ERG10/YPL028W Summary Help

Standard Name ERG10 1, 2
Systematic Name YPL028W
Alias LPB3 , TSM0115
Feature Type ORF, Verified
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 (1 and see Summary Paragraph)
Name Description ERGosterol biosynthesis 1, 2
Chromosomal Location
ChrXVI:498096 to 499292 | ORF Map | GBrowse
Gbrowse
Genetic position: -22 cM
Gene Ontology Annotations All ERG10 GO evidence and references
  View Computational GO annotations for ERG10
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 11 genes
Resources
Pathways
Classical genetics
null
Large-scale survey
null
reduction of function
repressible
Resources
106 total interaction(s) for 93 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 19
  • Affinity Capture-RNA: 6
  • Co-purification: 1
  • PCA: 2

Genetic Interactions
  • Negative Genetic: 70
  • Positive Genetic: 6
  • Synthetic Lethality: 2

Resources
Expression Summary
histogram
Resources
Length (a.a.) 398
Molecular Weight (Da) 41,728
Isoelectric Point (pI) 7.38
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXVI:498096 to 499292 | ORF Map | GBrowse
SGD ORF map
Genetic position: -22 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1197 498096..499292 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000005949
SUMMARY PARAGRAPH for ERG10

ERG10 encodes acetyl-CoA C-acetyltransferase (also called acetoacetyl-CoA thiolase), a cytosolic enzyme that transfers an acetyl group from one acetyl-CoA molecule to another, forming acetoacetyl-CoA (1, 3). The formation of acetoacetyl-CoA is the first step in the biosynthesis of mevalonate, which is required in turn for the biosynthesis of sterols and nonsterol isoprenoids (3); in yeast, ergosterol is the end product of the sterol biosynthetic pathway (4, 5).

Cells lacking Erg10p are viable but lack detectable acetyl-CoA C-acetyltransferase and are mevalonate auxotrophs (1). Expression of ERG10 is regulated by a sterol-mediated feedback system (6).

Enzymes similar to Erg10p are found in many diverse organisms (1); the enzymes from Saccharomyces uvarum and radish can complement S. cerevisiae erg10 mutants (7, 8).

Last updated: 2000-08-21 Contact SGD

References cited on this page View Complete Literature Guide for ERG10
1) Hiser L, et al.  (1994) ERG10 from Saccharomyces cerevisiae encodes acetoacetyl-CoA thiolase. J Biol Chem 269(50):31383-9
2) Karst F and Lacroute F  (1977) Ertosterol biosynthesis in Saccharomyces cerevisiae: mutants deficient in the early steps of the pathway. Mol Gen Genet 154(3):269-77
3) Stryer L  (1995) Biochemistry (4th ed.). New York: W. H. Freeman and Company
4) Paltauf F, et al.  (1992) "Regulation and compartmentalization of lipid synthesis in yeast." Pp. 415-500 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression, edited by Jones EW, Pringle JR and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
5) Parks LW, et al.  (1995) Biochemical and physiological effects of sterol alterations in yeast--a review. Lipids 30(3):227-30
6) Dimster-Denk D and Rine J  (1996) Transcriptional regulation of a sterol-biosynthetic enzyme by sterol levels in Saccharomyces cerevisiae. Mol Cell Biol 16(8):3981-9
7) Dequin S, et al.  (1988) Cloning, sequencing and analysis of the yeast S. uvarum ERG10 gene encoding acetoacetyl CoA thiolase. Curr Genet 13(6):471-8
8) Vollack KU and Bach TJ  (1996) Cloning of a cDNA encoding cytosolic acetoacetyl-coenzyme A thiolase from radish by functional expression in Saccharomyces cerevisiae. Plant Physiol 111(4):1097-107