<p>Pantothenate kinase (PanK, <db_xref db="EC" dbkey="2.7.1.33"/>) catalyses the conversion of CAATP and pantothenate to ADP and D-4'-phosphopantothenate, the key regulatory step in the biosynthesis of coenzyme A (CoA) [<cite idref="PUB00015018"/>]. Members in this entry represents a two-domain form with an additional C-terminal domain of unknown function. <db_xref db="INTERPRO" dbkey="IPR014454"/> represents the single-domain form of PanK.</p> <p>This type of pantothenate kinase is typical for eukaryotes. It is not related by sequence to bacterial PanK (<db_xref db="INTERPRO" dbkey="IPR004566"/>) and differs in a number of biochemical properties (such as inhibition by acetyl-CoA) [<cite idref="PUB00015018"/>, <cite idref="PUB00015017"/>]. However, this group also includes proteins from several Gram-positive bacteria (<db_xref db="PIRSF" dbkey="PIRSF036940"/>) that are suggested to have originated from the eukaryotic form by lateral transfer [<cite idref="PUB00015017"/>].</p> <p>Hallervorden-Spatz syndrome is caused by a defect in a pantothenate kinase gene [<cite idref="PUB00027731"/>].</p> <p>For additional information please see [<cite idref="PUB00015016"/>].</p> Pantothenate kinase, acetyl-CoA regulated, two-domain type