The following enzymes have been shown [1,2] to be evolutionary related:
Acetate kinase (EC 2.7.2.1) (acetokinase) (gene ackA) from bacteria and
archaebacteria. This enzyme is involved in the interconversion of acetate
and acetyl-CoA via the acetyl phosphate intermediate. In anaerobic growth
it provides ATP by catabolyzing acetate phosphate into acetate.
Butyrate kinase (EC 2.7.2.7) (gene buk). This enzyme is involved in the
interconversion of butyrate and butyryl-CoA via the butyryl phosphate
intermediate. Butyrate kinase is involved in the acidogenic phase of
fermentation.
Propionate kinase (EC 2.7.2,.) (gene tdcD) from Escherichia coli.
We have developed two signature patterns for these enzymes; the first one is
located in the N-terminal section and the second in the central section. Both
of them are glycine-rich and could be involved in substrate or ATP-binding.
Last update:
December 2004 / Pattern and text revised.
Technical section
PROSITE methods (with tools and information) covered by this documentation:
References
1
Authors
Grundy F.J., Waters D.A., Allen S.H.G., Henkin T.M.
Title
Regulation of the Bacillus subtilis acetate kinase gene by CcpA.
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