An official website of the United States government

erg1 - squalene monooxygenase Erg1 (fission yeast)

Symbol
Dates
  • Create:
    2016-09-14
  • Modify:
    2025-01-18

1 Names and Identifiers

1.1 Other Identifiers

1.1.1 Enzyme Commission (EC) Number

1.1.2 PomBase Systematic ID

1.1.3 VEuPathDB ID

2 Proteins

2.1 Protein Function

Squalene epoxidase; part of the third module of ergosterol biosynthesis pathway that includes by the late steps of the pathway (PMID: 33223513). Erg1 catalyzes the epoxidation of squalene into 2,3-epoxysqualene (PMID: 33223513). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. The lanosterol 14-alpha-demethylase erg11/cyp1 catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. In the next steps, a complex process involving various demethylation, reduction and desaturation reactions catalyzed by the C-14 reductase erg24 and the C-4 demethylation complex erg25-erg26-erg27 leads to the production of zymosterol. Erg28 likely functions in the C-4 demethylation complex reaction by tethering erg26 and Erg27 to the endoplasmic reticulum or to facilitate interaction between these proteins. Then, the sterol 24-C-methyltransferase erg6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase erg2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturases erg31 and erg32 then catalyze the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase erg4 to produce ergosterol (Probable) (PMID: 18310029). In the genus Schizosaccharomyces, a second route exists between lanosterol and fecosterol, via the methylation of lanosterol to eburicol by erg6, followed by C14-demethylation by erg11/cyp1 and C4-demethylation by the demethylation complex erg25-erg26-erg27 (Probable) (PMID: 8586261).

2.2 Protein 3D Structures

2.2.1 AlphaFold Structures

Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605

2.3 Protein Targets

3 Interactions and Pathways

3.1 Interactions

3.2 Pathways

4 Biochemical Reactions

5 Expression

6 Literature

6.1 Consolidated References

6.2 Gene-Chemical Co-Occurrences in Literature

6.3 Gene-Gene Co-Occurrences in Literature

6.4 Gene-Disease Co-Occurrences in Literature

7 Information Sources

  1. NCBI Gene
    LICENSE
    NCBI Website and Data Usage Policies and Disclaimers
    https://www.ncbi.nlm.nih.gov/home/about/policies/
  2. PubChem
  3. BioGRID
    LICENSE
    The MIT License (MIT); Copyright Mike Tyers Lab
    https://wiki.thebiogrid.org/doku.php/terms_and_conditions
  4. NCBI Gene Expression Omnibus (GEO)
  5. PomBase: Fission Yeast Resource
    LICENSE
    All data curated by PomBase, including data from Canto community curation, are licensed under the Creative Commons Attribution 4.0 International license.
    https://www.pombase.org/about/terms-of-use
  6. UniProt
    LICENSE
    We have chosen to apply the Creative Commons Attribution (CC BY 4.0, http://creativecommons.org/licenses/by/4.0/) License to all copyrightable parts of our databases.
    https://www.uniprot.org/help/license
  7. VEuPathDB: The Eukaryotic Pathogen, Vector and Host Informatics Resource
    LICENSE
    All data on VEuPathDB websites are provided freely for public use.
    https://veupathdb.org/veupathdb/app/static-content/about.html
  8. AlphaFold DB
    LICENSE
    All of the data provided is freely available for both academic and commercial use under Creative Commons Attribution 4.0 (CC-BY 4.0) licence terms.
    https://alphafold.ebi.ac.uk/faq
  9. Rhea - annotated reactions database
    LICENSE
    Rhea has chosen to apply the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/). This means that you are free to copy, distribute, display and make commercial use of the database in all legislations, provided you credit (cite) Rhea.
    https://www.rhea-db.org/help/license-disclaimer
CONTENTS