ADP-specific phosphofructokinase/glucokinase (IPR007666)

Short name: ADP_PFK/GK

Overlapping homologous superfamilies

Family relationships


Although ATP is the most common phosphoryl group donor for kinases, certain hyperthermophilic archaea, such as Thermococcus litoralis and Pyrococcus furiosus, utilise unusual ADP-dependent glucokinases (ADPGKs) and phosphofructokinases (ADPPKKs) in their glycolytic pathways [PMID: 11286887, PMID: 12237466, PMID: 12909015]. ADPGKs and ADPPFKs exhibit significant similarity, and form an ADP-dependent kinase (ADPK) family, which was tentatively named the PFKC family [PMID: 11778837]. A ~460-residue ADPK domain is also found in a bifunctional ADP-dependent gluco/phosphofructo- kinase (ADP-GK/PFK) from Methanocaldococcus jannaschii (Methanococcus jannaschii) as well as in homologous hypothetical proteins present in several eukaryotes [PMID: 11717273].

The whole structure of the ADPK domain can be divided into large and small alpha/beta subdomains. 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 [PMID: 11286887, PMID: 12237466, PMID: 12909015].

GO terms

Biological Process

GO:0005975 carbohydrate metabolic process

Molecular Function

GO:0016773 phosphotransferase activity, alcohol group as acceptor

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles