COX10/YPL172C Summary Help

Standard Name COX10
Systematic Name YPL172C
Feature Type ORF, Verified
Description Heme A:farnesyltransferase; catalyzes the first step in the conversion of protoheme to the heme A prosthetic group required for cytochrome c oxidase activity; human ortholog is associated with mitochondrial disorders (1, 2 and see Summary Paragraph)
Name Description Cytochrome c OXidase
Chromosomal Location
ChrXVI:225741 to 224353 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All COX10 GO evidence and references
  View Computational GO annotations for COX10
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Regulators 2 genes
Classical genetics
Large-scale survey
205 total interaction(s) for 163 unique genes/features.
Physical Interactions
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 2
  • Biochemical Activity: 1

Genetic Interactions
  • Dosage Lethality: 1
  • Dosage Rescue: 4
  • Negative Genetic: 176
  • Phenotypic Enhancement: 1
  • Positive Genetic: 12
  • Synthetic Growth Defect: 3
  • Synthetic Rescue: 4

Expression Summary
Length (a.a.) 462
Molecular Weight (Da) 52,147
Isoelectric Point (pI) 10.7
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXVI:225741 to 224353 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1389 225741..224353 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000006093

The COX10 gene encodes the mitochondrial enzyme hemeA:farnesyltransferase, also known as heme O synthase or protoheme IX farnesyltransferase (3, 4). It catalyzes the transfer of a farnesyl group to protoheme IX, forming heme O. Heme O is then converted to heme A, probably by the action of a monooxygenase composed of Cox15p, Yah1p, and Arh1p (5). Two heme A molecules generated by this pathway are incorporated into the Cox1p subunit of cytochrome c oxidase, which is the terminal member of the mitochondrial electron transport chain involved in cellular respiration.

Because the heme A cofactor is essential to cytochrome c oxidase and Cox10p is required for its synthesis, cox10 mutations lead to a deficiency in respiratory growth. Cytochrome c oxidase subunits are present in the cox10 mutant but are not assembled into a functional enzyme (6).

Homologs of Cox10p are found in various organisms from prokaryotes to humans (6, 7, 8, 9, 2). The human homolog functionally complements the yeast cox10 mutation (2). Mutations in the human homolog lead to cytochrome c oxidase deficiency, which may manifest itself as tubulopathy, leukodystrophy, Leigh syndrome, or infantile hypertrophic cardiomyopathy (1, 10).

Last updated: 2006-07-20 Contact SGD

References cited on this page View Complete Literature Guide for COX10
1) Valnot I, et al.  (2000) A mutation in the human heme A:farnesyltransferase gene (COX10 ) causes cytochrome c oxidase deficiency. Hum Mol Genet 9(8):1245-9
2) Glerum DM and Tzagoloff A  (1994) Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant. Proc Natl Acad Sci U S A 91(18):8452-6
3) Tzagoloff A, et al.  (1993) On the functions of the yeast COX10 and COX11 gene products. Biochem Mol Biol Int 31(3):593-8
4) Sickmann A, et al.  (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc Natl Acad Sci U S A 100(23):13207-12
5) Barros MH, et al.  (2002) Mitochondrial ferredoxin is required for heme A synthesis in Saccharomyces cerevisiae. J Biol Chem 277(12):9997-10002
6) Nobrega MP, et al.  (1990) COX10 codes for a protein homologous to the ORF1 product of Paracoccus denitrificans and is required for the synthesis of yeast cytochrome oxidase. J Biol Chem 265(24):14220-6
7) Hill J, et al.  (1992) Demonstration by FTIR that the bo-type ubiquinol oxidase of Escherichia coli contains a heme-copper binuclear center similar to that in cytochrome c oxidase and that proper assembly of the binuclear center requires the cyoE gene product. Biochemistry 31(46):11435-40
8) Cao J, et al.  (1992) Cytochrome aa3 of Rhodobacter sphaeroides as a model for mitochondrial cytochrome c oxidase. The coxII/coxIII operon codes for structural and assembly proteins homologous to those in yeast. J Biol Chem 267(34):24273-8
9) Svensson B, et al.  (1993) Bacillus subtilis CtaA and CtaB function in haem A biosynthesis. Mol Microbiol 10(1):193-201
10) Moraes CT, et al.  (2004) Defects in the biosynthesis of mitochondrial heme c and heme a in yeast and mammals. Biochim Biophys Acta 1659(2-3):153-9