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 . 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 .
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.
October 2006 / First entry.
PROSITE method (with tools and information) covered by this documentation:
Ito S. Fushinobu S. Yoshioka I. Koga S. Matsuzawa H. Wakagi T.
Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon.
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