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PROSITE documentation PDOC00996 [for PROSITE entry PS51219]

Dephospho-CoA kinase (DPCK) domain profile





Description

Dephospho-coenzyme A kinase (DPCK) (EC 2.7.1.24) 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 2.7.7.3), 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.

Technical section

PROSITE method (with tools and information) covered by this documentation:

DPCK, PS51219; Dephospho-CoA kinase (DPCK) domain profile  (MATRIX)


References

1AuthorsObmolova G. Teplyakov A. Bonander N. Eisenstein E. Howard A.J. Gilliland G.L.
TitleCrystal structure of dephospho-coenzyme A kinase from Haemophilus influenzae.
SourceJ. Struct. Biol. 136:119-125(2001).
PubMed ID11886213
DOI10.1006/jsbi.2001.4428

2AuthorsO'Toole N. Barbosa J.A.R.G. Li Y. Hung L.-W. Matte A. Cygler M.
TitleCrystal structure of a trimeric form of dephosphocoenzyme A kinase from Escherichia coli.
SourceProtein Sci. 12:327-336(2003).
PubMed ID12538896



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