The domain within your query sequence starts at position 13 and ends at position 186; the E-value for the HMG_CoA_synt_N domain shown below is 4e-111.



PFAM accession number:PF01154
Interpro abstract (IPR013528):

Hydroxymethylglutaryl-CoA synthase ( EC ) catalyses the condensation of acetyl-CoA with acetoacetyl-CoA to produce HMG-CoA and CoA, the second reaction in the mevalonate-dependent isoprenoid biosynthesis pathway. HMG-CoA synthase contains an important catalytic cysteine residue that acts as a nucleophile in the first step of the reaction: the acetylation of the enzyme by acetyl-CoA (its first substrate) to produce an acetyl-enzyme thioester, releasing the reduced coenzyme A. The subsequent nucleophilic attack on acetoacetyl-CoA (its second substrate) leads to the formation of HMG-CoA [ (PUBMED:15498869) ].

HMG-CoA synthase occurs in eukaryotes, archaea and certain bacteria [ (PUBMED:15546978) ]. In vertebrates, there are two isozymes located in different subcellular compartments: a cytosolic form that is the starting point of the mevalonate pathway (leads to cholesterol and other sterolic and isoprenoid compounds), and a mitochondrial form responsible for ketone body biosynthesis. HMG-CoA is also found in other eukaryotes such as insects, plants and fungi [ (PUBMED:16640729) ]. In bacteria, isoprenoid precursors are generally synthesised via an alternative, non-mevalonate pathway, however a number of Gram-positive pathogens utilise a mevalonate pathway involving HMG-CoA synthase that is parallel to that found in eukaryotes [ (PUBMED:17128980) (PUBMED:16245942) ].

This entry represents the N-terminal domain of HMG-CoA synthase enzymes from both eukaryotes and prokaryotes.

GO process:isoprenoid biosynthetic process (GO:0008299)
GO function:hydroxymethylglutaryl-CoA synthase activity (GO:0004421)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry HMG_CoA_synt_N