S. cerevisiae Gene ERG10 (YPL028W)
  Description: Acetyl-CoA C-acetyltransferase (acetoacetyl-CoA thiolase), cytosolic enzyme that transfers an acetyl group from one acetyl-CoA molecule to another, forming acetoacetyl-CoA involved in the first step in mevalonate biosynthesis
Transcript (Including UTRs)
   Position: sacCer3 chrXVI:498,096-499,292 Size: 1,197 Total Exon Count: 1 Strand: +
Coding Region
   Position: sacCer3 chrXVI:498,096-499,292 Size: 1,197 Coding Exon Count: 1 

Page IndexSequence and LinksUniProtKB CommentsProtein StructureOther SpeciesGO Annotations
Other NamesMethods
Data last updated at UCSC: 2011-08-29

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chrXVI:498,096-499,292)mRNAProtein (398 aa)
Gene SorterGenome BrowserOther Species FASTASGDUniProtKB

-  Comments and Description Text from UniProtKB
  ID: THIL_YEAST
DESCRIPTION: RecName: Full=Acetyl-CoA acetyltransferase; EC=2.3.1.9; AltName: Full=Acetoacetyl-CoA thiolase; AltName: Full=Ergosterol biosynthesis protein 10;
FUNCTION: Catalyzes the formation of acetoacetyl-CoA in the biosynthesis of mevalonate, an intermediate required for the biosynthesis of sterols and nonsterol isoprenoids.
CATALYTIC ACTIVITY: 2 acetyl-CoA = CoA + acetoacetyl-CoA.
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.16 mM for CoA; KM=0.35 mM for acetoacetyl-CoA; pH dependence: Optimum pH is 8.8;
PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
SUBUNIT: Multimeric.
SUBCELLULAR LOCATION: Cytoplasm.
INDUCTION: Induced by low intracellular sterol levels.
MISCELLANEOUS: Present with 60895 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the thiolase family.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR002155 - Thiolase
IPR016039 - Thiolase-like
IPR016038 - Thiolase-like_subgr
IPR020615 - Thiolase_acyl_enz_int_AS
IPR020610 - Thiolase_AS
IPR020617 - Thiolase_C
IPR020613 - Thiolase_CS
IPR020616 - Thiolase_N

Pfam Domains:
PF02803 - Thiolase, C-terminal domain
PF00108 - Thiolase, N-terminal domain

ModBase Predicted Comparative 3D Structure on P41338
FrontTopSide
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
HumanMouseRatZebrafishD. melanogasterC. elegans
Genome BrowserGenome BrowserGenome BrowserNo orthologGenome BrowserGenome Browser
Gene DetailsGene DetailsGene Details Gene DetailsGene Details
Gene SorterGene SorterGene Sorter Gene SorterGene Sorter