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PROSITE documentation PDOC51255 [for PROSITE entry PS51255]

ADP-dependent kinase (ADPK) domain profile





Description

Although ATP is the most common phosphoryl group donor for kinases, certain hyperthermophilic archaea, such as Thermococcus litoralis and Pyrococcus furiosus, utilize unusual ADP-dependent glucokinases (ADPGKs) and phosphofructokinases (ADPPKKs) in their glycolytic pathways [1,2,3]. ADPGKs and ADPPFKs exhibit significant similarity, and form an ADP-dependent kinase (ADPK) family, which was tentatively named the PFKC family [4]. A ~460-residue ADPK domain is also found in a bifunctional ADP-dependent gluco/phosphofructo-kinase (ADP-GK/PFK) from Methanococcus jannaschii as well as in homologous hypothetical proteins present in several eukaryotes [5].

The whole structure of the ADPK domain can be divided into large and small α/β subdomains (see <PDB:1GC5; A>). The larger subdomain, which carries the ADP binding site, consists of a twisted 12-stranded β sheet flanked on both faces by 13 α helices and three 3(10) helices, forming an α/β 3-layer sandwich. The smaller subdomain, which covers the active site, forms an α/β two-layer structure containing 5 β strands and four α helices. The ADP molecule is buried in a shallow pocket in the large subdomain. The binding of substrate sugar induces a structural change, the small domain closing to form a complete substrate sugar binding site [1,2,3].

The profile we developed covers the entire ADPK domain.

Last update:

October 2006 / First entry.

Technical section

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

ADPK, PS51255; ADP-dependent kinase (ADPK) domain profile  (MATRIX)


References

1AuthorsIto S. Fushinobu S. Yoshioka I. Koga S. Matsuzawa H. Wakagi T.
TitleStructural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon.
SourceStructure 9:205-214(2001).
PubMed ID11286887

2AuthorsTsuge H. Sakuraba H. Kobe T. Kujime A. Katunuma N. Ohshima T.
TitleCrystal structure of the ADP-dependent glucokinase from Pyrococcus horikoshii at 2.0-A resolution: a large conformational change in ADP-dependent glucokinase.
SourceProtein Sci. 11:2456-2463(2002).
PubMed ID12237466

3AuthorsIto S. Fushinobu S. Jeong J.-J. Yoshioka I. Koga S. Shoun H. Wakagi T.
TitleCrystal structure of an ADP-dependent glucokinase from Pyrococcus furiosus: implications for a sugar-induced conformational change in ADP-dependent kinase.
SourceJ. Mol. Biol. 331:871-883(2003).
PubMed ID12909015

4AuthorsRonimus R.S. Morgan H.W.
TitleThe biochemical properties and phylogenies of phosphofructokinases from extremophiles.
SourceExtremophiles 5:357-373(2001).
PubMed ID11778837

5AuthorsVerhees C.H. Tuininga J.E. Kengen S.W.M. Stams A.J.M. van der Oost J. de Vos W.M.
TitleADP-dependent phosphofructokinases in mesophilic and thermophilic methanogenic archaea.
SourceJ. Bacteriol. 183:7145-7153(2001).
PubMed ID11717273
DOI10.1128/JB.183.24.7145-7153.2001



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