Pantoate kinase (IPR012043)

Short name: PoK

Overlapping homologous superfamilies

Family relationships



This group of enzymes belongs to the GHMP kinase domain superfamily. Pantoate kinase (PoK) works with phosphopantothenate synthetase (PPS) in the coenzyme A (CoA) biosynthesis pathway in the Archaea. It phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in the CoA biosynthesis pathway [PMID: 19666462].

GHMP kinases are a unique class of ATP-dependent enzymes (the abbreviation of which refers to the original members: galactokinase, homoserine kinase, mevalonate kinase, and phosphomevalonate kinase) [PMID: 8382990]. Enzymes belonging to this superfamily contain three well-conserved motifs, the second of which has the typical sequence Pro-X-X-X-Gly-Leu-X-Ser-Ser-Ala and is involved in ATP binding [PMID: 11188689]. The phosphate binding loop in GHMP kinases is distinct from the classical P-loops found in many ATP/GTP binding proteins. The bound ADP molecule adopts a rare syn conformation and is in the opposite orientation from those bound to the P-loop-containing proteins [PMID: 11188689]. GHMP kinases display a distinctly bilobal appearance with their N-terminal subdomains dominated by a mixed beta-sheet flanked on one side by alpha-helices and their C-terminal subdomains containing a four stranded anti-parallel beta-sheet [PMID: 12796487, PMID: 11188689, PMID: 12771135, PMID: 12001237].

nzymes necessary for CoA biosynthesis in the Archaea.

Contributing signatures

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