(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Alphaproteobacteria: NE > Rhodobacterales: NE > Rhodobacteraceae: NE > Paracoccus: NE > Paracoccus denitrificans: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MTLAYETVSENRSFGGIQGVYRHQSQATGTPMTFAIYLPPDARHGKVPVL WYLSGLTCTHENAMTKAGAQEWAAEYGIAVIFPDTSPRGEGVANDETYDL GQGAGFYVDATEAPWAPHFRMWHYVTHELPELVFNNFPLDREAQGITGHS MGGHGALTIAMTFPERYRSVSAFAPIAHPSESDWGRKQFAAYLGDDKAAW KRHDSTILMREKGYPGEVLIDQGASDQFLDLLKPEALAHAMAERRQPGTF RMQQGYDHSYFFVQSFMADHIPLARGALG
Reference
Title: S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification. Harms N, Ras J, Reijnders WNM, van Spanning RJM, Stouthamer AH Ref: Journal of Bacteriology, 178:6296, 1996 : PubMed
Downstream of flhA, the Paracoccus denitrificans gene encoding glutathione-dependent formaldehyde dehydrogenase, an open reading frame was identified and called fghA. The gene product of fghA showed appreciable similarity with human esterase D and with the deduced amino acid sequences of open reading frames found in Escherichia coli, Haemophilus influenzae, and Saccharomyces cerevisiae. Mutating fghA strongly reduced S-formylglutathione hydrolase activity. The mutant was unable to grow on methanol and methylamine, indicating that the enzyme is essential for methylotrophic growth. S-Formylglutathione hydrolase appears to be part of a formaldehyde detoxification pathway that is universal in nature.
