Acetoin utilization protein AcuC (IPR003085)

Short name: AcuC

Overlapping homologous superfamilies

Family relationships


Histones can be reversibly acetylated on several lysine residues. Regulation of transcription is caused in part by this mechanism. Histone deacetylases catalyse the removal of the acetyl group. Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are all members of this ancient protein superfamily [PMID: 9278492].

Histone deacetylases (HDA), acetoin utilisation proteins (ACUC) and acetylpolyamine amidohydrolases (APHA) form an ancient protein superfamily and are all believed to catalyse the deacetylation of a substrate [PMID: 9278492]. HDAs are found in eukaryotes, from yeast to humans; ACUCs are found in eubacteria; and APHAs occur in archaeal bacteria, eubacteria and some eukaryotic organisms [PMID: 9278492]. HDA nomenclature is confusing: the family can also be identified by the codes RPD, HOS, HD and HDAC, regardless of specific sequence similarities. HDAs may have evolved at least twice from APHAs, the more recent gene duplication event resembling APHAs more closely [PMID: 9278492].

Disrupting the expression of ACUC results in diminished growth of bacteria on acetoin and butanediol. Acetoin is a bacterial fermentation product that can be converted to acetate via the butanediol cycle in the absence of other carbon sources; its degradation is believed to be caused by deacetylation mediated by ACUC [PMID: 9278492].

GO terms

Biological Process

GO:0045149 acetoin metabolic process

Molecular Function

No terms assigned in this category.

Cellular Component

No terms assigned in this category.

Contributing signatures

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