rhmA:Quickview: Difference between revisions

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!align=left {{table_heading_style}} |Function from GO
!align=left {{table_heading_style}} |Function from GO
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'''Molecular Function'''
<GO_nr />
* GO:0016832 aldehyde-lyase activity ([http://www.geneontology.org/GO.evidence.shtml IDA])
* GO:0000287 magnesium ion binding ([http://www.geneontology.org/GO.evidence.shtml IPI])
* GO:0016151 nickel ion binding ([http://www.geneontology.org/GO.evidence.shtml IDA])
* GO:0005515 protein binding ([http://www.geneontology.org/GO.evidence.shtml IPI])
'''Biological Process'''
* GO:0006725 cellular aromatic compound metabolic process ([http://www.geneontology.org/GO.evidence.shtml ISS])
'''Cellular Component'''
* GO:0005737 cytoplasm ([http://www.geneontology.org/GO.evidence.shtml IDA])
 
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!align=left {{table_heading_style}} |Knock-Out Phenotype
!align=left {{table_heading_style}} |Knock-Out Phenotype

Revision as of 19:17, 2 February 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]

Function from GO

<GO_nr />

Knock-Out Phenotype
Regulation/Expression

transcription unit(s): yfaU[2]

Regulation/Activity
Quick Links

DNA display    Protein display    Pubmed(yfaU)    Textpresso(yfaU)

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Notes

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YfaU is crystallized.[5]



References

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  1. ↑ 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. ↑ 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. ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ 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. ↑ 5.0 5.1 EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
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