Escherichia coli K-12: a cooperatively developed annotation snapshot--2005.

Article Details

Citation

Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G 3rd, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL

Escherichia coli K-12: a cooperatively developed annotation snapshot--2005.

Nucleic Acids Res. 2006 Jan 5;34(1):1-9. Print 2006.

PubMed ID
16397293 [ View in PubMed
]
Abstract

The goal of this group project has been to coordinate and bring up-to-date information on all genes of Escherichia coli K-12. Annotation of the genome of an organism entails identification of genes, the boundaries of genes in terms of precise start and end sites, and description of the gene products. Known and predicted functions were assigned to each gene product on the basis of experimental evidence or sequence analysis. Since both kinds of evidence are constantly expanding, no annotation is complete at any moment in time. This is a snapshot analysis based on the most recent genome sequences of two E.coli K-12 bacteria. An accurate and up-to-date description of E.coli K-12 genes is of particular importance to the scientific community because experimentally determined properties of its gene products provide fundamental information for annotation of innumerable genes of other organisms. Availability of the complete genome sequence of two K-12 strains allows comparison of their genotypes and mutant status of alleles.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Evolved beta-galactosidase subunit alphaP06864Details
DNA gyrase subunit BP0AES6Details
UDP-N-acetylglucosamine 2-epimeraseP27828Details
ATP-dependent DNA helicase RecQP15043Details
Maltodextrin phosphorylaseP00490Details
Porphobilinogen deaminaseP06983Details
L-rhamnose isomeraseP32170Details
Branched-chain-amino-acid aminotransferaseP0AB80Details
Oxidoreductase YdhFP76187Details
RNA 3'-terminal phosphate cyclaseP46849Details
Transketolase 1P27302Details
Rhomboid protease GlpGP09391Details