{PDOC51255}
{PS51255; ADPK}
{BEGIN}
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* ADP-dependent kinase (ADPK) domain profile *
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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 [1-3]. 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
alpha/beta subdomains (see <PDB:1GC5; A>). The larger subdomain, which carries
the ADP  binding site, consists of a twisted 12-stranded beta sheet flanked on
both faces  by 13 alpha helices and three 3(10) helices, forming an alpha/beta
3-layer sandwich.  The  smaller subdomain, which covers the active site, forms
an alpha/beta  two-layer  structure  containing  5 beta strands and four alpha
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 [1-3].

The profile we developed covers the entire ADPK domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: October 2006 / First entry.

[ 1] 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."
     Structure 9:205-214(2001).
     PubMed=11286887
[ 2] Tsuge H., Sakuraba H., Kobe T., Kujime A., Katunuma N., Ohshima T.
     "Crystal structure of the ADP-dependent glucokinase from Pyrococcus
     horikoshii at 2.0-A resolution: a large conformational change in
     ADP-dependent glucokinase."
     Protein Sci. 11:2456-2463(2002).
     PubMed=12237466
[ 3] Ito S., Fushinobu S., Jeong J.-J., Yoshioka I., Koga S., Shoun H.,
     Wakagi T.
     "Crystal structure of an ADP-dependent glucokinase from Pyrococcus
     furiosus: implications for a sugar-induced conformational change in
     ADP-dependent kinase."
     J. Mol. Biol. 331:871-883(2003).
     PubMed=12909015
[ 4] Ronimus R.S., Morgan H.W.
     "The biochemical properties and phylogenies of phosphofructokinases
     from extremophiles."
     Extremophiles 5:357-373(2001).
     PubMed=11778837
[ 5] Verhees C.H., Tuininga J.E., Kengen S.W.M., Stams A.J.M.,
     van der Oost J., de Vos W.M.
     "ADP-dependent phosphofructokinases in mesophilic and thermophilic
     methanogenic archaea."
     J. Bacteriol. 183:7145-7153(2001).
     PubMed=11717273; DOI=10.1128/JB.183.24.7145-7153.2001

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