Fig. 7-6. Multiple amino acid alignment of the AroD 

 domain of AroD«E with its homologues. Nine proteins have 

 been aligned and conserved regions are boxed. Three 

 conserved residues that have been shown as active site 

 residues in E. coli have asterisks (H (25) , L (20) , M 

 (47) } . The amino acid residue numbers for each sequence 

 are on the right of the figure: 









Accession 



Designation 



Organism 



Protein 



Number 



Eco-AroD 



Escherichia coli 



dehydroquinase 



S14750 



Sty-AroD 



Salmonella typhimurium 



dehydroquinase 



P24670 



Bsu-AroD 



Bacillus subtilus 



dehydroquinase 



L09228 



Efa-AroD 



Enterococcus faecalis 



dehydroquinase 



L23802 



Nta-AroD»E 



Nicotiana tabacum 



bifunctional S-protein 



- 



Sce-Arol 



Saccharomyces cerivisiae 



arom pentafunctional protein 



P08566 



Eni-AroM 



Emericella nidulans 



arom pentafunctional protein 



P07547 



Ncr-Qa-lS 



Neurospora crassa 



quinate repressor protein 



P11637 



Eni-QutR 



Emericella nidulans 



quinate repressor protein 



M59935 



