difference between revisions
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DhaM is phosphorylated by PTS proteins HPr and Protein I. DhaM contains homology to Hpr and part of Enzyme I. DhaM lacks a homologous PEP binding site and catalytic region of HPr. The N-terminal dimerization domain is homologous to an EIIa domain and is the phosphate donor region. H431 accepts phosphate from Hpr and relays it to H10 and H170.<ref name='LIB:EcoGene'/> | |||
Revision as of 02:09, 3 March 2009
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| Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
| References | Suggestions |
| Gene Name |
dhaM (synonyms: dhaH, ECK1186, b1198, JW5185, ycgC, ptsD)[1][2] |
|---|---|
| Product(s) |
DhaH product[1]: fused predicted dihydroxyacetone-specific PTS enzymes: HPr component product, EI component product, DhaM product, B1198 product, YcgC product, PtsD product |
| Description |
dihydroxyacetone kinase subunit M[2][3] Component of dihydroxyacetone kinase[3] |
| Knock-Out Phenotype | |
| Regulation/Expression | |
| Regulation/Activity |
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| edit table |
See Help:Quickview for help with entering information in the Quickview table.
Notes
DhaM is phosphorylated by PTS proteins HPr and Protein I. DhaM contains homology to Hpr and part of Enzyme I. DhaM lacks a homologous PEP binding site and catalytic region of HPr. The N-terminal dimerization domain is homologous to an EIIa domain and is the phosphate donor region. H431 accepts phosphate from Hpr and relays it to H10 and H170.[4]
References
- ↑ 1.0 1.1 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
- ↑ 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.