rhmA:Quickview: Difference between revisions
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!align=left | !align=left |Standard Name | ||
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''yfaU'' | ''yfaU'' | ||
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!align=left | !align=left |Gene Synonym(s) | ||
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''ECK2238, b2245, JW2239''<ref name='LIB:Riley_2006'/> | ''ECK2238, b2245, JW2239''<ref name='LIB:Riley_2006'/> | ||
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!align=left | !align=left |Product Desc. | ||
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predicted aldolase<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>. Crystal structure shows that YfaU is a | predicted aldolase<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>. Crystal structure shows that YfaU is a | ||
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Putative HHED aldolase, function unknown<ref name='LIB:EcoGene'/> | Putative HHED aldolase, function unknown<ref name='LIB:EcoGene'/> | ||
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!align=left | !align=left |Product Synonyms(s) | ||
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predicted 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase<ref name='LIB:Riley_2006'/>, B2245<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, YfaU<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/> | predicted 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase<ref name='LIB:Riley_2006'/>, B2245<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, YfaU<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/> | ||
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!align=left | !align=left |Knock-Out Phenotype | ||
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!align=left | !align=left |Regulation/Expression | ||
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transcription unit(s): [[:Category:Txn_unit:yfaU|yfaU]]<ref name='LIB:EcoCyc10.6'/> | transcription unit(s): [[:Category:Txn_unit:yfaU|yfaU]]<ref name='LIB:EcoCyc10.6'/> | ||
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!align=left | !align=left |Regulation/Activity | ||
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Revision as of 02:02, 10 January 2010
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| Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
| References | Suggestions |
See Help:Quickview for help with entering information in the Quickview table.
| Standard Name |
yfaU |
|---|---|
| Gene Synonym(s) |
ECK2238, b2245, JW2239[1] |
| Product Desc. |
predicted aldolase[2][3]. Crystal structure shows that YfaU is a metal-dependent class II aldolase belonging to the pyruvate/enolpyruvate binding (�/R)8 barrel superfamily.[4], Genomic context suggested a 2-dehydro-3-deoxy sugar aldolase function rather than the 4-hydroxy-2-ketoheptane- 1,7-dioate aldolase function as annotated in the databases based on homology with the related HpcH. Functional assignment of YfaW as a L-rhamnonate dehydratase suggested 2-dehydro-3-deoxy-L-rhamnonate is the physiological substrate of YfaU, and enzyme kinetic measurements support this assignment. Putative HHED aldolase, function unknown[5] |
| Product Synonyms(s) |
predicted 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase[1], B2245[2][1], YfaU[2][1] |
| Knock-Out Phenotype | |
| Regulation/Expression | |
| Regulation/Activity |
|
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Notes
YfaU is crystallized.[5]
References
- ↑ 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
- ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ Rea, D et al. (2008) Crystal structure and functional assignment of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12. Biochemistry 47 9955-65 PubMed
- ↑ 5.0 5.1 EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.