Mycobacterium tuberculosis strain π Mycobacterium tuberculosis strain π blueTB molecules protein image

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catalyses the fifth step in the biosynthesis of aromatic amino acids ( ) from chorismate (see also AroQ). It is part of a multifunctional enyzme found in bacteria, plants and fungi, but not in animals. belongs to the shikimate kinase and catalyses the following reaction:

ATP + shikimate = ADP + shikimate 3-phosphate ( )


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The structural model was obtained from PDB entry , and the description from . Click here to search for at PDB.


is a peptide of with a and a The sequence is relatively rich in arginine and contains several . The putative nucleotide binding region spans amino acid residues 9-16 and pos58-84 contains a shikimate kinase signature.

Intragenome comparison reveals no highly homologous genes in . The search for homologues in reveals amino acid sequence homology to many bacterial shikimate kinases. More functional links are available from the .


The gene is encoded in a In the M. tuberculosis laboratory strain H37Rv it is a known as which corresponds to gene in the clinical isolate CDC 1551. It can be found on .


On the circular M. tuberculosis chromosome lies at .

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blueTB molecules are published by Paul Imboden, Dr. PI Bioconsulting. Authorization to photocopy or reproduce this entry for personal use is granted. Copyright @ 2005 Paul Imboden, Dr. PI Bioconsulting. Last modified May 17, 2008 . Disclaimer: blueTB and the author reserves the right to modify and cancel any statement in these documents and regrets, that he cannot accept any responsibility for the consequences of any such changes. to the best of my knowledge all information is correct, but I cannot accept liability for any errors. References for this blueTB entry are:

Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Barrell BG, et al. Nature, 393:537-44 (1998) and the Mycobacterium tuberculosis sequencing project from the Sanger Centre.

Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains. Fleischmann RD, Alland D, Eisen JA, Carpenter L, White O, Peterson J, DeBoy R, Dodson R, Gwinn M, Haft D, Hickey E, Kolonay JF, Nelson WC, Umayam LA, Ermolaeva M, Salzberg SL, Delcher A, Utterback T, Weidman J, Khouri H, Gill J, Mikula A, Bishai W, Jacobs Jr WR Jr, Venter JC, Fraser CM. J Bacteriol. 184:5479-90 (2002) and the Mycobacterium tuberculosis sequencing project from TIGR .

3. Dr. PI's Mtbook, The Mycobacterium tuberculosis genome in a book. Paul Imboden, Dr.PI Bioconsulting. mtbook.drpi.ch/ Release 1.8.0 Jan 2004, which itself is based mainly on reference 1.

Crystallographic studies of shikimate binding and induced conformational changes in Mycobacterium tuberculosis shikimate kinase. Dhaliwal B, Nichols CE, Ren J, Lockyer M, Charles I, Hawkins AR, Stammers DK. FEBS Lett. 574:49-54 (2004)
 

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