cd07792: FGGY_GK1-3_metazoa (this model, PSSM-Id:212664 is obsolete and has been replaced by 466802)
Metazoan glycerol kinase 1 and 3-like proteins; belongs to the FGGY family of carbohydrate kinases
This subgroup corresponds to a group of metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK1 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs, which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. GKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Comment:based on Escherichia coli glycerol kinase (GK) and other FGGY-GKs
Comment:FGGY proteins contain two domains, separated by a deep cleft that forms the active site. The N-terminal domain is primarily involved in substrate binding, while the C-terminal domain is mainly responsible for ATP binding.
Jiyao W et al.(2023). "The conserved domain database in 2023.",