|PROSITE documentation PDOC00996 [for PROSITE entry PS51219]|
Dephospho-coenzyme A kinase (DPCK) (EC 22.214.171.124) catalyzes the final step in coenzyme A (CoA) biosynthesis, the phosphorylation of the 3'-hydroxyl group of ribose using ATP as a phosphate donor. DPCK is present in a wide range of organisms, including bacteria, fungi, plants and animals. Whereas bacterial DPCK is found in stand-alone form, mammalian DPCK is associated with another enzyme of the CoA biosynthetic pathway, phosphopantetheine adenylyltransferase (PPAT) (EC 126.96.36.199), in bifunctional coenzyme A synthase (CoA synthase) [1,2].
The DPCK domain contains an ATP/GTP-binding Walker A motif (P-loop) (see <PDOC00017>) in its N-terminal extremity. It is structurally similar to many nucleoside kinases and other P-loop-containing nucleotide triphosphate hydrolases, despite having negligible sequence similarity to these enzymes. The DPCK domain consists of five parallel β-strands flanked by α-helices (see <PDB:1JJV>) [1,2].
The profile we developed covers the entire DPCK domain.Last update:
June 2006 / Pattern removed, profile added and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Obmolova G. Teplyakov A. Bonander N. Eisenstein E. Howard A.J. Gilliland G.L.|
|Title||Crystal structure of dephospho-coenzyme A kinase from Haemophilus influenzae.|
|Source||J. Struct. Biol. 136:119-125(2001).|
|2||Authors||O'Toole N. Barbosa J.A.R.G. Li Y. Hung L.-W. Matte A. Cygler M.|
|Title||Crystal structure of a trimeric form of dephosphocoenzyme A kinase from Escherichia coli.|
|Source||Protein Sci. 12:327-336(2003).|